cached image

Neville R. Kallenbach - Publications

Affiliations: 
New York University, New York, NY, United States 
Area:
Biophysical chemistry of proteins and nucleic acids
Website:
http://chemistry.as.nyu.edu/object/nevillerkallenbach.html

164/500 high-probability publications. We are testing a new system for linking publications to authors. You can help! If you notice any inaccuracies, please sign in and mark papers as correct or incorrect matches. If you identify any major omissions or other inaccuracies in the publication list, please let us know.

Year Citation  Score
2015 Bahar AA, Liu Z, Garafalo M, Kallenbach N, Ren D. Controlling Persister and Biofilm Cells of Gram-Negative Bacteria with a New 1,3,5-Triazine Derivative. Pharmaceuticals (Basel, Switzerland). 8: 696-710. PMID 26473884 DOI: 10.3390/Ph8040696  0.407
2015 Bahar AA, Liu Z, Totsingan F, Buitrago C, Kallenbach N, Ren D. Synthetic dendrimeric peptide active against biofilm and persister cells of Pseudomonas aeruginosa. Applied Microbiology and Biotechnology. 99: 8125-35. PMID 26012420 DOI: 10.1007/S00253-015-6645-7  0.437
2014 Xiao X, Kallenbach N, Zhang Y. Peptide Conformation Analysis Using an Integrated Bayesian Approach. Journal of Chemical Theory and Computation. 10: 4152-4159. PMID 25221447 DOI: 10.1021/Ct500433D  0.424
2014 Miller SE, Watkins AM, Kallenbach NR, Arora PS. Effects of side chains in helix nucleation differ from helix propagation. Proceedings of the National Academy of Sciences of the United States of America. 111: 6636-41. PMID 24753597 DOI: 10.1073/Pnas.1322833111  0.44
2013 Vanderlee G, Liu Z, Kallenbach NR, Yip CM. Action of Arginine and Tryptophan Containing Antimicrobial Peptides on Supported Lipid Bilayers Biophysical Journal. 104: 236a. DOI: 10.1016/J.Bpj.2012.11.1335  0.438
2013 Vanderlee G, Liu Z, Kallenbach NR, Yip CM. Action of Arginine and Tryptophan Containing Antimicrobial Peptides on Supported Lipid Bilayers Biophysical Journal. 104: 236a. DOI: 10.1016/j.bpj.2012.11.1335  0.37
2012 Kallenbach NR, Dominguez R. Dystrophin's tandem calponin-homology domains: is the case closed? Biophysical Journal. 103: 1818-9. PMID 23199908 DOI: 10.1016/J.Bpj.2012.09.037  0.343
2012 Miller SE, Kallenbach NR, Arora PS. Reversible α-helix formation controlled by a hydrogen bond surrogate. Tetrahedron. 68: 4434-4437. PMID 23144512 DOI: 10.1016/J.Tet.2011.12.068  0.36
2012 He L, Navarro AE, Shi Z, Kallenbach NR. End effects influence short model peptide conformation. Journal of the American Chemical Society. 134: 1571-6. PMID 22176215 DOI: 10.1021/Ja2070363  0.731
2012 Liu Z, Cai Y, Young AW, Totsingan F, Jiwrajka N, Shi Z, Kallenbach NR. OH radical production stimulated by (RW)4D, a synthetic antimicrobial agent and indolicidin Medchemcomm. 3: 1548-1554. DOI: 10.1039/C2Md20272G  0.56
2011 Chen X, Zhang M, Zhou C, Kallenbach NR, Ren D. Control of bacterial persister cells by Trp/Arg-containing antimicrobial peptides. Applied and Environmental Microbiology. 77: 4878-85. PMID 21622798 DOI: 10.1128/Aem.02440-10  0.524
2011 Shi Z, Kallenbach NR. Ramachandran redux. Proceedings of the National Academy of Sciences of the United States of America. 108: 3-4. PMID 21178075 DOI: 10.1073/Pnas.1017021108  0.565
2011 Young AW, Liu Z, Zhou C, Totsingan F, Jiwrajka N, Shi Z, Kallenbach NR. Structure and antimicrobial properties of multivalent short peptides Medchemcomm. 2: 308-314. DOI: 10.1039/C0Md00247J  0.665
2011 Shi Z, Zhou C, Liu Z, Totsingan F, Kallenbach NR. Amino Acid-Based Dendrimers Amino Acids, Peptides and Proteins in Organic Chemistry. 4: 491-517. DOI: 10.1002/9783527631827.ch15  0.599
2010 Hou S, Liu Z, Young AW, Mark SL, Kallenbach NR, Ren D. Effects of Trp- and Arg-containing antimicrobial-peptide structure on inhibition of Escherichia coli planktonic growth and biofilm formation. Applied and Environmental Microbiology. 76: 1967-74. PMID 20097816 DOI: 10.1128/Aem.02321-09  0.465
2010 Totsingan F, Jain V, Bracken WC, Faccini A, Tedeschi T, Marchelli R, Corradini R, Kallenbach NR, Green MM. Conformational heterogeneity in PNA:PNA duplexes Macromolecules. 43: 2692-2703. DOI: 10.1021/Ma902797F  0.387
2009 Hou S, Zhou C, Liu Z, Young AW, Shi Z, Ren D, Kallenbach NR. Antimicrobial dendrimer active against Escherichia coli biofilms. Bioorganic & Medicinal Chemistry Letters. 19: 5478-81. PMID 19682902 DOI: 10.1016/J.Bmcl.2009.07.077  0.648
2009 Stoddard E, Ni H, Cannon G, Zhou C, Kallenbach N, Malamud D, Weissman D. gp340 promotes transcytosis of human immunodeficiency virus type 1 in genital tract-derived cell lines and primary endocervical tissue. Journal of Virology. 83: 8596-603. PMID 19553331 DOI: 10.1128/Jvi.00744-09  0.431
2009 Chen K, Liu Z, Zhou C, Bracken WC, Kallenbach NR. Extended conformations in alanine peptides Biophysical Journal. 96: 4a-5a. DOI: 10.1016/J.Bpj.2008.12.916  0.693
2008 Bell AJ, Chauhan S, Woodson SA, Kallenbach NR. Interactions of recombinant HMGB proteins with branched RNA substrates. Biochemical and Biophysical Research Communications. 377: 262-7. PMID 18845125 DOI: 10.1016/J.Bbrc.2008.09.131  0.356
2008 Deng Y, Liu J, Zheng Q, Li Q, Kallenbach NR, Lu M. A heterospecific leucine zipper tetramer. Chemistry & Biology. 15: 908-19. PMID 18804028 DOI: 10.1016/J.Chembiol.2008.07.008  0.407
2008 Chapman R, Kulp JL, Patgiri A, Kallenbach NR, Bracken C, Arora PS. Trapping a folding intermediate of the alpha-helix: stabilization of the pi-helix. Biochemistry. 47: 4189-95. PMID 18335996 DOI: 10.1021/Bi800136M  0.38
2008 Zhou C, Min J, Liu Z, Young A, Deshazer H, Gao T, Chang YT, Kallenbach NR. Synthesis and biological evaluation of novel 1,3,5-triazine derivatives as antimicrobial agents. Bioorganic & Medicinal Chemistry Letters. 18: 1308-11. PMID 18226902 DOI: 10.1016/J.Bmcl.2008.01.031  0.569
2007 Liu J, Zheng Q, Deng Y, Li Q, Kallenbach NR, Lu M. Conformational specificity of the lac repressor coiled-coil tetramerization domain. Biochemistry. 46: 14951-9. PMID 18052214 DOI: 10.1021/Bi701930D  0.436
2007 Chen K, Liu Z, Zhou C, Bracken WC, Kallenbach NR. Spin relaxation enhancement confirms dominance of extended conformations in short alanine peptides. Angewandte Chemie (International Ed. in English). 46: 9036-9. PMID 17943945 DOI: 10.1002/Anie.200703376  0.64
2007 Liu Z, Young AW, Hu P, Rice AJ, Zhou C, Zhang Y, Kallenbach NR. Tuning the membrane selectivity of antimicrobial peptides by using multivalent design. Chembiochem : a European Journal of Chemical Biology. 8: 2063-5. PMID 17924379 DOI: 10.1002/Cbic.200700502  0.556
2007 Deng Y, Zheng Q, Liu J, Cheng CS, Kallenbach NR, Lu M. Self-assembly of coiled-coil tetramers in the 1.40 A structure of a leucine-zipper mutant. Protein Science : a Publication of the Protein Society. 16: 323-8. PMID 17189475 DOI: 10.1110/Ps.062590807  0.359
2007 Liu Z, Brady A, Young A, Rasimick B, Chen K, Zhou C, Kallenbach NR. Length effects in antimicrobial peptides of the (RW)n series. Antimicrobial Agents and Chemotherapy. 51: 597-603. PMID 17145799 DOI: 10.1128/Aac.00828-06  0.671
2006 Liu J, Deng Y, Zheng Q, Cheng CS, Kallenbach NR, Lu M. A parallel coiled-coil tetramer with offset helices. Biochemistry. 45: 15224-31. PMID 17176044 DOI: 10.1021/Bi061914M  0.448
2006 Liu J, Zheng Q, Deng Y, Cheng CS, Kallenbach NR, Lu M. A seven-helix coiled coil. Proceedings of the National Academy of Sciences of the United States of America. 103: 15457-62. PMID 17030805 DOI: 10.1073/Pnas.0604871103  0.407
2006 Liu J, Zheng Q, Deng Y, Kallenbach NR, Lu M. Conformational transition between four and five-stranded phenylalanine zippers determined by a local packing interaction. Journal of Molecular Biology. 361: 168-79. PMID 16828114 DOI: 10.1016/J.Jmb.2006.05.063  0.442
2006 Liu Z, Deshazer H, Rice AJ, Chen K, Zhou C, Kallenbach NR. Multivalent antimicrobial peptides from a reactive polymer scaffold. Journal of Medicinal Chemistry. 49: 3436-9. PMID 16759083 DOI: 10.1021/Jm0601452  0.649
2006 Shi Z, Chen K, Liu Z, Kallenbach NR. Conformation of the backbone in unfolded proteins. Chemical Reviews. 106: 1877-97. PMID 16683759 DOI: 10.1021/Cr040433A  0.66
2006 Deng Y, Liu J, Zheng Q, Eliezer D, Kallenbach NR, Lu M. Antiparallel four-stranded coiled coil specified by a 3-3-1 hydrophobic heptad repeat. Structure (London, England : 1993). 14: 247-55. PMID 16472744 DOI: 10.1016/J.Str.2005.10.010  0.396
2006 Shi Z, Chen K, Liu Z, Sosnick TR, Kallenbach NR. PII structure in the model peptides for unfolded proteins: studies on ubiquitin fragments and several alanine-rich peptides containing QQQ, SSS, FFF, and VVV. Proteins. 63: 312-21. PMID 16362932 DOI: 10.1002/Prot.20788  0.71
2005 Shi Z, Chen K, Liu Z, Ng A, Bracken WC, Kallenbach NR. Polyproline II propensities from GGXGG peptides reveal an anticorrelation with beta-sheet scales. Proceedings of the National Academy of Sciences of the United States of America. 102: 17964-8. PMID 16330763 DOI: 10.1073/Pnas.0507124102  0.676
2005 Chen K, Liu Z, Zhou C, Shi Z, Kallenbach NR. Neighbor effect on PPII conformation in alanine peptides. Journal of the American Chemical Society. 127: 10146-7. PMID 16028907 DOI: 10.1021/Ja052094O  0.732
2005 Lee-Huang S, Maiorov V, Huang PL, Ng A, Lee HC, Chang YT, Kallenbach N, Huang PL, Chen HC. Structural and functional modeling of human lysozyme reveals a unique nonapeptide, HL9, with anti-HIV activity. Biochemistry. 44: 4648-55. PMID 15779891 DOI: 10.1021/Bi0477081  0.346
2004 Liu Z, Chen K, Ng A, Shi Z, Woody RW, Kallenbach NR. Solvent dependence of PII conformation in model alanine peptides. Journal of the American Chemical Society. 126: 15141-50. PMID 15548011 DOI: 10.1021/Ja047594G  0.683
2004 Liu J, Yong W, Deng Y, Kallenbach NR, Lu M. Atomic structure of a tryptophan-zipper pentamer. Proceedings of the National Academy of Sciences of the United States of America. 101: 16156-61. PMID 15520380 DOI: 10.1073/Pnas.0405319101  0.393
2004 Chen K, Liu Z, Kallenbach NR. The polyproline II conformation in short alanine peptides is noncooperative. Proceedings of the National Academy of Sciences of the United States of America. 101: 15352-7. PMID 15489268 DOI: 10.1073/Pnas.0406657101  0.612
2004 McColl IH, Blanch EW, Hecht L, Kallenbach NR, Barron LD. Vibrational Raman optical activity characterization of poly(l-proline) II helix in alanine oligopeptides. Journal of the American Chemical Society. 126: 5076-7. PMID 15099084 DOI: 10.1021/Ja049271Q  0.385
2004 Cao W, Bracken C, Kallenbach NR, Lu M. Helix formation and the unfolded state of a 52-residue helical protein. Protein Science : a Publication of the Protein Society. 13: 177-89. PMID 14691233 DOI: 10.1110/Ps.03383004  0.379
2003 Ding L, Chen K, Santini PA, Shi Z, Kallenbach NR. The pentapeptide GGAGG has PII conformation. Journal of the American Chemical Society. 125: 8092-3. PMID 12837065 DOI: 10.1021/Ja035551E  0.676
2002 Shi Z, Olson CA, Bell AJ, Kallenbach NR. Non-classical helix-stabilizing interactions: C-H...O H-bonding between Phe and Glu side chains in alpha-helical peptides. Biophysical Chemistry. 101: 267-79. PMID 12488007 DOI: 10.1016/S0301-4622(02)00171-0  0.52
2002 Bell AJ, Xin H, Taudte S, Shi Z, Kallenbach NR. Metal-dependent stabilization of an active HMG protein. Protein Engineering. 15: 817-25. PMID 12468716 DOI: 10.1093/Protein/15.10.817  0.774
2002 Shi Z, Olson CA, Kallenbach NR, Sosnick TR. D/H amide isotope effect in model alpha-helical peptides. Journal of the American Chemical Society. 124: 13994-5. PMID 12440888 DOI: 10.1021/Ja027740N  0.551
2002 Shi Z, Woody RW, Kallenbach NR. Is polyproline II a major backbone conformation in unfolded proteins? Advances in Protein Chemistry. 62: 163-240. PMID 12418104 DOI: 10.1016/S0065-3233(02)62008-X  0.585
2002 Shi Z, Olson CA, Rose GD, Baldwin RL, Kallenbach NR. Polyproline II structure in a sequence of seven alanine residues. Proceedings of the National Academy of Sciences of the United States of America. 99: 9190-5. PMID 12091708 DOI: 10.1073/Pnas.112193999  0.606
2002 Shi Z, Olson CA, Kallenbach NR. Cation-pi interaction in model alpha-helical peptides. Journal of the American Chemical Society. 124: 3284-91. PMID 11916412 DOI: 10.1021/Ja0174938  0.573
2002 Shi Z, Krantz BA, Kallenbach N, Sosnick TR. Contribution of hydrogen bonding to protein stability estimated from isotope effects. Biochemistry. 41: 2120-9. PMID 11841202 DOI: 10.1021/Bi011307T  0.526
2001 Shi Z, Olson CA, Bell AJ, Kallenbach NR. Stabilization of alpha-helix structure by polar side-chain interactions: complex salt bridges, cation-pi interactions, and C-H em leader O H-bonds. Biopolymers. 60: 366-80. PMID 12115147 DOI: 10.1002/1097-0282(2001)60:5<366::Aid-Bip10177>3.0.Co;2-5  0.574
2001 Taudte S, Xin H, Bell AJ, Kallenbach NR. Interactions between HMG boxes. Protein Engineering. 14: 1015-23. PMID 11809932 DOI: 10.1093/Protein/14.12.1015  0.782
2001 Olson CA, Shi Z, Kallenbach NR. Polar interactions with aromatic side chains in alpha-helical peptides: Ch...O H-bonding and cation-pi interactions. Journal of the American Chemical Society. 123: 6451-2. PMID 11427086 DOI: 10.1021/ja015590v  0.466
2001 Olson CA, Spek EJ, Shi Z, Vologodskii A, Kallenbach NR. Cooperative helix stabilization by complex Arg-Glu salt bridges. Proteins. 44: 123-32. PMID 11391775 DOI: 10.1002/Prot.1079  0.583
2001 Kallenbach N. Breaking open a protein barrel Proceedings of the National Academy of Sciences of the United States of America. 98: 2958-2960. PMID 11248013 DOI: 10.1073/Pnas.071051798  0.37
2000 Xin H, Taudte S, Kallenbach NR, Limbach MP, Zitomer RS. DNA binding by single HMG box model proteins. Nucleic Acids Research. 28: 4044-50. PMID 11024186 DOI: 10.1093/Nar/28.20.4044  0.779
2000 Taudte S, Xin H, Kallenbach NR. Alanine mutagenesis of high-mobility-group-protein-1 box B (HMG1-B). The Biochemical Journal. 347: 807-14. PMID 10769186 DOI: 10.1042/0264-6021:3470807  0.781
1999 Lu M, Shu W, Ji H, Spek E, Wang L, Kallenbach NR. Helix capping in the GCN4 leucine zipper. Journal of Molecular Biology. 288: 743-52. PMID 10329176 DOI: 10.1006/Jmbi.1999.2707  0.422
1999 Kallenbach NR, Gong Y. C-terminal capping motifs in model helical peptides. Bioorganic & Medicinal Chemistry. 7: 143-51. PMID 10199664 DOI: 10.1016/S0968-0896(98)00231-4  0.44
1999 Spek EJ, Olson CA, Shi Z, Kallenbach NR. Alanine is an intrinsic α-helix stabilizing amino acid Journal of the American Chemical Society. 121: 5571-5572. DOI: 10.1021/Ja990056X  0.498
1998 Wang L, Kallenbach NR. Proteolysis as a measure of the free energy difference between cytochrome c and its derivatives. Protein Science : a Publication of the Protein Society. 7: 2460-4. PMID 9828013 DOI: 10.1002/Pro.5560071124  0.306
1998 Spek EJ, Bui AH, Lu M, Kallenbach NR. Surface salt bridges stabilize the GCN4 leucine zipper. Protein Science : a Publication of the Protein Society. 7: 2431-7. PMID 9828010 DOI: 10.1002/Pro.5560071121  0.373
1998 Kallenbach NR, Spek EJ. Modified amino acids as probes of helix stability. Methods in Enzymology. 295: 26-41. PMID 9750212 DOI: 10.1016/S0076-6879(98)95033-9  0.321
1998 Wang L, Chen RX, Kallenbach NR. Proteolysis as a probe of thermal unfolding of cytochrome c. Proteins. 30: 435-41. PMID 9533627 DOI: 10.1002/(Sici)1097-0134(19980301)30:4<435::Aid-Prot10>3.0.Co;2-J  0.349
1998 Yang J, Zhao K, Gong Y, Vologodskii A, Kallenbach NR. α-Helix nucleation constant in copolypeptides of alanine and ornithine or lysine Journal of the American Chemical Society. 120: 10646-10652. DOI: 10.1021/Ja982319D  0.426
1998 Mayne L, Englander SW, Qiu R, Yang J, Gong Y, Spek EJ, Kallenbach NR. Stabilizing effect of a multiple salt bridge in a prenucleated peptide Journal of the American Chemical Society. 120: 10643-10645. DOI: 10.1021/Ja981592C  0.584
1997 Yang J, Spek EJ, Gong Y, Zhou H, Kallenbach NR. The role of context on alpha-helix stabilization: host-guest analysis in a mixed background peptide model. Protein Science : a Publication of the Protein Society. 6: 1264-72. PMID 9194186 DOI: 10.1002/Pro.5560060614  0.446
1997 Gibb CL, Cheng W, Morozov VN, Kallenbach NR. Effect of nuclear protein HMG1 on in vitro slippage synthesis of the tandem repeat dTG x dCA. Biochemistry. 36: 5418-24. PMID 9154923 DOI: 10.1021/Bi962037V  0.381
1997 Zhong M, Marky LA, Kallenbach NR, Kupke DW. Thermodynamics of dT--dT base pair mismatching in linear DNA duplexes and three-arm DNA junctions. Biochemistry. 36: 2485-91. PMID 9054553 DOI: 10.1021/Bi962373B  0.368
1996 Berger JS, Ernst JA, Nicoletta AC, Hull LA, Yang J, Qiu R, Morozov VN, Kallenbach NR. Stabilization of helical peptides by mixed spaced salt bridges. Journal of Biomolecular Structure & Dynamics. 14: 285-91. PMID 9016406 DOI: 10.1080/07391102.1996.10508124  0.58
1996 Zhao Y, Cheng W, Gibb CL, Gupta G, Kallenbach NR. HMG box proteins interact with multiple tandemly repeated (GCC)n (GGC)m DNA sequences. Journal of Biomolecular Structure & Dynamics. 14: 235-8. PMID 8913860 DOI: 10.1080/07391102.1996.10508113  0.412
1995 Guo Q, Lu M, Kallenbach NR. Effect of hemimethylation and methylation of adenine on the structure and stability of model DNA duplexes. Biochemistry. 34: 16359-64. PMID 8845361 DOI: 10.1021/Bi00050A016  0.331
1995 Gong Y, Zhou HX, Guo M, Kallenbach NR. Structural analysis of the N- and C-termini in a peptide with consensus sequence. Protein Science : a Publication of the Protein Society. 4: 1446-56. PMID 8520470 DOI: 10.1002/Pro.5560040802  0.43
1995 Zhong M, Lin L, Kallenbach NR. A method for probing the topography and interactions of proteins: footprinting of myoglobin. Proceedings of the National Academy of Sciences of the United States of America. 92: 2111-5. PMID 7892233 DOI: 10.1073/Pnas.92.6.2111  0.323
1994 Zhou HX, Lyu P, Wemmer DE, Kallenbach NR. Alpha helix capping in synthetic model peptides by reciprocal side chain-main chain interactions: evidence for an N terminal "capping box". Proteins. 18: 1-7. PMID 8146119 DOI: 10.1002/Prot.340180103  0.453
1994 Hernández LI, Zhong M, Courtney SH, Marky LA, Kallenbach NR. Equilibrium analysis of ethidium binding to DNA containing base mismatches and branches. Biochemistry. 33: 13140-6. PMID 7947720 DOI: 10.1021/Bi00248A025  0.372
1994 Seeman NC, Kallenbach NR. DNA branched junctions. Annual Review of Biophysics and Biomolecular Structure. 23: 53-86. PMID 7919792 DOI: 10.1146/Annurev.Bb.23.060194.000413  0.301
1994 Lin L, Pinker RJ, Phillips GN, Kallenbach NR. Stabilization of myoglobin by multiple alanine substitutions in helical positions. Protein Science : a Publication of the Protein Society. 3: 1430-5. PMID 7833805 DOI: 10.1002/Pro.5560030909  0.377
1994 Lin L, Pinker RJ, Forde K, Rose GD, Kallenbach NR. Molten globular characteristics of the native state of apomyoglobin. Nature Structural Biology. 1: 447-52. PMID 7664063 DOI: 10.1038/Nsb0794-447  0.363
1994 Zhong M, Kallenbach NR. Mapping tRNA and 5S RNA tertiary structures by charge dependent Fe(II)-catalyzed cleavage. Journal of Biomolecular Structure & Dynamics. 11: 901-11. PMID 7515624 DOI: 10.1080/07391102.1994.10508040  0.312
1993 Zhong M, Kallenbach NR. Conformation and thermodynamics of DNA "necks". Models for three-arm branch formation in a duplex. Journal of Molecular Biology. 230: 766-78. PMID 8478932 DOI: 10.1006/Jmbi.1993.1199  0.381
1993 Guo Q, Lu M, Kallenbach NR. Effect of thymine tract length on the structure and stability of model telomeric sequences. Biochemistry. 32: 3596-603. PMID 8466901 DOI: 10.1021/Bi00065A010  0.373
1993 Lu M, Guo Q, Kallenbach NR. Thermodynamics of G-tetraplex formation by telomeric DNAs. Biochemistry. 32: 598-601. PMID 8422371 DOI: 10.1021/Bi00053A027  0.376
1993 Lyu PC, Wemmer DE, Zhou HX, Pinker RJ, Kallenbach NR. Capping interactions in isolated alpha helices: position-dependent substitution effects and structure of a serine-capped peptide helix. Biochemistry. 32: 421-5. PMID 8422351 DOI: 10.1021/Bi00053A006  0.464
1993 Morozov VN, Sherman J, Kallenbach NR, Du SM, Seeman NC. A scanning tunnelling microscopy study of the formation and chemical activation of step defects on the basal plane of pyrolytic graphite. Journal of Microscopy. 170: 237-45. PMID 8396646 DOI: 10.1111/J.1365-2818.1993.Tb03347.X  0.459
1993 Gupta G, Garcia AE, Guo Q, Lu M, Kallenbach NR. Structure of a parallel-stranded tetramer of the Oxytricha telomeric DNA sequence dT4G4. Biochemistry. 32: 7098-103. PMID 8393704 DOI: 10.1021/Bi00079A005  0.381
1993 Pinker RJ, Lin L, Rose GD, Kallenbach NR. Effects of alanine substitutions in alpha-helices of sperm whale myoglobin on protein stability. Protein Science : a Publication of the Protein Society. 2: 1099-105. PMID 8358293 DOI: 10.1002/Pro.5560020704  0.425
1993 Zhong M, Rashes MS, Kallenbach NR. Effect of T-T base mismatches on three-arm DNA junctions. Biochemistry. 32: 6898-907. PMID 8334121 DOI: 10.1021/Bi00078A013  0.357
1993 Lin L, Pinker RJ, Kallenbach NR. Alpha-helix stability and the native state of myoglobin. Biochemistry. 32: 12638-43. PMID 8251481 DOI: 10.1021/Bi00210A011  0.441
1993 Pinker RJ, Kallenbach NR, Rose GD. Effect of alanine substitutions in alpha helices of sperm whale myoglobin on stability of the native protein Protein Engineering Design & Selection. 6. DOI: 10.1093/Protein/6.Supplement.21-B  0.322
1992 Lyu PC, Gans PJ, Kallenbach NR. Energetic contribution of solvent-exposed ion pairs to alpha-helix structure. Journal of Molecular Biology. 223: 343-50. PMID 1731079 DOI: 10.1016/0022-2836(92)90735-3  0.469
1992 Lu M, Guo Q, Kallenbach NR. Interaction of drugs with branched DNA structures. Critical Reviews in Biochemistry and Molecular Biology. 27: 157-90. PMID 1587142 DOI: 10.3109/10409239209082562  0.312
1992 Lu M, Guo Q, Kallenbach NR, Sheardy RD. Conformational properties of B-Z junctions in DNA. Biochemistry. 31: 4712-9. PMID 1581320 DOI: 10.1021/Bi00134A026  0.361
1992 Guo Q, Lu M, Marky LA, Kallenbach NR. Interaction of the dye ethidium bromide with DNA containing guanine repeats. Biochemistry. 31: 2451-5. PMID 1547228 DOI: 10.1021/Bi00124A002  0.335
1992 Lu M, Guo Q, Marky LA, Seeman NC, Kallenbach NR. Thermodynamics of DNA branching. Journal of Molecular Biology. 223: 781-9. PMID 1542118 DOI: 10.1016/0022-2836(92)90989-W  0.38
1992 Zhong M, Rashes MS, Marky LA, Kallenbach NR. T-T base mismatches enhance drug binding at the branch site in a four-arm DNA junction. Biochemistry. 31: 8064-71. PMID 1510989 DOI: 10.1021/Bi00149A042  0.347
1991 Lyu PC, Sherman JC, Chen A, Kallenbach NR. Alpha-helix stabilization by natural and unnatural amino acids with alkyl side chains. Proceedings of the National Academy of Sciences of the United States of America. 88: 5317-20. PMID 2052608 DOI: 10.1073/Pnas.88.12.5317  0.565
1991 Lu M, Guo Q, Kallenbach NR. Effect of sequence on the structure of three-arm DNA junctions. Biochemistry. 30: 5815-20. PMID 2043622 DOI: 10.1021/Bi00238A001  0.356
1991 Lu M, Guo Q, Seeman NC, Kallenbach NR. Parallel and antiparallel Holliday junctions differ in structure and stability. Journal of Molecular Biology. 221: 1419-32. PMID 1942060 DOI: 10.1016/0022-2836(91)90942-Y  0.362
1991 Guo Q, Lu M, Kallenbach NR. Conformational preference and ligand binding properties of DNA junctions are determined by sequence at the branch. Biopolymers. 31: 359-72. PMID 1907507 DOI: 10.1002/Bip.360310402  0.39
1991 Gans PJ, Lyu PC, Manning MC, Woody RW, Kallenbach NR. The helix-coil transition in heterogeneous peptides with specific side-chain interactions: theory and comparison with CD spectral data. Biopolymers. 31: 1605-14. PMID 1814507 DOI: 10.1002/Bip.360311315  0.443
1991 Lu M, Guo Q, Krishnan B, Golik J, Rosenberg IE, Doyle TW, Kallenbach NR. Determination of DNA cleavage specificity by esperamicins. Journal of Biomolecular Structure & Dynamics. 9: 285-98. PMID 1741964 DOI: 10.1080/07391102.1991.10507913  0.364
1991 Lu M, Guo Q, Kallenbach NR. Site-specific interaction of the antitumor antibiotic dynemicin with branched DNA molecules. Journal of Biomolecular Structure & Dynamics. 9: 271-83. PMID 1741963 DOI: 10.1080/07391102.1991.10507912  0.367
1991 Guo Q, Lu M, Shahrestanifar M, Sheardy RD, Kallenbach NR. Drug binding to a DNA BZ molecule: analysis by chemical footprinting. Biochemistry. 30: 11735-41. PMID 1721536 DOI: 10.1021/Bi00115A001  0.349
1991 Lyu PC, Wang PC, Liff MI, Kallenbach NR. Local effect of glycine substitution in a model helical peptide Journal of the American Chemical Society. 113: 3568-3572. DOI: 10.1021/Ja00009A052  0.448
1991 Liff MI, Lyu PC, Kallenbach NR. Analysis of asymmetry in the distribution of helical residues in peptides by 1H nuclear magnetic resonance Journal of the American Chemical Society. 113: 1014-1019. DOI: 10.1021/Ja00003A041  0.324
1990 Lu M, Guo Q, Pasternack RF, Wink DJ, Seeman NC, Kallenbach NR. Drug binding by branched DNA: selective interaction of tetrapyridyl porphyrins with an immobile junction. Biochemistry. 29: 1614-24. PMID 2334721 DOI: 10.1021/Bi00458A037  0.315
1990 Kallenbach NR, Lu M, Vasant Kumar N, Nelson JW. Distribution of charged residues stabilizes individual helices in myoglobins. Journal of Biomolecular Structure & Dynamics. 7: 973-83. PMID 2310526 DOI: 10.1080/07391102.1990.10508536  0.4
1990 Lyu PC, Liff MI, Marky LA, Kallenbach NR. Side chain contributions to the stability of alpha-helical structure in peptides. Science (New York, N.Y.). 250: 669-73. PMID 2237416 DOI: 10.1126/Science.2237416  0.432
1990 Guo Q, Lu M, Churchill ME, Tullius TD, Kallenbach NR. Asymmetric structure of a three-arm DNA junction. Biochemistry. 29: 10927-34. PMID 2176888 DOI: 10.1021/Bi00501A010  0.359
1990 Lu M, Guo Q, Seeman NC, Kallenbach NR. Drug binding by branched DNA: selective interaction of the dye stains-all with an immobile junction. Biochemistry. 29: 3407-12. PMID 2110476 DOI: 10.1021/Bi00465A038  0.343
1990 Guo Q, Lu M, Seeman NC, Kallenbach NR. Drug binding by branched DNA molecules: analysis by chemical footprinting of intercalation into an immobile junction. Biochemistry. 29: 570-8. PMID 2105745 DOI: 10.1021/Bi00454A034  0.332
1989 Seeman NC, Chen JH, Kallenbach NR. Gel electrophoretic analysis of DNA branched junctions. Electrophoresis. 10: 345-54. PMID 2548837 DOI: 10.1002/Elps.1150100512  0.381
1989 Nelson JW, Kallenbach NR. Persistence of the alpha-helix stop signal in the S-peptide in trifluoroethanol solutions. Biochemistry. 28: 5256-61. PMID 2548607 DOI: 10.1021/Bi00438A050  0.384
1989 Guo Q, Seeman NC, Kallenbach NR. Site-specific interaction of intercalating drugs with a branched DNA molecule. Biochemistry. 28: 2355-9. PMID 2543439 DOI: 10.1021/Bi00432A001  0.353
1989 Chen JH, Kallenbach NR, Seeman NC. A specific quadrilateral synthesized from DNA branched junctions Journal of the American Chemical Society. 111: 6402-6407. DOI: 10.1021/Ja00198A063  0.315
1989 Lyu PC, Marky LA, Kallenbach NR. The role of ion pairs in α-helix stability: Two new designed helical peptides Journal of the American Chemical Society. 111: 2733-2734. DOI: 10.1021/Ja00189A067  0.342
1988 Chen JH, Seeman NC, Kallenbach NR. Tracts of A.T base pairs retard the electrophoretic mobility of short DNA duplexes. Nucleic Acids Research. 16: 6803-12. PMID 3405750 DOI: 10.1093/Nar/16.14.6803  0.342
1988 Churchill ME, Tullius TD, Kallenbach NR, Seeman NC. A Holliday recombination intermediate is twofold symmetric. Proceedings of the National Academy of Sciences of the United States of America. 85: 4653-6. PMID 3387432 DOI: 10.1073/Pnas.85.13.4653  0.381
1988 Kumar NV, Wemmer DE, Kallenbach NR. Structure of P401 (mast cell degranulating peptide) in solution. Biophysical Chemistry. 31: 113-9. PMID 3233281 DOI: 10.1016/0301-4622(88)80015-2  0.383
1988 Petrillo ML, Newton CJ, Cunningham RP, Ma RI, Kallenbach NR, Seeman NC. The ligation and flexibility of four-arm DNA junctions. Biopolymers. 27: 1337-52. PMID 3219399 DOI: 10.1002/Bip.360270902  0.384
1988 Mueller JE, Kemper B, Cunningham RP, Kallenbach NR, Seeman NC. T4 endonuclease VII cleaves the crossover strands of Holliday junction analogs. Proceedings of the National Academy of Sciences of the United States of America. 85: 9441-5. PMID 3200829 DOI: 10.1073/Pnas.85.24.9441  0.344
1988 Chen JH, Churchill ME, Tullius TD, Kallenbach NR, Seeman NC. Construction and analysis of monomobile DNA junctions. Biochemistry. 27: 6032-8. PMID 3191106 DOI: 10.1021/Bi00416A031  0.357
1987 Marky LA, Kallenbach NR, McDonough KA, Seeman NC, Breslauer KJ. The melting behavior of a DNA junction structure: a calorimetric and spectroscopic study. Biopolymers. 26: 1621-34. PMID 3663876 DOI: 10.1002/Bip.360260912  0.331
1986 Ma RI, Kallenbach NR, Sheardy RD, Petrillo ML, Seeman NC. Three-arm nucleic acid junctions are flexible. Nucleic Acids Research. 14: 9745-53. PMID 3808954 DOI: 10.1093/Nar/14.24.9745  0.361
1986 Nelson JW, Kallenbach NR. Stabilization of the ribonuclease S-peptide alpha-helix by trifluoroethanol. Proteins. 1: 211-7. PMID 3449856 DOI: 10.1002/Prot.340010303  0.376
1986 Wemmer DE, Kumar NV, Metrione RM, Lazdunski M, Drobny G, Kallenbach NR. NMR analysis and sequence of toxin II from the sea anemone Radianthus paumotensis. Biochemistry. 25: 6842-9. PMID 2879552 DOI: 10.1021/Bi00370A017  0.369
1983 Wemmer D, Kallenbach NR. Structure of apamin in solution: a two-dimensional nuclear magnetic resonance study. Biochemistry. 22: 1901-6. PMID 6849893 DOI: 10.1021/Bi00277A025  0.348
1983 Kallenbach NR, Ma RI, Wand AJ, Veeneman GH, van Boom JH, Seeman NC. Fourth rank immobile nucleic acid junctions. Journal of Biomolecular Structure & Dynamics. 1: 159-68. PMID 6401109 DOI: 10.1080/07391102.1983.10507432  0.337
1983 Englander SW, Kallenbach NR. Hydrogen exchange and structural dynamics of proteins and nucleic acids. Quarterly Reviews of Biophysics. 16: 521-655. PMID 6204354 DOI: 10.1017/S0033583500005217  0.358
1983 Seeman NC, Kallenbach NR. Design of immobile nucleic acid junctions. Biophysical Journal. 44: 201-9. PMID 6197102 DOI: 10.1016/S0006-3495(83)84292-1  0.392
1983 Kallenbach NR, Ma RI, Seeman NC. An immobile nucleic acid junction constructed from oligonucleotides Nature. 305: 829-831. DOI: 10.1038/305829A0  0.407
1981 Fritzsche H, Cross TA, Opella SJ, Kallenbach NR. Structure and architecture of the bacterial virus fd. An infrared linear dichroism study. Biophysical Chemistry. 14: 283-91. PMID 7326351 DOI: 10.1016/0301-4622(81)85029-6  0.376
1981 DiVerdi JA, Opella SJ, Ma RI, Kallenbach NR, Seeman NC. 31P NMR of DNA in eukaryotic chromosomal complexes. Biochemical and Biophysical Research Communications. 102: 885-90. PMID 7306194 DOI: 10.1016/0006-291X(81)91620-X  0.354
1981 Young PR, Kallenbach NR. Binding of 9-aminoacridine to deoxydinucleoside phosphates of defined sequence: Preferences and stereochemistry Journal of Molecular Biology. 145: 785-813. PMID 7265221 DOI: 10.1016/0022-2836(81)90315-6  0.356
1981 Young PR, Ma RI, Marfey P, Kallenbach NR. Frameshift mutagenesis of 9-aminoacridine derivatives in Salmonella typhimurium Mutation Research/Genetic Toxicology. 90: 1-10. PMID 7029266 DOI: 10.1016/0165-1218(81)90045-8  0.321
1980 Englander SW, Calhoun DB, Englander JJ, Kallenbach NR, Liem RK, Malin EL, Mandal C, Rogero JR. Individual breathing reactions measured in hemoglobin by hydrogen exchange methods. Biophysical Journal. 32: 577-89. PMID 7248462 DOI: 10.1016/S0006-3495(80)84991-5  0.318
1980 Mandal C, Englander SW, Kallenbach NR. Hydrogen-deuterium exchange analysis of ligand-macromolecule interactions: Ethidium-deoxyribonucleic acid system Biochemistry. 19: 5819-5825. PMID 7193049 DOI: 10.1021/Bi00566A025  0.351
1980 Englander SW, Kallenbach NR, Heeger AJ, Krumhansl JA, Litwin S. Nature of the open state in long polynucleotide double helices: Possibility of soliton excitations Proceedings of the National Academy of Sciences of the United States of America. 77: 7222-7226. PMID 6938969 DOI: 10.1073/Pnas.77.12.7222  0.368
1980 Young PR, Kallenbach NR. Site exclusion and sequence specificity in binding of 9-aminoacridine to the deoxytetranucleotide dpApGpCpT Proceedings of the National Academy of Sciences of the United States of America. 77: 6453-6457. PMID 6935659 DOI: 10.1073/Pnas.77.11.6453  0.34
1980 Mandal C, Englander S, Young P, Kallenbach N. Fluctuational opening-closing reactions in dna and mononucleosome cores of chromatin probed by h-exchange and ligand binding reactions Biophysical Journal. 32: 623-625. DOI: 10.1016/S0006-3495(80)84996-4  0.339
1979 Helfgott D, Kallenbach NR. Increased binding of ethidium bromide to polynucleotide duplexes containing mismatched bases Nucleic Acids Research. 7: 1011-1017. PMID 503848 DOI: 10.1093/Nar/7.4.1011  0.366
1979 Mandal C, Kallenbach NR, Englander SW. Base-pair opening and closing reactions in the double helix. A stopped-flow hydrogen exchange study in poly(rA) · poly(rU) Journal of Molecular Biology. 135: 391-411. PMID 43902 DOI: 10.1016/0022-2836(79)90443-1  0.339
1978 Young PR, Kallenbach NR. Secondary structure in polyuridylic acid. Non-classical hydrogen bonding and the function of the ribose 2′-hydroxyl group Journal of Molecular Biology. 126: 467-479. PMID 745237 DOI: 10.1016/0022-2836(78)90053-0  0.353
1977 Kallenbach NR. On the secondary structure in mRNA Biosystems. 9: 201-210. PMID 597592 DOI: 10.1016/0303-2647(77)90004-1  0.365
1976 Ramstein J, Leng M, Kallenbach NR. Binding isotherms and the interaction between proflavine and a DNA of high G · C content Biophysical Chemistry. 5: 319-326. PMID 974225 DOI: 10.1016/0301-4622(76)80043-9  0.318
1975 Rubin H, Kallenbach NR. Conformational statistics of short RNA chains The Journal of Chemical Physics. 62: 2766-2776. DOI: 10.1063/1.430811  0.358
1973 Appleby DW, Kallenbach NR. Theory of oligonucleotide stabilization. I. The effect of single strand stacking Biopolymers. 12: 2093-2120. PMID 4744753 DOI: 10.1002/Bip.1973.360120915  0.326
1973 Kallenbach NR, Ma RI, Ofengand J, Siddiqui MAQ. Thermal transitions in E. coli tRNA(fMet) and two of its molecular fragments Biopolymers. 12: 1247-1257. PMID 4581148 DOI: 10.1002/Bip.1973.360120605  0.308
1972 Goldstein RN, Stefanovic S, Kallenbach NR. On the conformation of transfer RNA in solution: Dependence of denaturation temperature and structural parameters of mixed and formylmethionyl Escherichia coli transfer RNA on sodium ion concentration Journal of Molecular Biology. 69: 217-236. PMID 4560948 DOI: 10.1016/0022-2836(72)90227-6  0.329
1972 Englander JJ, Kallenbach NR, Englander SW. Hydrogen exchange study of some polynucleotides and transfer RNA Journal of Molecular Biology. 63: 153-169. PMID 4552761 DOI: 10.1016/0022-2836(72)90527-X  0.316
1968 Kallenbach NR. Theory of thermal transitions in low molecular weight RNA chains Journal of Molecular Biology. 37: 445-466. PMID 5719218 DOI: 10.1016/0022-2836(68)90114-9  0.311
1968 Kallenbach NR. Replication of DNA in bacteria with heterogeneous generation times Journal of Theoretical Biology. 18: 19-33. PMID 5648880 DOI: 10.1016/0022-5193(68)90168-9  0.306
1966 Crothers DM, Kallenbach NR. On the helix-coil transition in heterogeneous polymers The Journal of Chemical Physics. 45: 917-927. DOI: 10.1063/1.1727704  0.561
1965 CROTHERS DM, KALLENBACH NR, ZIMM BH. THE MELTING TRANSITION OF LOW-MOLECULAR-WEIGHT DNA: THEORY AND EXPERIMENT. Journal of Molecular Biology. 11: 802-20. PMID 14338789 DOI: 10.1016/S0022-2836(65)80037-7  0.662
1963 Kallenbach NR, Crothers DM, Mortimer RG. Interpretation of the kinetics of helix formation Biochemical and Biophysical Research Communications. 11: 213-216. PMID 13961970 DOI: 10.1016/0006-291X(63)90336-X  0.518
1962 Zimm BH, Kallenbach NR. Selected Aspects of the Physical Chemistry of Polynucleotides and Nucleic Acids Annual Review of Physical Chemistry. 13: 171-194. DOI: 10.1146/Annurev.Pc.13.100162.001131  0.577
1962 Zimm BH, Kallenbach NR. Selected Aspects of the Physical Chemistry of Polynucleotides and Nucleic Acids Annual Review of Physical Chemistry. 13: 171-194. DOI: 10.1146/Annurev.Pc.13.100162.001131  0.577
1962 Zimm BH, Kallenbach NR. Selected Aspects of the Physical Chemistry of Polynucleotides and Nucleic Acids Annual Review of Physical Chemistry. 13: 171-194. DOI: 10.1146/Annurev.Pc.13.100162.001131  0.577
1962 Zimm BH, Kallenbach NR. Selected Aspects of the Physical Chemistry of Polynucleotides and Nucleic Acids Annual Review of Physical Chemistry. 13: 171-194. DOI: 10.1146/Annurev.Pc.13.100162.001131  0.577
1962 Zimm BH, Kallenbach NR. Selected Aspects of the Physical Chemistry of Polynucleotides and Nucleic Acids Annual Review of Physical Chemistry. 13: 171-194. DOI: 10.1146/Annurev.Pc.13.100162.001131  0.577
1962 Zimm BH, Kallenbach NR. Selected Aspects of the Physical Chemistry of Polynucleotides and Nucleic Acids Annual Review of Physical Chemistry. 13: 171-194. DOI: 10.1146/Annurev.Pc.13.100162.001131  0.577
1962 Zimm BH, Kallenbach NR. Selected Aspects of the Physical Chemistry of Polynucleotides and Nucleic Acids Annual Review of Physical Chemistry. 13: 171-194. DOI: 10.1146/Annurev.Pc.13.100162.001131  0.577
Low-probability matches (unlikely to be authored by this person)
1970 Litwin S, Kallenbach NR. Kinetics of DNA replication in bacteria with heterogeneous generation times Journal of Theoretical Biology. 27: 357-376. PMID 5472450 DOI: 10.1016/S0022-5193(70)80002-9  0.3
1971 Wang AC, Kallenbach NR. Helical complexes of polyriboinosinic acid with copolymers of polyribocytidylic acid containing inosine, adenosine and uridine residues Journal of Molecular Biology. 62: 591-607. PMID 5136583 DOI: 10.1016/0022-2836(71)90158-6  0.299
1979 Kallenbach NR, Brentani MM, Brentani RR. Direct differential absorbance profiles of denaturing transitions in ribosomal and mRNA. Biopolymers. 18: 1515-31. PMID 465652 DOI: 10.1002/Bip.1979.360180614  0.295
1984 Preisler RS, Mandal C, Englander SW, Kallenbach NR, Frazier J, Miles HT, Howard FB. Premelting and the hydrogen-exchange open state in synthetic RNA duplexes. Biopolymers. 23: 2099-125. PMID 6498293 DOI: 10.1002/Bip.360231102  0.29
1994 Zhou HX, Lyu PC, Wemmer DE, Kallenbach NR. Structure of a C-Terminal .alpha.-Helix Cap in a Synthetic Peptide Journal of the American Chemical Society. 116: 1139-1140. DOI: 10.1021/Ja00082A049  0.29
1994 Zhou HX, Lyu PC, Wemmer DE, Kallenbach NR. Structure of a C-Terminal .alpha.-Helix Cap in a Synthetic Peptide Journal of the American Chemical Society. 116: 1139-1140. DOI: 10.1021/Ja00082A049  0.29
1994 Zhou HX, Lyu PC, Wemmer DE, Kallenbach NR. Structure of a C-Terminal .alpha.-Helix Cap in a Synthetic Peptide Journal of the American Chemical Society. 116: 1139-1140. DOI: 10.1021/Ja00082A049  0.29
1994 Zhou HX, Lyu PC, Wemmer DE, Kallenbach NR. Structure of a C-Terminal .alpha.-Helix Cap in a Synthetic Peptide Journal of the American Chemical Society. 116: 1139-1140. DOI: 10.1021/Ja00082A049  0.29
1994 Zhou HX, Lyu PC, Wemmer DE, Kallenbach NR. Structure of a C-Terminal .alpha.-Helix Cap in a Synthetic Peptide Journal of the American Chemical Society. 116: 1139-1140. DOI: 10.1021/Ja00082A049  0.29
1982 Young PR, Nandi US, Kallenbach NR. Binding of mercury(II) to poly(dA-dT) studied by proton nuclear magnetic resonance. Biochemistry. 21: 62-6. PMID 6460526 DOI: 10.1021/Bi00530A012  0.288
1972 Kallenbach NR, Drost SD. Effect of non-complementary nucleotides on the rate of helix formation: kinetics of formation of poly (I)-poly (C,I) and poly (I)-poly (C,U) complexes Biopolymers - Peptide Science Section. 11: 1613-1620. PMID 5056085 DOI: 10.1002/Bip.1972.360110808  0.287
1986 Hardin CC, Gollnick P, Kallenbach NR, Cohn M, Horowitz J. Fluorine-19 nuclear magnetic resonance studies of the structure of 5-fluorouracil-substituted Escherichia coli transfer RNA. Biochemistry. 25: 5699-709. PMID 3535884 DOI: 10.1021/Bi00367A053  0.28
1994 Zhou HX, Hull LA, Kallenbach NR, Mayne L, Bai Y, Englander SW. Quantitative evaluation of stabilizing interactions in a prenucleated .alpha.-helix by hydrogen exchange Journal of the American Chemical Society. 116: 6482-6483. DOI: 10.1021/Ja00093A078  0.279
1978 Kallenbach NR, Appleby DW, Bradley CH. 31P magnetic resonance of DNA in nucleosome core particles of chromatin Nature. 272: 134-138. PMID 628441 DOI: 10.1038/272134A0  0.278
1975 Kaufmann G, Kallenbach NR. Determination of recognition sites of T4 RNA ligase on the 3' OH and 5' P termini of polyribonucleotide chains Nature. 254: 452-454. PMID 1118037 DOI: 10.1038/254452A0  0.277
1995 Spek EJ, Gong Y, Kallenbach NR. Intermolecular Interactions In Alpha Helical Oligo- And Poly(L-Glutamic Acid) At Acidic Ph Journal of the American Chemical Society. 117: 10773-10774. DOI: 10.1021/Ja00148A032  0.276
2009 Chen K, Liu Z, Zhou C, Bracken WC, Kallenbach NR. Extended conformations in alanine peptides Biophysical Journal. 96: 4a-5a. DOI: 10.1016/j.bpj.2008.12.916  0.269
2009 Chen K, Liu Z, Zhou C, Bracken WC, Kallenbach NR. Extended conformations in alanine peptides Biophysical Journal. 96: 4a-5a. DOI: 10.1016/j.bpj.2008.12.916  0.269
2009 Chen K, Liu Z, Zhou C, Bracken WC, Kallenbach NR. Extended conformations in alanine peptides Biophysical Journal. 96: 4a-5a. DOI: 10.1016/j.bpj.2008.12.916  0.269
2009 Chen K, Liu Z, Zhou C, Bracken WC, Kallenbach NR. Extended conformations in alanine peptides Biophysical Journal. 96: 4a-5a. DOI: 10.1016/j.bpj.2008.12.916  0.269
2009 Chen K, Liu Z, Zhou C, Bracken WC, Kallenbach NR. Extended conformations in alanine peptides Biophysical Journal. 96: 4a-5a. DOI: 10.1016/j.bpj.2008.12.916  0.269
2009 Chen K, Liu Z, Zhou C, Bracken WC, Kallenbach NR. Extended conformations in alanine peptides Biophysical Journal. 96: 4a-5a. DOI: 10.1016/j.bpj.2008.12.916  0.269
2009 Chen K, Liu Z, Zhou C, Bracken WC, Kallenbach NR. Extended conformations in alanine peptides Biophysical Journal. 96: 4a-5a. DOI: 10.1016/j.bpj.2008.12.916  0.269
2009 Chen K, Liu Z, Zhou C, Bracken WC, Kallenbach NR. Extended conformations in alanine peptides Biophysical Journal. 96: 4a-5a. DOI: 10.1016/j.bpj.2008.12.916  0.269
2009 Chen K, Liu Z, Zhou C, Bracken WC, Kallenbach NR. Extended conformations in alanine peptides Biophysical Journal. 96: 4a-5a. DOI: 10.1016/j.bpj.2008.12.916  0.269
2009 Chen K, Liu Z, Zhou C, Bracken WC, Kallenbach NR. Extended conformations in alanine peptides Biophysical Journal. 96: 4a-5a. DOI: 10.1016/j.bpj.2008.12.916  0.269
2009 Chen K, Liu Z, Zhou C, Bracken WC, Kallenbach NR. Extended conformations in alanine peptides Biophysical Journal. 96: 4a-5a. DOI: 10.1016/j.bpj.2008.12.916  0.269
2009 Chen K, Liu Z, Zhou C, Bracken WC, Kallenbach NR. Extended conformations in alanine peptides Biophysical Journal. 96: 4a-5a. DOI: 10.1016/j.bpj.2008.12.916  0.269
2009 Chen K, Liu Z, Zhou C, Bracken WC, Kallenbach NR. Extended conformations in alanine peptides Biophysical Journal. 96: 4a-5a. DOI: 10.1016/j.bpj.2008.12.916  0.269
2009 Chen K, Liu Z, Zhou C, Bracken WC, Kallenbach NR. Extended conformations in alanine peptides Biophysical Journal. 96: 4a-5a. DOI: 10.1016/j.bpj.2008.12.916  0.269
2009 Chen K, Liu Z, Zhou C, Bracken WC, Kallenbach NR. Extended conformations in alanine peptides Biophysical Journal. 96: 4a-5a. DOI: 10.1016/j.bpj.2008.12.916  0.269
2009 Chen K, Liu Z, Zhou C, Bracken WC, Kallenbach NR. Extended conformations in alanine peptides Biophysical Journal. 96: 4a-5a. DOI: 10.1016/j.bpj.2008.12.916  0.269
2009 Chen K, Liu Z, Zhou C, Bracken WC, Kallenbach NR. Extended conformations in alanine peptides Biophysical Journal. 96: 4a-5a. DOI: 10.1016/j.bpj.2008.12.916  0.269
2009 Chen K, Liu Z, Zhou C, Bracken WC, Kallenbach NR. Extended conformations in alanine peptides Biophysical Journal. 96: 4a-5a. DOI: 10.1016/j.bpj.2008.12.916  0.269
2009 Chen K, Liu Z, Zhou C, Bracken WC, Kallenbach NR. Extended conformations in alanine peptides Biophysical Journal. 96: 4a-5a. DOI: 10.1016/j.bpj.2008.12.916  0.269
2009 Chen K, Liu Z, Zhou C, Bracken WC, Kallenbach NR. Extended conformations in alanine peptides Biophysical Journal. 96: 4a-5a. DOI: 10.1016/j.bpj.2008.12.916  0.269
2009 Chen K, Liu Z, Zhou C, Bracken WC, Kallenbach NR. Extended conformations in alanine peptides Biophysical Journal. 96: 4a-5a. DOI: 10.1016/j.bpj.2008.12.916  0.269
2009 Chen K, Liu Z, Zhou C, Bracken WC, Kallenbach NR. Extended conformations in alanine peptides Biophysical Journal. 96: 4a-5a. DOI: 10.1016/j.bpj.2008.12.916  0.269
2009 Chen K, Liu Z, Zhou C, Bracken WC, Kallenbach NR. Extended conformations in alanine peptides Biophysical Journal. 96: 4a-5a. DOI: 10.1016/j.bpj.2008.12.916  0.269
2009 Chen K, Liu Z, Zhou C, Bracken WC, Kallenbach NR. Extended conformations in alanine peptides Biophysical Journal. 96: 4a-5a. DOI: 10.1016/j.bpj.2008.12.916  0.269
2009 Chen K, Liu Z, Zhou C, Bracken WC, Kallenbach NR. Extended conformations in alanine peptides Biophysical Journal. 96: 4a-5a. DOI: 10.1016/j.bpj.2008.12.916  0.269
2009 Chen K, Liu Z, Zhou C, Bracken WC, Kallenbach NR. Extended conformations in alanine peptides Biophysical Journal. 96: 4a-5a. DOI: 10.1016/j.bpj.2008.12.916  0.269
2009 Chen K, Liu Z, Zhou C, Bracken WC, Kallenbach NR. Extended conformations in alanine peptides Biophysical Journal. 96: 4a-5a. DOI: 10.1016/j.bpj.2008.12.916  0.269
2009 Chen K, Liu Z, Zhou C, Bracken WC, Kallenbach NR. Extended conformations in alanine peptides Biophysical Journal. 96: 4a-5a. DOI: 10.1016/j.bpj.2008.12.916  0.269
2009 Chen K, Liu Z, Zhou C, Bracken WC, Kallenbach NR. Extended conformations in alanine peptides Biophysical Journal. 96: 4a-5a. DOI: 10.1016/j.bpj.2008.12.916  0.269
2009 Chen K, Liu Z, Zhou C, Bracken WC, Kallenbach NR. Extended conformations in alanine peptides Biophysical Journal. 96: 4a-5a. DOI: 10.1016/j.bpj.2008.12.916  0.269
2009 Chen K, Liu Z, Zhou C, Bracken WC, Kallenbach NR. Extended conformations in alanine peptides Biophysical Journal. 96: 4a-5a. DOI: 10.1016/j.bpj.2008.12.916  0.269
2009 Chen K, Liu Z, Zhou C, Bracken WC, Kallenbach NR. Extended conformations in alanine peptides Biophysical Journal. 96: 4a-5a. DOI: 10.1016/j.bpj.2008.12.916  0.269
2009 Chen K, Liu Z, Zhou C, Bracken WC, Kallenbach NR. Extended conformations in alanine peptides Biophysical Journal. 96: 4a-5a. DOI: 10.1016/j.bpj.2008.12.916  0.269
2009 Chen K, Liu Z, Zhou C, Bracken WC, Kallenbach NR. Extended conformations in alanine peptides Biophysical Journal. 96: 4a-5a. DOI: 10.1016/j.bpj.2008.12.916  0.269
2009 Chen K, Liu Z, Zhou C, Bracken WC, Kallenbach NR. Extended conformations in alanine peptides Biophysical Journal. 96: 4a-5a. DOI: 10.1016/j.bpj.2008.12.916  0.269
2009 Chen K, Liu Z, Zhou C, Bracken WC, Kallenbach NR. Extended conformations in alanine peptides Biophysical Journal. 96: 4a-5a. DOI: 10.1016/j.bpj.2008.12.916  0.269
2009 Chen K, Liu Z, Zhou C, Bracken WC, Kallenbach NR. Extended conformations in alanine peptides Biophysical Journal. 96: 4a-5a. DOI: 10.1016/j.bpj.2008.12.916  0.269
2009 Chen K, Liu Z, Zhou C, Bracken WC, Kallenbach NR. Extended conformations in alanine peptides Biophysical Journal. 96: 4a-5a. DOI: 10.1016/j.bpj.2008.12.916  0.269
2009 Chen K, Liu Z, Zhou C, Bracken WC, Kallenbach NR. Extended conformations in alanine peptides Biophysical Journal. 96: 4a-5a. DOI: 10.1016/j.bpj.2008.12.916  0.269
2009 Chen K, Liu Z, Zhou C, Bracken WC, Kallenbach NR. Extended conformations in alanine peptides Biophysical Journal. 96: 4a-5a. DOI: 10.1016/j.bpj.2008.12.916  0.269
2009 Chen K, Liu Z, Zhou C, Bracken WC, Kallenbach NR. Extended conformations in alanine peptides Biophysical Journal. 96: 4a-5a. DOI: 10.1016/j.bpj.2008.12.916  0.269
2009 Chen K, Liu Z, Zhou C, Bracken WC, Kallenbach NR. Extended conformations in alanine peptides Biophysical Journal. 96: 4a-5a. DOI: 10.1016/j.bpj.2008.12.916  0.269
2009 Chen K, Liu Z, Zhou C, Bracken WC, Kallenbach NR. Extended conformations in alanine peptides Biophysical Journal. 96: 4a-5a. DOI: 10.1016/j.bpj.2008.12.916  0.269
2009 Chen K, Liu Z, Zhou C, Bracken WC, Kallenbach NR. Extended conformations in alanine peptides Biophysical Journal. 96: 4a-5a. DOI: 10.1016/j.bpj.2008.12.916  0.269
2009 Chen K, Liu Z, Zhou C, Bracken WC, Kallenbach NR. Extended conformations in alanine peptides Biophysical Journal. 96: 4a-5a. DOI: 10.1016/j.bpj.2008.12.916  0.269
2009 Chen K, Liu Z, Zhou C, Bracken WC, Kallenbach NR. Extended conformations in alanine peptides Biophysical Journal. 96: 4a-5a. DOI: 10.1016/j.bpj.2008.12.916  0.269
2009 Chen K, Liu Z, Zhou C, Bracken WC, Kallenbach NR. Extended conformations in alanine peptides Biophysical Journal. 96: 4a-5a. DOI: 10.1016/j.bpj.2008.12.916  0.269
2009 Chen K, Liu Z, Zhou C, Bracken WC, Kallenbach NR. Extended conformations in alanine peptides Biophysical Journal. 96: 4a-5a. DOI: 10.1016/j.bpj.2008.12.916  0.269
2009 Chen K, Liu Z, Zhou C, Bracken WC, Kallenbach NR. Extended conformations in alanine peptides Biophysical Journal. 96: 4a-5a. DOI: 10.1016/j.bpj.2008.12.916  0.269
1977 Litwin S, Kallenbach NR. On the localization of the origin of DNA replication in E. coli Journal of Theoretical Biology. 64: 747-760. PMID 321880 DOI: 10.1016/0022-5193(77)90273-9  0.268
1974 Hossain A, Kallenbach NR. Purification and subunit structure of tryptophanyl tRNA synthetase (TRS) from baker's yeast Febs Letters. 45: 202-205. PMID 4606970 DOI: 10.1016/0014-5793(74)80845-8  0.268
1978 Baker BM, Vanderkooi J, Kallenbach NR. Base stacking in a fluorescent dinucleoside monophosphate: εApεA Biopolymers. 17: 1361-1372. DOI: 10.1002/Bip.1978.360170519  0.264
1990 Lu M, Guo Q, Wink DJ, Kallenbach NR. Charge dependence of Fe(II)-catalyzed DNA cleavage. Nucleic Acids Research. 18: 3333-7. PMID 2356123 DOI: 10.1093/Nar/18.11.3333  0.264
1989 Pease JH, Kumar NV, Schweitz H, Kallenbach NR, Wemmer DE. NMR studies of toxin III from the sea anemone Radianthus paumotensis and comparison of its secondary structure with related toxins. Biochemistry. 28: 2199-204. PMID 2566327 DOI: 10.1021/bi00431a034  0.262
1993 Lin L, Kallenbach NR. Conservative substitutions at internal sites in sperm whale myoglobin reveal correlations with alpha helix propensity Protein Engineering Design & Selection. 6. DOI: 10.1093/Protein/6.Supplement.18-B  0.262
1995 Kallenbach NR. Breathing life into the folding pathway of cytochrome c. Nature Structural Biology. 2: 813-6. PMID 7552698 DOI: 10.1038/Nsb1095-813  0.261
1998 Morozov VN, Morozova TY, Kallenbach NR. Atomic force microscopy of structures produced by electrospraying polymer solutions International Journal of Mass Spectrometry. 178: 143-159. DOI: 10.1016/S1387-3806(98)14083-6  0.261
1985 Kumar NV, Kallenbach NR. Hydrogen exchange of individual amide protons in the F helix of cyanometmyoglobin. Biochemistry. 24: 7658-62. PMID 3004560 DOI: 10.1021/Bi00347A024  0.253
1994 Zhong M, Rashes MS, Leontis NB, Kallenbach NR. Effects of unpaired bases on the conformation and stability of three-arm DNA junctions. Biochemistry. 33: 3660-7. PMID 8142364 DOI: 10.1021/Bi00178A024  0.253
1997 Spek EJ, Wu HC, Kallenbach NR. The role of alanine sequences in forming β-sheets of spider dragline silk [10] Journal of the American Chemical Society. 119: 5053-5054. DOI: 10.1021/Ja963218N  0.249
1994 Zhou HX, Lyu PC, Wemmer DE, Kallenbach NR. Structure of a C-terminal α-helix cap in a synthetic peptide Journal of the American Chemical Society. 116: 1139-1140.  0.245
1985 Seeman NC, Maestre MF, Ma RI, Kallenbach NR. Physical characterization of a nucleic acid junction. Progress in Clinical and Biological Research. 172: 99-108. PMID 3991700  0.242
1989 Lu M, Guo Q, Seeman NC, Kallenbach NR. DNase I cleavage of branched DNA molecules. The Journal of Biological Chemistry. 264: 20851-4. PMID 2592355  0.24
1990 Kimball A, Guo Q, Lu M, Cunningham RP, Kallenbach NR, Seeman NC, Tullius TD. Construction and analysis of parallel and antiparallel Holliday junctions. The Journal of Biological Chemistry. 265: 6544-7. PMID 2157702  0.239
1985 Wemmer DE, Wand AJ, Seeman NC, Kallenbach NR. NMR analysis of DNA junctions: imino proton NMR studies of individual arms and intact junction. Biochemistry. 24: 5745-9. PMID 4084489 DOI: 10.1021/bi00342a009  0.237
1990 Lu M, Guo Q, Mueller JE, Kemper B, Studier FW, Seeman NC, Kallenbach NR. Characterization of a bimobile DNA junction. The Journal of Biological Chemistry. 265: 16778-85. PMID 2170355  0.23
1992 Lu M, Guo Q, Kallenbach NR. Structure and stability of sodium and potassium complexes of dT4G4 and dT4G4T. Biochemistry. 31: 2455-9. PMID 1547229  0.224
1990 Mueller JE, Newton CJ, Jensch F, Kemper B, Cunningham RP, Kallenbach NR, Seeman NC. Resolution of Holliday junction analogs by T4 endonuclease VII can be directed by substrate structure. The Journal of Biological Chemistry. 265: 13918-24. PMID 2199447  0.223
1980 Englander SW, Kallenbach NR, Heeger AJ, Krumhansl JA, Litwin S. Soliton-like states for opening in polynucleotide double helices Ferroelectrics. 30: 167-167. DOI: 10.1080/00150198008209510  0.216
1992 Guo Q, Lu M, Kallenbach NR. Adenine affects the structure and stability of telomeric sequences. The Journal of Biological Chemistry. 267: 15293-300. PMID 1639776  0.209
1976 Kallenbach NR, Daniel WE, Kaminker MA. Nuclear magnetic resonance study of hydrogen-bonded ring protons in oligonucleotide helices involving classical and nonclassical base pairs Biochemistry. 15: 1218-1224. PMID 1252442  0.203
2013 Vanderlee G, Liu Z, Kallenbach NR, Yip CM. Action of Arginine and Tryptophan Containing Antimicrobial Peptides on Supported Lipid Bilayers Biophysical Journal. 104: 236a. DOI: 10.1016/j.bpj.2012.11.1335  0.199
2013 Vanderlee G, Liu Z, Kallenbach NR, Yip CM. Action of Arginine and Tryptophan Containing Antimicrobial Peptides on Supported Lipid Bilayers Biophysical Journal. 104: 236a. DOI: 10.1016/j.bpj.2012.11.1335  0.199
2013 Vanderlee G, Liu Z, Kallenbach NR, Yip CM. Action of Arginine and Tryptophan Containing Antimicrobial Peptides on Supported Lipid Bilayers Biophysical Journal. 104: 236a. DOI: 10.1016/j.bpj.2012.11.1335  0.199
2013 Vanderlee G, Liu Z, Kallenbach NR, Yip CM. Action of Arginine and Tryptophan Containing Antimicrobial Peptides on Supported Lipid Bilayers Biophysical Journal. 104: 236a. DOI: 10.1016/j.bpj.2012.11.1335  0.199
2013 Vanderlee G, Liu Z, Kallenbach NR, Yip CM. Action of Arginine and Tryptophan Containing Antimicrobial Peptides on Supported Lipid Bilayers Biophysical Journal. 104: 236a. DOI: 10.1016/j.bpj.2012.11.1335  0.199
2013 Vanderlee G, Liu Z, Kallenbach NR, Yip CM. Action of Arginine and Tryptophan Containing Antimicrobial Peptides on Supported Lipid Bilayers Biophysical Journal. 104: 236a. DOI: 10.1016/j.bpj.2012.11.1335  0.199
2013 Vanderlee G, Liu Z, Kallenbach NR, Yip CM. Action of Arginine and Tryptophan Containing Antimicrobial Peptides on Supported Lipid Bilayers Biophysical Journal. 104: 236a. DOI: 10.1016/j.bpj.2012.11.1335  0.199
2013 Vanderlee G, Liu Z, Kallenbach NR, Yip CM. Action of Arginine and Tryptophan Containing Antimicrobial Peptides on Supported Lipid Bilayers Biophysical Journal. 104: 236a. DOI: 10.1016/j.bpj.2012.11.1335  0.199
2013 Vanderlee G, Liu Z, Kallenbach NR, Yip CM. Action of Arginine and Tryptophan Containing Antimicrobial Peptides on Supported Lipid Bilayers Biophysical Journal. 104: 236a. DOI: 10.1016/j.bpj.2012.11.1335  0.199
2013 Vanderlee G, Liu Z, Kallenbach NR, Yip CM. Action of Arginine and Tryptophan Containing Antimicrobial Peptides on Supported Lipid Bilayers Biophysical Journal. 104: 236a. DOI: 10.1016/j.bpj.2012.11.1335  0.199
2013 Vanderlee G, Liu Z, Kallenbach NR, Yip CM. Action of Arginine and Tryptophan Containing Antimicrobial Peptides on Supported Lipid Bilayers Biophysical Journal. 104: 236a. DOI: 10.1016/j.bpj.2012.11.1335  0.199
2013 Vanderlee G, Liu Z, Kallenbach NR, Yip CM. Action of Arginine and Tryptophan Containing Antimicrobial Peptides on Supported Lipid Bilayers Biophysical Journal. 104: 236a. DOI: 10.1016/j.bpj.2012.11.1335  0.199
2013 Vanderlee G, Liu Z, Kallenbach NR, Yip CM. Action of Arginine and Tryptophan Containing Antimicrobial Peptides on Supported Lipid Bilayers Biophysical Journal. 104: 236a. DOI: 10.1016/j.bpj.2012.11.1335  0.199
2013 Vanderlee G, Liu Z, Kallenbach NR, Yip CM. Action of Arginine and Tryptophan Containing Antimicrobial Peptides on Supported Lipid Bilayers Biophysical Journal. 104: 236a. DOI: 10.1016/j.bpj.2012.11.1335  0.199
2013 Vanderlee G, Liu Z, Kallenbach NR, Yip CM. Action of Arginine and Tryptophan Containing Antimicrobial Peptides on Supported Lipid Bilayers Biophysical Journal. 104: 236a. DOI: 10.1016/j.bpj.2012.11.1335  0.199
2013 Vanderlee G, Liu Z, Kallenbach NR, Yip CM. Action of Arginine and Tryptophan Containing Antimicrobial Peptides on Supported Lipid Bilayers Biophysical Journal. 104: 236a. DOI: 10.1016/j.bpj.2012.11.1335  0.199
2013 Vanderlee G, Liu Z, Kallenbach NR, Yip CM. Action of Arginine and Tryptophan Containing Antimicrobial Peptides on Supported Lipid Bilayers Biophysical Journal. 104: 236a. DOI: 10.1016/j.bpj.2012.11.1335  0.199
2013 Vanderlee G, Liu Z, Kallenbach NR, Yip CM. Action of Arginine and Tryptophan Containing Antimicrobial Peptides on Supported Lipid Bilayers Biophysical Journal. 104: 236a. DOI: 10.1016/j.bpj.2012.11.1335  0.199
2013 Vanderlee G, Liu Z, Kallenbach NR, Yip CM. Action of Arginine and Tryptophan Containing Antimicrobial Peptides on Supported Lipid Bilayers Biophysical Journal. 104: 236a. DOI: 10.1016/j.bpj.2012.11.1335  0.199
2013 Vanderlee G, Liu Z, Kallenbach NR, Yip CM. Action of Arginine and Tryptophan Containing Antimicrobial Peptides on Supported Lipid Bilayers Biophysical Journal. 104: 236a. DOI: 10.1016/j.bpj.2012.11.1335  0.199
2013 Vanderlee G, Liu Z, Kallenbach NR, Yip CM. Action of Arginine and Tryptophan Containing Antimicrobial Peptides on Supported Lipid Bilayers Biophysical Journal. 104: 236a. DOI: 10.1016/j.bpj.2012.11.1335  0.199
2013 Vanderlee G, Liu Z, Kallenbach NR, Yip CM. Action of Arginine and Tryptophan Containing Antimicrobial Peptides on Supported Lipid Bilayers Biophysical Journal. 104: 236a. DOI: 10.1016/j.bpj.2012.11.1335  0.199
2013 Vanderlee G, Liu Z, Kallenbach NR, Yip CM. Action of Arginine and Tryptophan Containing Antimicrobial Peptides on Supported Lipid Bilayers Biophysical Journal. 104: 236a. DOI: 10.1016/j.bpj.2012.11.1335  0.199
2013 Vanderlee G, Liu Z, Kallenbach NR, Yip CM. Action of Arginine and Tryptophan Containing Antimicrobial Peptides on Supported Lipid Bilayers Biophysical Journal. 104: 236a. DOI: 10.1016/j.bpj.2012.11.1335  0.199
2013 Vanderlee G, Liu Z, Kallenbach NR, Yip CM. Action of Arginine and Tryptophan Containing Antimicrobial Peptides on Supported Lipid Bilayers Biophysical Journal. 104: 236a. DOI: 10.1016/j.bpj.2012.11.1335  0.199
2013 Vanderlee G, Liu Z, Kallenbach NR, Yip CM. Action of Arginine and Tryptophan Containing Antimicrobial Peptides on Supported Lipid Bilayers Biophysical Journal. 104: 236a. DOI: 10.1016/j.bpj.2012.11.1335  0.199
2013 Vanderlee G, Liu Z, Kallenbach NR, Yip CM. Action of Arginine and Tryptophan Containing Antimicrobial Peptides on Supported Lipid Bilayers Biophysical Journal. 104: 236a. DOI: 10.1016/j.bpj.2012.11.1335  0.199
2013 Vanderlee G, Liu Z, Kallenbach NR, Yip CM. Action of Arginine and Tryptophan Containing Antimicrobial Peptides on Supported Lipid Bilayers Biophysical Journal. 104: 236a. DOI: 10.1016/j.bpj.2012.11.1335  0.199
2013 Vanderlee G, Liu Z, Kallenbach NR, Yip CM. Action of Arginine and Tryptophan Containing Antimicrobial Peptides on Supported Lipid Bilayers Biophysical Journal. 104: 236a. DOI: 10.1016/j.bpj.2012.11.1335  0.199
2013 Vanderlee G, Liu Z, Kallenbach NR, Yip CM. Action of Arginine and Tryptophan Containing Antimicrobial Peptides on Supported Lipid Bilayers Biophysical Journal. 104: 236a. DOI: 10.1016/j.bpj.2012.11.1335  0.199
2013 Vanderlee G, Liu Z, Kallenbach NR, Yip CM. Action of Arginine and Tryptophan Containing Antimicrobial Peptides on Supported Lipid Bilayers Biophysical Journal. 104: 236a. DOI: 10.1016/j.bpj.2012.11.1335  0.199
2013 Vanderlee G, Liu Z, Kallenbach NR, Yip CM. Action of Arginine and Tryptophan Containing Antimicrobial Peptides on Supported Lipid Bilayers Biophysical Journal. 104: 236a. DOI: 10.1016/j.bpj.2012.11.1335  0.199
2013 Vanderlee G, Liu Z, Kallenbach NR, Yip CM. Action of Arginine and Tryptophan Containing Antimicrobial Peptides on Supported Lipid Bilayers Biophysical Journal. 104: 236a. DOI: 10.1016/j.bpj.2012.11.1335  0.199
2013 Vanderlee G, Liu Z, Kallenbach NR, Yip CM. Action of Arginine and Tryptophan Containing Antimicrobial Peptides on Supported Lipid Bilayers Biophysical Journal. 104: 236a. DOI: 10.1016/j.bpj.2012.11.1335  0.199
2013 Vanderlee G, Liu Z, Kallenbach NR, Yip CM. Action of Arginine and Tryptophan Containing Antimicrobial Peptides on Supported Lipid Bilayers Biophysical Journal. 104: 236a. DOI: 10.1016/j.bpj.2012.11.1335  0.199
2013 Vanderlee G, Liu Z, Kallenbach NR, Yip CM. Action of Arginine and Tryptophan Containing Antimicrobial Peptides on Supported Lipid Bilayers Biophysical Journal. 104: 236a. DOI: 10.1016/j.bpj.2012.11.1335  0.199
2013 Vanderlee G, Liu Z, Kallenbach NR, Yip CM. Action of Arginine and Tryptophan Containing Antimicrobial Peptides on Supported Lipid Bilayers Biophysical Journal. 104: 236a. DOI: 10.1016/j.bpj.2012.11.1335  0.199
2013 Vanderlee G, Liu Z, Kallenbach NR, Yip CM. Action of Arginine and Tryptophan Containing Antimicrobial Peptides on Supported Lipid Bilayers Biophysical Journal. 104: 236a. DOI: 10.1016/j.bpj.2012.11.1335  0.199
2013 Vanderlee G, Liu Z, Kallenbach NR, Yip CM. Action of Arginine and Tryptophan Containing Antimicrobial Peptides on Supported Lipid Bilayers Biophysical Journal. 104: 236a. DOI: 10.1016/j.bpj.2012.11.1335  0.199
2013 Vanderlee G, Liu Z, Kallenbach NR, Yip CM. Action of Arginine and Tryptophan Containing Antimicrobial Peptides on Supported Lipid Bilayers Biophysical Journal. 104: 236a. DOI: 10.1016/j.bpj.2012.11.1335  0.199
2013 Vanderlee G, Liu Z, Kallenbach NR, Yip CM. Action of Arginine and Tryptophan Containing Antimicrobial Peptides on Supported Lipid Bilayers Biophysical Journal. 104: 236a. DOI: 10.1016/j.bpj.2012.11.1335  0.199
2013 Vanderlee G, Liu Z, Kallenbach NR, Yip CM. Action of Arginine and Tryptophan Containing Antimicrobial Peptides on Supported Lipid Bilayers Biophysical Journal. 104: 236a. DOI: 10.1016/j.bpj.2012.11.1335  0.199
2013 Vanderlee G, Liu Z, Kallenbach NR, Yip CM. Action of Arginine and Tryptophan Containing Antimicrobial Peptides on Supported Lipid Bilayers Biophysical Journal. 104: 236a. DOI: 10.1016/j.bpj.2012.11.1335  0.199
2013 Vanderlee G, Liu Z, Kallenbach NR, Yip CM. Action of Arginine and Tryptophan Containing Antimicrobial Peptides on Supported Lipid Bilayers Biophysical Journal. 104: 236a. DOI: 10.1016/j.bpj.2012.11.1335  0.199
2013 Vanderlee G, Liu Z, Kallenbach NR, Yip CM. Action of Arginine and Tryptophan Containing Antimicrobial Peptides on Supported Lipid Bilayers Biophysical Journal. 104: 236a. DOI: 10.1016/j.bpj.2012.11.1335  0.199
2013 Vanderlee G, Liu Z, Kallenbach NR, Yip CM. Action of Arginine and Tryptophan Containing Antimicrobial Peptides on Supported Lipid Bilayers Biophysical Journal. 104: 236a. DOI: 10.1016/j.bpj.2012.11.1335  0.199
2013 Vanderlee G, Liu Z, Kallenbach NR, Yip CM. Action of Arginine and Tryptophan Containing Antimicrobial Peptides on Supported Lipid Bilayers Biophysical Journal. 104: 236a. DOI: 10.1016/j.bpj.2012.11.1335  0.199
2013 Vanderlee G, Liu Z, Kallenbach NR, Yip CM. Action of Arginine and Tryptophan Containing Antimicrobial Peptides on Supported Lipid Bilayers Biophysical Journal. 104: 236a. DOI: 10.1016/j.bpj.2012.11.1335  0.199
2013 Vanderlee G, Liu Z, Kallenbach NR, Yip CM. Action of Arginine and Tryptophan Containing Antimicrobial Peptides on Supported Lipid Bilayers Biophysical Journal. 104: 236a. DOI: 10.1016/j.bpj.2012.11.1335  0.199
2013 Vanderlee G, Liu Z, Kallenbach NR, Yip CM. Action of Arginine and Tryptophan Containing Antimicrobial Peptides on Supported Lipid Bilayers Biophysical Journal. 104: 236a. DOI: 10.1016/j.bpj.2012.11.1335  0.199
1990 Beveridge DL, Hilbers CW, Kallenbach NR, Redfield AG, Rich A, Sarma RH, Seeman NC, Wang AH. Seventh conversation in the discipline biomolecular stereodynamics state university of new york at albany, june 18·22, 1991 Journal of Biomolecular Structure and Dynamics. 8: viii-xii. DOI: 10.1080/07391102.1990.10507820  0.187
1994 Kallenbach NR, Zhong M, Rashes MS, Hernandez L, Lu M, Guo Q. Structure and drug-binding properties of unusual DNAs Clinical Chemistry. 40: 646.  0.185
1991 Lu M, Guo Q, Studier FW, Kallenbach NR. Resolution of branched DNA substrates by T7 endonuclease I and its inhibition. The Journal of Biological Chemistry. 266: 2531-6. PMID 1990002  0.183
1994 Beveridge DL, Hilbers CW, Kallenbach NR, Lilley D, Olson WK, Shakked Z, Redfield AG, Rich A, Sarma RH. Ninth conversation in the discipline biomolecular stereodynamics the university, albany, new york, june 20-24, 1995 Journal of Biomolecular Structure & Dynamics. 12. PMID 22671956 DOI: 10.1080/07391102.1994.10508756  0.178
1968 Kallenbach NR, Ma R. Initiation of deoxyribonucleic acid synthesis after thymine starvation of Bacillus subtilis Journal of Bacteriology. 95: 304-309. PMID 4966542  0.165
1994 Kallenbach NR, Zhong M. DNA cruciforms Current Opinion in Structural Biology. 4: 365-371. DOI: 10.1016/S0959-440X(94)90104-X  0.155
1980 Mandal C, Englander S, Young P, Kallenbach N. Fluctuational opening-closing reactions in dna and mononucleosome cores of chromatin probed by h-exchange and ligand binding reactions Biophysical Journal. 32: 623-625. DOI: 10.1016/S0006-3495(80)84996-4  0.146
1980 Mandal C, Englander S, Young P, Kallenbach N. Fluctuational opening-closing reactions in dna and mononucleosome cores of chromatin probed by h-exchange and ligand binding reactions Biophysical Journal. 32: 623-625. DOI: 10.1016/S0006-3495(80)84996-4  0.146
1980 Mandal C, Englander S, Young P, Kallenbach N. Fluctuational opening-closing reactions in dna and mononucleosome cores of chromatin probed by h-exchange and ligand binding reactions Biophysical Journal. 32: 623-625. DOI: 10.1016/S0006-3495(80)84996-4  0.146
1980 Mandal C, Englander S, Young P, Kallenbach N. Fluctuational opening-closing reactions in dna and mononucleosome cores of chromatin probed by h-exchange and ligand binding reactions Biophysical Journal. 32: 623-625. DOI: 10.1016/S0006-3495(80)84996-4  0.146
1980 Mandal C, Englander S, Young P, Kallenbach N. Fluctuational opening-closing reactions in dna and mononucleosome cores of chromatin probed by h-exchange and ligand binding reactions Biophysical Journal. 32: 623-625. DOI: 10.1016/S0006-3495(80)84996-4  0.146
1980 Mandal C, Englander S, Young P, Kallenbach N. Fluctuational opening-closing reactions in dna and mononucleosome cores of chromatin probed by h-exchange and ligand binding reactions Biophysical Journal. 32: 623-625. DOI: 10.1016/S0006-3495(80)84996-4  0.146
1980 Mandal C, Englander S, Young P, Kallenbach N. Fluctuational opening-closing reactions in dna and mononucleosome cores of chromatin probed by h-exchange and ligand binding reactions Biophysical Journal. 32: 623-625. DOI: 10.1016/S0006-3495(80)84996-4  0.146
1980 Mandal C, Englander S, Young P, Kallenbach N. Fluctuational opening-closing reactions in dna and mononucleosome cores of chromatin probed by h-exchange and ligand binding reactions Biophysical Journal. 32: 623-625. DOI: 10.1016/S0006-3495(80)84996-4  0.146
1980 Mandal C, Englander S, Young P, Kallenbach N. Fluctuational opening-closing reactions in dna and mononucleosome cores of chromatin probed by h-exchange and ligand binding reactions Biophysical Journal. 32: 623-625. DOI: 10.1016/S0006-3495(80)84996-4  0.146
1980 Mandal C, Englander S, Young P, Kallenbach N. Fluctuational opening-closing reactions in dna and mononucleosome cores of chromatin probed by h-exchange and ligand binding reactions Biophysical Journal. 32: 623-625. DOI: 10.1016/S0006-3495(80)84996-4  0.146
1980 Mandal C, Englander S, Young P, Kallenbach N. Fluctuational opening-closing reactions in dna and mononucleosome cores of chromatin probed by h-exchange and ligand binding reactions Biophysical Journal. 32: 623-625. DOI: 10.1016/S0006-3495(80)84996-4  0.146
1980 Mandal C, Englander S, Young P, Kallenbach N. Fluctuational opening-closing reactions in dna and mononucleosome cores of chromatin probed by h-exchange and ligand binding reactions Biophysical Journal. 32: 623-625. DOI: 10.1016/S0006-3495(80)84996-4  0.146
1980 Mandal C, Englander S, Young P, Kallenbach N. Fluctuational opening-closing reactions in dna and mononucleosome cores of chromatin probed by h-exchange and ligand binding reactions Biophysical Journal. 32: 623-625. DOI: 10.1016/S0006-3495(80)84996-4  0.146
1980 Mandal C, Englander S, Young P, Kallenbach N. Fluctuational opening-closing reactions in dna and mononucleosome cores of chromatin probed by h-exchange and ligand binding reactions Biophysical Journal. 32: 623-625. DOI: 10.1016/S0006-3495(80)84996-4  0.146
1980 Mandal C, Englander S, Young P, Kallenbach N. Fluctuational opening-closing reactions in dna and mononucleosome cores of chromatin probed by h-exchange and ligand binding reactions Biophysical Journal. 32: 623-625. DOI: 10.1016/S0006-3495(80)84996-4  0.146
1980 Mandal C, Englander S, Young P, Kallenbach N. Fluctuational opening-closing reactions in dna and mononucleosome cores of chromatin probed by h-exchange and ligand binding reactions Biophysical Journal. 32: 623-625. DOI: 10.1016/S0006-3495(80)84996-4  0.146
1980 Mandal C, Englander S, Young P, Kallenbach N. Fluctuational opening-closing reactions in dna and mononucleosome cores of chromatin probed by h-exchange and ligand binding reactions Biophysical Journal. 32: 623-625. DOI: 10.1016/S0006-3495(80)84996-4  0.146
1980 Mandal C, Englander S, Young P, Kallenbach N. Fluctuational opening-closing reactions in dna and mononucleosome cores of chromatin probed by h-exchange and ligand binding reactions Biophysical Journal. 32: 623-625. DOI: 10.1016/S0006-3495(80)84996-4  0.146
1980 Mandal C, Englander S, Young P, Kallenbach N. Fluctuational opening-closing reactions in dna and mononucleosome cores of chromatin probed by h-exchange and ligand binding reactions Biophysical Journal. 32: 623-625. DOI: 10.1016/S0006-3495(80)84996-4  0.146
1980 Mandal C, Englander S, Young P, Kallenbach N. Fluctuational opening-closing reactions in dna and mononucleosome cores of chromatin probed by h-exchange and ligand binding reactions Biophysical Journal. 32: 623-625. DOI: 10.1016/S0006-3495(80)84996-4  0.146
1980 Mandal C, Englander S, Young P, Kallenbach N. Fluctuational opening-closing reactions in dna and mononucleosome cores of chromatin probed by h-exchange and ligand binding reactions Biophysical Journal. 32: 623-625. DOI: 10.1016/S0006-3495(80)84996-4  0.146
1980 Mandal C, Englander S, Young P, Kallenbach N. Fluctuational opening-closing reactions in dna and mononucleosome cores of chromatin probed by h-exchange and ligand binding reactions Biophysical Journal. 32: 623-625. DOI: 10.1016/S0006-3495(80)84996-4  0.146
1980 Mandal C, Englander S, Young P, Kallenbach N. Fluctuational opening-closing reactions in dna and mononucleosome cores of chromatin probed by h-exchange and ligand binding reactions Biophysical Journal. 32: 623-625. DOI: 10.1016/S0006-3495(80)84996-4  0.146
1980 Mandal C, Englander S, Young P, Kallenbach N. Fluctuational opening-closing reactions in dna and mononucleosome cores of chromatin probed by h-exchange and ligand binding reactions Biophysical Journal. 32: 623-625. DOI: 10.1016/S0006-3495(80)84996-4  0.146
1980 Mandal C, Englander S, Young P, Kallenbach N. Fluctuational opening-closing reactions in dna and mononucleosome cores of chromatin probed by h-exchange and ligand binding reactions Biophysical Journal. 32: 623-625. DOI: 10.1016/S0006-3495(80)84996-4  0.146
1980 Mandal C, Englander S, Young P, Kallenbach N. Fluctuational opening-closing reactions in dna and mononucleosome cores of chromatin probed by h-exchange and ligand binding reactions Biophysical Journal. 32: 623-625. DOI: 10.1016/S0006-3495(80)84996-4  0.146
1980 Mandal C, Englander S, Young P, Kallenbach N. Fluctuational opening-closing reactions in dna and mononucleosome cores of chromatin probed by h-exchange and ligand binding reactions Biophysical Journal. 32: 623-625. DOI: 10.1016/S0006-3495(80)84996-4  0.146
1980 Mandal C, Englander S, Young P, Kallenbach N. Fluctuational opening-closing reactions in dna and mononucleosome cores of chromatin probed by h-exchange and ligand binding reactions Biophysical Journal. 32: 623-625. DOI: 10.1016/S0006-3495(80)84996-4  0.146
1980 Mandal C, Englander S, Young P, Kallenbach N. Fluctuational opening-closing reactions in dna and mononucleosome cores of chromatin probed by h-exchange and ligand binding reactions Biophysical Journal. 32: 623-625. DOI: 10.1016/S0006-3495(80)84996-4  0.146
1980 Mandal C, Englander S, Young P, Kallenbach N. Fluctuational opening-closing reactions in dna and mononucleosome cores of chromatin probed by h-exchange and ligand binding reactions Biophysical Journal. 32: 623-625. DOI: 10.1016/S0006-3495(80)84996-4  0.146
1980 Mandal C, Englander S, Young P, Kallenbach N. Fluctuational opening-closing reactions in dna and mononucleosome cores of chromatin probed by h-exchange and ligand binding reactions Biophysical Journal. 32: 623-625. DOI: 10.1016/S0006-3495(80)84996-4  0.146
1980 Mandal C, Englander S, Young P, Kallenbach N. Fluctuational opening-closing reactions in dna and mononucleosome cores of chromatin probed by h-exchange and ligand binding reactions Biophysical Journal. 32: 623-625. DOI: 10.1016/S0006-3495(80)84996-4  0.146
1980 Mandal C, Englander S, Young P, Kallenbach N. Fluctuational opening-closing reactions in dna and mononucleosome cores of chromatin probed by h-exchange and ligand binding reactions Biophysical Journal. 32: 623-625. DOI: 10.1016/S0006-3495(80)84996-4  0.146
1980 Mandal C, Englander S, Young P, Kallenbach N. Fluctuational opening-closing reactions in dna and mononucleosome cores of chromatin probed by h-exchange and ligand binding reactions Biophysical Journal. 32: 623-625. DOI: 10.1016/S0006-3495(80)84996-4  0.146
1980 Mandal C, Englander S, Young P, Kallenbach N. Fluctuational opening-closing reactions in dna and mononucleosome cores of chromatin probed by h-exchange and ligand binding reactions Biophysical Journal. 32: 623-625. DOI: 10.1016/S0006-3495(80)84996-4  0.146
1980 Mandal C, Englander S, Young P, Kallenbach N. Fluctuational opening-closing reactions in dna and mononucleosome cores of chromatin probed by h-exchange and ligand binding reactions Biophysical Journal. 32: 623-625. DOI: 10.1016/S0006-3495(80)84996-4  0.146
1980 Mandal C, Englander S, Young P, Kallenbach N. Fluctuational opening-closing reactions in dna and mononucleosome cores of chromatin probed by h-exchange and ligand binding reactions Biophysical Journal. 32: 623-625. DOI: 10.1016/S0006-3495(80)84996-4  0.146
1980 Mandal C, Englander S, Young P, Kallenbach N. Fluctuational opening-closing reactions in dna and mononucleosome cores of chromatin probed by h-exchange and ligand binding reactions Biophysical Journal. 32: 623-625. DOI: 10.1016/S0006-3495(80)84996-4  0.146
1980 Mandal C, Englander S, Young P, Kallenbach N. Fluctuational opening-closing reactions in dna and mononucleosome cores of chromatin probed by h-exchange and ligand binding reactions Biophysical Journal. 32: 623-625. DOI: 10.1016/S0006-3495(80)84996-4  0.146
1980 Mandal C, Englander S, Young P, Kallenbach N. Fluctuational opening-closing reactions in dna and mononucleosome cores of chromatin probed by h-exchange and ligand binding reactions Biophysical Journal. 32: 623-625. DOI: 10.1016/S0006-3495(80)84996-4  0.146
1980 Mandal C, Englander S, Young P, Kallenbach N. Fluctuational opening-closing reactions in dna and mononucleosome cores of chromatin probed by h-exchange and ligand binding reactions Biophysical Journal. 32: 623-625. DOI: 10.1016/S0006-3495(80)84996-4  0.146
1980 Mandal C, Englander S, Young P, Kallenbach N. Fluctuational opening-closing reactions in dna and mononucleosome cores of chromatin probed by h-exchange and ligand binding reactions Biophysical Journal. 32: 623-625. DOI: 10.1016/S0006-3495(80)84996-4  0.146
1980 Mandal C, Englander S, Young P, Kallenbach N. Fluctuational opening-closing reactions in dna and mononucleosome cores of chromatin probed by h-exchange and ligand binding reactions Biophysical Journal. 32: 623-625. DOI: 10.1016/S0006-3495(80)84996-4  0.146
1980 Mandal C, Englander S, Young P, Kallenbach N. Fluctuational opening-closing reactions in dna and mononucleosome cores of chromatin probed by h-exchange and ligand binding reactions Biophysical Journal. 32: 623-625. DOI: 10.1016/S0006-3495(80)84996-4  0.146
1980 Mandal C, Englander S, Young P, Kallenbach N. Fluctuational opening-closing reactions in dna and mononucleosome cores of chromatin probed by h-exchange and ligand binding reactions Biophysical Journal. 32: 623-625. DOI: 10.1016/S0006-3495(80)84996-4  0.146
1980 Mandal C, Englander S, Young P, Kallenbach N. Fluctuational opening-closing reactions in dna and mononucleosome cores of chromatin probed by h-exchange and ligand binding reactions Biophysical Journal. 32: 623-625. DOI: 10.1016/S0006-3495(80)84996-4  0.146
1980 Mandal C, Englander S, Young P, Kallenbach N. Fluctuational opening-closing reactions in dna and mononucleosome cores of chromatin probed by h-exchange and ligand binding reactions Biophysical Journal. 32: 623-625. DOI: 10.1016/S0006-3495(80)84996-4  0.146
1980 Mandal C, Englander S, Young P, Kallenbach N. Fluctuational opening-closing reactions in dna and mononucleosome cores of chromatin probed by h-exchange and ligand binding reactions Biophysical Journal. 32: 623-625. DOI: 10.1016/S0006-3495(80)84996-4  0.146
1980 Englander SW, Kallenbach NR, Heeger AJ, Krumhansl JA, Litwin S. Soliton-like states for opening in polynucleotide double helices Ferroelectrics. 30: 167-167. DOI: 10.1080/00150198008209510  0.141
1980 Englander SW, Kallenbach NR, Heeger AJ, Krumhansl JA, Litwin S. Soliton-like states for opening in polynucleotide double helices Ferroelectrics. 30: 167-167. DOI: 10.1080/00150198008209510  0.141
1980 Englander SW, Kallenbach NR, Heeger AJ, Krumhansl JA, Litwin S. Soliton-like states for opening in polynucleotide double helices Ferroelectrics. 30: 167-167. DOI: 10.1080/00150198008209510  0.141
1980 Englander SW, Kallenbach NR, Heeger AJ, Krumhansl JA, Litwin S. Soliton-like states for opening in polynucleotide double helices Ferroelectrics. 30: 167-167. DOI: 10.1080/00150198008209510  0.141
1980 Englander SW, Kallenbach NR, Heeger AJ, Krumhansl JA, Litwin S. Soliton-like states for opening in polynucleotide double helices Ferroelectrics. 30: 167-167. DOI: 10.1080/00150198008209510  0.141
1980 Englander SW, Kallenbach NR, Heeger AJ, Krumhansl JA, Litwin S. Soliton-like states for opening in polynucleotide double helices Ferroelectrics. 30: 167-167. DOI: 10.1080/00150198008209510  0.141
1980 Englander SW, Kallenbach NR, Heeger AJ, Krumhansl JA, Litwin S. Soliton-like states for opening in polynucleotide double helices Ferroelectrics. 30: 167-167. DOI: 10.1080/00150198008209510  0.141
1980 Englander SW, Kallenbach NR, Heeger AJ, Krumhansl JA, Litwin S. Soliton-like states for opening in polynucleotide double helices Ferroelectrics. 30: 167-167. DOI: 10.1080/00150198008209510  0.141
1980 Englander SW, Kallenbach NR, Heeger AJ, Krumhansl JA, Litwin S. Soliton-like states for opening in polynucleotide double helices Ferroelectrics. 30: 167-167. DOI: 10.1080/00150198008209510  0.141
1980 Englander SW, Kallenbach NR, Heeger AJ, Krumhansl JA, Litwin S. Soliton-like states for opening in polynucleotide double helices Ferroelectrics. 30: 167-167. DOI: 10.1080/00150198008209510  0.141
1980 Englander SW, Kallenbach NR, Heeger AJ, Krumhansl JA, Litwin S. Soliton-like states for opening in polynucleotide double helices Ferroelectrics. 30: 167-167. DOI: 10.1080/00150198008209510  0.141
1980 Englander SW, Kallenbach NR, Heeger AJ, Krumhansl JA, Litwin S. Soliton-like states for opening in polynucleotide double helices Ferroelectrics. 30: 167-167. DOI: 10.1080/00150198008209510  0.141
1980 Englander SW, Kallenbach NR, Heeger AJ, Krumhansl JA, Litwin S. Soliton-like states for opening in polynucleotide double helices Ferroelectrics. 30: 167-167. DOI: 10.1080/00150198008209510  0.141
1980 Englander SW, Kallenbach NR, Heeger AJ, Krumhansl JA, Litwin S. Soliton-like states for opening in polynucleotide double helices Ferroelectrics. 30: 167-167. DOI: 10.1080/00150198008209510  0.141
1980 Englander SW, Kallenbach NR, Heeger AJ, Krumhansl JA, Litwin S. Soliton-like states for opening in polynucleotide double helices Ferroelectrics. 30: 167-167. DOI: 10.1080/00150198008209510  0.141
1980 Englander SW, Kallenbach NR, Heeger AJ, Krumhansl JA, Litwin S. Soliton-like states for opening in polynucleotide double helices Ferroelectrics. 30: 167-167. DOI: 10.1080/00150198008209510  0.141
1980 Englander SW, Kallenbach NR, Heeger AJ, Krumhansl JA, Litwin S. Soliton-like states for opening in polynucleotide double helices Ferroelectrics. 30: 167-167. DOI: 10.1080/00150198008209510  0.141
1980 Englander SW, Kallenbach NR, Heeger AJ, Krumhansl JA, Litwin S. Soliton-like states for opening in polynucleotide double helices Ferroelectrics. 30: 167-167. DOI: 10.1080/00150198008209510  0.141
1980 Englander SW, Kallenbach NR, Heeger AJ, Krumhansl JA, Litwin S. Soliton-like states for opening in polynucleotide double helices Ferroelectrics. 30: 167-167. DOI: 10.1080/00150198008209510  0.141
1980 Englander SW, Kallenbach NR, Heeger AJ, Krumhansl JA, Litwin S. Soliton-like states for opening in polynucleotide double helices Ferroelectrics. 30: 167-167. DOI: 10.1080/00150198008209510  0.141
1980 Englander SW, Kallenbach NR, Heeger AJ, Krumhansl JA, Litwin S. Soliton-like states for opening in polynucleotide double helices Ferroelectrics. 30: 167-167. DOI: 10.1080/00150198008209510  0.141
1980 Englander SW, Kallenbach NR, Heeger AJ, Krumhansl JA, Litwin S. Soliton-like states for opening in polynucleotide double helices Ferroelectrics. 30: 167-167. DOI: 10.1080/00150198008209510  0.141
1980 Englander SW, Kallenbach NR, Heeger AJ, Krumhansl JA, Litwin S. Soliton-like states for opening in polynucleotide double helices Ferroelectrics. 30: 167-167. DOI: 10.1080/00150198008209510  0.141
1980 Englander SW, Kallenbach NR, Heeger AJ, Krumhansl JA, Litwin S. Soliton-like states for opening in polynucleotide double helices Ferroelectrics. 30: 167-167. DOI: 10.1080/00150198008209510  0.141
1980 Englander SW, Kallenbach NR, Heeger AJ, Krumhansl JA, Litwin S. Soliton-like states for opening in polynucleotide double helices Ferroelectrics. 30: 167-167. DOI: 10.1080/00150198008209510  0.141
1980 Englander SW, Kallenbach NR, Heeger AJ, Krumhansl JA, Litwin S. Soliton-like states for opening in polynucleotide double helices Ferroelectrics. 30: 167-167. DOI: 10.1080/00150198008209510  0.141
1980 Englander SW, Kallenbach NR, Heeger AJ, Krumhansl JA, Litwin S. Soliton-like states for opening in polynucleotide double helices Ferroelectrics. 30: 167-167. DOI: 10.1080/00150198008209510  0.141
1980 Englander SW, Kallenbach NR, Heeger AJ, Krumhansl JA, Litwin S. Soliton-like states for opening in polynucleotide double helices Ferroelectrics. 30: 167-167. DOI: 10.1080/00150198008209510  0.141
1980 Englander SW, Kallenbach NR, Heeger AJ, Krumhansl JA, Litwin S. Soliton-like states for opening in polynucleotide double helices Ferroelectrics. 30: 167-167. DOI: 10.1080/00150198008209510  0.141
1980 Englander SW, Kallenbach NR, Heeger AJ, Krumhansl JA, Litwin S. Soliton-like states for opening in polynucleotide double helices Ferroelectrics. 30: 167-167. DOI: 10.1080/00150198008209510  0.141
1980 Englander SW, Kallenbach NR, Heeger AJ, Krumhansl JA, Litwin S. Soliton-like states for opening in polynucleotide double helices Ferroelectrics. 30: 167-167. DOI: 10.1080/00150198008209510  0.141
1980 Englander SW, Kallenbach NR, Heeger AJ, Krumhansl JA, Litwin S. Soliton-like states for opening in polynucleotide double helices Ferroelectrics. 30: 167-167. DOI: 10.1080/00150198008209510  0.141
1980 Englander SW, Kallenbach NR, Heeger AJ, Krumhansl JA, Litwin S. Soliton-like states for opening in polynucleotide double helices Ferroelectrics. 30: 167-167. DOI: 10.1080/00150198008209510  0.141
1980 Englander SW, Kallenbach NR, Heeger AJ, Krumhansl JA, Litwin S. Soliton-like states for opening in polynucleotide double helices Ferroelectrics. 30: 167-167. DOI: 10.1080/00150198008209510  0.141
1980 Englander SW, Kallenbach NR, Heeger AJ, Krumhansl JA, Litwin S. Soliton-like states for opening in polynucleotide double helices Ferroelectrics. 30: 167-167. DOI: 10.1080/00150198008209510  0.141
1980 Englander SW, Kallenbach NR, Heeger AJ, Krumhansl JA, Litwin S. Soliton-like states for opening in polynucleotide double helices Ferroelectrics. 30: 167-167. DOI: 10.1080/00150198008209510  0.141
1980 Englander SW, Kallenbach NR, Heeger AJ, Krumhansl JA, Litwin S. Soliton-like states for opening in polynucleotide double helices Ferroelectrics. 30: 167-167. DOI: 10.1080/00150198008209510  0.141
1980 Englander SW, Kallenbach NR, Heeger AJ, Krumhansl JA, Litwin S. Soliton-like states for opening in polynucleotide double helices Ferroelectrics. 30: 167-167. DOI: 10.1080/00150198008209510  0.141
1980 Englander SW, Kallenbach NR, Heeger AJ, Krumhansl JA, Litwin S. Soliton-like states for opening in polynucleotide double helices Ferroelectrics. 30: 167-167. DOI: 10.1080/00150198008209510  0.141
1980 Englander SW, Kallenbach NR, Heeger AJ, Krumhansl JA, Litwin S. Soliton-like states for opening in polynucleotide double helices Ferroelectrics. 30: 167-167. DOI: 10.1080/00150198008209510  0.141
1980 Englander SW, Kallenbach NR, Heeger AJ, Krumhansl JA, Litwin S. Soliton-like states for opening in polynucleotide double helices Ferroelectrics. 30: 167-167. DOI: 10.1080/00150198008209510  0.141
1980 Englander SW, Kallenbach NR, Heeger AJ, Krumhansl JA, Litwin S. Soliton-like states for opening in polynucleotide double helices Ferroelectrics. 30: 167-167. DOI: 10.1080/00150198008209510  0.141
1980 Englander SW, Kallenbach NR, Heeger AJ, Krumhansl JA, Litwin S. Soliton-like states for opening in polynucleotide double helices Ferroelectrics. 30: 167-167. DOI: 10.1080/00150198008209510  0.141
1980 Englander SW, Kallenbach NR, Heeger AJ, Krumhansl JA, Litwin S. Soliton-like states for opening in polynucleotide double helices Ferroelectrics. 30: 167-167. DOI: 10.1080/00150198008209510  0.141
1980 Englander SW, Kallenbach NR, Heeger AJ, Krumhansl JA, Litwin S. Soliton-like states for opening in polynucleotide double helices Ferroelectrics. 30: 167-167. DOI: 10.1080/00150198008209510  0.141
1980 Englander SW, Kallenbach NR, Heeger AJ, Krumhansl JA, Litwin S. Soliton-like states for opening in polynucleotide double helices Ferroelectrics. 30: 167-167. DOI: 10.1080/00150198008209510  0.141
1980 Englander SW, Kallenbach NR, Heeger AJ, Krumhansl JA, Litwin S. Soliton-like states for opening in polynucleotide double helices Ferroelectrics. 30: 167-167. DOI: 10.1080/00150198008209510  0.141
1980 Englander SW, Kallenbach NR, Heeger AJ, Krumhansl JA, Litwin S. Soliton-like states for opening in polynucleotide double helices Ferroelectrics. 30: 167-167. DOI: 10.1080/00150198008209510  0.141
1980 Englander SW, Kallenbach NR, Heeger AJ, Krumhansl JA, Litwin S. Soliton-like states for opening in polynucleotide double helices Ferroelectrics. 30: 167-167. DOI: 10.1080/00150198008209510  0.141
1980 Englander SW, Kallenbach NR, Heeger AJ, Krumhansl JA, Litwin S. Soliton-like states for opening in polynucleotide double helices Ferroelectrics. 30: 167-167. DOI: 10.1080/00150198008209510  0.141
1980 Englander SW, Kallenbach NR, Heeger AJ, Krumhansl JA, Litwin S. Soliton-like states for opening in polynucleotide double helices Ferroelectrics. 30: 167-167. DOI: 10.1080/00150198008209510  0.141
1978 Reuben J, Baker BM, Kallenbach NR. Structure of mutagen nucleic acid complexes in solution. Proton chemical shifts in 9-aminoacridine complexes with dG-dC, dC-dG, and dA-dT-dG-dC-dA-dT. Biochemistry. 17: 2915-9. PMID 687569 DOI: 10.1021/Bi00607A033  0.136
1978 Reuben J, Baker BM, Kallenbach NR. Structure of mutagen nucleic acid complexes in solution. Proton chemical shifts in 9-aminoacridine complexes with dG-dC, dC-dG, and dA-dT-dG-dC-dA-dT. Biochemistry. 17: 2915-9. PMID 687569 DOI: 10.1021/Bi00607A033  0.136
1978 Reuben J, Baker BM, Kallenbach NR. Structure of mutagen nucleic acid complexes in solution. Proton chemical shifts in 9-aminoacridine complexes with dG-dC, dC-dG, and dA-dT-dG-dC-dA-dT. Biochemistry. 17: 2915-9. PMID 687569 DOI: 10.1021/Bi00607A033  0.136
1993 Morozov VN, Seeman NC, Kallenbach NR. New methods for depositing and imaging molecules in scanning tunneling microscopy. Scanning Microscopy. 7: 757-76; discussion 7. PMID 8146612  0.136
1994 Zhou HX, Hull LA, Kallenbach NR, Mayne L, Bai Y, Walter Englander S. Quantitative evaluation of stabilizing interactions in a prenucleated α-helix by hydrogen exchange Journal of the American Chemical Society. 116: 6482-6483.  0.125
1995 Spek EJ, Gong Y, Kallenbach NR. Intermolecular interactions in α helical oligo- and poly(L-glutamic acid) at acidic pH Journal of the American Chemical Society. 117: 10773-10774.  0.123
1993 Kallenbach NR. α-helix stability and the native state of myoglobin Biochemistry®. 12638-12643.  0.112
1987 Seeman NC, Newton CJ, Petrillo ML, Chen J, Mueller JE, Maiorella JA, Sheardy RD, Ma R, Kallenbach NR. Nucleic acid junctions and macromolecular design Acta Crystallographica Section a Foundations of Crystallography. 43: C37-C37. DOI: 10.1107/S0108767387084460  0.11
1987 Seeman NC, Newton CJ, Petrillo ML, Chen J, Mueller JE, Maiorella JA, Sheardy RD, Ma R, Kallenbach NR. Nucleic acid junctions and macromolecular design Acta Crystallographica Section a Foundations of Crystallography. 43: C37-C37. DOI: 10.1107/S0108767387084460  0.11
1987 Seeman NC, Newton CJ, Petrillo ML, Chen J, Mueller JE, Maiorella JA, Sheardy RD, Ma R, Kallenbach NR. Nucleic acid junctions and macromolecular design Acta Crystallographica Section a Foundations of Crystallography. 43: C37-C37. DOI: 10.1107/S0108767387084460  0.11
1987 Seeman NC, Newton CJ, Petrillo ML, Chen J, Mueller JE, Maiorella JA, Sheardy RD, Ma R, Kallenbach NR. Nucleic acid junctions and macromolecular design Acta Crystallographica Section a Foundations of Crystallography. 43: C37-C37. DOI: 10.1107/S0108767387084460  0.11
1987 Seeman NC, Newton CJ, Petrillo ML, Chen J, Mueller JE, Maiorella JA, Sheardy RD, Ma R, Kallenbach NR. Nucleic acid junctions and macromolecular design Acta Crystallographica Section a Foundations of Crystallography. 43: C37-C37. DOI: 10.1107/S0108767387084460  0.11
1987 Seeman NC, Newton CJ, Petrillo ML, Chen J, Mueller JE, Maiorella JA, Sheardy RD, Ma R, Kallenbach NR. Nucleic acid junctions and macromolecular design Acta Crystallographica Section a Foundations of Crystallography. 43: C37-C37. DOI: 10.1107/S0108767387084460  0.11
1987 Seeman NC, Newton CJ, Petrillo ML, Chen J, Mueller JE, Maiorella JA, Sheardy RD, Ma R, Kallenbach NR. Nucleic acid junctions and macromolecular design Acta Crystallographica Section a Foundations of Crystallography. 43: C37-C37. DOI: 10.1107/S0108767387084460  0.11
1987 Seeman NC, Newton CJ, Petrillo ML, Chen J, Mueller JE, Maiorella JA, Sheardy RD, Ma R, Kallenbach NR. Nucleic acid junctions and macromolecular design Acta Crystallographica Section a Foundations of Crystallography. 43: C37-C37. DOI: 10.1107/S0108767387084460  0.11
1987 Seeman NC, Newton CJ, Petrillo ML, Chen J, Mueller JE, Maiorella JA, Sheardy RD, Ma R, Kallenbach NR. Nucleic acid junctions and macromolecular design Acta Crystallographica Section a Foundations of Crystallography. 43: C37-C37. DOI: 10.1107/S0108767387084460  0.11
1987 Seeman NC, Newton CJ, Petrillo ML, Chen J, Mueller JE, Maiorella JA, Sheardy RD, Ma R, Kallenbach NR. Nucleic acid junctions and macromolecular design Acta Crystallographica Section a Foundations of Crystallography. 43: C37-C37. DOI: 10.1107/S0108767387084460  0.11
1987 Seeman NC, Newton CJ, Petrillo ML, Chen J, Mueller JE, Maiorella JA, Sheardy RD, Ma R, Kallenbach NR. Nucleic acid junctions and macromolecular design Acta Crystallographica Section a Foundations of Crystallography. 43: C37-C37. DOI: 10.1107/S0108767387084460  0.11
1987 Seeman NC, Newton CJ, Petrillo ML, Chen J, Mueller JE, Maiorella JA, Sheardy RD, Ma R, Kallenbach NR. Nucleic acid junctions and macromolecular design Acta Crystallographica Section a Foundations of Crystallography. 43: C37-C37. DOI: 10.1107/S0108767387084460  0.11
1987 Seeman NC, Newton CJ, Petrillo ML, Chen J, Mueller JE, Maiorella JA, Sheardy RD, Ma R, Kallenbach NR. Nucleic acid junctions and macromolecular design Acta Crystallographica Section a Foundations of Crystallography. 43: C37-C37. DOI: 10.1107/S0108767387084460  0.11
1987 Seeman NC, Newton CJ, Petrillo ML, Chen J, Mueller JE, Maiorella JA, Sheardy RD, Ma R, Kallenbach NR. Nucleic acid junctions and macromolecular design Acta Crystallographica Section a Foundations of Crystallography. 43: C37-C37. DOI: 10.1107/S0108767387084460  0.11
1987 Seeman NC, Newton CJ, Petrillo ML, Chen J, Mueller JE, Maiorella JA, Sheardy RD, Ma R, Kallenbach NR. Nucleic acid junctions and macromolecular design Acta Crystallographica Section a Foundations of Crystallography. 43: C37-C37. DOI: 10.1107/S0108767387084460  0.11
1987 Seeman NC, Newton CJ, Petrillo ML, Chen J, Mueller JE, Maiorella JA, Sheardy RD, Ma R, Kallenbach NR. Nucleic acid junctions and macromolecular design Acta Crystallographica Section a Foundations of Crystallography. 43: C37-C37. DOI: 10.1107/S0108767387084460  0.11
1987 Seeman NC, Newton CJ, Petrillo ML, Chen J, Mueller JE, Maiorella JA, Sheardy RD, Ma R, Kallenbach NR. Nucleic acid junctions and macromolecular design Acta Crystallographica Section a Foundations of Crystallography. 43: C37-C37. DOI: 10.1107/S0108767387084460  0.11
1987 Seeman NC, Newton CJ, Petrillo ML, Chen J, Mueller JE, Maiorella JA, Sheardy RD, Ma R, Kallenbach NR. Nucleic acid junctions and macromolecular design Acta Crystallographica Section a Foundations of Crystallography. 43: C37-C37. DOI: 10.1107/S0108767387084460  0.11
1987 Seeman NC, Newton CJ, Petrillo ML, Chen J, Mueller JE, Maiorella JA, Sheardy RD, Ma R, Kallenbach NR. Nucleic acid junctions and macromolecular design Acta Crystallographica Section a Foundations of Crystallography. 43: C37-C37. DOI: 10.1107/S0108767387084460  0.11
1987 Seeman NC, Newton CJ, Petrillo ML, Chen J, Mueller JE, Maiorella JA, Sheardy RD, Ma R, Kallenbach NR. Nucleic acid junctions and macromolecular design Acta Crystallographica Section a Foundations of Crystallography. 43: C37-C37. DOI: 10.1107/S0108767387084460  0.11
1987 Seeman NC, Newton CJ, Petrillo ML, Chen J, Mueller JE, Maiorella JA, Sheardy RD, Ma R, Kallenbach NR. Nucleic acid junctions and macromolecular design Acta Crystallographica Section a Foundations of Crystallography. 43: C37-C37. DOI: 10.1107/S0108767387084460  0.11
1987 Seeman NC, Newton CJ, Petrillo ML, Chen J, Mueller JE, Maiorella JA, Sheardy RD, Ma R, Kallenbach NR. Nucleic acid junctions and macromolecular design Acta Crystallographica Section a Foundations of Crystallography. 43: C37-C37. DOI: 10.1107/S0108767387084460  0.11
1987 Seeman NC, Newton CJ, Petrillo ML, Chen J, Mueller JE, Maiorella JA, Sheardy RD, Ma R, Kallenbach NR. Nucleic acid junctions and macromolecular design Acta Crystallographica Section a Foundations of Crystallography. 43: C37-C37. DOI: 10.1107/S0108767387084460  0.11
1987 Seeman NC, Newton CJ, Petrillo ML, Chen J, Mueller JE, Maiorella JA, Sheardy RD, Ma R, Kallenbach NR. Nucleic acid junctions and macromolecular design Acta Crystallographica Section a Foundations of Crystallography. 43: C37-C37. DOI: 10.1107/S0108767387084460  0.11
1987 Seeman NC, Newton CJ, Petrillo ML, Chen J, Mueller JE, Maiorella JA, Sheardy RD, Ma R, Kallenbach NR. Nucleic acid junctions and macromolecular design Acta Crystallographica Section a Foundations of Crystallography. 43: C37-C37. DOI: 10.1107/S0108767387084460  0.11
1987 Seeman NC, Newton CJ, Petrillo ML, Chen J, Mueller JE, Maiorella JA, Sheardy RD, Ma R, Kallenbach NR. Nucleic acid junctions and macromolecular design Acta Crystallographica Section a Foundations of Crystallography. 43: C37-C37. DOI: 10.1107/S0108767387084460  0.11
1987 Seeman NC, Newton CJ, Petrillo ML, Chen J, Mueller JE, Maiorella JA, Sheardy RD, Ma R, Kallenbach NR. Nucleic acid junctions and macromolecular design Acta Crystallographica Section a Foundations of Crystallography. 43: C37-C37. DOI: 10.1107/S0108767387084460  0.11
1987 Seeman NC, Newton CJ, Petrillo ML, Chen J, Mueller JE, Maiorella JA, Sheardy RD, Ma R, Kallenbach NR. Nucleic acid junctions and macromolecular design Acta Crystallographica Section a Foundations of Crystallography. 43: C37-C37. DOI: 10.1107/S0108767387084460  0.11
1987 Seeman NC, Newton CJ, Petrillo ML, Chen J, Mueller JE, Maiorella JA, Sheardy RD, Ma R, Kallenbach NR. Nucleic acid junctions and macromolecular design Acta Crystallographica Section a Foundations of Crystallography. 43: C37-C37. DOI: 10.1107/S0108767387084460  0.11
1987 Seeman NC, Newton CJ, Petrillo ML, Chen J, Mueller JE, Maiorella JA, Sheardy RD, Ma R, Kallenbach NR. Nucleic acid junctions and macromolecular design Acta Crystallographica Section a Foundations of Crystallography. 43: C37-C37. DOI: 10.1107/S0108767387084460  0.11
1987 Seeman NC, Newton CJ, Petrillo ML, Chen J, Mueller JE, Maiorella JA, Sheardy RD, Ma R, Kallenbach NR. Nucleic acid junctions and macromolecular design Acta Crystallographica Section a Foundations of Crystallography. 43: C37-C37. DOI: 10.1107/S0108767387084460  0.11
1987 Seeman NC, Newton CJ, Petrillo ML, Chen J, Mueller JE, Maiorella JA, Sheardy RD, Ma R, Kallenbach NR. Nucleic acid junctions and macromolecular design Acta Crystallographica Section a Foundations of Crystallography. 43: C37-C37. DOI: 10.1107/S0108767387084460  0.11
1987 Seeman NC, Newton CJ, Petrillo ML, Chen J, Mueller JE, Maiorella JA, Sheardy RD, Ma R, Kallenbach NR. Nucleic acid junctions and macromolecular design Acta Crystallographica Section a Foundations of Crystallography. 43: C37-C37. DOI: 10.1107/S0108767387084460  0.11
1987 Seeman NC, Newton CJ, Petrillo ML, Chen J, Mueller JE, Maiorella JA, Sheardy RD, Ma R, Kallenbach NR. Nucleic acid junctions and macromolecular design Acta Crystallographica Section a Foundations of Crystallography. 43: C37-C37. DOI: 10.1107/S0108767387084460  0.11
1987 Seeman NC, Newton CJ, Petrillo ML, Chen J, Mueller JE, Maiorella JA, Sheardy RD, Ma R, Kallenbach NR. Nucleic acid junctions and macromolecular design Acta Crystallographica Section a Foundations of Crystallography. 43: C37-C37. DOI: 10.1107/S0108767387084460  0.11
1987 Seeman NC, Newton CJ, Petrillo ML, Chen J, Mueller JE, Maiorella JA, Sheardy RD, Ma R, Kallenbach NR. Nucleic acid junctions and macromolecular design Acta Crystallographica Section a Foundations of Crystallography. 43: C37-C37. DOI: 10.1107/S0108767387084460  0.11
1987 Seeman NC, Newton CJ, Petrillo ML, Chen J, Mueller JE, Maiorella JA, Sheardy RD, Ma R, Kallenbach NR. Nucleic acid junctions and macromolecular design Acta Crystallographica Section a Foundations of Crystallography. 43: C37-C37. DOI: 10.1107/S0108767387084460  0.11
1987 Seeman NC, Newton CJ, Petrillo ML, Chen J, Mueller JE, Maiorella JA, Sheardy RD, Ma R, Kallenbach NR. Nucleic acid junctions and macromolecular design Acta Crystallographica Section a Foundations of Crystallography. 43: C37-C37. DOI: 10.1107/S0108767387084460  0.11
1987 Seeman NC, Newton CJ, Petrillo ML, Chen J, Mueller JE, Maiorella JA, Sheardy RD, Ma R, Kallenbach NR. Nucleic acid junctions and macromolecular design Acta Crystallographica Section a Foundations of Crystallography. 43: C37-C37. DOI: 10.1107/S0108767387084460  0.11
1987 Seeman NC, Newton CJ, Petrillo ML, Chen J, Mueller JE, Maiorella JA, Sheardy RD, Ma R, Kallenbach NR. Nucleic acid junctions and macromolecular design Acta Crystallographica Section a Foundations of Crystallography. 43: C37-C37. DOI: 10.1107/S0108767387084460  0.11
1987 Seeman NC, Newton CJ, Petrillo ML, Chen J, Mueller JE, Maiorella JA, Sheardy RD, Ma R, Kallenbach NR. Nucleic acid junctions and macromolecular design Acta Crystallographica Section a Foundations of Crystallography. 43: C37-C37. DOI: 10.1107/S0108767387084460  0.11
1987 Seeman NC, Newton CJ, Petrillo ML, Chen J, Mueller JE, Maiorella JA, Sheardy RD, Ma R, Kallenbach NR. Nucleic acid junctions and macromolecular design Acta Crystallographica Section a Foundations of Crystallography. 43: C37-C37. DOI: 10.1107/S0108767387084460  0.11
1987 Seeman NC, Newton CJ, Petrillo ML, Chen J, Mueller JE, Maiorella JA, Sheardy RD, Ma R, Kallenbach NR. Nucleic acid junctions and macromolecular design Acta Crystallographica Section a Foundations of Crystallography. 43: C37-C37. DOI: 10.1107/S0108767387084460  0.11
1987 Seeman NC, Newton CJ, Petrillo ML, Chen J, Mueller JE, Maiorella JA, Sheardy RD, Ma R, Kallenbach NR. Nucleic acid junctions and macromolecular design Acta Crystallographica Section a Foundations of Crystallography. 43: C37-C37. DOI: 10.1107/S0108767387084460  0.11
1987 Seeman NC, Newton CJ, Petrillo ML, Chen J, Mueller JE, Maiorella JA, Sheardy RD, Ma R, Kallenbach NR. Nucleic acid junctions and macromolecular design Acta Crystallographica Section a Foundations of Crystallography. 43: C37-C37. DOI: 10.1107/S0108767387084460  0.11
1987 Seeman NC, Newton CJ, Petrillo ML, Chen J, Mueller JE, Maiorella JA, Sheardy RD, Ma R, Kallenbach NR. Nucleic acid junctions and macromolecular design Acta Crystallographica Section a Foundations of Crystallography. 43: C37-C37. DOI: 10.1107/S0108767387084460  0.11
1987 Seeman NC, Newton CJ, Petrillo ML, Chen J, Mueller JE, Maiorella JA, Sheardy RD, Ma R, Kallenbach NR. Nucleic acid junctions and macromolecular design Acta Crystallographica Section a Foundations of Crystallography. 43: C37-C37. DOI: 10.1107/S0108767387084460  0.11
1987 Seeman NC, Newton CJ, Petrillo ML, Chen J, Mueller JE, Maiorella JA, Sheardy RD, Ma R, Kallenbach NR. Nucleic acid junctions and macromolecular design Acta Crystallographica Section a Foundations of Crystallography. 43: C37-C37. DOI: 10.1107/S0108767387084460  0.11
1987 Seeman NC, Newton CJ, Petrillo ML, Chen J, Mueller JE, Maiorella JA, Sheardy RD, Ma R, Kallenbach NR. Nucleic acid junctions and macromolecular design Acta Crystallographica Section a Foundations of Crystallography. 43: C37-C37. DOI: 10.1107/S0108767387084460  0.11
1978 Reuben J, Baker BM, Kallenbach NR. Structure of mutagen nucleic acid complexes in solution. Proton chemical shifts in 9-aminoacridine complexes with dG-dC, dC-dG, and dA-dT-dG-dC-dA-dT Biochemistry. 17: 2915-2919. DOI: 10.1021/bi00607a033  0.105
1978 Reuben J, Baker BM, Kallenbach NR. Structure of mutagen nucleic acid complexes in solution. Proton chemical shifts in 9-aminoacridine complexes with dG-dC, dC-dG, and dA-dT-dG-dC-dA-dT Biochemistry. 17: 2915-2919. DOI: 10.1021/bi00607a033  0.105
1978 Reuben J, Baker BM, Kallenbach NR. Structure of mutagen nucleic acid complexes in solution. Proton chemical shifts in 9-aminoacridine complexes with dG-dC, dC-dG, and dA-dT-dG-dC-dA-dT Biochemistry. 17: 2915-2919. DOI: 10.1021/bi00607a033  0.105
1978 Reuben J, Baker BM, Kallenbach NR. Structure of mutagen nucleic acid complexes in solution. Proton chemical shifts in 9-aminoacridine complexes with dG-dC, dC-dG, and dA-dT-dG-dC-dA-dT Biochemistry. 17: 2915-2919. DOI: 10.1021/bi00607a033  0.105
1978 Reuben J, Baker BM, Kallenbach NR. Structure of mutagen nucleic acid complexes in solution. Proton chemical shifts in 9-aminoacridine complexes with dG-dC, dC-dG, and dA-dT-dG-dC-dA-dT Biochemistry. 17: 2915-2919. DOI: 10.1021/bi00607a033  0.105
1978 Reuben J, Baker BM, Kallenbach NR. Structure of mutagen nucleic acid complexes in solution. Proton chemical shifts in 9-aminoacridine complexes with dG-dC, dC-dG, and dA-dT-dG-dC-dA-dT Biochemistry. 17: 2915-2919. DOI: 10.1021/bi00607a033  0.105
1978 Reuben J, Baker BM, Kallenbach NR. Structure of mutagen nucleic acid complexes in solution. Proton chemical shifts in 9-aminoacridine complexes with dG-dC, dC-dG, and dA-dT-dG-dC-dA-dT Biochemistry. 17: 2915-2919. DOI: 10.1021/bi00607a033  0.105
1978 Reuben J, Baker BM, Kallenbach NR. Structure of mutagen nucleic acid complexes in solution. Proton chemical shifts in 9-aminoacridine complexes with dG-dC, dC-dG, and dA-dT-dG-dC-dA-dT Biochemistry. 17: 2915-2919. DOI: 10.1021/bi00607a033  0.105
1978 Reuben J, Baker BM, Kallenbach NR. Structure of mutagen nucleic acid complexes in solution. Proton chemical shifts in 9-aminoacridine complexes with dG-dC, dC-dG, and dA-dT-dG-dC-dA-dT Biochemistry. 17: 2915-2919. DOI: 10.1021/bi00607a033  0.105
1978 Reuben J, Baker BM, Kallenbach NR. Structure of mutagen nucleic acid complexes in solution. Proton chemical shifts in 9-aminoacridine complexes with dG-dC, dC-dG, and dA-dT-dG-dC-dA-dT Biochemistry. 17: 2915-2919. DOI: 10.1021/bi00607a033  0.105
1978 Reuben J, Baker BM, Kallenbach NR. Structure of mutagen nucleic acid complexes in solution. Proton chemical shifts in 9-aminoacridine complexes with dG-dC, dC-dG, and dA-dT-dG-dC-dA-dT Biochemistry. 17: 2915-2919. DOI: 10.1021/bi00607a033  0.105
1978 Reuben J, Baker BM, Kallenbach NR. Structure of mutagen nucleic acid complexes in solution. Proton chemical shifts in 9-aminoacridine complexes with dG-dC, dC-dG, and dA-dT-dG-dC-dA-dT Biochemistry. 17: 2915-2919. DOI: 10.1021/bi00607a033  0.105
1978 Reuben J, Baker BM, Kallenbach NR. Structure of mutagen nucleic acid complexes in solution. Proton chemical shifts in 9-aminoacridine complexes with dG-dC, dC-dG, and dA-dT-dG-dC-dA-dT Biochemistry. 17: 2915-2919. DOI: 10.1021/bi00607a033  0.105
1978 Reuben J, Baker BM, Kallenbach NR. Structure of mutagen nucleic acid complexes in solution. Proton chemical shifts in 9-aminoacridine complexes with dG-dC, dC-dG, and dA-dT-dG-dC-dA-dT Biochemistry. 17: 2915-2919. DOI: 10.1021/bi00607a033  0.105
1978 Reuben J, Baker BM, Kallenbach NR. Structure of mutagen nucleic acid complexes in solution. Proton chemical shifts in 9-aminoacridine complexes with dG-dC, dC-dG, and dA-dT-dG-dC-dA-dT Biochemistry. 17: 2915-2919. DOI: 10.1021/bi00607a033  0.105
1978 Reuben J, Baker BM, Kallenbach NR. Structure of mutagen nucleic acid complexes in solution. Proton chemical shifts in 9-aminoacridine complexes with dG-dC, dC-dG, and dA-dT-dG-dC-dA-dT Biochemistry. 17: 2915-2919. DOI: 10.1021/bi00607a033  0.105
1978 Reuben J, Baker BM, Kallenbach NR. Structure of mutagen nucleic acid complexes in solution. Proton chemical shifts in 9-aminoacridine complexes with dG-dC, dC-dG, and dA-dT-dG-dC-dA-dT Biochemistry. 17: 2915-2919. DOI: 10.1021/bi00607a033  0.105
1978 Reuben J, Baker BM, Kallenbach NR. Structure of mutagen nucleic acid complexes in solution. Proton chemical shifts in 9-aminoacridine complexes with dG-dC, dC-dG, and dA-dT-dG-dC-dA-dT Biochemistry. 17: 2915-2919. DOI: 10.1021/bi00607a033  0.105
1978 Reuben J, Baker BM, Kallenbach NR. Structure of mutagen nucleic acid complexes in solution. Proton chemical shifts in 9-aminoacridine complexes with dG-dC, dC-dG, and dA-dT-dG-dC-dA-dT Biochemistry. 17: 2915-2919. DOI: 10.1021/bi00607a033  0.105
1978 Reuben J, Baker BM, Kallenbach NR. Structure of mutagen nucleic acid complexes in solution. Proton chemical shifts in 9-aminoacridine complexes with dG-dC, dC-dG, and dA-dT-dG-dC-dA-dT Biochemistry. 17: 2915-2919. DOI: 10.1021/bi00607a033  0.105
1978 Reuben J, Baker BM, Kallenbach NR. Structure of mutagen nucleic acid complexes in solution. Proton chemical shifts in 9-aminoacridine complexes with dG-dC, dC-dG, and dA-dT-dG-dC-dA-dT Biochemistry. 17: 2915-2919. DOI: 10.1021/bi00607a033  0.105
1978 Reuben J, Baker BM, Kallenbach NR. Structure of mutagen nucleic acid complexes in solution. Proton chemical shifts in 9-aminoacridine complexes with dG-dC, dC-dG, and dA-dT-dG-dC-dA-dT Biochemistry. 17: 2915-2919. DOI: 10.1021/bi00607a033  0.105
1978 Reuben J, Baker BM, Kallenbach NR. Structure of mutagen nucleic acid complexes in solution. Proton chemical shifts in 9-aminoacridine complexes with dG-dC, dC-dG, and dA-dT-dG-dC-dA-dT Biochemistry. 17: 2915-2919. DOI: 10.1021/bi00607a033  0.105
1978 Reuben J, Baker BM, Kallenbach NR. Structure of mutagen nucleic acid complexes in solution. Proton chemical shifts in 9-aminoacridine complexes with dG-dC, dC-dG, and dA-dT-dG-dC-dA-dT Biochemistry. 17: 2915-2919. DOI: 10.1021/bi00607a033  0.105
1978 Reuben J, Baker BM, Kallenbach NR. Structure of mutagen nucleic acid complexes in solution. Proton chemical shifts in 9-aminoacridine complexes with dG-dC, dC-dG, and dA-dT-dG-dC-dA-dT Biochemistry. 17: 2915-2919. DOI: 10.1021/bi00607a033  0.105
1978 Reuben J, Baker BM, Kallenbach NR. Structure of mutagen nucleic acid complexes in solution. Proton chemical shifts in 9-aminoacridine complexes with dG-dC, dC-dG, and dA-dT-dG-dC-dA-dT Biochemistry. 17: 2915-2919. DOI: 10.1021/bi00607a033  0.105
1978 Reuben J, Baker BM, Kallenbach NR. Structure of mutagen nucleic acid complexes in solution. Proton chemical shifts in 9-aminoacridine complexes with dG-dC, dC-dG, and dA-dT-dG-dC-dA-dT Biochemistry. 17: 2915-2919. DOI: 10.1021/bi00607a033  0.105
1978 Reuben J, Baker BM, Kallenbach NR. Structure of mutagen nucleic acid complexes in solution. Proton chemical shifts in 9-aminoacridine complexes with dG-dC, dC-dG, and dA-dT-dG-dC-dA-dT Biochemistry. 17: 2915-2919. DOI: 10.1021/bi00607a033  0.105
1978 Reuben J, Baker BM, Kallenbach NR. Structure of mutagen nucleic acid complexes in solution. Proton chemical shifts in 9-aminoacridine complexes with dG-dC, dC-dG, and dA-dT-dG-dC-dA-dT Biochemistry. 17: 2915-2919. DOI: 10.1021/bi00607a033  0.105
1978 Reuben J, Baker BM, Kallenbach NR. Structure of mutagen nucleic acid complexes in solution. Proton chemical shifts in 9-aminoacridine complexes with dG-dC, dC-dG, and dA-dT-dG-dC-dA-dT Biochemistry. 17: 2915-2919. DOI: 10.1021/bi00607a033  0.105
1978 Reuben J, Baker BM, Kallenbach NR. Structure of mutagen nucleic acid complexes in solution. Proton chemical shifts in 9-aminoacridine complexes with dG-dC, dC-dG, and dA-dT-dG-dC-dA-dT Biochemistry. 17: 2915-2919. DOI: 10.1021/bi00607a033  0.105
1978 Reuben J, Baker BM, Kallenbach NR. Structure of mutagen nucleic acid complexes in solution. Proton chemical shifts in 9-aminoacridine complexes with dG-dC, dC-dG, and dA-dT-dG-dC-dA-dT Biochemistry. 17: 2915-2919. DOI: 10.1021/bi00607a033  0.105
1978 Reuben J, Baker BM, Kallenbach NR. Structure of mutagen nucleic acid complexes in solution. Proton chemical shifts in 9-aminoacridine complexes with dG-dC, dC-dG, and dA-dT-dG-dC-dA-dT Biochemistry. 17: 2915-2919. DOI: 10.1021/bi00607a033  0.105
1978 Reuben J, Baker BM, Kallenbach NR. Structure of mutagen nucleic acid complexes in solution. Proton chemical shifts in 9-aminoacridine complexes with dG-dC, dC-dG, and dA-dT-dG-dC-dA-dT Biochemistry. 17: 2915-2919. DOI: 10.1021/bi00607a033  0.105
1978 Reuben J, Baker BM, Kallenbach NR. Structure of mutagen nucleic acid complexes in solution. Proton chemical shifts in 9-aminoacridine complexes with dG-dC, dC-dG, and dA-dT-dG-dC-dA-dT Biochemistry. 17: 2915-2919. DOI: 10.1021/bi00607a033  0.105
1978 Reuben J, Baker BM, Kallenbach NR. Structure of mutagen nucleic acid complexes in solution. Proton chemical shifts in 9-aminoacridine complexes with dG-dC, dC-dG, and dA-dT-dG-dC-dA-dT Biochemistry. 17: 2915-2919. DOI: 10.1021/bi00607a033  0.105
1981 Cohn M, Horowitz JH, Kallenbach NR. 19F NMR study of 5-fluorouridine w8 =tRNA substituted TRNA molecules in solution Federation Proceedings. 40: 619.  0.1
1977 Kallenbach NR, Berman HM. RNA structure Quarterly Reviews of Biophysics. 10: 138-236. PMID 333501  0.098
Hide low-probability matches.