Erik R. P. Zuiderweg - Publications

University of Michigan, Ann Arbor, Ann Arbor, MI 
NMR studies of Biomacromolecular Conformation, Dynamics and Interactions in Solution

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Year Citation  Score
2018 Taylor IR, Ahmad A, Wu T, Nordhues BA, Bhullar A, Gestwicki JE, Zuiderweg ERP. The disorderly conduct of Hsc70 and its interaction with the Alzheimer's related Tau protein. The Journal of Biological Chemistry. PMID 29764935 DOI: 10.1074/jbc.RA118.002234  0.48
2018 Taylor IR, Dunyak BM, Komiyama T, Shao H, Ran X, Assimon VA, Kalyanaraman C, Rauch JN, Jacobson MP, Zuiderweg ERP, Gestwicki JE. High Throughput Screen for Inhibitors of Protein-Protein Interactions in a Reconstituted Heat Shock Protein 70 (Hsp70) Complex. The Journal of Biological Chemistry. PMID 29414793 DOI: 10.1074/jbc.RA117.001575  0.48
2017 Cesa LC, Shao H, Srinivasan SR, Tse E, Jain C, Zuiderweg ERP, Southworth DR, Mapp AK, Gestwicki JE. X-Linked Inhibitor of Apoptosis Protein (XIAP) is a Client of Heat Shock Protein 70 (Hsp70) and a Biomarker of its Inhibition. The Journal of Biological Chemistry. PMID 29255093 DOI: 10.1074/jbc.RA117.000634  0.48
2017 Zuiderweg ER, Hightower LE, Gestwicki JE. The remarkable multivalency of the Hsp70 chaperones. Cell Stress & Chaperones. PMID 28220454 DOI: 10.1007/s12192-017-0776-y  0.48
2016 Zuiderweg ER, Gestwicki JE. Backbone and methyl resonance assignments of the 42 kDa human Hsc70 nucleotide binding domain in the ADP state. Biomolecular Nmr Assignments. PMID 27699616 DOI: 10.1007/s12104-016-9711-x  0.48
2016 Young ZT, Rauch JN, Assimon VA, Jinwal UK, Ahn M, Li X, Dunyak BM, Ahmad A, Carlson GA, Srinivasan SR, Zuiderweg ER, Dickey CA, Gestwicki JE. Stabilizing the Hsp70-Tau Complex Promotes Turnover in Models of Tauopathy. Cell Chemical Biology. PMID 27499529 DOI: 10.1016/j.chembiol.2016.04.014  0.68
2016 Rauch JN, Zuiderweg ER, Gestwicki JE. Non-Canonical Interactions Between Heat Shock Cognate Protein 70 (Hsc70) and Bcl2-Associated Anthanogene (BAG) Co-Chaperones Are Important for Client Release. The Journal of Biological Chemistry. PMID 27474739 DOI: 10.1074/jbc.M116.742502  0.48
2016 Morozova K, Clement CC, Kaushik S, Stiller B, Arias E, Ahmad A, Rauch JN, Chatterjee V, Melis C, Scharf B, Gestwicki JE, Cuervo AM, Zuiderweg ER, Santambrogio L. Hsc-70 Structural and Biological Interaction with Phosphatidylserine in Endosomal Microautophagy. The Journal of Biological Chemistry. PMID 27405763 DOI: 10.1074/jbc.M116.736744  0.48
2016 Stull FW, Bernard SM, Sapra A, Smith JL, Zuiderweg ER, Palfey BA. Deprotonations in the Reaction of Flavin-Dependent Thymidylate Synthase. Biochemistry. PMID 27214228 DOI: 10.1021/acs.biochem.6b00510  0.68
2015 Fontaine SN, Rauch JN, Nordhues BA, Assimon VA, Stothert AR, Jinwal UK, Sabbagh JJ, Chang L, Stevens SM, Zuiderweg ER, Gestwicki JE, Dickey CA. Isoform-selective Genetic Inhibition of Constitutive Cytosolic Hsp70 Activity Promotes Client Tau Degradation Using an Altered Co-chaperone Complement. The Journal of Biological Chemistry. 290: 13115-27. PMID 25864199 DOI: 10.1074/jbc.M115.637595  0.68
2015 Bagai I, Sarangi R, Fleischhacker AS, Sharma A, Hoffman BM, Zuiderweg ER, Ragsdale SW. Spectroscopic studies reveal that the heme regulatory motifs of heme oxygenase-2 are dynamically disordered and exhibit redox-dependent interaction with heme. Biochemistry. 54: 2693-708. PMID 25849895 DOI: 10.1021/bi501489r  0.68
2015 Plegaria JS, Dzul SP, Zuiderweg ER, Stemmler TL, Pecoraro VL. Apoprotein Structure and Metal Binding Characterization of a de Novo Designed Peptide, α3DIV, that Sequesters Toxic Heavy Metals. Biochemistry. 54: 2858-73. PMID 25790102 DOI: 10.1021/acs.biochem.5b00064  0.68
2014 Spencer AL, Bagai I, Becker DF, Zuiderweg ER, Ragsdale SW. Protein/protein interactions in the mammalian heme degradation pathway: heme oxygenase-2, cytochrome P450 reductase, and biliverdin reductase. The Journal of Biological Chemistry. 289: 29836-58. PMID 25196843 DOI: 10.1074/jbc.M114.582783  0.68
2014 Connarn JN, Assimon VA, Reed RA, Tse E, Southworth DR, Zuiderweg ER, Gestwicki JE, Sun D. The molecular chaperone Hsp70 activates protein phosphatase 5 (PP5) by binding the tetratricopeptide repeat (TPR) domain. The Journal of Biological Chemistry. 289: 2908-17. PMID 24327656 DOI: 10.1074/jbc.M113.519421  0.68
2013 Li X, Srinivasan SR, Connarn J, Ahmad A, Young ZT, Kabza AM, Zuiderweg ER, Sun D, Gestwicki JE. Analogs of the Allosteric Heat Shock Protein 70 (Hsp70) Inhibitor, MKT-077, as Anti-Cancer Agents. Acs Medicinal Chemistry Letters. 4. PMID 24312699 DOI: 10.1021/ml400204n  0.48
2013 Zuiderweg ER, Bagai I, Rossi P, Bertelsen EB. EZ-ASSIGN, a program for exhaustive NMR chemical shift assignments of large proteins from complete or incomplete triple-resonance data. Journal of Biomolecular Nmr. 57: 179-91. PMID 24022834 DOI: 10.1007/s10858-013-9778-y  0.68
2013 Smith MC, Scaglione KM, Assimon VA, Patury S, Thompson AD, Dickey CA, Southworth DR, Paulson HL, Gestwicki JE, Zuiderweg ER. The E3 ubiquitin ligase CHIP and the molecular chaperone Hsc70 form a dynamic, tethered complex. Biochemistry. 52: 5354-64. PMID 23865999 DOI: 10.1021/bi4009209  0.68
2013 Cesa LC, Patury S, Komiyama T, Ahmad A, Zuiderweg ER, Gestwicki JE. Inhibitors of difficult protein-protein interactions identified by high-throughput screening of multiprotein complexes. Acs Chemical Biology. 8: 1988-97. PMID 23819499 DOI: 10.1021/cb400356m  0.68
2013 Zuiderweg ER, Bertelsen EB, Rousaki A, Mayer MP, Gestwicki JE, Ahmad A. Allostery in the Hsp70 chaperone proteins. Topics in Current Chemistry. 328: 99-153. PMID 22576356 DOI: 10.1007/128_2012_323  0.56
2012 Chakraborty S, Iranzo O, Zuiderweg ER, Pecoraro VL. Experimental and theoretical evaluation of multisite cadmium(II) exchange in designed three-stranded coiled-coil peptides. Journal of the American Chemical Society. 134: 6191-203. PMID 22394049 DOI: 10.1021/ja210510g  0.68
2012 Zuiderweg ERP, Ahmad A. Reply to Sousa et al.: Evaluation of competing J domain:Hsp70 complex models in light of methods used Proceedings of the National Academy of Sciences of the United States of America. 109: E735. DOI: 10.1073/pnas.1121554109  0.48
2011 Ahmad A, Bhattacharya A, McDonald RA, Cordes M, Ellington B, Bertelsen EB, Zuiderweg ER. Heat shock protein 70 kDa chaperone/DnaJ cochaperone complex employs an unusual dynamic interface. Proceedings of the National Academy of Sciences of the United States of America. 108: 18966-71. PMID 22065753 DOI: 10.1073/pnas.1111220108  0.68
2011 Rousaki A, Miyata Y, Jinwal UK, Dickey CA, Gestwicki JE, Zuiderweg ER. Allosteric drugs: the interaction of antitumor compound MKT-077 with human Hsp70 chaperones. Journal of Molecular Biology. 411: 614-32. PMID 21708173 DOI: 10.1016/j.jmb.2011.06.003  0.68
2011 Chang L, Miyata Y, Ung PM, Bertelsen EB, McQuade TJ, Carlson HA, Zuiderweg ER, Gestwicki JE. Chemical screens against a reconstituted multiprotein complex: myricetin blocks DnaJ regulation of DnaK through an allosteric mechanism. Chemistry & Biology. 18: 210-21. PMID 21338918 DOI: 10.1016/j.chembiol.2010.12.010  0.68
2011 Bagai I, Ragsdale SW, Zuiderweg ER. Pseudo-4D triple resonance experiments to resolve HN overlap in the backbone assignment of unfolded proteins. Journal of Biomolecular Nmr. 49: 69-74. PMID 21190062 DOI: 10.1007/s10858-010-9465-1  0.68
2011 Zuiderweg ERP, Rousaki A. Gradient-enhanced TROSY described with Cartesian product operators Concepts in Magnetic Resonance Part a: Bridging Education and Research. 38: 280-288. DOI: 10.1002/cmr.a.20228  0.56
2010 Wisén S, Bertelsen EB, Thompson AD, Patury S, Ung P, Chang L, Evans CG, Walter GM, Wipf P, Carlson HA, Brodsky JL, Zuiderweg ER, Gestwicki JE. Binding of a small molecule at a protein-protein interface regulates the chaperone activity of hsp70-hsp40. Acs Chemical Biology. 5: 611-22. PMID 20481474 DOI: 10.1021/cb1000422  0.68
2010 Crippen GM, Rousaki A, Revington M, Zhang Y, Zuiderweg ER. SAGA: rapid automatic mainchain NMR assignment for large proteins. Journal of Biomolecular Nmr. 46: 281-98. PMID 20232231 DOI: 10.1007/s10858-010-9403-2  0.68
2010 Bhattacharya A, Revington M, Zuiderweg ER. Measurement and interpretation of 15N-1H residual dipolar couplings in larger proteins. Journal of Magnetic Resonance (San Diego, Calif. : 1997). 203: 11-28. PMID 20018538 DOI: 10.1016/j.jmr.2009.11.014  0.44
2009 Jinwal UK, Miyata Y, Koren J, Jones JR, Trotter JH, Chang L, O'Leary J, Morgan D, Lee DC, Shults CL, Rousaki A, Weeber EJ, Zuiderweg ER, Gestwicki JE, Dickey CA. Chemical manipulation of hsp70 ATPase activity regulates tau stability. The Journal of Neuroscience : the Official Journal of the Society For Neuroscience. 29: 12079-88. PMID 19793966 DOI: 10.1523/JNEUROSCI.3345-09.2009  0.68
2009 Weaver DS, Zuiderweg ER. Protein proton-proton dynamics from amide proton spin flip rates. Journal of Biomolecular Nmr. 45: 99-119. PMID 19636797 DOI: 10.1007/s10858-009-9351-x  0.68
2009 Bertelsen EB, Chang L, Gestwicki JE, Zuiderweg ER. Solution conformation of wild-type E. coli Hsp70 (DnaK) chaperone complexed with ADP and substrate. Proceedings of the National Academy of Sciences of the United States of America. 106: 8471-6. PMID 19439666 DOI: 10.1073/pnas.0903503106  0.48
2009 Bhattacharya A, Kurochkin AV, Yip GN, Zhang Y, Bertelsen EB, Zuiderweg ER. Allostery in Hsp70 chaperones is transduced by subdomain rotations. Journal of Molecular Biology. 388: 475-90. PMID 19361428 DOI: 10.1016/j.jmb.2009.01.062  0.68
2008 Weaver DS, Zuiderweg ER. Eta(z)/kappa: a transverse relaxation optimized spectroscopy NMR experiment measuring longitudinal relaxation interference. The Journal of Chemical Physics. 128: 155103. PMID 18433284 DOI: 10.1063/1.2889923  0.68
2008 Chang L, Bertelsen EB, Wisén S, Larsen EM, Zuiderweg ER, Gestwicki JE. High-throughput screen for small molecules that modulate the ATPase activity of the molecular chaperone DnaK. Analytical Biochemistry. 372: 167-76. PMID 17904512 DOI: 10.1016/j.ab.2007.08.020  0.48
2007 Jordan DM, Mills KM, Andricioaei I, Bhattacharya A, Palmo K, Zuiderweg ER. Parameterization of peptide 13C carbonyl chemical shielding anisotropy in molecular dynamics simulations. Chemphyschem : a European Journal of Chemical Physics and Physical Chemistry. 8: 1375-85. PMID 17526036 DOI: 10.1002/cphc.200700003  0.68
2006 Wang T, Weaver DS, Cai S, Zuiderweg ER. Quantifying Lipari-Szabo modelfree parameters from 13CO NMR relaxation experiments. Journal of Biomolecular Nmr. 36: 79-102. PMID 17013680 DOI: 10.1007/s10858-006-9047-4  0.68
2006 Garimella R, Liu X, Qiao W, Liang X, Zuiderweg ER, Riley MI, Van Doren SR. Hsc70 contacts helix III of the J domain from polyomavirus T antigens: addressing a dilemma in the chaperone hypothesis of how they release E2F from pRb. Biochemistry. 45: 6917-29. PMID 16734427 DOI: 10.1021/bi060411d  0.68
2005 Wang J, Wang T, Zuiderweg ER, Crippen GM. CASA: an efficient automated assignment of protein mainchain NMR data using an ordered tree search algorithm. Journal of Biomolecular Nmr. 33: 261-79. PMID 16341754 DOI: 10.1007/s10858-005-4079-8  0.68
2005 Deep S, Im SC, Zuiderweg ER, Waskell L. Characterization and calculation of a cytochrome c-cytochrome b5 complex using NMR data. Biochemistry. 44: 10654-68. PMID 16060674 DOI: 10.1021/bi050482x  0.68
2005 Yip GN, Zuiderweg ER. Improvement of duty-cycle heating compensation in NMR spin relaxation experiments. Journal of Magnetic Resonance (San Diego, Calif. : 1997). 176: 171-8. PMID 16009587 DOI: 10.1016/j.jmr.2005.06.003  1
2005 Revington M, Zhang Y, Yip GN, Kurochkin AV, Zuiderweg ER. NMR investigations of allosteric processes in a two-domain Thermus thermophilus Hsp70 molecular chaperone. Journal of Molecular Biology. 349: 163-83. PMID 15876376 DOI: 10.1016/j.jmb.2005.03.033  0.68
2005 Wang T, Frederick KK, Igumenova TI, Wand AJ, Zuiderweg ER. Changes in calmodulin main-chain dynamics upon ligand binding revealed by cross-correlated NMR relaxation measurements. Journal of the American Chemical Society. 127: 828-9. PMID 15656608 DOI: 10.1021/ja045743p  0.68
2004 Yip GN, Zuiderweg ER. A phase cycle scheme that significantly suppresses offset-dependent artifacts in the R2-CPMG 15N relaxation experiment. Journal of Magnetic Resonance (San Diego, Calif. : 1997). 171: 25-36. PMID 15504678 DOI: 10.1016/j.jmr.2004.06.021  1
2004 Revington M, Zuiderweg ER. TROSY-driven NMR backbone assignments of the 381-residue nucleotide-binding domain of the Thermus Thermophilus DnaK molecular chaperone. Journal of Biomolecular Nmr. 30: 113-4. PMID 15452445 DOI: 10.1023/B:JNMR.0000042961.48233.f9  0.44
2004 Zhang Y, Zuiderweg ER. The 70-kDa heat shock protein chaperone nucleotide-binding domain in solution unveiled as a molecular machine that can reorient its functional subdomains. Proceedings of the National Academy of Sciences of the United States of America. 101: 10272-7. PMID 15232009 DOI: 10.1073/pnas.0401313101  0.68
2004 Revington M, Holder TM, Zuiderweg ER. NMR study of nucleotide-induced changes in the nucleotide binding domain of Thermus thermophilus Hsp70 chaperone DnaK: implications for the allosteric mechanism. The Journal of Biological Chemistry. 279: 33958-67. PMID 15175340 DOI: 10.1074/jbc.M313967200  0.68
2003 Kern D, Zuiderweg ER. The role of dynamics in allosteric regulation. Current Opinion in Structural Biology. 13: 748-57. PMID 14675554 DOI: 10.1016/  0.68
2003 Shao W, Im SC, Zuiderweg ER, Waskell L. Mapping the binding interface of the cytochrome b5-cytochrome c complex by nuclear magnetic resonance. Biochemistry. 42: 14774-84. PMID 14674751 DOI: 10.1021/bi030145t  0.68
2003 Stevens SY, Cai S, Pellecchia M, Zuiderweg ER. The solution structure of the bacterial HSP70 chaperone protein domain DnaK(393-507) in complex with the peptide NRLLLTG. Protein Science : a Publication of the Protein Society. 12: 2588-96. PMID 14573869 DOI: 10.1110/ps.03269103  0.32
2003 Huber-Lang MS, Sarma JV, McGuire SR, Lu KT, Padgaonkar VA, Younkin EM, Guo RF, Weber CH, Zuiderweg ER, Zetoune FS, Ward PA. Structure-function relationships of human C5a and C5aR. Journal of Immunology (Baltimore, Md. : 1950). 170: 6115-24. PMID 12794141  0.68
2002 Khandelwal P, Keliikuli K, Smith CL, Saper MA, Zuiderweg ER. Solution structure and phosphopeptide binding to the N-terminal domain of Yersinia YopH: comparison with a crystal structure. Biochemistry. 41: 11425-37. PMID 12234185 DOI: 10.1021/bi026333l  0.68
2002 Chung DA, Zuiderweg ER, Fowler CB, Soyer OS, Mosberg HI, Neubig RR. NMR structure of the second intracellular loop of the alpha 2A adrenergic receptor: evidence for a novel cytoplasmic helix. Biochemistry. 41: 3596-604. PMID 11888275 DOI: 10.1021/bi015811+  0.68
2002 Pang Y, Buck M, Zuiderweg ER. Backbone dynamics of the ribonuclease binase active site area using multinuclear ((15)N and (13)CO) NMR relaxation and computational molecular dynamics. Biochemistry. 41: 2655-66. PMID 11851412 DOI: 10.1021/bi011657f  0.68
2001 Smith CL, Khandelwal P, Keliikuli K, Zuiderweg ER, Saper MA. Structure of the type III secretion and substrate-binding domain of Yersinia YopH phosphatase. Molecular Microbiology. 42: 967-79. PMID 11737640 DOI: 10.1046/j.0950-382X.2001.02711.x  0.68
2001 Khandelwal P, Keliikuli K, Smit CL, Saper MA, Zuiderweg ER. 1H, 15N and 13C assignments of the N-terminal domain of Yersinia outer protein H in its apo form and in complex with a phosphotyrosine peptide. Journal of Biomolecular Nmr. 21: 69-70. PMID 11693571 DOI: 10.1023/A:1011971202626  0.68
2001 Hall DA, Vander Kooi CW, Stasik CN, Stevens SY, Zuiderweg ER, Matthews RG. Mapping the interactions between flavodoxin and its physiological partners flavodoxin reductase and cobalamin-dependent methionine synthase. Proceedings of the National Academy of Sciences of the United States of America. 98: 9521-6. PMID 11493691 DOI: 10.1073/pnas.171168898  0.68
2001 Wang L, Pang Y, Holder T, Brender JR, Kurochkin AV, Zuiderweg ER. Functional dynamics in the active site of the ribonuclease binase. Proceedings of the National Academy of Sciences of the United States of America. 98: 7684-9. PMID 11438724 DOI: 10.1073/pnas.121069998  0.68
2000 Wang L, Kurochkin AV, Zuiderweg ER. An iterative fitting procedure for the determination of longitudinal NMR cross-correlation rates. Journal of Magnetic Resonance (San Diego, Calif. : 1997). 144: 175-85. PMID 10783290 DOI: 10.1006/jmre.2000.2064  0.36
2000 Pellecchia M, Montgomery DL, Stevens SY, Vander Kooi CW, Feng HP, Gierasch LM, Zuiderweg ER. Structural insights into substrate binding by the molecular chaperone DnaK. Nature Structural Biology. 7: 298-303. PMID 10742174 DOI: 10.1038/74062  0.68
2000 Pellecchia M, Vander Kooi CW, Keliikuli K, Zuiderweg ER. Magnetization transfer via residual dipolar couplings: application to proton-proton correlations in partially aligned proteins. Journal of Magnetic Resonance (San Diego, Calif. : 1997). 143: 435-9. PMID 10729274 DOI: 10.1006/jmre.2000.2058  0.68
2000 Pang Y, Zuiderweg ERP. Determination of protein backbone 13CO chemical shift anisotropy tensors in solution Journal of the American Chemical Society. 122: 4841-4842. DOI: 10.1021/ja994184x  0.68
1999 Vander Kooi CW, Kupce E, Zuiderweg ER, Pellecchia M. Line narrowing in spectra of proteins dissolved in a dilute liquid crystalline phase by band-selective adiabatic decoupling: application to 1HN-15N residual dipolar coupling measurements. Journal of Biomolecular Nmr. 15: 335-8. PMID 10685341 DOI: 10.1023/A:1008387305293  0.68
1999 Stevens SY, Hu W, Gladysheva T, Rosen BP, Zuiderweg ER, Lee L. Secondary structure and fold homology of the ArsC protein from the Escherichia coli arsenic resistance plasmid R773. Biochemistry. 38: 10178-86. PMID 10433726 DOI: 10.1021/bi990333c  0.68
1999 Morshauser RC, Hu W, Wang H, Pang Y, Flynn GC, Zuiderweg ER. High-resolution solution structure of the 18 kDa substrate-binding domain of the mammalian chaperone protein Hsc70. Journal of Molecular Biology. 289: 1387-403. PMID 10373374 DOI: 10.1006/jmbi.1999.2776  0.68
1999 Pang Y, Wang L, Pellecchia M, Kurochkin AV, Zuiderweg ERP. Evidence for extensive anisotropic local motions in a small enzyme using a new method to determine NMR cross-correlated relaxation rates in the absence of resolved scalar coupling Journal of Biomolecular Nmr. 14: 297-306. DOI: 10.1023/A:1008358716358  0.68
1999 Pellecchia M, Pang Y, Wang L, Kurochkin AV, Kumar A, Zuiderweg ERP. Quantitative measurement of cross-correlations between 15N and 13CO chemical shift anisotropy relaxation mechanisms by multiple quantum NMR Journal of the American Chemical Society. 121: 9165-9170. DOI: 10.1021/ja991155d  0.68
1998 Pang Y, Zeng L, Kurochkin AV, Zuiderweg ER. High-resolution detection of five frequencies in a single 3D spectrum: HNHCACO--a bidirectional coherence transfer experiment. Journal of Biomolecular Nmr. 11: 185-90. PMID 9679293  0.68
1998 Fischer MW, Zeng L, Majumdar A, Zuiderweg ER. Characterizing semilocal motions in proteins by NMR relaxation studies. Proceedings of the National Academy of Sciences of the United States of America. 95: 8016-9. PMID 9653132 DOI: 10.1073/pnas.95.14.8016  0.36
1998 Wang H, Kurochkin AV, Pang Y, Hu W, Flynn GC, Zuiderweg ER. NMR solution structure of the 21 kDa chaperone protein DnaK substrate binding domain: a preview of chaperone-protein interaction. Biochemistry. 37: 7929-40. PMID 9609686 DOI: 10.1021/bi9800855  0.68
1998 Ziehler WA, Yang J, Kurochkin AV, Sandusky PO, Zuiderweg ER, Engelke DR. Structural analysis of the P10/11-P12 RNA domain of yeast RNase P RNA and its interaction with magnesium. Biochemistry. 37: 3549-57. PMID 9521676 DOI: 10.1021/bi972886y  0.68
1997 Buchler NE, Zuiderweg ER, Wang H, Goldstein RA. Protein heteronuclear NMR assignments using mean-field simulated annealing. Journal of Magnetic Resonance (San Diego, Calif. : 1997). 125: 34-42. PMID 9245358 DOI: 10.1006/jmre.1997.1106  0.68
1997 Fischer MWF, Zeng L, Pang Y, Hu W, Majumdar A, Zuiderweg ERP. Experimental characterization of models for backbone picosecond dynamics in proteins. Quantification of NMR auto- and cross-correlation relaxation mechanisms involving different nuclei of the peptide plane Journal of the American Chemical Society. 119: 12629-12642. DOI: 10.1021/ja972083y  0.68
1996 Zuiderweg ER, Zeng L, Brutscher B, Morshauser RC. Band-selective hetero- and homonuclear cross-polarization using trains of shaped pulses. Journal of Biomolecular Nmr. 8: 147-60. PMID 22911139 DOI: 10.1007/BF00211161  0.36
1996 Zeng L, Fischer MW, Zuiderweg ER. Study of protein dynamics in solution by measurement of (13)C (α)- (13)CO NOE and (13)CO longitudinal relaxation. Journal of Biomolecular Nmr. 7: 157-62. PMID 22911008 DOI: 10.1007/BF00203826  0.36
1996 Cain RJ, Glick GD, Zuiderweg ER. Extracting quantitative information from two- and three-dimensional NOE spectra measured with short recycle delays. Journal of Magnetic Resonance. Series B. 113: 252-5. PMID 8995844  0.68
1996 Fischer MWF, Zeng L, Zuiderweg ERP. Use of13C-13C NOE for the assignment of NMR lines of larger labeled proteins at larger magnetic fields Journal of the American Chemical Society. 118: 12457-12458.  0.36
1996 Zeng L, Fischer MWF, Zuiderweg ERP. Study of protein dynamics in solution by measurement of 13Cα-13CO NOE and 13CO longitudinal relaxation Journal of Biomolecular Nmr. 7: 157-162.  0.36
1995 Van Doren SR, Kurochkin AV, Hu W, Ye QZ, Johnson LL, Hupe DJ, Zuiderweg ER. Solution structure of the catalytic domain of human stromelysin complexed with a hydrophobic inhibitor. Protein Science : a Publication of the Protein Society. 4: 2487-98. PMID 8580839 DOI: 10.1002/pro.5560041205  0.68
1995 Sandusky P, Wooten EW, Kurochkin AV, Kavanaugh T, Mandecki W, Zuiderweg ER. Occurrence, solution structure and stability of DNA hairpins stabilized by a GA/CG helix unit. Nucleic Acids Research. 23: 4717-25. PMID 8524666  0.36
1995 Fischer MW, Majumdar A, Dahlquist FW, Zuiderweg ER. 15N, 13C, and 1H NMR assignments and secondary structure for T4-lysozyme. Journal of Magnetic Resonance. Series B. 108: 143-54. PMID 7648012 DOI: 10.1006/jmrb.1995.1115  0.68
1995 Cain RJ, Zuiderweg ER, Glick GD. Solution structure of a DNA hairpin and its disulfide cross-linked analog. Nucleic Acids Research. 23: 2153-60. PMID 7610043 DOI: 10.1093/nar/23.12.2153  0.68
1995 Wang H, Zuiderweg ERP, Glick GD. Solution structure of a disulfide cross-linked DNA hairpin Journal of the American Chemical Society. 117: 2981-2991.  0.68
1994 Zuiderweg ERP, Van Doren SR. Modern multidimensional protein NMR spectroscopy. I. Resonance assignment methods Trends in Analytical Chemistry. 13: 24-36. DOI: 10.1016/0165-9936(94)85056-9  0.68
1994 Wang H, Osborne SE, Zuiderweg ERP, Glick GD. Three-dimensional structure of a disulfide-stabilized non-ground-state DNA hairpin Journal of the American Chemical Society. 116: 5021-5022.  0.68
1993 Van Doren SR, Kurochkin AV, Ye QZ, Johnson LL, Hupe DJ, Zuiderweg ER. Assignments for the main-chain nuclear magnetic resonances and delineation of the secondary structure of the catalytic domain of human stromelysin-1 as obtained from triple-resonance 3D NMR experiments. Biochemistry. 32: 13109-22. PMID 8241165 DOI: 10.1021/bi00211a021  0.68
1993 Zuiderweg ERP, van Doren SR, Kurochkin AV, Neubig RR, Majumdar A. Modern NMR spectroscopy of proteins and peptides in solution and its relevance to drug design Perspectives in Drug Discovery and Design. 1: 391-417. DOI: 10.1007/BF02174537  0.68
1993 Wang H, Glick GD, Zuiderweg ERP. A Three-Dimensional Method for the Separation of Zero-Quantum Coherence and NOE in NOESY Spectra Journal of Magnetic Resonance, Series A. 102: 116-121. DOI: 10.1006/jmra.1993.1078  0.68
1991 Buko AM, Kentzer EJ, Petros A, Menon G, Zuiderweg ER, Sarin VK. Characterization of a posttranslational fucosylation in the growth factor domain of urinary plasminogen activator. Proceedings of the National Academy of Sciences of the United States of America. 88: 3992-6. PMID 2023947  0.68
1989 Greer J, Mollison KW, Carter GW, Zuiderweg ER. Comparative modeling of proteins in the complement pathway. Progress in Clinical and Biological Research. 289: 385-97. PMID 2786214  0.68
1988 Nettesheim DG, Edalji RP, Mollison KW, Greer J, Zuiderweg ER. Secondary structure of complement component C3a anaphylatoxin in solution as determined by NMR spectroscopy: differences between crystal and solution conformations. Proceedings of the National Academy of Sciences of the United States of America. 85: 5036-40. PMID 3260670  0.68
1985 Zuiderweg ER, Scheek RM, Kaptein R. Two-dimensional 1H-nmr studies on the lac repressor DNA binding domain: further resonance assignments and identification of nuclear Overhauser enhancements. Biopolymers. 24: 2257-77. PMID 3912012 DOI: 10.1002/bip.360241208  0.72
1985 Zuiderweg ER, Scheek RM, Boelens R, van Gunsteren WF, Kaptein R. Determination of protein structures from nuclear magnetic resonance data using a restrained molecular dynamics approach: the lac repressor DNA binding domain. Biochimie. 67: 707-15. PMID 3910108  0.72
1985 Kaptein R, Zuiderweg ER, Scheek RM, Boelens R, van Gunsteren WF. A protein structure from nuclear magnetic resonance data. lac repressor headpiece. Journal of Molecular Biology. 182: 179-82. PMID 3889346  0.72
1984 Zuiderweg ER, Billeter M, Boelens R, Scheek RM, Wüthrich K, Kaptein R. Spatial arrangement of the three alpha helices in the solution conformation of E. coli lac repressor DNA-binding domain. Febs Letters. 174: 243-7. PMID 6381097  0.72
1983 Zuiderweg ER, Kaptein R, Wüthrich K. Sequence-specific resonance assignments in the 1H nuclear-magnetic-resonance spectrum of the lac repressor DNA-binding domain 1-51 from Escherichia coli by two-dimensional spectroscopy. European Journal of Biochemistry / Febs. 137: 279-92. PMID 6360686  0.68
1983 Zuiderweg ER, Kaptein R, Wüthrich K. Secondary structure of the lac repressor DNA-binding domain by two-dimensional 1H nuclear magnetic resonance in solution. Proceedings of the National Academy of Sciences of the United States of America. 80: 5837-41. PMID 6351066  0.68
1983 Scheek RM, Zuiderweg ER, Klappe KJ, van Boom JH, Kaptein R, Rüterjans H, Beyreuther K. lac Repressor headpiece binds specifically to half of the lac operator: a proton nuclear magnetic resonance study. Biochemistry. 22: 228-35. PMID 6338916 DOI: 10.1021/BI00270A033  0.72
1983 Wagner G, Zuiderweg ER. Two-dimensional double quantum 1H NMR spectroscopy of proteins. Biochemical and Biophysical Research Communications. 113: 854-60. PMID 6307305  0.88
1981 Zuiderweg ER, Scheek RM, Veeneman G, van Boom JH, Kaptein R, Rüterjans H, Beyreuther K. 1H NMR studies of lac-operator DNA fragments. Nucleic Acids Research. 9: 6553-69. PMID 7322923 DOI: 10.1093/NAR/9.23.6553  0.72
1981 Zuiderweg ER, Hamers LF, Rollema HS, de Bruin SH, Hilbers CW. 31P NMR study of the kinetics of binding of myo-inositol hexakisphosphate to human hemoglobin. Observation of fast-exchange kinetics in high-affinity systems. European Journal of Biochemistry / Febs. 118: 95-104. PMID 7285916  0.64
1981 Zuiderweg ER, Hamers LF, de Bruin SH, Hilbers CW. Equilibrium aspects of the binding of myo-inositol hexakisphosphate to human hemoglobin as studied by 31P NMR and pH-stat techniques. European Journal of Biochemistry / Febs. 118: 85-94. PMID 7285915  0.68
1979 van Beek GG, Zuiderweg ER, de Bruin SH. The binding of chloride ions to ligated and unligated human hemoglobin and its influence on the Bohr effect. European Journal of Biochemistry / Febs. 99: 379-83. PMID 40792  0.64
1979 Zuiderweg ER, van Beek GG, de Bruin SH. The influence of electrostatic interaction on the proton-binding behaviour of myo-inositol hexakisphosphate. European Journal of Biochemistry / Febs. 94: 297-306. PMID 35351  0.68
1978 Van Beek GG, Zuiderweg ER, De Bruin SH. The binding of protons and inositol hexakisphosphate to ligated and unligated human des-Arg141alpha-hemoglobin. European Journal of Biochemistry / Febs. 92: 309-16. PMID 32039  0.64
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