| Year |
Citation |
Score |
| 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 |
0.401 |
|
| 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 |
0.518 |
|
| 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 |
0.418 |
|
| 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 |
0.444 |
|
| 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 |
0.422 |
|
| 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 |
0.376 |
|
| 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 |
0.404 |
|
| 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 |
0.401 |
|
| 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 |
0.358 |
|
| 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 |
0.388 |
|
| 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 |
0.498 |
|
| 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 |
0.379 |
|
| 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 |
0.381 |
|
| 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 |
0.449 |
|
| 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 |
0.401 |
|
| 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 |
0.786 |
|
| 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 |
0.334 |
|
| 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 |
0.625 |
|
| 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 |
0.781 |
|
| 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 |
0.409 |
|
| 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 |
0.486 |
|
| 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 |
0.771 |
|
| 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 |
0.563 |
|
| 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 |
0.756 |
|
| 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 |
0.312 |
|
| 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 |
0.511 |
|
| 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 |
0.791 |
|
| 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 |
0.397 |
|
| 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 |
0.417 |
|
| 2008 |
Bhattacharya A, Kurochkin A, Yip G, Bertelsen E, Zuiderweg E. Structural basis of the allosteric trigger of the Hsp70 chaperone proteins. Nature Precedings. 1-1. DOI: 10.1038/Npre.2008.1978.1 |
0.795 |
|
| 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 |
0.517 |
|
| 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 |
0.318 |
|
| 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 |
0.388 |
|
| 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 |
0.403 |
|
| 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 |
0.665 |
|
| 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 |
0.75 |
|
| 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 |
0.783 |
|
| 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 |
0.379 |
|
| 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 |
0.738 |
|
| 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 |
0.522 |
|
| 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 |
0.511 |
|
| 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 |
0.475 |
|
| 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 |
0.353 |
|
| 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 |
0.414 |
|
| 2003 |
Cai S, Stevens SY, Budor AP, Zuiderweg ER. Solvent interaction of a Hsp70 chaperone substrate-binding domain investigated with water-NOE NMR experiments. Biochemistry. 42: 11100-8. PMID 14503860 DOI: 10.1021/bi030097c |
0.485 |
|
| 2003 |
Wang T, Cai S, Zuiderweg ER. Temperature dependence of anisotropic protein backbone dynamics. Journal of the American Chemical Society. 125: 8639-43. PMID 12848571 DOI: 10.1021/ja034077+ |
0.348 |
|
| 2003 |
Hinton A, Zuiderweg ER, Ackerman SH. A purified subfragment of yeast Atp11p retains full molecular chaperone activity. The Journal of Biological Chemistry. 278: 34110-3. PMID 12829692 DOI: 10.1074/Jbc.M305353200 |
0.41 |
|
| 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 |
0.452 |
|
| 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+ |
0.334 |
|
| 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 |
0.6 |
|
| 2002 |
Zuiderweg ER. Mapping protein-protein interactions in solution by NMR spectroscopy. Biochemistry. 41: 1-7. PMID 11771996 DOI: 10.1021/bi011870b |
0.4 |
|
| 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 |
0.468 |
|
| 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 |
0.394 |
|
| 2001 |
Stevens SY, Sanker S, Kent C, Zuiderweg ER. Delineation of the allosteric mechanism of a cytidylyltransferase exhibiting negative cooperativity. Nature Structural Biology. 8: 947-52. PMID 11685240 DOI: 10.1038/Nsb1101-947 |
0.432 |
|
| 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 |
0.428 |
|
| 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 |
0.618 |
|
| 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 |
0.308 |
|
| 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 |
0.489 |
|
| 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 |
0.42 |
|
| 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 |
0.38 |
|
| 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 |
0.394 |
|
| 1999 |
Morshauser RC, Zuiderweg ER. High-resolution four-dimensional HMQC-NOESY-HSQC spectroscopy. Journal of Magnetic Resonance (San Diego, Calif. : 1997). 139: 232-9. PMID 10423360 DOI: 10.1006/jmre.1999.1802 |
0.346 |
|
| 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 |
0.689 |
|
| 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 DOI: 10.1023/A:1008229723544 |
0.574 |
|
| 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 |
0.372 |
|
| 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 |
0.701 |
|
| 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 |
0.323 |
|
| 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 |
0.361 |
|
| 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 |
0.335 |
|
| 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 |
0.395 |
|
| 1995 |
Morshauser RC, Wang H, Flynn GC, Zuiderweg ER. The peptide-binding domain of the chaperone protein Hsc70 has an unusual secondary structure topology. Biochemistry. 34: 6261-6. PMID 7756251 DOI: 10.1021/Bi00019A001 |
0.449 |
|
| 1995 |
Wang H, Zuiderweg ER. HCCH-TOCSY spectroscopy of 13C-labeled proteins in H2O using heteronuclear cross-polarization and pulsed-field gradients. Journal of Biomolecular Nmr. 5: 207-11. PMID 7703702 DOI: 10.1007/BF00208812 |
0.325 |
|
| 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 |
0.343 |
|
| 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 |
0.335 |
|
| 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 |
0.38 |
|
| 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 DOI: 10.1073/Pnas.88.9.3992 |
0.373 |
|
| 1990 |
Fesik SW, Zuiderweg ER, Olejniczak ET, Gampe RT. NMR methods for determining the structures of enzyme/inhibitor complexes as an aid in drug design. Biochemical Pharmacology. 40: 161-7. PMID 2115336 DOI: 10.1016/0006-2952(90)90191-M |
0.352 |
|
| 1989 |
Zuiderweg ER, Nettesheim DG, Mollison KW, Carter GW. Tertiary structure of human complement component C5a in solution from nuclear magnetic resonance data. Biochemistry. 28: 172-85. PMID 2784981 DOI: 10.1021/Bi00427A025 |
0.321 |
|
| 1989 |
Zuiderweg ER, Fesik SW. Heteronuclear three-dimensional NMR spectroscopy of the inflammatory protein C5a. Biochemistry. 28: 2387-91. PMID 2730871 DOI: 10.1021/Bi00432A008 |
0.349 |
|
| 1989 |
Fesik SW, Gampe RT, Zuiderweg ER, Kohlbrenner WE, Weigl D. Heteronuclear three-dimensional NMR spectroscopy applied to CMP-KDO synthetase (27.5 kD). Biochemical and Biophysical Research Communications. 159: 842-7. PMID 2539129 DOI: 10.1016/0006-291X(89)90071-5 |
0.319 |
|
| 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 |
0.536 |
|
| 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 DOI: 10.1016/S0300-9084(85)80158-9 |
0.647 |
|
| 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 DOI: 10.1016/0022-2836(85)90036-1 |
0.633 |
|
| 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 DOI: 10.1016/0014-5793(84)81166-7 |
0.683 |
|
| 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 DOI: 10.1111/J.1432-1033.1983.Tb07827.X |
0.605 |
|
| 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 DOI: 10.1073/Pnas.80.19.5837 |
0.633 |
|
| 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 |
0.533 |
|
| 1983 |
Wagner G, Zuiderweg ER. Two-dimensional double quantum 1H NMR spectroscopy of proteins. Biochemical and Biophysical Research Communications. 113: 854-60. PMID 6307305 DOI: 10.1016/0006-291X(83)91077-X |
0.395 |
|
| 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 |
0.426 |
|
| 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 |
0.561 |
|
| 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 DOI: 10.1111/J.1432-1033.1981.Tb05489.X |
0.522 |
|
| Show low-probability matches. |
