| Year |
Citation |
Score |
| 2019 |
Panova S, Cliff MJ, Macek P, Blackledge M, Jensen MR, Nissink JWM, Embrey KJ, Davies R, Waltho JP. Mapping Hidden Residual Structure within the Myc bHLH-LZ Domain Using Chemical Denaturant Titration. Structure (London, England : 1993). PMID 31402220 DOI: 10.1016/J.Str.2019.07.006 |
0.399 |
|
| 2019 |
Cruz-Navarrete FA, Baxter NJ, Wood HP, Hounslow AM, Waltho JP. H, N and C backbone resonance assignments of the P146A variant of β-phosphoglucomutase from Lactococcus lactis in its substrate-free form. Biomolecular Nmr Assignments. PMID 31396843 DOI: 10.1007/S12104-019-09904-Y |
0.406 |
|
| 2019 |
Czarnota S, Johannissen LO, Baxter NJ, Rummel F, Wilson AL, Cliff MJ, Levy CW, Scrutton NS, Waltho JP, Hay S. Equatorial Active Site Compaction and Electrostatic Reorganization in Catechol--methyltransferase. Acs Catalysis. 9: 4394-4401. PMID 31080692 DOI: 10.1021/Acscatal.9B00174 |
0.396 |
|
| 2019 |
Iorgu AI, Cliff MJ, Waltho JP, Scrutton NS, Hay S. Isotopically labeled flavoenzymes and their uses in probing reaction mechanisms. Methods in Enzymology. 620: 145-166. PMID 31072485 DOI: 10.1016/Bs.Mie.2019.03.009 |
0.343 |
|
| 2018 |
Iorgu AI, Baxter NJ, Cliff MJ, Levy C, Waltho JP, Hay S, Scrutton NS. Nonequivalence of Second Sphere "Noncatalytic" Residues in Pentaerythritol Tetranitrate Reductase in Relation to Local Dynamics Linked to H-Transfer in Reactions with NADH and NADPH Coenzymes. Acs Catalysis. 8: 11589-11599. PMID 31119061 DOI: 10.1021/Acscatal.8B02810 |
0.377 |
|
| 2018 |
Bennet IA, Finger LD, Baxter NJ, Ambrose B, Hounslow AM, Thompson MJ, Exell JC, Shahari NNBM, Craggs TD, Waltho JP, Grasby JA. Regional conformational flexibility couples substrate specificity and scissile phosphate diester selectivity in human flap endonuclease 1. Nucleic Acids Research. PMID 29718417 DOI: 10.1093/Nar/Gky293 |
0.324 |
|
| 2018 |
Macek P, Cliff MJ, Embrey KJ, Holdgate GA, Nissink JWM, Panova S, Waltho JP, Davies RA. Myc Phosphorylation in its Basic Helix-Loop-Helix Region Destabilizes Transient α-Helical Structures, Disrupting Max and DNA Binding. The Journal of Biological Chemistry. PMID 29695509 DOI: 10.1074/Jbc.Ra118.002709 |
0.36 |
|
| 2018 |
Johnson LA, Robertson AJ, Baxter NJ, Trevitt CR, Bisson C, Jin Y, Wood HP, Hounslow AM, Cliff MJ, Blackburn GM, Bowler MW, Waltho JP. van der Waals Contact between Nucleophile and Transferring Phosphorus Is Insufficient To Achieve Enzyme Transition-State Architecture Acs Catalysis. 8: 8140-8153. DOI: 10.1021/Acscatal.8B01612 |
0.606 |
|
| 2017 |
Iorgu AI, Baxter NJ, Cliff MJ, Waltho JP, Hay S, Scrutton NS. (1)H, (15)N and (13)C backbone resonance assignments of pentaerythritol tetranitrate reductase from Enterobacter cloacae PB2. Biomolecular Nmr Assignments. PMID 29168057 DOI: 10.1007/S12104-017-9791-2 |
0.375 |
|
| 2017 |
Serimbetov Z, Baxter NJ, Cliff MJ, Waltho JP. (1)H, (15)N, (13)C backbone resonance assignments of human phosphoglycerate kinase in a transition state analogue complex with ADP, 3-phosphoglycerate and magnesium trifluoride. Biomolecular Nmr Assignments. PMID 28866776 DOI: 10.1007/S12104-017-9758-3 |
0.451 |
|
| 2017 |
Jin Y, Molt RW, Pellegrini E, Cliff MJ, Bowler MW, Richards NGJ, Blackburn GM, Waltho JP. Assessing the Influence of Mutation on GTPase Transition States by Using X-ray Crystallography, (19) F NMR, and DFT Approaches. Angewandte Chemie (International Ed. in English). 56: 9732-9735. PMID 28498638 DOI: 10.1002/Anie.201703074 |
0.591 |
|
| 2017 |
Jin Y, Richards NG, Waltho JP, Blackburn GM. Metal Fluorides as Analogues for Studies on Phosphoryl Transfer Enzymes. Angewandte Chemie (International Ed. in English). 56: 4110-4128. PMID 27862756 DOI: 10.1002/Anie.201606474 |
0.644 |
|
| 2017 |
Blackburn GM, Cherfils J, Moss GP, Richards NGJ, Waltho JP, Williams NH, Wittinghofer A. How to name atoms in phosphates, polyphosphates, their derivatives and mimics, and transition state analogues for enzyme-catalysed phosphoryl transfer reactions (IUPAC Recommendations 2016) Pure and Applied Chemistry. 89: 653-675. DOI: 10.1515/Pac-2016-0202 |
0.571 |
|
| 2017 |
Jin Y, Richards NG, Waltho JP, Blackburn GM. Metallfluoride als Analoga für Studien an Phosphoryltransferenzymen Angewandte Chemie. 129: 4172-4192. DOI: 10.1002/Ange.201606474 |
0.491 |
|
| 2016 |
Czarnota S, Baxter NJ, Cliff MJ, Waltho JP, Scrutton NS, Hay S. (1)H, (15)N, (13)C backbone resonance assignments of human soluble catechol O-methyltransferase in complex with S-adenosyl-L-methionine and 3,5-dinitrocatechol. Biomolecular Nmr Assignments. PMID 27981425 DOI: 10.1007/S12104-016-9720-9 |
0.337 |
|
| 2016 |
Jin Y, Molt RW, Waltho JP, Richards NG, Blackburn GM. (19)F NMR and DFT Analysis Reveal Structural and Electronic Transition State Features for RhoA-Catalyzed GTP Hydrolysis. Angewandte Chemie (International Ed. in English). 55: 3318-22. PMID 26822702 DOI: 10.1002/Anie.201509477 |
0.611 |
|
| 2015 |
Davis PJ, Holmes D, Waltho JP, Staniforth RA. Limited Proteolysis Reveals That Amyloids from the 3D Domain-Swapping Cystatin B Have a Non-Native β-Sheet Topology. Journal of Molecular Biology. PMID 26004542 DOI: 10.1016/J.Jmb.2015.05.014 |
0.354 |
|
| 2015 |
Kiraly P, Adams RW, Paudel L, Foroozandeh M, Aguilar JA, Timári I, Cliff MJ, Nilsson M, Sándor P, Batta G, Waltho JP, Kövér KE, Morris GA. Real-time pure shift ¹⁵N HSQC of proteins: a real improvement in resolution and sensitivity. Journal of Biomolecular Nmr. 62: 43-52. PMID 25737243 DOI: 10.1007/S10858-015-9913-Z |
0.317 |
|
| 2014 |
Jin Y, Bhattasali D, Pellegrini E, Forget SM, Baxter NJ, Cliff MJ, Bowler MW, Jakeman DL, Blackburn GM, Waltho JP. α-Fluorophosphonates reveal how a phosphomutase conserves transition state conformation over hexose recognition in its two-step reaction. Proceedings of the National Academy of Sciences of the United States of America. 111: 12384-9. PMID 25104750 DOI: 10.1073/Pnas.1402850111 |
0.62 |
|
| 2014 |
Trevitt CR, Hosszu LL, Batchelor M, Panico S, Terry C, Nicoll AJ, Risse E, Taylor WA, Sandberg MK, Al-Doujaily H, Linehan JM, Saibil HR, Scott DJ, Collinge J, Waltho JP, et al. N-terminal domain of prion protein directs its oligomeric association. The Journal of Biological Chemistry. 289: 25497-508. PMID 25074940 DOI: 10.1074/Jbc.M114.566588 |
0.36 |
|
| 2014 |
Krishnan R, Tsubery H, Proschitsky MY, Asp E, Lulu M, Gilead S, Gartner M, Waltho JP, Davis PJ, Hounslow AM, Kirschner DA, Inouye H, Myszka DG, Wright J, Solomon B, et al. A bacteriophage capsid protein provides a general amyloid interaction motif (GAIM) that binds and remodels misfolded protein assemblies. Journal of Molecular Biology. 426: 2500-19. PMID 24768993 DOI: 10.1016/J.Jmb.2014.04.015 |
0.315 |
|
| 2013 |
Pudney CR, Guerriero A, Baxter NJ, Johannissen LO, Waltho JP, Hay S, Scrutton NS. Fast protein motions are coupled to enzyme H-transfer reactions. Journal of the American Chemical Society. 135: 2512-7. PMID 23373704 DOI: 10.1021/Ja311277K |
0.312 |
|
| 2012 |
Blackburn GM, Bowler MW, Jin Y, Waltho JP. Reflections on biocatalysis involving phosphorus. Biochemistry. Biokhimii͡A. 77: 1083-96. PMID 23157289 DOI: 10.1134/S000629791210001X |
0.653 |
|
| 2012 |
Milanesi L, Waltho JP, Hunter CA, Shaw DJ, Beddard GS, Reid GD, Dev S, Volk M. Measurement of energy landscape roughness of folded and unfolded proteins. Proceedings of the National Academy of Sciences of the United States of America. 109: 19563-8. PMID 23150572 DOI: 10.1073/Pnas.1211764109 |
0.34 |
|
| 2012 |
Jin Y, Cliff MJ, Baxter NJ, Dannatt HR, Hounslow AM, Bowler MW, Blackburn GM, Waltho JP. Charge-balanced metal fluoride complexes for protein kinase A with adenosine diphosphate and substrate peptide SP20. Angewandte Chemie (International Ed. in English). 51: 12242-5. PMID 23125010 DOI: 10.1002/Anie.201204266 |
0.592 |
|
| 2012 |
Paramore R, Morgan GJ, Davis PJ, Sharma CA, Hounslow A, Taler-Ver?i? A, Zerovnik E, Waltho JP, Cliff MJ, Staniforth RA. Mapping local structural perturbations in the native state of stefin B (cystatin B) under amyloid forming conditions. Frontiers in Molecular Neuroscience. 5: 94. PMID 23091450 DOI: 10.3389/Fnmol.2012.00094 |
0.355 |
|
| 2012 |
Griffin JL, Bowler MW, Baxter NJ, Leigh KN, Dannatt HR, Hounslow AM, Blackburn GM, Webster CE, Cliff MJ, Waltho JP. Near attack conformers dominate β-phosphoglucomutase complexes where geometry and charge distribution reflect those of substrate. Proceedings of the National Academy of Sciences of the United States of America. 109: 6910-5. PMID 22505741 DOI: 10.1073/Pnas.1116855109 |
0.578 |
|
| 2011 |
Jelinska C, Davis PJ, Kenig M, Zerovnik E, Kokalj SJ, Gun?ar G, Turk D, Turk V, Clarke DT, Waltho JP, Staniforth RA. Modulation of contact order effects in the two-state folding of stefins A and B. Biophysical Journal. 100: 2268-74. PMID 21539796 DOI: 10.1016/J.Bpj.2011.03.024 |
0.355 |
|
| 2011 |
Xiaoxia L, Marston JP, Baxter NJ, Hounslow AM, Yufen Z, Blackburn GM, Cliff MJ, Waltho JP. Prioritization of charge over geometry in transition state analogues of a dual specificity protein kinase. Journal of the American Chemical Society. 133: 3989-94. PMID 21348513 DOI: 10.1021/Ja1090035 |
0.575 |
|
| 2010 |
Nicoll AJ, Trevitt CR, Tattum MH, Risse E, Quarterman E, Ibarra AA, Wright C, Jackson GS, Sessions RB, Farrow M, Waltho JP, Clarke AR, Collinge J. Pharmacological chaperone for the structured domain of human prion protein. Proceedings of the National Academy of Sciences of the United States of America. 107: 17610-5. PMID 20876144 DOI: 10.1073/Pnas.1009062107 |
0.357 |
|
| 2010 |
Hosszu LL, Tattum MH, Jones S, Trevitt CR, Wells MA, Waltho JP, Collinge J, Jackson GS, Clarke AR. The H187R mutation of the human prion protein induces conversion of recombinant prion protein to the PrP(Sc)-like form. Biochemistry. 49: 8729-38. PMID 20718410 DOI: 10.1021/Bi100572J |
0.347 |
|
| 2010 |
Cliff MJ, Bowler MW, Varga A, Marston JP, Szabó J, Hounslow AM, Baxter NJ, Blackburn GM, Vas M, Waltho JP. Transition state analogue structures of human phosphoglycerate kinase establish the importance of charge balance in catalysis. Journal of the American Chemical Society. 132: 6507-16. PMID 20397725 DOI: 10.1021/Ja100974T |
0.578 |
|
| 2010 |
Baxter NJ, Bowler MW, Alizadeh T, Cliff MJ, Hounslow AM, Wu B, Berkowitz DB, Williams NH, Blackburn GM, Waltho JP. Atomic details of near-transition state conformers for enzyme phosphoryl transfer revealed by MgF-3 rather than by phosphoranes. Proceedings of the National Academy of Sciences of the United States of America. 107: 4555-60. PMID 20164409 DOI: 10.1073/Pnas.0910333106 |
0.596 |
|
| 2010 |
Marston JP, Cliff MJ, Reed MA, Blackburn GM, Hounslow AM, Craven CJ, Waltho JP. Structural tightening and interdomain communication in the catalytic cycle of phosphoglycerate kinase. Journal of Molecular Biology. 396: 345-60. PMID 19944703 DOI: 10.1016/J.Jmb.2009.11.052 |
0.583 |
|
| 2010 |
Bowler MW, Cliff MJ, Waltho JP, Blackburn GM. Why did Nature select phosphate for its dominant roles in biology? New Journal of Chemistry. 34: 784-794. DOI: 10.1039/B9Nj00718K |
0.565 |
|
| 2009 |
Baxter NJ, Hounslow AM, Bowler MW, Williams NH, Blackburn GM, Waltho JP. MgF(3)(-) and alpha-galactose 1-phosphate in the active site of beta-phosphoglucomutase form a transition state analogue of phosphoryl transfer. Journal of the American Chemical Society. 131: 16334-5. PMID 19852484 DOI: 10.1021/Ja905972M |
0.58 |
|
| 2009 |
Menon BR, Waltho JP, Scrutton NS, Heyes DJ. Cryogenic and laser photoexcitation studies identify multiple roles for active site residues in the light-driven enzyme protochlorophyllide oxidoreductase. The Journal of Biological Chemistry. 284: 18160-6. PMID 19439417 DOI: 10.1074/Jbc.M109.020719 |
0.401 |
|
| 2009 |
Hosszu LL, Trevitt CR, Jones S, Batchelor M, Scott DJ, Jackson GS, Collinge J, Waltho JP, Clarke AR. Conformational properties of beta-PrP. The Journal of Biological Chemistry. 284: 21981-90. PMID 19369250 DOI: 10.1074/Jbc.M809173200 |
0.407 |
|
| 2009 |
Hart T, Hosszu LL, Trevitt CR, Jackson GS, Waltho JP, Collinge J, Clarke AR. Folding kinetics of the human prion protein probed by temperature jump. Proceedings of the National Academy of Sciences of the United States of America. 106: 5651-6. PMID 19321423 DOI: 10.1073/Pnas.0811457106 |
0.375 |
|
| 2009 |
Golicnik M, Olguin LF, Feng G, Baxter NJ, Waltho JP, Williams NH, Hollfelder F. Kinetic analysis of beta-phosphoglucomutase and its inhibition by magnesium fluoride. Journal of the American Chemical Society. 131: 1575-88. PMID 19132841 DOI: 10.1021/Ja806421F |
0.37 |
|
| 2009 |
Cliff MJ, Craven CJ, Marston JP, Hounslow AM, Clarke AR, Waltho JP. The denatured state of N-PGK is compact and predominantly disordered. Journal of Molecular Biology. 385: 266-77. PMID 18948115 DOI: 10.1016/J.Jmb.2008.10.004 |
0.398 |
|
| 2009 |
Skerget K, Vilfan A, Pompe-Novak M, Turk V, Waltho JP, Turk D, Zerovnik E. The mechanism of amyloid-fibril formation by stefin B: temperature and protein concentration dependence of the rates. Proteins. 74: 425-36. PMID 18636508 DOI: 10.1002/Prot.22156 |
0.345 |
|
| 2009 |
Volk M, Milanesi L, Waltho JP, Hunter CA, Dev S, Shaw DJ, Beddard GS, Reid GD. Universal Scaling Law for Polypeptide Backbone Dynamics on the Pico- to Millisecond Time Scale Biophysical Journal. 96: 322a-323a. DOI: 10.1016/J.Bpj.2008.12.1619 |
0.312 |
|
| 2008 |
Milanesi L, Jelinska C, Hunter CA, Hounslow AM, Staniforth RA, Waltho JP. A method for the reversible trapping of proteins in non-native conformations. Biochemistry. 47: 13620-34. PMID 19035655 DOI: 10.1021/Bi801362F |
0.375 |
|
| 2008 |
Milanesi L, Tomas S, Hunter CA, Weinstein JA, Edge R, Navaratnam S, Waltho JP, Best J. A pulse--radiolysis approach to fast reductive cleavage of a disulfide bond to uncage enzyme activity. Free Radical Biology & Medicine. 45: 1271-8. PMID 18760345 DOI: 10.1016/J.Freeradbiomed.2008.07.024 |
0.304 |
|
| 2008 |
Baxter NJ, Blackburn GM, Marston JP, Hounslow AM, Cliff MJ, Bermel W, Williams NH, Hollfelder F, Wemmer DE, Waltho JP. Anionic charge is prioritized over geometry in aluminum and magnesium fluoride transition state analogs of phosphoryl transfer enzymes. Journal of the American Chemical Society. 130: 3952-8. PMID 18318536 DOI: 10.1021/Ja078000N |
0.565 |
|
| 2008 |
Morgan GJ, Giannini S, Hounslow AM, Craven CJ, Zerovnik E, Turk V, Waltho JP, Staniforth RA. Exclusion of the native alpha-helix from the amyloid fibrils of a mixed alpha/beta protein. Journal of Molecular Biology. 375: 487-98. PMID 18021806 DOI: 10.1016/J.Jmb.2007.10.033 |
0.348 |
|
| 2007 |
Jenko Kokalj S, Guncar G, Stern I, Morgan G, Rabzelj S, Kenig M, Staniforth RA, Waltho JP, Zerovnik E, Turk D. Essential role of proline isomerization in stefin B tetramer formation. Journal of Molecular Biology. 366: 1569-79. PMID 17217964 DOI: 10.1016/J.Jmb.2006.12.025 |
0.328 |
|
| 2006 |
Cliff MJ, Alizadeh T, Jelinska C, Craven CJ, Staniforth RA, Waltho JP. A thiol labelling competition experiment as a probe for sidechain packing in the kinetic folding intermediate of N-PGK. Journal of Molecular Biology. 364: 810-23. PMID 17030040 DOI: 10.1016/J.Jmb.2006.09.014 |
0.413 |
|
| 2006 |
Baxter NJ, Olguin LF, Golicnik M, Feng G, Hounslow AM, Bermel W, Blackburn GM, Hollfelder F, Waltho JP, Williams NH. A Trojan horse transition state analogue generated by MgF3- formation in an enzyme active site. Proceedings of the National Academy of Sciences of the United States of America. 103: 14732-7. PMID 16990434 DOI: 10.1073/Pnas.0604448103 |
0.574 |
|
| 2006 |
Wells MA, Jelinska C, Hosszu LL, Craven CJ, Clarke AR, Collinge J, Waltho JP, Jackson GS. Multiple forms of copper (II) co-ordination occur throughout the disordered N-terminal region of the prion protein at pH 7.4. The Biochemical Journal. 400: 501-10. PMID 16925523 DOI: 10.1042/Bj20060721 |
0.308 |
|
| 2006 |
Wells MA, Jackson GS, Jones S, Hosszu LL, Craven CJ, Clarke AR, Collinge J, Waltho JP. A reassessment of copper(II) binding in the full-length prion protein. The Biochemical Journal. 399: 435-44. PMID 16824036 DOI: 10.1042/Bj20060458 |
0.315 |
|
| 2006 |
Berrisford JM, Hounslow AM, Akerboom J, Hagen WR, Brouns SJ, van der Oost J, Murray IA, Michael Blackburn G, Waltho JP, Rice DW, Baker PJ. Evidence supporting a cis-enediol-based mechanism for Pyrococcus furiosus phosphoglucose isomerase. Journal of Molecular Biology. 358: 1353-66. PMID 16580686 DOI: 10.1016/J.Jmb.2006.03.015 |
0.368 |
|
| 2006 |
Reed MA, Jelinska C, Syson K, Cliff MJ, Splevins A, Alizadeh T, Hounslow AM, Staniforth RA, Clarke AR, Craven CJ, Waltho JP. The denatured state under native conditions: a non-native-like collapsed state of N-PGK. Journal of Molecular Biology. 357: 365-72. PMID 16430920 DOI: 10.1016/J.Jmb.2005.12.080 |
0.417 |
|
| 2006 |
Kenig M, Jenko-Kokalj S, Tusek-Znidaric M, Pompe-Novak M, Guncar G, Turk D, Waltho JP, Staniforth RA, Avbelj F, Zerovnik E. Folding and amyloid-fibril formation for a series of human stefins' chimeras: any correlation? Proteins. 62: 918-27. PMID 16342276 DOI: 10.1002/Prot.20812 |
0.333 |
|
| 2005 |
Hosszu LL, Wells MA, Jackson GS, Jones S, Batchelor M, Clarke AR, Craven CJ, Waltho JP, Collinge J. Definable equilibrium states in the folding of human prion protein. Biochemistry. 44: 16649-57. PMID 16342955 DOI: 10.1021/Bi051277K |
0.425 |
|
| 2005 |
Syson K, Thirlway J, Hounslow AM, Soultanas P, Waltho JP. Solution structure of the helicase-interaction domain of the primase DnaG: a model for helicase activation. Structure (London, England : 1993). 13: 609-16. PMID 15837199 DOI: 10.1016/J.Str.2005.01.022 |
0.325 |
|
| 2005 |
Zhong Q, Watson MJ, Lazar CS, Hounslow AM, Waltho JP, Gill GN. Determinants of the endosomal localization of sorting nexin 1. Molecular Biology of the Cell. 16: 2049-57. PMID 15673616 DOI: 10.1091/Mbc.E04-06-0504 |
0.314 |
|
| 2004 |
Hosszu LL, Jackson GS, Trevitt CR, Jones S, Batchelor M, Bhelt D, Prodromidou K, Clarke AR, Waltho JP, Collinge J. The residue 129 polymorphism in human prion protein does not confer susceptibility to Creutzfeldt-Jakob disease by altering the structure or global stability of PrPC. The Journal of Biological Chemistry. 279: 28515-21. PMID 15123682 DOI: 10.1074/Jbc.M313762200 |
0.31 |
|
| 2004 |
Japelj B, Waltho JP, Jerala R. Comparison of backbone dynamics of monomeric and domain-swapped stefin A. Proteins. 54: 500-12. PMID 14747998 DOI: 10.1002/Prot.10624 |
0.38 |
|
| 2004 |
Sanders A, Jeremy Craven C, Higgins LD, Giannini S, Conroy MJ, Hounslow AM, Waltho JP, Staniforth RA. Cystatin forms a tetramer through structural rearrangement of domain-swapped dimers prior to amyloidogenesis. Journal of Molecular Biology. 336: 165-78. PMID 14741212 DOI: 10.1016/J.Jmb.2003.12.011 |
0.379 |
|
| 2003 |
Reed MA, Hounslow AM, Sze KH, Barsukov IG, Hosszu LL, Clarke AR, Craven CJ, Waltho JP. Effects of domain dissection on the folding and stability of the 43 kDa protein PGK probed by NMR. Journal of Molecular Biology. 330: 1189-201. PMID 12860138 DOI: 10.1016/S0022-2836(03)00625-9 |
0.405 |
|
| 2003 |
Zerovnik E, Turk V, Waltho JP. Amyloid fibril formation by human stefin B: influence of the initial pH-induced intermediate state. Biochemical Society Transactions. 30: 543-7. PMID 12196133 DOI: 10.1042/Bst0300543 |
0.312 |
|
| 2003 |
Mattinen ML, Pääkkönen K, Ikonen T, Craven J, Drakenberg T, Serimaa R, Waltho J, Annila A. Quaternary structure built from subunits combining NMR and small-angle x-ray scattering data. Biophysical Journal. 83: 1177-83. PMID 12124297 DOI: 10.1016/S0006-3495(02)75241-7 |
0.365 |
|
| 2001 |
Staniforth RA, Giannini S, Higgins LD, Conroy MJ, Hounslow AM, Jerala R, Craven CJ, Waltho JP. Three-dimensional domain swapping in the folded and molten-globule states of cystatins, an amyloid-forming structural superfamily. The Embo Journal. 20: 4774-81. PMID 11532941 DOI: 10.1093/Emboj/20.17.4774 |
0.397 |
|
| 2001 |
Thaw P, Baxter NJ, Hounslow AM, Price C, Waltho JP, Craven CJ. Structure of TCTP reveals unexpected relationship with guanine nucleotide-free chaperones. Nature Structural Biology. 8: 701-4. PMID 11473261 DOI: 10.1038/90415 |
0.314 |
|
| 2001 |
Jackson GS, Murray I, Hosszu LL, Gibbs N, Waltho JP, Clarke AR, Collinge J. Location and properties of metal-binding sites on the human prion protein. Proceedings of the National Academy of Sciences of the United States of America. 98: 8531-5. PMID 11438695 DOI: 10.1073/Pnas.151038498 |
0.327 |
|
| 2000 |
Craven CJ, Baxter NJ, Murray EH, Hill NJ, Martin JR, Ylinenjärvi K, Björk I, Waltho JP, Murray IA. Wild-type and met-65 → Leu variants of human cystatin A are functionally and structurally identical Biochemistry. 39: 15783-15790. PMID 11123903 DOI: 10.1021/Bi0017069 |
0.367 |
|
| 2000 |
Staniforth RA, Dean JL, Zhong Q, Zerovnik E, Clarke AR, Waltho JP. The major transition state in folding need not involve the immobilization of side chains. Proceedings of the National Academy of Sciences of the United States of America. 97: 5790-5. PMID 10823937 DOI: 10.1073/Pnas.97.11.5790 |
0.374 |
|
| 1999 |
Zerovnik E, Virden R, Jerala R, Kroon-Zitko L, Turk V, Waltho JP. Differences in the effects of TFE on the folding pathways of human stefins A and B. Proteins. 36: 205-16. PMID 10398367 DOI: 10.1002/(Sici)1097-0134(19990801)36:2<205::Aid-Prot6>3.0.Co;2-4 |
0.313 |
|
| 1999 |
Czaplewski LG, McKeating J, Craven CJ, Higgins LD, Appay V, Brown A, Dudgeon T, Howard LA, Meyers T, Owen J, Palan SR, Tan P, Wilson G, Woods NR, Heyworth CM, ... ... Waltho JP, et al. Identification of amino acid residues critical for aggregation of human CC chemokines macrophage inflammatory protein (MIP)-1alpha, MIP-1beta, and RANTES. Characterization of active disaggregated chemokine variants. The Journal of Biological Chemistry. 274: 16077-84. PMID 10347159 DOI: 10.1074/Jbc.274.23.16077 |
0.311 |
|
| 1999 |
Jackson GS, Hill AF, Joseph C, Hosszu L, Power A, Waltho JP, Clarke AR, Collinge J. Multiple folding pathways for heterologously expressed human prion protein. Biochimica Et Biophysica Acta. 1431: 1-13. PMID 10209273 DOI: 10.1016/S0167-4838(99)00038-2 |
0.389 |
|
| 1999 |
Jackson GS, Hosszu LL, Power A, Hill AF, Kenney J, Saibil H, Craven CJ, Waltho JP, Clarke AR, Collinge J. Reversible conversion of monomeric human prion protein between native and fibrilogenic conformations. Science (New York, N.Y.). 283: 1935-7. PMID 10082469 DOI: 10.1126/Science.283.5409.1935 |
0.331 |
|
| 1999 |
Hurd PJ, Whitmarsh AJ, Baldwin GS, Kelly SM, Waltho JP, Price NC, Connolly BA, Hornby DP. Mechanism-based inhibition of C5-cytosine DNA methyltransferases by 2-H pyrimidinone. Journal of Molecular Biology. 286: 389-401. PMID 9973559 DOI: 10.1006/Jmbi.1998.2491 |
0.311 |
|
| 1998 |
Baxter NJ, Hosszu LLP, Waltho JP, Williamson MP. Characterisation of low free-energy excited states of folded proteins. Journal of Molecular Biology. 284: 1625-1639. PMID 9878375 DOI: 10.1006/Jmbi.1998.2265 |
0.409 |
|
| 1998 |
Žerovnik E, Jerala R, Virden R, Žitko LK, Turk V, Waltho JP. On the mechanism of human stefin B folding: II. Folding from GuHCl unfolded, TFE denatured, acid denatured, and acid intermediate states Proteins. 32: 304-313. PMID 9715907 DOI: 10.1002/(Sici)1097-0134(19980815)32:3<304::Aid-Prot6>3.0.Co;2-H |
0.335 |
|
| 1998 |
Parker MJ, Dempsey CE, Hosszu LL, Waltho JP, Clarke AR. Topology, sequence evolution and folding dynamics of an immunoglobulin domain. Nature Structural Biology. 5: 194-8. PMID 9501912 DOI: 10.1038/Nsb0398-194 |
0.385 |
|
| 1997 |
Hosszu LL, Craven CJ, Parker MJ, Lorch M, Spencer J, Clarke AR, Waltho JP. Structure of a kinetic protein folding intermediate by equilibrium amide exchange. Nature Structural Biology. 4: 801-4. PMID 9334744 DOI: 10.1038/Nsb1097-801 |
0.397 |
|
| 1997 |
Clarke AR, Waltho JP. Protein folding and intermediates. Current Opinion in Biotechnology. 8: 400-10. PMID 9273848 DOI: 10.1016/S0958-1669(97)80060-2 |
0.351 |
|
| 1997 |
Hosszu LL, Craven CJ, Spencer J, Parker MJ, Clarke AR, Kelly M, Waltho JP. Is the structure of the N-domain of phosphoglycerate kinase affected by isolation from the intact molecule? Biochemistry. 36: 333-40. PMID 9003185 DOI: 10.1021/Bi961784P |
0.383 |
|
| 1996 |
Parker MJ, Spencer J, Jackson GS, Burston SG, Hosszu LL, Craven CJ, Waltho JP, Clarke AR. Domain behavior during the folding of a thermostable phosphoglycerate kinase. Biochemistry. 35: 15740-52. PMID 8961937 DOI: 10.1021/Bi961330S |
0.39 |
|
| 1996 |
Craven CJ, Whitehead B, Jones SK, Thulin E, Blackburn GM, Waltho JP. Complexes formed between calmodulin and the antagonists J-8 and TFP in solution. Biochemistry. 35: 10287-99. PMID 8756684 DOI: 10.1021/Bi9605043 |
0.524 |
|
| 1995 |
Shore P, Bisset L, Lakey J, Waltho JP, Virden R, Sharrocks AD. Characterization of the Elk-1 ETS DNA-binding domain Journal of Biological Chemistry. 270: 5805-5811. PMID 7890710 DOI: 10.1074/Jbc.270.11.5805 |
0.331 |
|
| 1995 |
Martin JR, Craven CJ, Jerala R, Kroon-Zitko L, Zerovnik E, Turk V, Waltho JP. The three-dimensional solution structure of human stefin A. Journal of Molecular Biology. 246: 331-343. PMID 7869384 DOI: 10.1006/Jmbi.1994.0088 |
0.39 |
|
| 1995 |
Finn BE, Evenäs J, Drakenberg T, Waltho JP, Thulin E, Forsén S. Calcium-induced structural changes and domain autonomy in calmodulin. Nature Structural Biology. 2: 777-83. PMID 7552749 DOI: 10.1038/Nsb0995-777 |
0.348 |
|
| 1995 |
Groves P, Searle MS, Waltho JP, Williams DH. Asymmetry in the structure of glycopeptide antibiotic dimers: NMR studies of the ristocetin A complex with a bacterial cell wall analogue Journal of the American Chemical Society. 117: 7958-7964. DOI: 10.1021/Ja00135A014 |
0.321 |
|
| 1994 |
Ford K, Waltho J, Hornby D. Component analysis and characterization of a nuclear deoxyribonucleotidase Biochemical Journal. 298: 727-732. PMID 8141789 DOI: 10.1042/Bj2980727 |
0.341 |
|
| 1994 |
Martin JR, Jerala R, Kroon-Zitko L, Zerovnik E, Turk V, Waltho JP. Structural characterisation of human stefin A in solution and implications for binding to cysteine proteinases. European Journal of Biochemistry. 225: 1181-94. PMID 7957209 DOI: 10.1111/J.1432-1033.1994.1181B.X |
0.398 |
|
| 1989 |
Waltho JP, Feher VA, Lerner RA, Wright PE. Conformation of a T cell stimulating peptide in aqueous solution Febs Letters. 250: 400-404. PMID 2787756 DOI: 10.1016/0014-5793(89)80764-1 |
0.302 |
|
| 1988 |
Waltho JP, Cavanagh J, Williams DH. Aspects of molecular recognition: use of a truncated driven pseudo-NOESY experiment to elucidate the environment of intermolecular electrostatic interactions in vancomycin Journal of the Chemical Society, Chemical Communications. 707-709. DOI: 10.1039/C39880000707 |
0.329 |
|
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