| Year |
Citation |
Score |
| 2019 |
Ye X, Lin J, Mayne L, Shorter J, Englander SW. Hydrogen exchange reveals Hsp104 architecture, structural dynamics, and energetics in physiological solution. Proceedings of the National Academy of Sciences of the United States of America. PMID 30918129 DOI: 10.1073/pnas.1816184116 |
0.44 |
|
| 2018 |
Karch KR, Coradin M, Zandarashvili L, Kan ZY, Gerace M, Englander SW, Black BE, Garcia BA. Hydrogen-Deuterium Exchange Coupled to Top- and Middle-Down Mass Spectrometry Reveals Histone Tail Dynamics before and after Nucleosome Assembly. Structure (London, England : 1993). PMID 30293810 DOI: 10.1016/j.str.2018.08.006 |
0.44 |
|
| 2018 |
Ye X, Mayne L, Kan ZY, Englander SW. Folding of maltose binding protein outside of and in GroEL. Proceedings of the National Academy of Sciences of the United States of America. PMID 29295923 DOI: 10.1073/pnas.1716168115 |
0.44 |
|
| 2017 |
Englander SW, Mayne L. Reply to Eaton and Wolynes: How do proteins fold? Proceedings of the National Academy of Sciences of the United States of America. PMID 29087353 DOI: 10.1073/pnas.1716929114 |
0.44 |
|
| 2017 |
Englander SW, Mayne L. The case for defined protein folding pathways. Proceedings of the National Academy of Sciences of the United States of America. PMID 28630329 DOI: 10.1073/pnas.1706196114 |
0.44 |
|
| 2017 |
Chetty PS, Mayne L, Lund-Katz S, Englander SW, Phillips MC. Helical structure, stability, and dynamics in human apolipoprotein E3 and E4 by hydrogen exchange and mass spectrometry. Proceedings of the National Academy of Sciences of the United States of America. PMID 28096372 DOI: 10.1073/pnas.1617523114 |
0.44 |
|
| 2016 |
Englander SW, Mayne L, Kan ZY, Hu W. Protein Folding-How and Why: By Hydrogen Exchange, Fragment Separation, and Mass Spectrometry. Annual Review of Biophysics. PMID 27145881 DOI: 10.1146/annurev-biophys-062215-011121 |
0.44 |
|
| 2016 |
Hu W, Kan ZY, Mayne L, Englander SW. Cytochrome c folds through foldon-dependent native-like intermediates in an ordered pathway. Proceedings of the National Academy of Sciences of the United States of America. PMID 26966231 DOI: 10.1073/pnas.1522674113 |
0.88 |
|
| 2015 |
Casina VC, Hu W, Mao JH, Lu RN, Hanby HA, Pickens B, Kan ZY, Lim WK, Mayne L, Ostertag EM, Kacir S, Siegel DL, Englander SW, Zheng XL. High-resolution epitope mapping by HX MS reveals the pathogenic mechanism and a possible therapy for autoimmune TTP syndrome. Proceedings of the National Academy of Sciences of the United States of America. 112: 9620-5. PMID 26203127 DOI: 10.1073/pnas.1512561112 |
0.88 |
|
| 2014 |
Englander SW, Mayne L. The nature of protein folding pathways Proceedings of the National Academy of Sciences of the United States of America. 111: 15873-15880. PMID 25326421 DOI: 10.1073/pnas.1411798111 |
0.88 |
|
| 2013 |
Walters BT, Mayne L, Hinshaw JR, Sosnick TR, Englander SW. Folding of a large protein at high structural resolution. Proceedings of the National Academy of Sciences of the United States of America. 110: 18898-903. PMID 24191053 DOI: 10.1073/pnas.1319482110 |
0.88 |
|
| 2013 |
Kan ZY, Walters BT, Mayne L, Englander SW. Protein hydrogen exchange at residue resolution by proteolytic fragmentation mass spectrometry analysis Proceedings of the National Academy of Sciences of the United States of America. 110: 16438-16443. PMID 24019478 DOI: 10.1073/pnas.1315532110 |
0.88 |
|
| 2013 |
Hu W, Walters BT, Kan ZY, Mayne L, Rosen LE, Marqusee S, Englander SW. Stepwise protein folding at near amino acid resolution by hydrogen exchange and mass spectrometry. Proceedings of the National Academy of Sciences of the United States of America. 110: 7684-9. PMID 23603271 DOI: 10.1073/pnas.1305887110 |
0.88 |
|
| 2013 |
Chetty PS, Nguyen D, Nickel M, Lund-Katz S, Mayne L, Englander SW, Phillips MC. Comparison of apoA-I helical structure and stability in discoidal and spherical HDL particles by HX and mass spectrometry. Journal of Lipid Research. 54: 1589-97. PMID 23580759 DOI: 10.1194/jlr.M034785 |
0.88 |
|
| 2012 |
Walters BT, Ricciuti A, Mayne L, Englander SW. Minimizing back exchange in the hydrogen exchange-mass spectrometry experiment Journal of the American Society For Mass Spectrometry. 23: 2132-2139. PMID 22965280 DOI: 10.1007/s13361-012-0476-x |
0.88 |
|
| 2012 |
Chetty PS, Mayne L, Kan ZY, Lund-Katz S, Englander SW, Phillips MC. Apolipoprotein A-I helical structure and stability in discoidal high-density lipoprotein (HDL) particles by hydrogen exchange and mass spectrometry Proceedings of the National Academy of Sciences of the United States of America. 109: 11687-11692. PMID 22745166 DOI: 10.1073/pnas.1209305109 |
0.88 |
|
| 2012 |
Skinner JJ, Lim WK, Bédard S, Black BE, Englander SW. Protein hydrogen exchange: testing current models. Protein Science : a Publication of the Protein Society. 21: 987-95. PMID 22544567 DOI: 10.1002/pro.2082 |
0.88 |
|
| 2012 |
Skinner JJ, Lim WK, Bédard S, Black BE, Englander SW. Protein dynamics viewed by hydrogen exchange. Protein Science : a Publication of the Protein Society. 21: 996-1005. PMID 22544544 DOI: 10.1002/pro.2081 |
0.88 |
|
| 2011 |
Kan ZY, Mayne L, Sevugan Chetty P, Englander SW. ExMS: Data analysis for HX-MS experiments Journal of the American Society For Mass Spectrometry. 22: 1906-1915. PMID 21952778 DOI: 10.1007/s13361-011-0236-3 |
0.88 |
|
| 2011 |
Mayne L, Kan ZY, Sevugan Chetty P, Ricciuti A, Walters BT, Englander SW. Many overlapping peptides for protein hydrogen exchange experiments by the fragment separation-mass spectrometry method Journal of the American Society For Mass Spectrometry. 22: 1898-1905. PMID 21952777 DOI: 10.1007/s13361-011-0235-4 |
0.88 |
|
| 2011 |
Panchenko T, Sorensen TC, Woodcock CL, Kan ZY, Wood S, Resch MG, Luger K, Englander SW, Hansen JC, Black BE. Replacement of histone H3 with CENP-A directs global nucleosome array condensation and loosening of nucleosome superhelical termini. Proceedings of the National Academy of Sciences of the United States of America. 108: 16588-93. PMID 21949362 DOI: 10.1073/pnas.1113621108 |
0.88 |
|
| 2009 |
Chetty PS, Mayne L, Lund-Katz S, Stranz D, Englander SW, Phillips MC. Helical structure and stability in human apolipoprotein A-I by hydrogen exchange and mass spectrometry Proceedings of the National Academy of Sciences of the United States of America. 106: 19005-19010. PMID 19850866 DOI: 10.1073/pnas.0909708106 |
0.88 |
|
| 2009 |
Lim WK, Rösgen J, Englander SW. Urea, but not guanidinium, destabilizes proteins by forming hydrogen bonds to the peptide group Proceedings of the National Academy of Sciences of the United States of America. 106: 2595-2600. PMID 19196963 DOI: 10.1073/pnas.0812588106 |
0.88 |
|
| 2008 |
Skinner JJ, Wood S, Shorter J, Englander SW, Black BE. The Mad2 partial unfolding model: regulating mitosis through Mad2 conformational switching. The Journal of Cell Biology. 183: 761-8. PMID 19029339 DOI: 10.1083/jcb.200808122 |
0.88 |
|
| 2008 |
Bédard S, Krishna MMG, Mayne L, Englander SW. Protein folding: Independent unrelated pathways or predetermined pathway with optional errors Proceedings of the National Academy of Sciences of the United States of America. 105: 7182-7187. PMID 18480257 DOI: 10.1073/pnas.0801864105 |
0.88 |
|
| 2008 |
Bédard S, Mayne LC, Peterson RW, Wand AJ, Englander SW. The Foldon Substructure of Staphylococcal Nuclease Journal of Molecular Biology. 376: 1142-1154. PMID 18201720 DOI: 10.1016/j.jmb.2007.12.020 |
0.88 |
|
| 2007 |
Englander SW, Mayne L, Krishna MMG. Protein folding and misfolding: Mechanism and principles Quarterly Reviews of Biophysics. 40: 287-326. PMID 18405419 DOI: 10.1017/S0033583508004654 |
0.88 |
|
| 2007 |
Krishna MMG, Maity H, Rumbley JN, Englander SW. Branching in the sequential folding pathway of cytochrome c Protein Science. 16: 1946-1956. PMID 17660254 DOI: 10.1110/ps.072922307 |
0.88 |
|
| 2007 |
Krishna MMG, Englander SW. A unified mechanism for protein folding: Predetermined pathways with optional errors Protein Science. 16: 449-464. PMID 17322530 DOI: 10.1110/ps.062655907 |
0.88 |
|
| 2006 |
Englander SW. Hydrogen Exchange and Mass Spectrometry: A Historical Perspective Journal of the American Society For Mass Spectrometry. 17: 1481-1489. PMID 16876429 DOI: 10.1016/j.jasms.2006.06.006 |
0.88 |
|
| 2006 |
Krishna MMG, Maity H, Rumbley JN, Lin Y, Englander SW. Order of Steps in the Cytochrome c Folding Pathway: Evidence for a Sequential Stabilization Mechanism Journal of Molecular Biology. 359: 1410-1419. PMID 16690080 DOI: 10.1016/j.jmb.2006.04.035 |
0.88 |
|
| 2006 |
Maity H, Rumbley JN, Englander SW. Functional role of a protein foldon - An Ω-loop foldon controls the alkaline transition in ferricytochrome c Proteins: Structure, Function and Genetics. 63: 349-355. PMID 16287119 DOI: 10.1002/prot.20757 |
0.88 |
|
| 2005 |
Del Mar C, Greenbaum EA, Mayne L, Englander SW, Woods VL. Structure and properties of α-synuclein and other amyloids determined at the amino acid level Proceedings of the National Academy of Sciences of the United States of America. 102: 15477-15482. PMID 16223878 DOI: 10.1073/pnas.0507405102 |
0.88 |
|
| 2005 |
Maity H, Maity M, Krishna MMG, Mayne L, Englander SW. Protein folding: The stepwise assembly of foldon units Proceedings of the National Academy of Sciences of the United States of America. 102: 4741-4746. PMID 15774579 DOI: 10.1073/pnas.0501043102 |
0.88 |
|
| 2005 |
Krishna MMG, Englander SW. The N-terminal to C-terminal motif in protein folding and function Proceedings of the National Academy of Sciences of the United States of America. 102: 1053-1058. PMID 15657118 DOI: 10.1073/pnas.0409114102 |
0.88 |
|
| 2005 |
Greenbaum EA, Graves CL, Mishizen-Eberz AJ, Lupoli MA, Lynch DR, Englander SW, Axelsen PH, Giasson BI. The E46K mutation in alpha-synuclein increases amyloid fibril formation. The Journal of Biological Chemistry. 280: 7800-7. PMID 15632170 DOI: 10.1074/jbc.M411638200 |
0.88 |
|
| 2004 |
Krishna MMG, Hoang L, Lin Y, Englander SW. Hydrogen exchange methods to study protein folding Methods. 34: 51-64. PMID 15283915 DOI: 10.1016/j.ymeth.2004.03.005 |
0.88 |
|
| 2003 |
Krishna MM, Lin Y, Mayne L, Englander SW. Intimate view of a kinetic protein folding intermediate: residue-resolved structure, interactions, stability, folding and unfolding rates, homogeneity. Journal of Molecular Biology. 334: 501-13. PMID 14623190 |
0.44 |
|
| 2003 |
Liu W, Rumbley J, Englander SW, Wand AJ. Backbone and side-chain heteronuclear resonance assignments and hyperfine NMR shifts in horse cytochrome c Protein Science. 12: 2104-2108. PMID 12931009 DOI: 10.1110/ps.03211303 |
0.88 |
|
| 2003 |
Hoang L, Maity H, Krishna MMG, Lin Y, Englander SW. Folding units govern the cytochrome c alkaline transition Journal of Molecular Biology. 331: 37-43. PMID 12875834 DOI: 10.1016/S0022-2836(03)00698-3 |
0.88 |
|
| 2003 |
Krishna MMG, Lin Y, Rumbley JN, Englander SW. Cooperative omega loops in cytochrome c: Role in folding and function Journal of Molecular Biology. 331: 29-36. PMID 12875833 DOI: 10.1016/S0022-2836(03)00697-1 |
0.88 |
|
| 2003 |
Englander JJ, Del Mar C, Li W, Englander SW, Kim JS, Stranz DD, Hamuro Y, Woods VL. Protein structure change studied by hydrogen-deuterium exchange, functional labeling, and mass spectrometry Proceedings of the National Academy of Sciences of the United States of America. 100: 7057-7062. PMID 12773622 DOI: 10.1073/pnas.1232301100 |
0.88 |
|
| 2003 |
Maity H, Lim WK, Rumbley JN, Englander SW. Protein hydrogen exchange mechanism: Local fluctuations Protein Science. 12: 153-160. PMID 12493838 DOI: 10.1110/ps.0225803 |
0.88 |
|
| 2002 |
Englander SW, Mayne L, Rumbley JN. Submolecular cooperativity produces multi-state protein unfolding and refolding Biophysical Chemistry. 101: 57-65. PMID 12487989 DOI: 10.1016/S0301-4622(02)00190-4 |
0.88 |
|
| 2002 |
Krantz BA, Mayne L, Rumbley J, Englander SW, Sosnick TR. Fast and slow intermediate accumulation and the initial barrier mechanism in protein folding. Journal of Molecular Biology. 324: 359-71. PMID 12441113 DOI: 10.1016/S0022-2836(02)01029-X |
0.88 |
|
| 2002 |
Rumbley JN, Hoang L, Englander SW. Recombinant equine cytochrome c in Escherichia coli: High-level expression, characterization, and folding and assembly mutants Biochemistry. 41: 13894-13901. PMID 12437346 DOI: 10.1021/bi026543y |
0.88 |
|
| 2002 |
Hoang L, Bédard S, Krishna MMG, Lin Y, Englander SW. Cytochrome c folding pathway: Kinetic native-state hydrogen exchange Proceedings of the National Academy of Sciences of the United States of America. 99: 12173-12178. PMID 12196629 DOI: 10.1073/pnas.152439199 |
0.88 |
|
| 2001 |
Duvvuri U, Goldberg AD, Kranz JK, Hoang L, Reddy R, Wehrli FW, Wand AJ, Englander SW, Leigh JS. Water magnetic relaxation dispersion in biological systems: the contribution of proton exchange and implications for the noninvasive detection of cartilage degradation. Proceedings of the National Academy of Sciences of the United States of America. 98: 12479-84. PMID 11606754 DOI: 10.1073/pnas.221471898 |
0.88 |
|
| 2001 |
Englander SW, Krishna MM. Hydrogen exchange. Nature Structural Biology. 8: 741-2. PMID 11524670 DOI: 10.1038/nsb0901-741 |
0.88 |
|
| 2001 |
Englander SW, Hiller R. Dynamics and thermodynamics of hyperthermophilic proteins by hydrogen exchange Methods in Enzymology. 334: 342-350. PMID 11398477 DOI: 10.1016/S0076-6879(01)34481-6 |
0.88 |
|
| 2001 |
Huyghues-Despointes BM, Pace CN, Englander SW, Scholtz JM. Measuring the conformational stability of a protein by hydrogen exchange. Methods in Molecular Biology (Clifton, N.J.). 168: 69-92. PMID 11357629 |
0.88 |
|
| 2001 |
Rumbley J, Hoang L, Mayne L, Englander SW. An amino acid code for protein folding Proceedings of the National Academy of Sciences of the United States of America. 98: 105-112. PMID 11136249 DOI: 10.1073/pnas.98.1.105 |
0.88 |
|
| 2000 |
Mayne L, Englander SW. Two-state vs. multistate protein unfolding studied by optical melting and hydrogen exchange Protein Science. 9: 1873-1877. PMID 11106159 |
0.88 |
|
| 2000 |
Englander SW. Protein folding intermediates and pathways studied by hydrogen exchange Annual Review of Biophysics and Biomolecular Structure. 29: 213-238. PMID 10940248 DOI: 10.1146/annurev.biophys.29.1.213 |
0.88 |
|
| 1999 |
Milne JS, Xu Y, Mayne LC, Englander SW. Experimental study of the protein folding landscape: Unfolding reactions in cytochrome c Journal of Molecular Biology. 290: 811-822. PMID 10395831 DOI: 10.1006/jmbi.1999.2924 |
0.88 |
|
| 1999 |
Shtilerman M, Lorimer GH, Englander SW. Chaperonin function: Folding by forced unfolding Science. 284: 822-825. PMID 10221918 DOI: 10.1126/science.284.5415.822 |
0.88 |
|
| 1998 |
Englander JJ, Louie G, McKinnie RE, Englander SW. Energetic components of the allosteric machinery in hemoglobin measured by hydrogen exchange Journal of Molecular Biology. 284: 1695-1706. PMID 9878380 DOI: 10.1006/jmbi.1998.2278 |
0.88 |
|
| 1998 |
Englander SW. Native-state HX Trends in Biochemical Sciences. 23: 378. PMID 9810223 DOI: 10.1016/S0968-0004(98)01281-X |
0.88 |
|
| 1998 |
Qi PX, Sosnick TR, Englander SW. The burst phase in ribonuclease A folding and solvent dependence of the unfolded state. Nature Structural Biology. 5: 882-4. PMID 9783747 DOI: 10.1038/2321 |
0.88 |
|
| 1998 |
Xu Y, Mayne L, Englander SW. Evidence for an unfolding and refolding pathway in cytochrome c Nature Structural Biology. 5: 774-778. PMID 9731770 DOI: 10.1038/1810 |
0.88 |
|
| 1998 |
Milne JS, Mayne L, Roder H, Wand AJ, Englander SW. Determinants of protein hydrogen exchange studied in equine cytochrome c Protein Science. 7: 739-745. PMID 9541406 |
0.88 |
|
| 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 |
0.88 |
|
| 1998 |
Englander SW, Sosnick TR, Mayne LC, Shtilerman M, Qi PX, Bai Y. Fast and Slow Folding in Cytochrome c Accounts of Chemical Research. 31: 737-744. |
0.88 |
|
| 1997 |
Hiller R, Zhou ZH, Adams MWW, Englander SW. Stability and dynamics in a hyperthermophilic protein with melting temperature close to 200°C Proceedings of the National Academy of Sciences of the United States of America. 94: 11329-11332. PMID 9326609 DOI: 10.1073/pnas.94.21.11329 |
0.88 |
|
| 1997 |
Sosnick TR, Shtilerman MD, Mayne L, Englander SW. Ultrafast signals in protein folding and the polypeptide contracted state. Proceedings of the National Academy of Sciences of the United States of America. 94: 8545-50. PMID 9238013 DOI: 10.1073/pnas.94.16.8545 |
0.88 |
|
| 1997 |
Englander SW, Mayne L, Bai Y, Sosnick TR. Hydrogen exchange: the modern legacy of Linderstrøm-Lang. Protein Science : a Publication of the Protein Society. 6: 1101-9. PMID 9144782 DOI: 10.1002/pro.5560060517 |
0.88 |
|
| 1996 |
Sosnick TR, Jackson S, Wilk RR, Englander SW, DeGrado WF. The role of helix formation in the folding of a fully alpha-helical coiled coil. Proteins. 24: 427-32. PMID 9162943 DOI: 10.1002/(SICI)1097-0134(199604)24:4<427::AID-PROT2>3.0.CO;2-B |
0.88 |
|
| 1996 |
Sosnick TR, Mayne L, Englander SW. Molecular collapse: the rate-limiting step in two-state cytochrome c folding. Proteins. 24: 413-26. PMID 9162942 DOI: 10.1002/(SICI)1097-0134(199604)24:4<413::AID-PROT1>3.0.CO;2-F |
0.88 |
|
| 1996 |
Bai Y, Englander SW. Future directions in folding: the multi-state nature of protein structure. Proteins. 24: 145-51. PMID 8820481 DOI: 10.1002/(SICI)1097-0134(199602)24:2<145::AID-PROT1>3.0.CO;2-I |
0.88 |
|
| 1996 |
Englander SW, Sosnick TR, Englander JJ, Mayne L. Mechanisms and uses of hydrogen exchange. Current Opinion in Structural Biology. 6: 18-23. PMID 8696968 DOI: 10.1016/S0959-440X(96)80090-X |
0.88 |
|
| 1996 |
Rodgers ME, Englander JJ, Englander SW, Harrington WF. Measurement of protein structure change in active muscle by hydrogen-tritium exchange Biophysical Chemistry. 59: 221-230. PMID 8672713 DOI: 10.1016/0301-4622(95)00133-6 |
0.88 |
|
| 1996 |
Carlacci L, Englander SW. Loop problem in proteins: Developments on the Monte Carlo simulated annealing approach Journal of Computational Chemistry. 17: 1002-1012. |
0.88 |
|
| 1995 |
Bai Y, Englander JJ, Mayne L, Milne JS, Englander SW. Thermodynamic parameters from hydrogen exchange measurements. Methods in Enzymology. 259: 344-56. PMID 8538461 DOI: 10.1016/0076-6879(95)59051-X |
0.88 |
|
| 1995 |
Bai Y, Sosnick TR, Mayne L, Englander SW. Protein folding intermediates: native-state hydrogen exchange. Science (New York, N.Y.). 269: 192-7. PMID 7618079 |
0.88 |
|
| 1994 |
Bai Y, Englander SW. Hydrogen bond strength and beta-sheet propensities: the role of a side chain blocking effect. Proteins. 18: 262-6. PMID 8202467 DOI: 10.1002/prot.340180307 |
0.88 |
|
| 1994 |
Englander SW, Englander JJ. Structure and energy change in hemoglobin by hydrogen exchange labeling. Methods in Enzymology. 232: 26-42. PMID 8057864 DOI: 10.1016/0076-6879(94)32041-1 |
0.88 |
|
| 1994 |
Sharp KA, Englander SW. How much is a stabilizing bond worth? Trends in Biochemical Sciences. 19: 526-9. PMID 7846760 DOI: 10.1016/0968-0004(94)90051-5 |
0.88 |
|
| 1994 |
Bai Y, Milne JS, Mayne L, Englander SW. Protein stability parameters measured by hydrogen exchange. Proteins. 20: 4-14. PMID 7824522 DOI: 10.1002/prot.340200103 |
0.88 |
|
| 1994 |
Jeng MF, Englander SW, Pardue K, Rogalskyj JS, McLendon G. Structural dynamics in an electron-transfer complex. Nature Structural Biology. 1: 234-8. PMID 7656052 |
0.88 |
|
| 1994 |
Sosnick TR, Mayne L, Hiller R, Englander SW. The barriers in protein folding. Nature Structural Biology. 1: 149-56. PMID 7656032 |
0.88 |
|
| 1994 |
Yu KR, Hijikata T, Lin ZX, Sweeney HL, Englander SW, Holtzer H. Truncated desmin in PtK2 cells induces desmin-vimentin-cytokeratin coprecipitation, involution of intermediate filament networks, and nuclear fragmentation: a model for many degenerative diseases. Proceedings of the National Academy of Sciences of the United States of America. 91: 2497-501. PMID 7511811 |
0.88 |
|
| 1993 |
Englander SW. In pursuit of protein folding. Science (New York, N.Y.). 262: 848-9. PMID 8235606 |
0.88 |
|
| 1993 |
Connelly GP, Bai Y, Jeng MF, Englander SW. Isotope effects in peptide group hydrogen exchange. Proteins. 17: 87-92. PMID 8234247 DOI: 10.1002/prot.340170111 |
0.88 |
|
| 1993 |
Bai Y, Milne JS, Mayne L, Englander SW. Primary structure effects on peptide group hydrogen exchange. Proteins. 17: 75-86. PMID 8234246 DOI: 10.1002/prot.340170110 |
0.88 |
|
| 1993 |
Carlacci L, Englander SW. The loop problem in proteins: a Monte Carlo simulated annealing approach. Biopolymers. 33: 1271-86. PMID 7689864 DOI: 10.1002/bip.360330812 |
0.88 |
|
| 1992 |
Englander SW, Englander JJ, McKinnie RE, Ackers GK, Turner GJ, Westrick JA, Gill SJ. Hydrogen exchange measurement of the free energy of structural and allosteric change in hemoglobin. Science (New York, N.Y.). 256: 1684-7. PMID 1609279 |
0.88 |
|
| 1992 |
Englander SW, Mayne L. Protein folding studied using hydrogen-exchange labeling and two-dimensional NMR. Annual Review of Biophysics and Biomolecular Structure. 21: 243-65. PMID 1525469 DOI: 10.1146/annurev.bb.21.060192.001331 |
0.88 |
|
| 1992 |
Mayne L, Paterson Y, Cerasoli D, Englander SW. Effect of antibody binding on protein motions studied by hydrogen-exchange labeling and two-dimensional NMR. Biochemistry. 31: 10678-85. PMID 1384698 DOI: 10.1021/bi00159a006 |
0.88 |
|
| 1991 |
Feng YQ, Wand AJ, Roder H, Englander SW. Chemical exchange in two dimensions in the 1H NMR assignment of cytochrome c. Biophysical Journal. 59: 323-8. PMID 1849027 DOI: 10.1016/S0006-3495(91)82226-3 |
0.88 |
|
| 1991 |
Jeng MF, Englander SW. Stable submolecular folding units in a non-compact form of cytochrome c. Journal of Molecular Biology. 221: 1045-61. PMID 1658332 DOI: 10.1016/0022-2836(91)80191-V |
0.88 |
|
| 1991 |
McKinnie RE, Englander JJ, Englander SW. Hydrogen-exchange labeling study of the allosteric R-state to T-state equilibrium in methemoglobin Chemical Physics. 158: 283-293. DOI: 10.1016/0301-0104(91)87072-4 |
0.88 |
|
| 1990 |
Vanderkooi JM, Englander SW, Papp S, Wright WW, Owen CS. Long-range electron exchange measured in proteins by quenching of tryptophan phosphorescence. Proceedings of the National Academy of Sciences of the United States of America. 87: 5099-103. PMID 2367526 DOI: 10.1073/pnas.87.13.5099 |
0.88 |
|
| 1990 |
Jeng MF, Englander SW, Elöve GA, Wand AJ, Roder H. Structural description of acid-denatured cytochrome c by hydrogen exchange and 2D NMR. Biochemistry. 29: 10433-7. PMID 2176867 |
0.88 |
|
| 1990 |
Feng Y, Roder H, Englander SW. Redox-dependent structure change and hyperfine nuclear magnetic resonance shifts in cytochrome c. Biochemistry. 29: 3494-504. PMID 2162193 |
0.88 |
|
| 1990 |
Feng YQ, Roder H, Englander SW. Assignment of paramagnetically shifted resonances in the 1H NMR spectrum of horse ferricytochrome c. Biophysical Journal. 57: 15-22. PMID 2153419 DOI: 10.1016/S0006-3495(90)82502-9 |
0.88 |
|
| 1990 |
Paterson Y, Englander SW, Roder H. An antibody binding site on cytochrome c defined by hydrogen exchange and two-dimensional NMR. Science (New York, N.Y.). 249: 755-9. PMID 1697101 |
0.88 |
|
| 1989 |
Feng Y, Roder H, Englander SW, Wand AJ, Di Stefano DL. Proton resonance assignments of horse ferricytochrome c. Biochemistry. 28: 195-203. PMID 2539855 |
0.88 |
|
| 1989 |
Wand AJ, Di Stefano DL, Feng YQ, Roder H, Englander SW. Proton resonance assignments of horse ferrocytochrome c. Biochemistry. 28: 186-94. PMID 2539854 |
0.88 |
|
| 1989 |
Kallenbach NR, Cornelius PA, Negus D, Montgomerie D, Englander S. Inactivation of viruses by ultraviolet light. Current Studies in Hematology and Blood Transfusion. 70-82. PMID 2491986 |
0.88 |
|
| 1988 |
Louie G, Englander JJ, Englander SW. Salt, phosphate and the Bohr effect at the hemoglobin beta chain C terminus studied by hydrogen exchange. Journal of Molecular Biology. 201: 765-72. PMID 3172204 DOI: 10.1016/0022-2836(88)90473-1 |
0.88 |
|
| 1988 |
Louie G, Tran T, Englander JJ, Englander SW. Allosteric energy at the hemoglobin beta chain C terminus studied by hydrogen exchange. Journal of Molecular Biology. 201: 755-64. PMID 3172203 DOI: 10.1016/0022-2836(88)90472-X |
0.88 |
|
| 1988 |
Roder H, Elöve GA, Englander SW. Structural characterization of folding intermediates in cytochrome c by H-exchange labelling and proton NMR. Nature. 335: 700-4. PMID 2845279 DOI: 10.1038/335700a0 |
0.88 |
|
| 1988 |
Englander SW, Roder H, Elove G, Louie G, Feng Y. Next dimension of protein structure. Dynamics and energetics Transactions of the American Crystallographic Association. 24: 107-129. |
0.88 |
|
| 1987 |
Englander SW, Wand AJ. Main-chain-directed strategy for the assignment of 1H NMR spectra of proteins. Biochemistry. 26: 5953-8. PMID 3689754 |
0.88 |
|
| 1987 |
Englander JJ, Englander SW. Hydrogen-tritium exchange survey of allosteric effects in hemoglobin. Biochemistry. 26: 1846-50. PMID 3593698 |
0.88 |
|
| 1987 |
Englander SW, Calhoun DB, Englander JJ. Biochemistry without oxygen. Analytical Biochemistry. 161: 300-6. PMID 3578795 DOI: 10.1016/0003-2697(87)90454-4 |
0.88 |
|
| 1987 |
Vanderkooi JM, Calhoun DB, Englander SW. On the prevalence of room-temperature protein phosphorescence. Science (New York, N.Y.). 236: 568-9. PMID 3576185 |
0.88 |
|
| 1986 |
Rogero JR, Englander JJ, Englander SW. Individual breathing reactions measured by functional labeling and hydrogen exchange methods. Methods in Enzymology. 131: 508-17. PMID 3773770 |
0.88 |
|
| 1986 |
Calhoun DB, Vanderkooi JM, Holtom GR, Englander SW. Protein fluorescence quenching by small molecules: protein penetration versus solvent exposure. Proteins. 1: 109-15. PMID 3130621 DOI: 10.1002/prot.340010202 |
0.88 |
|
| 1986 |
Wand AJ, Roder H, Englander SW. Two-dimensional 1H NMR studies of cytochrome c: hydrogen exchange in the N-terminal helix. Biochemistry. 25: 1107-14. PMID 3008820 |
0.88 |
|
| 1986 |
Wand AJ, Englander SW. Two-dimensional 1H NMR studies of cytochrome c: assignment of the N-terminal helix. Biochemistry. 25: 1100-6. PMID 3008819 |
0.88 |
|
| 1985 |
Englander JJ, Rogero JR, Englander SW. Protein hydrogen exchange studied by the fragment separation method. Analytical Biochemistry. 147: 234-44. PMID 2992314 DOI: 10.1016/0003-2697(85)90033-8 |
0.88 |
|
| 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 |
0.88 |
|
| 1983 |
Calhoun DB, Vanderkooi JM, Englander SW. Penetration of small molecules into proteins studied by quenching of phosphorescence and fluorescence Biochemistry. 22: 1533-1539. PMID 6342663 |
0.88 |
|
| 1983 |
Calhoun DB, Vanderkooi JM, Woodrow GV, Englander SW. Penetration of dioxygen into proteins studied by quenching of phosphorescence and fluorescence Biochemistry. 22: 1526-1532. PMID 6342662 |
0.88 |
|
| 1983 |
Englander JJ, Rogero JR, Englander SW. Identification of an allosterically sensitive unfolding unit in hemoglobin Journal of Molecular Biology. 169: 325-344. PMID 6312054 DOI: 10.1016/S0022-2836(83)80186-7 |
0.88 |
|
| 1983 |
Englander SW, Kallenbach NR. Hydrogen exchange and structural dynamics of proteins and nucleic acids. Quarterly Reviews of Biophysics. 16: 521-655. PMID 6204354 |
0.88 |
|
| 1983 |
Oberholtzer JC, Englander SW, Horwitz AF. Hydrogen-bonded conformation of hyaluronate oligosaccharide fragments in aqueous solution Febs Letters. 158: 305-309. DOI: 10.1016/0014-5793(83)80601-2 |
0.88 |
|
| 1982 |
Englander SW. Grant funding [3] Science. 217: 984. PMID 7112115 |
0.88 |
|
| 1982 |
Englander JJ, Downer NW, Englander SW. Re-examination of rhodopsin structure by hydrogen exchange Journal of Biological Chemistry. 257: 7982-7986. PMID 6979541 |
0.88 |
|
| 1981 |
Oberholtzer JC, Englander SW, Horwitz AF. Hydrogen-bonded structure of the complex N-linked fetuin glycopeptide. Biochemistry. 20: 4785-92. PMID 6170315 |
0.88 |
|
| 1980 |
Malin EL, Englander SW. The slowest allosterically responsive hydrogens in hemoglobin. Completion of the hydrogen exchange survey Journal of Biological Chemistry. 255: 10695-10701. PMID 7430145 |
0.88 |
|
| 1980 |
Liem RK, Calhoun DB, Englander JJ, Englander SW. A high energy structure change in hemoglobin studied by difference hydrogen exchange. The Journal of Biological Chemistry. 255: 10687-94. PMID 7430144 |
0.88 |
|
| 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 |
0.88 |
|
| 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 |
0.88 |
|
| 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 |
0.88 |
|
| 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 |
0.88 |
|
| 1960 |
Englander SW, Buzzell A, Lauffer MA. The relationship between inactivation of tobacco mosaic virus by X-rays and breakage of nucleic acid Bba - Biochimica Et Biophysica Acta. 40: 385-392. PMID 13820376 |
0.88 |
|
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