| Year |
Citation |
Score |
| 2013 |
Shivu B, Seshadri S, Li J, Oberg KA, Uversky VN, Fink AL. Distinct β-sheet structure in protein aggregates determined by ATR-FTIR spectroscopy. Biochemistry. 52: 5176-83. PMID 23837615 DOI: 10.1021/Bi400625V |
0.418 |
|
| 2013 |
Zhu M, Han S, Fink AL. Oxidized quercetin inhibits α-synuclein fibrillization. Biochimica Et Biophysica Acta. 1830: 2872-81. PMID 23295967 DOI: 10.1016/J.Bbagen.2012.12.027 |
0.317 |
|
| 2012 |
Ahmad A, Burns CS, Fink AL, Uversky VN. Peculiarities of copper binding to alpha-synuclein. Journal of Biomolecular Structure & Dynamics. 29: 825-42. PMID 22208282 DOI: 10.1080/073911012010525023 |
0.332 |
|
| 2011 |
Levitan K, Chereau D, Cohen SIA, Knowles TPJ, Dobson CM, Fink AL, Anderson JP, Goldstein JM, Millhauser GL. Conserved C-terminal charge exerts a profound influence on the aggregation rate of α-synuclein Journal of Molecular Biology. 411: 329-333. PMID 21689664 DOI: 10.1016/J.Jmb.2011.05.046 |
0.356 |
|
| 2011 |
Hong DP, Han S, Fink AL, Uversky VN. Characterization of the non-fibrillar α-synuclein oligomers. Protein and Peptide Letters. 18: 230-40. PMID 20858207 DOI: 10.2174/092986611794578332 |
0.429 |
|
| 2010 |
Meng X, Munishkina LA, Fink AL, Uversky VN. Effects of Various Flavonoids on the α-Synuclein Fibrillation Process. Parkinson's Disease. 2010: 650794. PMID 20976092 DOI: 10.4061/2010/650794 |
0.353 |
|
| 2010 |
Zhou W, Long C, Reaney SH, Di Monte DA, Fink AL, Uversky VN. Methionine oxidation stabilizes non-toxic oligomers of alpha-synuclein through strengthening the auto-inhibitory intra-molecular long-range interactions. Biochimica Et Biophysica Acta. 1802: 322-30. PMID 20026206 DOI: 10.1016/J.Bbadis.2009.12.004 |
0.37 |
|
| 2010 |
Zhou W, Long C, Fink AL, Uversky VN. 3, 4-Dihydroxyphenylacetic Acid (DOPAC) Impairs α-Synuclein Interaction with Lipids The Open Proteomics Journal. 3: 1-7. DOI: 10.2174/1875039701003010001 |
0.331 |
|
| 2009 |
Meng X, Munishkina LA, Fink AL, Uversky VN. Molecular mechanisms underlying the flavonoid-induced inhibition of alpha-synuclein fibrillation. Biochemistry. 48: 8206-24. PMID 19634918 DOI: 10.1021/Bi900506B |
0.377 |
|
| 2009 |
Zhou W, Gallagher A, Hong DP, Long C, Fink AL, Uversky VN. At low concentrations, 3,4-dihydroxyphenylacetic acid (DOPAC) binds non-covalently to alpha-synuclein and prevents its fibrillation. Journal of Molecular Biology. 388: 597-610. PMID 19328209 DOI: 10.1016/J.Jmb.2009.03.053 |
0.372 |
|
| 2009 |
Hong DP, Fink AL, Uversky VN. Smoking and Parkinson's disease: does nicotine affect alpha-synuclein fibrillation? Biochimica Et Biophysica Acta. 1794: 282-90. PMID 19013262 DOI: 10.1016/J.Bbapap.2008.09.026 |
0.33 |
|
| 2008 |
Munishkina LA, Fink AL, Uversky VN. Concerted action of metals and macromolecular crowding on the fibrillation of alpha-synuclein. Protein and Peptide Letters. 15: 1079-85. PMID 19075819 DOI: 10.2174/092986608786071102 |
0.337 |
|
| 2008 |
Hong DP, Fink AL, Uversky VN. Structural characteristics of alpha-synuclein oligomers stabilized by the flavonoid baicalein. Journal of Molecular Biology. 383: 214-23. PMID 18775438 DOI: 10.1016/J.Jmb.2008.08.039 |
0.42 |
|
| 2008 |
Ulrih NP, Barry CH, Fink AL. Impact of Tyr to Ala mutations on alpha-synuclein fibrillation and structural properties. Biochimica Et Biophysica Acta. 1782: 581-5. PMID 18692132 DOI: 10.1016/J.Bbadis.2008.07.004 |
0.423 |
|
| 2008 |
Munishkina LA, Ahmad A, Fink AL, Uversky VN. Guiding protein aggregation with macromolecular crowding. Biochemistry. 47: 8993-9006. PMID 18665616 DOI: 10.1021/Bi8008399 |
0.432 |
|
| 2008 |
Hu D, Qin Z, Xue B, Fink AL, Uversky VN. Effect of methionine oxidation on the structural properties, conformational stability, and aggregation of immunoglobulin light chain LEN. Biochemistry. 47: 8665-77. PMID 18652490 DOI: 10.1021/Bi800806D |
0.341 |
|
| 2008 |
Meng X, Fink AL, Uversky VN. The effect of membranes on the in vitro fibrillation of an amyloidogenic light-chain variable-domain SMA. Journal of Molecular Biology. 381: 989-99. PMID 18619464 DOI: 10.1016/J.Jmb.2008.06.062 |
0.328 |
|
| 2007 |
Qin Z, Hu D, Han S, Hong DP, Fink AL. Role of different regions of alpha-synuclein in the assembly of fibrils. Biochemistry. 46: 13322-30. PMID 17963364 DOI: 10.1021/Bi7014053 |
0.402 |
|
| 2007 |
Munishkina LA, Fink AL. Fluorescence as a method to reveal structures and membrane-interactions of amyloidogenic proteins. Biochimica Et Biophysica Acta. 1768: 1862-85. PMID 17493579 DOI: 10.1016/J.Bbamem.2007.03.015 |
0.354 |
|
| 2007 |
Qin Z, Hu D, Zhu M, Fink AL. Structural characterization of the partially folded intermediates of an immunoglobulin light chain leading to amyloid fibrillation and amorphous aggregation. Biochemistry. 46: 3521-31. PMID 17315948 DOI: 10.1021/Bi061716V |
0.376 |
|
| 2007 |
Martinez Z, Zhu M, Han S, Fink AL. GM1 specifically interacts with alpha-synuclein and inhibits fibrillation. Biochemistry. 46: 1868-77. PMID 17253773 DOI: 10.1021/Bi061749A |
0.348 |
|
| 2007 |
Qin Z, Hu D, Han S, Reaney SH, Di Monte DA, Fink AL. Effect of 4-hydroxy-2-nonenal modification on alpha-synuclein aggregation. The Journal of Biological Chemistry. 282: 5862-70. PMID 17189262 DOI: 10.1074/Jbc.M608126200 |
0.411 |
|
| 2006 |
Fink AL. The aggregation and fibrillation of alpha-synuclein. Accounts of Chemical Research. 39: 628-34. PMID 16981679 DOI: 10.1021/Ar050073T |
0.412 |
|
| 2006 |
Hong DP, Ahmad A, Fink AL. Fibrillation of human insulin A and B chains. Biochemistry. 45: 9342-53. PMID 16866381 DOI: 10.1021/Bi0604936 |
0.344 |
|
| 2006 |
Zhu M, Qin ZJ, Hu D, Munishkina LA, Fink AL. Alpha-synuclein can function as an antioxidant preventing oxidation of unsaturated lipid in vesicles. Biochemistry. 45: 8135-42. PMID 16800638 DOI: 10.1021/Bi052584T |
0.329 |
|
| 2006 |
Dusa A, Kaylor J, Edridge S, Bodner N, Hong DP, Fink AL. Characterization of oligomers during α-synuclein aggregation using intrinsic tryptophan fluorescence Biochemistry. 45: 2752-2760. PMID 16489768 DOI: 10.1021/Bi051426Z |
0.404 |
|
| 2006 |
Zhou W, Zhu M, Wilson MA, Petsko GA, Fink AL. The oxidation state of DJ-1 regulates its chaperone activity toward alpha-synuclein. Journal of Molecular Biology. 356: 1036-48. PMID 16403519 DOI: 10.1016/J.Jmb.2005.12.030 |
0.376 |
|
| 2005 |
Hong DP, Fink AL. Independent heterologous fibrillation of insulin and its B-chain peptide. Biochemistry. 44: 16701-9. PMID 16342960 DOI: 10.1021/Bi051658Y |
0.314 |
|
| 2005 |
Ahmad A, Uversky VN, Hong D, Fink AL. Early events in the fibrillation of monomeric insulin. The Journal of Biological Chemistry. 280: 42669-75. PMID 16246845 DOI: 10.1074/Jbc.M504298200 |
0.406 |
|
| 2005 |
Kaylor J, Bodner N, Edridge S, Yamin G, Hong DP, Fink AL. Characterization of oligomeric intermediates in α-synuclein fibrillation: FRET studies of Y125W/Y133F/Y136F α-synuclein Journal of Molecular Biology. 353: 357-372. PMID 16171820 DOI: 10.1016/J.Jmb.2005.08.046 |
0.43 |
|
| 2005 |
Liu IH, Uversky VN, Munishkina LA, Fink AL, Halfter W, Cole GJ. Agrin binds alpha-synuclein and modulates alpha-synuclein fibrillation. Glycobiology. 15: 1320-31. PMID 16037493 DOI: 10.1093/Glycob/Cwj014 |
0.385 |
|
| 2005 |
Yamin G, Munishkina LA, Karymov MA, Lyubchenko YL, Uversky VN, Fink AL. Forcing nonamyloidogenic beta-synuclein to fibrillate. Biochemistry. 44: 9096-107. PMID 15966733 DOI: 10.1021/Bi048778A |
0.395 |
|
| 2005 |
Uversky VN, Yamin G, Munishkina LA, Karymov MA, Millett IS, Doniach S, Lyubchenko YL, Fink AL. Effects of nitration on the structure and aggregation of alpha-synuclein. Brain Research. Molecular Brain Research. 134: 84-102. PMID 15790533 DOI: 10.1016/J.Molbrainres.2004.11.014 |
0.426 |
|
| 2005 |
Fink AL. Natively unfolded proteins. Current Opinion in Structural Biology. 15: 35-41. PMID 15718131 DOI: 10.1016/J.Sbi.2005.01.002 |
0.328 |
|
| 2005 |
Glaser CB, Yamin G, Uversky VN, Fink AL. Methionine oxidation, alpha-synuclein and Parkinson's disease. Biochimica Et Biophysica Acta. 1703: 157-69. PMID 15680224 DOI: 10.1016/J.Bbapap.2004.10.008 |
0.359 |
|
| 2004 |
Li J, Zhu M, Rajamani S, Uversky VN, Fink AL. Rifampicin inhibits alpha-synuclein fibrillation and disaggregates fibrils. Chemistry & Biology. 11: 1513-21. PMID 15556002 DOI: 10.1016/J.Chembiol.2004.08.025 |
0.387 |
|
| 2004 |
Munishkina LA, Cooper EM, Uversky VN, Fink AL. The effect of macromolecular crowding on protein aggregation and amyloid fibril formation. Journal of Molecular Recognition : Jmr. 17: 456-64. PMID 15362105 DOI: 10.1002/Jmr.699 |
0.369 |
|
| 2004 |
Munishkina LA, Fink AL, Uversky VN. Conformational prerequisites for formation of amyloid fibrils from histones. Journal of Molecular Biology. 342: 1305-24. PMID 15351653 DOI: 10.1016/J.Jmb.2004.06.094 |
0.411 |
|
| 2004 |
Uversky VN, Fink AL. Conformational constraints for amyloid fibrillation: the importance of being unfolded. Biochimica Et Biophysica Acta. 1698: 131-53. PMID 15134647 DOI: 10.1016/J.Bbapap.2003.12.008 |
0.44 |
|
| 2004 |
Zhu M, Rajamani S, Kaylor J, Han S, Zhou F, Fink AL. The flavonoid baicalein inhibits fibrillation of α-synuclein and disaggregates existing fibrils Journal of Biological Chemistry. 279: 26846-26857. PMID 15096521 DOI: 10.1074/Jbc.M403129200 |
0.394 |
|
| 2004 |
Hokenson MJ, Uversky VN, Goers J, Yamin G, Munishkina LA, Fink AL. Role of individual methionines in the fibrillation of methionine-oxidized alpha-synuclein. Biochemistry. 43: 4621-33. PMID 15078109 DOI: 10.1021/Bi049979H |
0.394 |
|
| 2004 |
Li J, Zhu M, Manning-Bog AB, Di Monte DA, Fink AL. Dopamine and L-dopa disaggregate amyloid fibrils: implications for Parkinson's and Alzheimer's disease. Faseb Journal : Official Publication of the Federation of American Societies For Experimental Biology. 18: 962-4. PMID 15059976 DOI: 10.1096/Fj.03-0770Fje |
0.309 |
|
| 2004 |
Zhu M, Han S, Zhou F, Carter SA, Fink AL. Annular oligomeric amyloid intermediates observed by in situ atomic force microscopy Journal of Biological Chemistry. 279: 24452-24459. PMID 15056656 DOI: 10.1074/Jbc.M400004200 |
0.404 |
|
| 2004 |
Munishkina LA, Henriques J, Uversky VN, Fink AL. Role of protein-water interactions and electrostatics in alpha-synuclein fibril formation. Biochemistry. 43: 3289-300. PMID 15023080 DOI: 10.1021/Bi034938R |
0.418 |
|
| 2004 |
Ahmad A, Millett IS, Doniach S, Uversky VN, Fink AL. Stimulation of insulin fibrillation by urea-induced intermediates. The Journal of Biological Chemistry. 279: 14999-5013. PMID 14736893 DOI: 10.1074/Jbc.M313134200 |
0.365 |
|
| 2003 |
Ahmad A, Millett IS, Doniach S, Uversky VN, Fink AL. Partially folded intermediates in insulin fibrillation. Biochemistry. 42: 11404-16. PMID 14516191 DOI: 10.1021/Bi034868O |
0.377 |
|
| 2003 |
Khurana R, Souillac PO, Coats AC, Minert L, Ionescu-Zanetti C, Carter SA, Solomon A, Fink AL. A model for amyloid fibril formation in immunoglobulin light chains based on comparison of amyloidogenic and benign proteins and specific antibody binding. Amyloid : the International Journal of Experimental and Clinical Investigation : the Official Journal of the International Society of Amyloidosis. 10: 97-109. PMID 12964417 DOI: 10.3109/13506120309041731 |
0.375 |
|
| 2003 |
Zhu M, Li J, Fink AL. The association of alpha-synuclein with membranes affects bilayer structure, stability, and fibril formation. The Journal of Biological Chemistry. 278: 40186-97. PMID 12885775 DOI: 10.1074/Jbc.M305326200 |
0.365 |
|
| 2003 |
Khurana R, Ionescu-Zanetti C, Pope M, Li J, Nielson L, Ramírez-Alvarado M, Regan L, Fink AL, Carter SA. A general model for amyloid fibril assembly based on morphological studies using atomic force microscopy. Biophysical Journal. 85: 1135-44. PMID 12885658 DOI: 10.1016/S0006-3495(03)74550-0 |
0.357 |
|
| 2003 |
Goers J, Manning-Bog AB, McCormack AL, Millett IS, Doniach S, Di Monte DA, Uversky VN, Fink AL. Nuclear localization of alpha-synuclein and its interaction with histones. Biochemistry. 42: 8465-71. PMID 12859192 DOI: 10.1021/Bi0341152 |
0.346 |
|
| 2003 |
Berriman J, Serpell LC, Oberg KA, Fink AL, Goedert M, Crowther RA. Tau filaments from human brain and from in vitro assembly of recombinant protein show cross-beta structure. Proceedings of the National Academy of Sciences of the United States of America. 100: 9034-8. PMID 12853572 DOI: 10.1073/Pnas.1530287100 |
0.321 |
|
| 2003 |
Souillac PO, Uversky VN, Fink AL. Structural transformations of oligomeric intermediates in the fibrillation of the immunoglobulin light chain LEN. Biochemistry. 42: 8094-104. PMID 12834361 DOI: 10.1021/Bi034652M |
0.44 |
|
| 2003 |
Yamin G, Glaser CB, Uversky VN, Fink AL. Certain metals trigger fibrillation of methionine-oxidized alpha-synuclein. The Journal of Biological Chemistry. 278: 27630-5. PMID 12754258 DOI: 10.1074/Jbc.M303302200 |
0.358 |
|
| 2003 |
Yamin G, Uversky VN, Fink AL. Nitration inhibits fibrillation of human alpha-synuclein in vitro by formation of soluble oligomers. Febs Letters. 542: 147-52. PMID 12729915 DOI: 10.1016/S0014-5793(03)00367-3 |
0.365 |
|
| 2003 |
Goers J, Uversky VN, Fink AL. Polycation-induced oligomerization and accelerated fibrillation of human alpha-synuclein in vitro. Protein Science : a Publication of the Protein Society. 12: 702-7. PMID 12649428 DOI: 10.1110/Ps.0230903 |
0.39 |
|
| 2003 |
Zhu M, Fink AL. Lipid binding inhibits alpha-synuclein fibril formation. The Journal of Biological Chemistry. 278: 16873-7. PMID 12621030 DOI: 10.1074/Jbc.M210136200 |
0.389 |
|
| 2003 |
Munishkina LA, Phelan C, Uversky VN, Fink AL. Conformational behavior and aggregation of α-synuclein in organic solvents: Modeling the effects of membranes Biochemistry. 42: 2720-2730. PMID 12614167 DOI: 10.1021/Bi027166S |
0.382 |
|
| 2003 |
Denning DP, Patel SS, Uversky V, Fink AL, Rexach M. Disorder in the nuclear pore complex: the FG repeat regions of nucleoporins are natively unfolded. Proceedings of the National Academy of Sciences of the United States of America. 100: 2450-5. PMID 12604785 DOI: 10.1073/Pnas.0437902100 |
0.319 |
|
| 2002 |
Uversky VN, Permyakov SE, Zagranichny VE, Rodionov IL, Fink AL, Cherskaya AM, Wasserman LA, Permyakov EA. Effect of zinc and temperature on the conformation of the gamma subunit of retinal phosphodiesterase: a natively unfolded protein. Journal of Proteome Research. 1: 149-59. PMID 12643535 DOI: 10.1021/Pr0155127 |
0.38 |
|
| 2002 |
Li J, Uversky VN, Fink AL. Conformational behavior of human alpha-synuclein is modulated by familial Parkinson's disease point mutations A30P and A53T. Neurotoxicology. 23: 553-67. PMID 12428728 DOI: 10.1016/S0161-813X(02)00066-9 |
0.47 |
|
| 2002 |
Uversky VN, Li J, Bower K, Fink AL. Synergistic effects of pesticides and metals on the fibrillation of alpha-synuclein: implications for Parkinson's disease. Neurotoxicology. 23: 527-36. PMID 12428725 DOI: 10.1016/S0161-813X(02)00067-0 |
0.344 |
|
| 2002 |
Goers J, Permyakov SE, Permyakov EA, Uversky VN, Fink AL. Conformational prerequisites for alpha-lactalbumin fibrillation. Biochemistry. 41: 12546-51. PMID 12369846 DOI: 10.1021/Bi0262698 |
0.453 |
|
| 2002 |
Zhu M, Souillac PO, Ionescu-Zanetti C, Carter SA, Fink AL. Surface-catalyzed amyloid fibril formation. The Journal of Biological Chemistry. 277: 50914-22. PMID 12356747 DOI: 10.1074/Jbc.M207225200 |
0.335 |
|
| 2002 |
Uversky VN, Fink AL. Amino acid determinants of alpha-synuclein aggregation: putting together pieces of the puzzle. Febs Letters. 522: 9-13. PMID 12095610 DOI: 10.1016/S0014-5793(02)02883-1 |
0.382 |
|
| 2002 |
Denning DP, Uversky V, Patel SS, Fink AL, Rexach M. The Saccharomyces cerevisiae nucleoporin Nup2p is a natively unfolded protein. The Journal of Biological Chemistry. 277: 33447-55. PMID 12065587 DOI: 10.1074/Jbc.M203499200 |
0.369 |
|
| 2002 |
Uversky VN, Yamin G, Souillac PO, Goers J, Glaser CB, Fink AL. Methionine oxidation inhibits fibrillation of human alpha-synuclein in vitro. Febs Letters. 517: 239-44. PMID 12062445 DOI: 10.1016/S0014-5793(02)02638-8 |
0.381 |
|
| 2002 |
Kuznetsova IM, Stepanenko OV, Turoverov KK, Zhu L, Zhou JM, Fink AL, Uversky VN. Unraveling multistate unfolding of rabbit muscle creatine kinase. Biochimica Et Biophysica Acta. 1596: 138-55. PMID 11983429 DOI: 10.1016/S0167-4838(02)00212-1 |
0.319 |
|
| 2002 |
Uversky VN, M Cooper E, Bower KS, Li J, Fink AL. Accelerated alpha-synuclein fibrillation in crowded milieu. Febs Letters. 515: 99-103. PMID 11943202 DOI: 10.1016/S0014-5793(02)02446-8 |
0.404 |
|
| 2002 |
Uversky VN, Fink AL. The chicken-egg scenario of protein folding revisited. Febs Letters. 515: 79-83. PMID 11943199 DOI: 10.1016/S0014-5793(02)02441-9 |
0.405 |
|
| 2002 |
Souillac PO, Uversky VN, Millett IS, Khurana R, Doniach S, Fink AL. Effect of association state and conformational stability on the kinetics of immunoglobulin light chain amyloid fibril formation at physiological pH. The Journal of Biological Chemistry. 277: 12657-65. PMID 11815605 DOI: 10.1074/Jbc.M109230200 |
0.434 |
|
| 2002 |
Souillac PO, Uversky VN, Millett IS, Khurana R, Doniach S, Fink AL. Elucidation of the molecular mechanism during the early events in immunoglobulin light chain amyloid fibrillation. Evidence for an off-pathway oligomer at acidic pH. The Journal of Biological Chemistry. 277: 12666-79. PMID 11815604 DOI: 10.1074/Jbc.M109229200 |
0.416 |
|
| 2002 |
Cohlberg JA, Li J, Uversky VN, Fink AL. Heparin and other glycosaminoglycans stimulate the formation of amyloid fibrils from alpha-synuclein in vitro. Biochemistry. 41: 1502-11. PMID 11814343 DOI: 10.1021/Bi011711S |
0.396 |
|
| 2002 |
Uversky VN, Li J, Fink AL. Trimethylamine-N-oxide-induced folding of alpha-synuclein. Febs Letters. 509: 31-5. PMID 11734201 DOI: 10.1016/S0014-5793(01)03121-0 |
0.43 |
|
| 2002 |
Manning-Bog AB, McCormack AL, Li J, Uversky VN, Fink AL, Di Monte DA. The herbicide paraquat causes up-regulation and aggregation of alpha-synuclein in mice: paraquat and alpha-synuclein. The Journal of Biological Chemistry. 277: 1641-4. PMID 11707429 DOI: 10.1074/Jbc.C100560200 |
0.363 |
|
| 2001 |
Uversky VN, Lee HJ, Li J, Fink AL, Lee SJ. Stabilization of partially folded conformation during alpha-synuclein oligomerization in both purified and cytosolic preparations. The Journal of Biological Chemistry. 276: 43495-8. PMID 11590163 DOI: 10.1074/Jbc.C100551200 |
0.425 |
|
| 2001 |
Li J, Uversky VN, Fink AL. Effect of familial Parkinson's disease point mutations A30P and A53T on the structural properties, aggregation, and fibrillation of human alpha-synuclein. Biochemistry. 40: 11604-13. PMID 11560511 DOI: 10.1021/Bi010616G |
0.399 |
|
| 2001 |
Uversky VN, Li J, Fink AL. Metal-triggered structural transformations, aggregation, and fibrillation of human alpha-synuclein. A possible molecular NK between Parkinson's disease and heavy metal exposure. The Journal of Biological Chemistry. 276: 44284-96. PMID 11553618 DOI: 10.1074/Jbc.M105343200 |
0.36 |
|
| 2001 |
Uversky VN, Li J, Fink AL. Pesticides directly accelerate the rate of alpha-synuclein fibril formation: a possible factor in Parkinson's disease. Febs Letters. 500: 105-8. PMID 11445065 DOI: 10.1016/S0014-5793(01)02597-2 |
0.394 |
|
| 2001 |
Nielsen L, Frokjaer S, Brange J, Uversky VN, Fink AL. Probing the mechanism of insulin fibril formation with insulin mutants. Biochemistry. 40: 8397-409. PMID 11444987 DOI: 10.1021/Bi0105983 |
0.367 |
|
| 2001 |
Khurana R, Uversky VN, Nielsen L, Fink AL. Is Congo Red an Amyloid-specific Dye? Journal of Biological Chemistry. 276: 22715-22721. PMID 11410601 DOI: 10.1074/Jbc.M011499200 |
0.407 |
|
| 2001 |
Nielsen L, Khurana R, Coats A, Frokjaer S, Brange J, Vyas S, Uversky VN, Fink AL. Effect of environmental factors on the kinetics of insulin fibril formation: Elucidation of the molecular mechanism Biochemistry. 40: 6036-6046. PMID 11352739 DOI: 10.1021/Bi002555C |
0.355 |
|
| 2001 |
Nishimura C, Uversky VN, Fink AL. Effect of salts on the stability and folding of staphylococcal nuclease. Biochemistry. 40: 2113-28. PMID 11329280 DOI: 10.1021/Bi000861K |
0.395 |
|
| 2001 |
Khurana R, Gillespie JR, Talapatra A, Minert LJ, Ionescu-Zanetti C, Millett I, Fink AL. Partially folded intermediates as critical precursors of light chain amyloid fibrils and amorphous aggregates Biochemistry. 40: 3525-3535. PMID 11297418 DOI: 10.1021/Bi001782B |
0.455 |
|
| 2001 |
Uversky VN, Li J, Fink AL. Evidence for a partially folded intermediate in alpha-synuclein fibril formation. The Journal of Biological Chemistry. 276: 10737-44. PMID 11152691 DOI: 10.1074/Jbc.M010907200 |
0.444 |
|
| 2000 |
Uversky VN, Gillespie JR, Fink AL. Why are "natively unfolded" proteins unstructured under physiologic conditions? Proteins. 41: 415-27. PMID 11025552 DOI: 10.1002/1097-0134(20001115)41:3<415::Aid-Prot130>3.0.Co;2-7 |
0.369 |
|
| 2000 |
Frate MC, Lietz EJ, Santos J, Rossi JPFC, Fink AL, Ermácora MR. Export and folding of signal‐sequenceless Bacillus licheniformisβ‐lactamase in Escherichia coli Febs Journal. 267: 3836-3847. PMID 10849003 DOI: 10.1046/J.1432-1327.2000.01422.X |
0.356 |
|
| 2000 |
Nishimura C, Riley R, Eastman P, Fink AL. Fluorescence energy transfer indicates similar transient and equilibrium intermediates in staphylococcal nuclease folding. Journal of Molecular Biology. 299: 1133-1146. PMID 10843864 DOI: 10.1006/Jmbi.2000.3804 |
0.422 |
|
| 2000 |
Hokenson MJ, Cope GA, Lewis ER, Oberg KA, Fink AL. Enzyme-induced strain/distortion in the ground-state ES complex in beta-lactamase catalysis revealed by FTIR. Biochemistry. 39: 6538-45. PMID 10828970 DOI: 10.1021/Bi9928041 |
0.302 |
|
| 2000 |
Lietz EJ, Truher H, Kahn D, Hokenson MJ, Fink AL. Lysine-73 is involved in the acylation and deacylation of β-lactamase Biochemistry. 39: 4971-4981. PMID 10819961 DOI: 10.1021/Bi992681K |
0.316 |
|
| 2000 |
Khurana R, Fink AL. Do parallel β-helix proteins have a unique Fourier transform infrared spectrum? Biophysical Journal. 78: 994-1000. PMID 10653812 DOI: 10.1016/S0006-3495(00)76657-4 |
0.322 |
|
| 2000 |
Uversky VN, Gillespie JR, Millett IS, Khodyakova AV, Vasilenko RN, Vasiliev AM, Rodionov IL, Kozlovskaya GD, Dolgikh DA, Fink AL, Doniach S, Permyakov EA, Abramov VM. Zn(2+)-mediated structure formation and compaction of the "natively unfolded" human prothymosin alpha. Biochemical and Biophysical Research Communications. 267: 663-8. PMID 10631119 DOI: 10.1006/Bbrc.1999.2013 |
0.411 |
|
| 2000 |
Fezoui Y, Hartley DM, Harper JD, Khurana R, Walsh DM, Condron MM, Fink AL, Teplow DB. An improved method of preparing the amyloid β-protein for fibrillogenesis and neurotoxicity experiments Neurobiology of Aging. 21: 77. DOI: 10.1016/S0197-4580(00)82569-5 |
0.303 |
|
| 1999 |
Segel DJ, Eliezer D, Uversky V, Fink AL, Hodgson KO, Doniach S. Transient dimer in the refolding kinetics of cytochrome c characterized by small-angle X-ray scattering. Biochemistry. 38: 15352-9. PMID 10563821 DOI: 10.1021/Bi991337K |
0.365 |
|
| 1999 |
Lonescu-Zanetti C, Khurana R, Gillespie JR, Petrick JS, Trabachino LC, Minert LJ, Carter SA, Fink AL. Monitoring the assembly of Ig light-chain amyloid fibrils by atomic force microscopy Proceedings of the National Academy of Sciences of the United States of America. 96: 13175-13179. PMID 10557293 DOI: 10.1073/Pnas.96.23.13175 |
0.34 |
|
| 1999 |
Uversky VN, Gillespie JR, Millett IS, Khodyakova AV, Vasiliev AM, Chernovskaya TV, Vasilenko RN, Kozlovskaya GD, Dolgikh DA, Fink AL, Doniach S, Abramov VM. Natively unfolded human prothymosin alpha adopts partially folded collapsed conformation at acidic pH. Biochemistry. 38: 15009-16. PMID 10555983 DOI: 10.1021/Bi990752+ |
0.421 |
|
| 1999 |
Fink AL. Chaperone-Mediated Protein Folding Physiological Reviews. 79: 425-449. PMID 10221986 DOI: 10.1152/Physrev.1999.79.2.425 |
0.356 |
|
| 1999 |
Uversky VN, Karnoup AS, Khurana R, Segel DJ, Doniach S, Fink AL. Association of partially-folded intermediates of staphylococcal nuclease induces structure and stability. Protein Science : a Publication of the Protein Society. 8: 161-73. PMID 10210194 DOI: 10.1110/Ps.8.1.161 |
0.429 |
|
| 1998 |
Chirico WJ, Markey ML, Fink AL. Conformational Changes of an Hsp70 Molecular Chaperone Induced by Nucleotides, Polypeptides, and N-Ethylmaleimide† Biochemistry. 37: 13862-13870. PMID 9753476 DOI: 10.1021/Bi980597J |
0.348 |
|
| 1998 |
Segel DJ, Fink AL, Hodgson KO, Doniach S. Protein denaturation: a small-angle X-ray scattering study of the ensemble of unfolded states of cytochrome c. Biochemistry. 37: 12443-51. PMID 9730816 DOI: 10.1021/Bi980535T |
0.323 |
|
| 1998 |
Uversky VN, Karnoup AS, Segel DJ, Seshadri S, Doniach S, Fink AL. Anion-induced folding of Staphylococcal nuclease: characterization of multiple equilibrium partially folded intermediates. Journal of Molecular Biology. 278: 879-94. PMID 9614949 DOI: 10.1006/Jmbi.1998.1741 |
0.39 |
|
| 1998 |
Uversky VN, Segel DJ, Doniach S, Fink AL. Association-induced folding of globular proteins. Proceedings of the National Academy of Sciences of the United States of America. 95: 5480-3. PMID 9576907 DOI: 10.1073/Pnas.95.10.5480 |
0.437 |
|
| 1998 |
Fink AL, Oberg KA, Seshadri S. Discrete intermediates versus molten globule models for protein folding: characterization of partially folded intermediates of apomyoglobin. Folding and Design. 3: 19-25. PMID 9502317 DOI: 10.1016/S1359-0278(98)00005-4 |
0.425 |
|
| 1998 |
Fink AL. Protein aggregation: folding aggregates, inclusion bodies and amyloid Folding and Design. 3. PMID 9502314 DOI: 10.1016/S1359-0278(98)00002-9 |
0.382 |
|
| 1998 |
Oberg KA, Fink AL. A New Attenuated Total Reflectance Fourier Transform Infrared Spectroscopy Method for the Study of Proteins in Solution Analytical Biochemistry. 256: 92-106. PMID 9466802 DOI: 10.1006/Abio.1997.2486 |
0.306 |
|
| 1997 |
Veeraraghavan S, Nall BT, Fink AL. Effect of prolyl isomerase on the folding reactions of staphylococcal nuclease Biochemistry. 36: 15134-15139. PMID 9398241 DOI: 10.1021/Bi971357R |
0.322 |
|
| 1996 |
Reid KL, Fink AL. Physical interactions between members of the DnaK chaperone machinery: characterization of the DnaK.GrpE complex. Cell Stress & Chaperones. 1: 127-37. PMID 9222598 DOI: 10.1379/1466-1268(1996)001<0127:Pibmot>2.3.Co;2 |
0.351 |
|
| 1995 |
Osuna J, Viadiu H, Fink AL, Soberón X. Substitution of Asp for Asn at Position 132 in the Active Site of TEM -Lactamase ACTIVITY TOWARD DIFFERENT SUBSTRATES AND EFFECTS OF NEIGHBORING RESIDUES Journal of Biological Chemistry. 270: 775-780. DOI: 10.1074/Jbc.270.2.775 |
0.331 |
|
| 1995 |
Oberg KA, Fink AL. Methods for collecting and analyzing attenuated total reflectance FTIR spectra of proteins in solution Techniques in Protein Chemistry. 6: 475-484. DOI: 10.1016/S1080-8914(06)80058-X |
0.323 |
|
| 1995 |
Palleros DR, Shi L, Reid K, Fink A. Hsp70-protein complexes: Their characterization by size-exclusion HPLC Techniques in Protein Chemistry. 6: 467-474. DOI: 10.1016/S1080-8914(06)80057-8 |
0.317 |
|
| 1994 |
Seshadri S, Oberg KA, Fink AL. Thermally denatured ribonuclease A retains secondary structure as shown by FTIR. Biochemistry. 33: 1351-5. PMID 8312253 DOI: 10.1021/Bi00172A010 |
0.372 |
|
| 1994 |
Oberg K, Chrunyk BA, Wetzel R, Fink AL. Native-like Secondary Structure in Interleukin-1.beta. Inclusion Bodies by Attenuated Total Reflectance FTIR Biochemistry. 33: 2628-2634. PMID 8117725 DOI: 10.1021/Bi00175A035 |
0.332 |
|
| 1994 |
Goto Y, Fink AL. Acid-Induced Folding Of Heme Proteins Methods in Enzymology. 232: 3-15. PMID 8057867 DOI: 10.1016/0076-6879(94)32039-X |
0.328 |
|
| 1994 |
Shi L, Palleros DR, Fink AL. Protein conformational changes induced by 1,1'-bis(4-anilino-5-naphthalenesulfonic acid): preferential binding to the molten globule of DnaK. Biochemistry. 33: 7536-7546. PMID 8011619 DOI: 10.1021/Bi00190A006 |
0.366 |
|
| 1994 |
Fink AL, Calciano LJ, Goto Y, Kurotsu T, Palleros DR. Classification of Acid Denaturation of Proteins: Intermediates and Unfolded States Biochemistry. 33: 12504-12511. PMID 7918473 DOI: 10.1021/Bi00207A018 |
0.398 |
|
| 1994 |
Escobar WA, Tan AK, Lewis ER, Fink AL. Site-directed mutagenesis of glutamate-166 in beta-lactamase leads to a branched path mechanism. Biochemistry. 33: 7619-26. PMID 7912106 DOI: 10.1021/Bi00190A015 |
0.363 |
|
| 1993 |
Palleros DR, Shi L, Reid KL, Fink AL. Three-state denaturation of DnaK induced by guanidine hydrochloride. Evidence for an expandable intermediate. Biochemistry. 32: 4314-21. PMID 8476860 DOI: 10.1021/Bi00067A021 |
0.347 |
|
| 1993 |
De Young LR, Dill KA, Fink AL. Aggregation and denaturation of apomyoglobin in aqueous urea solutions. Biochemistry. 32: 3877-86. PMID 8471600 DOI: 10.1021/Bi00066A006 |
0.418 |
|
| 1993 |
Nakano T, Antonino LC, Fox RO, Fink AL. Effect of proline mutations on the stability and kinetics of folding of staphylococcal nuclease. Biochemistry. 32: 2534-41. PMID 8448112 DOI: 10.1021/Bi00061A010 |
0.36 |
|
| 1993 |
Knox JR, Moews PC, Escobar WA, Fink AL. A catalytically-impaired class A β-lactamase : 2 Å crystal structure and kinetics of the Bacillus licheniformis E166A mutant Protein Engineering. 6: 11-18. PMID 8433965 DOI: 10.1093/Protein/6.1.11 |
0.342 |
|
| 1993 |
Palleros DR, Reid KL, Shi L, Welch WJ, Fink AL. ATP-induced protein-Hsp70 complex dissociation requires K+ but not ATP hydrolysis. Nature. 365: 664-6. PMID 8413631 DOI: 10.1038/365664A0 |
0.32 |
|
| 1993 |
Hamada D, Hoshino M, Kataoka M, Fink AL, Goto Y. Intermediate conformational states of apocytochrome c Biochemistry. 32: 10351-10358. PMID 8399178 DOI: 10.1021/Bi00090A010 |
0.367 |
|
| 1993 |
Hagihara Y, Aimoto S, Fink AL, Goto Y. Guanidine hydrochloride-induced folding of proteins. Journal of Molecular Biology. 231: 180-184. PMID 8389881 DOI: 10.1006/Jmbi.1993.1272 |
0.398 |
|
| 1993 |
Fink AL, Calciano LJ, Goto Y, Nishimura M, Swedberg SA. Characterization of the stable, acid-induced, molten globule-like state of staphylococcal nuclease. Protein Science. 2: 1155-1160. PMID 8358298 DOI: 10.1002/Pro.5560020710 |
0.39 |
|
| 1993 |
Palleros DR, Reid KL, Shi L, Fink AL. DnaK ATPase activity revisited. Febs Letters. 336: 124-8. PMID 8262193 DOI: 10.1016/0014-5793(93)81624-9 |
0.32 |
|
| 1993 |
De Young LR, Fink AL, Dill KA. Aggregation of globular proteins Accounts of Chemical Research. 26: 614-620. DOI: 10.1021/Ar00036A002 |
0.362 |
|
| 1992 |
Lustig B, Fink AL. Secondary structure formation precedes tertiary structure in the refolding of ribonuclease A. Biochimica Et Biophysica Acta. 1121: 229-33. PMID 1599946 DOI: 10.1016/0167-4838(92)90359-L |
0.342 |
|
| 1992 |
Lustig B, Fink AL. The thermal denaturation of ribonuclease A in aqueous-methanol solvents. Biochimica Et Biophysica Acta. 1119: 205-10. PMID 1540654 DOI: 10.1016/0167-4838(92)90393-R |
0.4 |
|
| 1991 |
Palleros DR, Welch WJ, Fink AL. Interaction of hsp70 with unfolded proteins: effects of temperature and nucleotides on the kinetics of binding. Proceedings of the National Academy of Sciences of the United States of America. 88: 5719-5723. PMID 1829527 DOI: 10.1073/Pnas.88.13.5719 |
0.349 |
|
| 1991 |
Escobar WA, Tan AK, Fink AL. Site-directed mutagenesis of .beta.-lactamase leading to accumulation of a catalytic intermediate Biochemistry. 30: 10783-10787. PMID 1681903 DOI: 10.1021/Bi00108A025 |
0.327 |
|
| 1991 |
Antonino LC, Kautz RA, Nakano T, Fox RO, Fink AL. Cold denaturation and 2H2O stabilization of a staphylococcal nuclease mutant. Proceedings of the National Academy of Sciences of the United States of America. 88: 7715-8. PMID 1652762 DOI: 10.1073/Pnas.88.17.7715 |
0.377 |
|
| 1990 |
Goto Y, Fink AL. Phase diagram for acidic conformational states of apomyoglobin Journal of Molecular Biology. 214: 803-805. PMID 2388268 DOI: 10.1016/0022-2836(90)90334-I |
0.32 |
|
| 1990 |
Swedberg SA, Pesek JJ, Fink AL. Attenuated total reflectance Fourier transform infrared analysis of an acyl-enzyme intermediate of α-chymotrypsin Analytical Biochemistry. 186: 153-158. PMID 2356965 DOI: 10.1016/0003-2697(90)90589-2 |
0.353 |
|
| 1990 |
Goto Y, Takahashi N, Fink AL. Mechanism of acid-induced folding of proteins. Biochemistry. 29: 3480-3488. PMID 2162192 DOI: 10.1021/Bi00466A009 |
0.342 |
|
| 1990 |
Goto Y, Calciano LJ, Fink AL. Acid-induced folding of proteins Proceedings of the National Academy of Sciences of the United States of America. 87: 573-577. PMID 2153957 DOI: 10.1073/Pnas.87.2.573 |
0.399 |
|
| 1990 |
Virden R, Tan AK, Fink AL. Cryoenzymology of staphylococcal beta-lactamase: trapping a serine-70-linked acyl-enzyme. Biochemistry. 29: 145-153. PMID 2108714 DOI: 10.1021/Bi00453A018 |
0.352 |
|
| 1990 |
Ellerby LM, Escobar WA, Fink AL, Mitchinson C, Wells JA. The role of lysine-234 in beta-lactamase catalysis probed by site-directed mutagenesis. Biochemistry. 29: 5797-806. PMID 1974463 DOI: 10.1021/Bi00476A022 |
0.372 |
|
| 1989 |
Goto Y, Fink AL. Conformational states in .beta.-lactamase: molten-globule states at acidic and alkaline pH with high salt Biochemistry. 28: 945-952. PMID 2496758 DOI: 10.1021/Bi00429A004 |
0.367 |
|
| 1988 |
Fink AL, Anderson WD, Hattersley JE, Lustig BS. The effect of methanol and temperature on the kinetics of refolding of ribonuclease A. Febs Letters. 236: 190-4. PMID 3402613 DOI: 10.1016/0014-5793(88)80312-0 |
0.36 |
|
| 1988 |
Biringer RG, Fink AL. Intermediates in the refolding of ribonuclease at subzero temperatures. 3. Multiple folding pathways. Biochemistry. 27: 315-325. PMID 3349035 DOI: 10.1021/Bi00401A048 |
0.41 |
|
| 1988 |
Biringer RG, Fink AL. Intermediates in the refolding of ribonuclease at subzero temperatures. 1. Monitoring by nitrotyrosine absorbance. Biochemistry. 27: 301-311. PMID 3349034 DOI: 10.1021/Bi00401A046 |
0.402 |
|
| 1988 |
Fink AL, Anderson WD, Antonino L. Trapping the fast-refolding state of ribonuclease A at subzero temperatures Febs Letters. 229: 123-126. PMID 3345833 DOI: 10.1016/0014-5793(88)80810-X |
0.375 |
|
| 1988 |
Berry SC, Fink AL, Shenvi AB, Kettner CA. Interaction of peptide boronic acids with elastase: circular dichroism studies. Proteins. 4: 205-210. PMID 3237718 DOI: 10.1002/Prot.340040307 |
0.329 |
|
| 1988 |
Biringer RG, Austin CM, Fink AL. Intermediates in the refolding of ribonuclease at subzero temperatures. 2. Monitoring by inhibitor binding and catalytic activity Biochemistry. 27: 311-315. PMID 2831957 DOI: 10.1021/Bi00401A047 |
0.334 |
|
| 1987 |
Fink AL, Painter B. Characterization of the unfolding of ribonuclease A in aqueous methanol solvents. Biochemistry. 26: 1665-1671. PMID 3593684 DOI: 10.1021/Bi00380A027 |
0.381 |
|
| 1987 |
Fink AL, Behner KM, Tan AK. Kinetic and structural characterization of reversibly inactivated beta-lactamase. Biochemistry. 26: 4248-4258. PMID 3117100 DOI: 10.1021/Bi00388A011 |
0.392 |
|
| 1987 |
Coll RJ, Fink AL. Cryoenzymology of human plasmin catalysis: comparison of cryosolvents and reactions with nitrophenyl ester and anilide substrates. Cryobiology. 24: 332-344. PMID 2957172 DOI: 10.1016/0011-2240(87)90037-X |
0.34 |
|
| 1986 |
Fink AL. Effects of cryoprotectants on enzyme structure. Cryobiology. 23: 28-37. PMID 3956227 DOI: 10.1016/0011-2240(86)90015-5 |
0.376 |
|
| 1986 |
Fink AL. [10]Protein folding in cryosolvents and at subzero temperatures Methods in Enzymology. 131: 173-185. PMID 3773757 DOI: 10.1016/0076-6879(86)31041-3 |
0.338 |
|
| 1985 |
Fink AL. The Molecular Basis of β-Lactamase Catalysis and Inhibition. Pharmaceutical Research. 2: 55-61. PMID 24272608 DOI: 10.1023/A:1016378325438 |
0.311 |
|
| 1984 |
Dunn BM, Fink AL. Cryoenzymology of porcine pepsin Biochemistry. 23: 5241-5247. PMID 6439238 DOI: 10.1021/Bi00317A023 |
0.387 |
|
| 1984 |
Hofmann T, Fink AL. Cryoenzymology of penicillopepsin Biochemistry. 23: 5247-5256. PMID 6391539 DOI: 10.1021/Bi00317A024 |
0.377 |
|
| 1984 |
Compton PD, Fink AL. Low-temperature reactions of trypsin with p-nitroanilide substrates: tetrahedral intermediate formation or enzyme isomerization. Biochemistry. 23: 2989-94. PMID 6087885 DOI: 10.1021/Bi00308A022 |
0.363 |
|
| 1984 |
Fink AL, Magnusdottir K. Cryoenzymology of β-Galactosidase: Effects of cryosolvents Journal of Protein Chemistry. 3: 229-241. DOI: 10.1007/Bf01034892 |
0.34 |
|
| 1982 |
Biringer RG, Fink AL. Methanol-stabilized intermediates in the thermal unfolding of ribonuclease A. Characterization by 1H nuclear magnetic resonance. Journal of Molecular Biology. 160: 87-116. PMID 7175932 DOI: 10.1016/0022-2836(82)90133-4 |
0.363 |
|
| 1982 |
Biringer RG, Fink AL. Observation of intermediates in the folding of ribonuclease A at low temperature using proton nuclear magnetic resonance. Biochemistry. 21: 4748-4755. PMID 7138825 DOI: 10.1021/Bi00262A035 |
0.356 |
|
| 1982 |
Coll RJ, Compton PD, Fink AL. Preparation and properties of covalent compounds and intermediates of serine proteases. Methods in Enzymology. 87: 66-76. PMID 6757654 DOI: 10.1016/S0076-6879(82)87008-0 |
0.319 |
|
| 1980 |
Fink AL, Homer R, Weber JP. Resolution of the individual steps in the reaction of lysozyme with the trimer and hexamer of N-acetyl-D-glucosamine at subzero temperatures. Biochemistry. 19: 811-20. PMID 7188855 DOI: 10.1021/Bi00545A030 |
0.344 |
|
| 1980 |
Compton P, Fink AL. The detection, accumulation and stabilization of a tetrahedral intermediate in trypsin catalysis Biochemical and Biophysical Research Communications. 93: 427-431. PMID 6770851 DOI: 10.1016/0006-291X(80)91095-5 |
0.357 |
|
| 1979 |
Fink AL, Geeves MA. Cryoenzymology: the study of enzyme catalysis at subzero temperatures. Methods in Enzymology. 63: 336-70. PMID 41158 DOI: 10.1016/0076-6879(79)63015-X |
0.505 |
|
| 1979 |
Fink AL, Meehan P. Detection and accumulation of tetrahedral intermediates in elastase catalysis. Proceedings of the National Academy of Sciences of the United States of America. 76: 1566-1569. PMID 36609 DOI: 10.1073/Pnas.76.4.1566 |
0.356 |
|
| 1979 |
Angelides KJ, Fink AL. Mechanism of thiol protease catalysis: detection and stabilization of a tetrahedral intermediate in papain catalysis. Biochemistry. 18: 2363-9. PMID 36130 DOI: 10.1021/Bi00578A035 |
0.309 |
|
| 1976 |
Fink AL, Angelides KJ. Papain-catalyzed reactions at subzero temperatures. Biochemistry. 15: 5287-93. PMID 999807 DOI: 10.1021/Bi00669A014 |
0.35 |
|
| 1976 |
Fink AL. Cryoenzymology of chymotrypsin: the detection of intermediates in the catalysis of a specific anilide substrate Biochemistry. 15: 1580-1586. PMID 944050 DOI: 10.1021/Bi00652A031 |
0.314 |
|
| 1976 |
Fink AL. Cryoenzymology: the use of sub-zero temperatures and fluid solutions in the study of enzyme mechanisms. Journal of Theoretical Biology. 61: 419-445. PMID 10476 DOI: 10.1016/0022-5193(76)90028-X |
0.346 |
|
| 1976 |
Fink AL, Ahmed AI. Formation of stable crystalline enzyme-substrate intermediates at sub-zero temperatures. Nature. 263: 294-7. PMID 8732 DOI: 10.1038/263294A0 |
0.321 |
|
| 1975 |
Fink AL, Angelides KJ. The beta-galactosidase-catalyzed hydrolysis of o-nitrophenol-beta-D-galactoside at subzero temperatures: evidence for a galactosyl-enzyme intermediate. Biochemical and Biophysical Research Communications. 64: 701-8. PMID 238516 DOI: 10.1016/0006-291X(75)90377-0 |
0.306 |
|
| 1974 |
Fink AL, Good NE. Evidence for a glucosyl-enzyme intermediate in the beta-glucosidase-catalyzed hydrolysis of p-nitrophenyl-beta-D-glucoside. Biochemical and Biophysical Research Communications. 58: 126-31. PMID 4831060 DOI: 10.1016/0006-291X(74)90900-0 |
0.336 |
|
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