| Year |
Citation |
Score |
| 2023 |
Roy M, Horovitz A. Distinguishing between concerted, sequential and barrierless conformational changes: Folding versus allostery. Current Opinion in Structural Biology. 83: 102721. PMID 37922762 DOI: 10.1016/j.sbi.2023.102721 |
0.306 |
|
| 2023 |
Roy M, Fleisher RC, Alexandrov AI, Horovitz A. Reduced ADP off-rate by the yeast CCT2 double mutation T394P/R510H which causes Leber congenital amaurosis in humans. Communications Biology. 6: 888. PMID 37644231 DOI: 10.1038/s42003-023-05261-8 |
0.345 |
|
| 2023 |
Liebermann DG, Jungwirth J, Riven I, Barak Y, Levy D, Horovitz A, Haran G. From Microstates to Macrostates in the Conformational Dynamics of GroEL: A Single-Molecule Förster Resonance Energy Transfer Study. The Journal of Physical Chemistry Letters. 6513-6521. PMID 37440608 DOI: 10.1021/acs.jpclett.3c01281 |
0.394 |
|
| 2022 |
Singh J, Anand R, Horovitz A. Cooperativity in ATP Hydrolysis by MopR Is Modulated by Its Signal Reception Domain and by Its Protein and Phenol Concentrations. Journal of Bacteriology. e0017922. PMID 35862728 DOI: 10.1128/jb.00179-22 |
0.378 |
|
| 2022 |
Horovitz A, Reingewertz TH, Cuéllar J, Valpuesta JM. Chaperonin Mechanisms: Multiple and (Mis)Understood? Annual Review of Biophysics. PMID 34982571 DOI: 10.1146/annurev-biophys-082521-113418 |
0.348 |
|
| 2018 |
Gruber R, Horovitz A. Unpicking allosteric mechanisms of homo-oligomeric proteins by determining their successive ligand binding constants. Philosophical Transactions of the Royal Society of London. Series B, Biological Sciences. 373. PMID 29735730 DOI: 10.1098/Rstb.2017.0176 |
0.331 |
|
| 2017 |
Gruber R, Levitt M, Horovitz A. Sequential allosteric mechanism of ATP hydrolysis by the CCT/TRiC chaperone is revealed through Arrhenius analysis. Proceedings of the National Academy of Sciences of the United States of America. PMID 28461478 DOI: 10.1073/Pnas.1617746114 |
0.4 |
|
| 2016 |
Korobko I, Nadler-Holly M, Horovitz A. Transient kinetic analysis of ATP hydrolysis by the CCT/TRiC chaperonin. Journal of Molecular Biology. PMID 27686496 DOI: 10.1016/J.Jmb.2016.09.017 |
0.469 |
|
| 2016 |
Gruber R, Horovitz A. Allosteric Mechanisms in Chaperonin Machines. Chemical Reviews. PMID 26726755 DOI: 10.1021/Acs.Chemrev.5B00556 |
0.493 |
|
| 2013 |
Horovitz A. Putting handcuffs on the chaperonin GroEL. Proceedings of the National Academy of Sciences of the United States of America. 110: 10884-5. PMID 23784780 DOI: 10.1073/Pnas.1309581110 |
0.386 |
|
| 2013 |
Dyachenko A, Gruber R, Shimon L, Horovitz A, Sharon M. Allosteric mechanisms can be distinguished using structural mass spectrometry. Proceedings of the National Academy of Sciences of the United States of America. 110: 7235-9. PMID 23589876 DOI: 10.1073/Pnas.1302395110 |
0.429 |
|
| 2012 |
Nadler-Holly M, Breker M, Gruber R, Azia A, Gymrek M, Eisenstein M, Willison KR, Schuldiner M, Horovitz A. Interactions of subunit CCT3 in the yeast chaperonin CCT/TRiC with Q/N-rich proteins revealed by high-throughput microscopy analysis. Proceedings of the National Academy of Sciences of the United States of America. 109: 18833-8. PMID 23112166 DOI: 10.1073/Pnas.1209277109 |
0.406 |
|
| 2012 |
Horovitz A. Molecular basis of allosteric transitions: GroEL Nato Science For Peace and Security Series a: Chemistry and Biology. 79-86. DOI: 10.1007/978-94-007-2530-0_7 |
0.307 |
|
| 2010 |
Amit M, Weisberg SJ, Nadler-Holly M, McCormack EA, Feldmesser E, Kaganovich D, Willison KR, Horovitz A. Equivalent mutations in the eight subunits of the chaperonin CCT produce dramatically different cellular and gene expression phenotypes. Journal of Molecular Biology. 401: 532-43. PMID 20600117 DOI: 10.1016/J.Jmb.2010.06.037 |
0.32 |
|
| 2010 |
Frank GA, Goomanovsky M, Davidi A, Ziv G, Horovitz A, Haran G. Out-of-equilibrium conformational cycling of GroEL under saturating ATP concentrations. Proceedings of the National Academy of Sciences of the United States of America. 107: 6270-4. PMID 20308583 DOI: 10.1073/Pnas.0910246107 |
0.316 |
|
| 2008 |
Papo N, Kipnis Y, Haran G, Horovitz A. Concerted release of substrate domains from GroEL by ATP is demonstrated with FRET. Journal of Molecular Biology. 380: 717-25. PMID 18556021 DOI: 10.1016/J.Jmb.2008.05.021 |
0.365 |
|
| 2008 |
Shimon L, Hynes GM, McCormack EA, Willison KR, Horovitz A. ATP-induced allostery in the eukaryotic chaperonin CCT is abolished by the mutation G345D in CCT4 that renders yeast temperature-sensitive for growth. Journal of Molecular Biology. 377: 469-77. PMID 18272176 DOI: 10.1016/J.Jmb.2008.01.011 |
0.431 |
|
| 2007 |
Jacob E, Horovitz A, Unger R. Different mechanistic requirements for prokaryotic and eukaryotic chaperonins: a lattice study. Bioinformatics (Oxford, England). 23: i240-8. PMID 17646302 DOI: 10.1093/bioinformatics/btm180 |
0.381 |
|
| 2007 |
Kipnis Y, Papo N, Haran G, Horovitz A. Concerted ATP-induced allosteric transitions in GroEL facilitate release of protein substrate domains in an all-or-none manner. Proceedings of the National Academy of Sciences of the United States of America. 104: 3119-24. PMID 17360617 DOI: 10.1073/Pnas.0700070104 |
0.437 |
|
| 2006 |
Danziger O, Shimon L, Horovitz A. Glu257 in GroEL is a sensor involved in coupling polypeptide substrate binding to stimulation of ATP hydrolysis. Protein Science : a Publication of the Protein Society. 15: 1270-6. PMID 16672234 DOI: 10.1110/Ps.062100606 |
0.765 |
|
| 2006 |
Horovitz A, Fridmann Y, Kafri G, Yifrach O. Allostery in chaperonins Rendiconti Lincei. 17: 115-131. DOI: 10.1007/BF02904504 |
0.763 |
|
| 2005 |
Horovitz A, Willison KR. Allosteric regulation of chaperonins. Current Opinion in Structural Biology. 15: 646-51. PMID 16249079 DOI: 10.1016/J.Sbi.2005.10.001 |
0.337 |
|
| 2005 |
Rivenzon-Segal D, Wolf SG, Shimon L, Willison KR, Horovitz A. Sequential ATP-induced allosteric transitions of the cytoplasmic chaperonin containing TCP-1 revealed by EM analysis. Nature Structural & Molecular Biology. 12: 233-7. PMID 15696173 DOI: 10.1038/Nsmb901 |
0.537 |
|
| 2004 |
Amir A, Horovitz A. Kinetic analysis of ATP-dependent inter-ring communication in GroEL. Journal of Molecular Biology. 338: 979-88. PMID 15111061 DOI: 10.1016/J.Jmb.2004.02.076 |
0.489 |
|
| 2003 |
Danziger O, Rivenzon-Segal D, Wolf SG, Horovitz A. Conversion of the allosteric transition of GroEL from concerted to sequential by the single mutation Asp-155 -> Ala. Proceedings of the National Academy of Sciences of the United States of America. 100: 13797-802. PMID 14615587 DOI: 10.1073/Pnas.2333925100 |
0.774 |
|
| 2003 |
Kafri G, Horovitz A. Transient kinetic analysis of ATP-induced allosteric transitions in the eukaryotic chaperonin containing TCP-1. Journal of Molecular Biology. 326: 981-7. PMID 12589746 DOI: 10.1016/S0022-2836(03)00046-9 |
0.441 |
|
| 2002 |
Horovitz A, Amir A, Danziger O, Kafri G. Phi value analysis of heterogeneity in pathways of allosteric transitions: Evidence for parallel pathways of ATP-induced conformational changes in a GroEL ring. Proceedings of the National Academy of Sciences of the United States of America. 99: 14095-7. PMID 12388779 DOI: 10.1073/Pnas.222303299 |
0.753 |
|
| 2002 |
Kass I, Horovitz A. Mapping pathways of allosteric communication in GroEL by analysis of correlated mutations. Proteins. 48: 611-7. PMID 12211028 DOI: 10.1002/Prot.10180 |
0.343 |
|
| 2002 |
Fridmann Y, Kafri G, Danziger O, Horovitz A. Dissociation of the GroEL-GroES asymmetric complex is accelerated by increased cooperativity in ATP binding to the GroEL ring distal to GroES. Biochemistry. 41: 5938-44. PMID 11980498 DOI: 10.1021/Bi020117V |
0.668 |
|
| 2001 |
Horovitz A, Fridmann Y, Kafri G, Yifrach O. Review: allostery in chaperonins. Journal of Structural Biology. 135: 104-14. PMID 11580260 DOI: 10.1006/Jsbi.2001.4377 |
0.761 |
|
| 2001 |
Kafri G, Willison KR, Horovitz A. Nested allosteric interactions in the cytoplasmic chaperonin containing TCP-1 Protein Science. 10: 445-449. PMID 11266630 DOI: 10.1110/Ps.44401 |
0.538 |
|
| 2000 |
Fridmann Y, Ulitzur S, Horovitz A. In vivo and in vitro function of GroEL mutants with impaired allosteric properties. The Journal of Biological Chemistry. 275: 37951-6. PMID 10973985 DOI: 10.1074/Jbc.M007594200 |
0.716 |
|
| 2000 |
Horovitz A, Yifrach O. On the relationship between the hill coefficients for steady-state and transient kinetic data: A criterion for concerted transitions in allosteric proteins Bulletin of Mathematical Biology. 62: 241-246. PMID 10824429 DOI: 10.1006/Bulm.1999.0150 |
0.314 |
|
| 2000 |
Yifrach O, Horovitz A. Coupling between protein folding and allostery in the GroE chaperonin system Proceedings of the National Academy of Sciences of the United States of America. 97: 1521-1524. PMID 10677493 DOI: 10.1073/Pnas.040449997 |
0.549 |
|
| 1998 |
Yifrach O, Horovitz A. Transient kinetic analysis of adenosine 5'-triphosphate binding-induced conformational changes in the allosteric chaperonin GroEL Biochemistry. 37: 7083-7088. PMID 9585518 DOI: 10.1021/Bi980370O |
0.434 |
|
| 1997 |
Inbar E, Horovitz A. GroES promotes the T to R transition of the GroEL ring distal to GroES in the GroEL-GroES complex Biochemistry. 36: 12276-12281. PMID 9315866 DOI: 10.1021/Bi9714870 |
0.42 |
|
| 1997 |
Aharoni A, Horovitz A. Detection of changes in pairwise interactions during allosteric transitions: Coupling between local and global conformational changes in GroEL Proceedings of the National Academy of Sciences of the United States of America. 94: 1698-1702. PMID 9050841 DOI: 10.1073/Pnas.94.5.1698 |
0.327 |
|
| 1996 |
Horovitz A. Double-mutant cycles: A powerful tool for analyzing protein structure and function Folding and Design. 1. PMID 9080186 DOI: 10.1016/S1359-0278(96)00056-9 |
0.337 |
|
| 1996 |
Yifrach O, Horovitz A. Allosteric control by ATP of non-folded protein binding to GroEL Journal of Molecular Biology. 255: 356-361. PMID 8568880 DOI: 10.1006/Jmbi.1996.0028 |
0.476 |
|
| 1995 |
Yifrach O, Horovitz A. Nested cooperativity in the ATPase activity of the oligomeric chaperonin GroEL Biochemistry. 34: 5303-5308. PMID 7727391 DOI: 10.1021/Bi00016A001 |
0.414 |
|
| 1995 |
Horovitz A. The relation between cooperativity in ligand binding and intramolecular cooperativity in allosteric proteins Proceedings of the Royal Society B: Biological Sciences. 259: 85-87. DOI: 10.1098/Rspb.1995.0013 |
0.354 |
|
| 1994 |
Kovalenko O, Yifrach O, Horovitz A. Residue Lysine-34 in GroES modulates allosteric transitions in GroEL Biochemistry. 33: 14974-14978. PMID 7999753 DOI: 10.1021/Bi00254A004 |
0.316 |
|
| 1994 |
Yifrach O, Horovitz A. Two lines of allosteric communication in the oligomeric chaperonin GroEL are revealed by the single mutation Arg196→Ala Journal of Molecular Biology. 243: 397-401. PMID 7966268 DOI: 10.1006/Jmbi.1994.1667 |
0.429 |
|
| 1994 |
Bochkareva ES, Horovitz A, Girshovich AS. Direct demonstration that ATP is in contact with Cys-137 in chaperonin GroEL Journal of Biological Chemistry. 269: 44-46. PMID 7903969 |
0.382 |
|
| 1993 |
Horovitz A, Bochkareva ES, Kovalenko O, Girshovich AS. Mutation Ala2 → Ser destabilizes intersubunit interactions in the molecular chaperone GroEL Journal of Molecular Biology. 231: 58-64. PMID 8098773 DOI: 10.1006/Jmbi.1993.1256 |
0.346 |
|
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