| Year |
Citation |
Score |
| 2020 |
Horwich AL, Fenton WA. Chaperonin-assisted protein folding: a chronologue. Quarterly Reviews of Biophysics. 53: e4. PMID 32070442 DOI: 10.1017/S0033583519000143 |
0.415 |
|
| 2018 |
Natesh R, Clare DK, Farr GW, Horwich AL, Saibil HR. A two-domain folding intermediate of RuBisCO in complex with the GroEL chaperonin. International Journal of Biological Macromolecules. PMID 29959019 DOI: 10.1016/J.Ijbiomac.2018.06.120 |
0.42 |
|
| 2016 |
Nagy M, Fenton WA, Li D, Furtak K, Horwich AL. Extended survival of misfolded G85R SOD1-linked ALS mice by transgenic expression of chaperone Hsp110. Proceedings of the National Academy of Sciences of the United States of America. PMID 27114530 DOI: 10.1073/Pnas.1604885113 |
0.348 |
|
| 2015 |
Ambrose AJ, Fenton W, Mason DJ, Chapman E, Horwich AL. Unfolded DapA forms aggregates when diluted into free solution, confounding comparison with folding by the GroEL/GroES chaperonin system. Febs Letters. 589: 497-9. PMID 25601566 DOI: 10.1016/J.Febslet.2015.01.008 |
0.317 |
|
| 2014 |
Horwich AL. Molecular chaperones in cellular protein folding: the birth of a field. Cell. 157: 285-8. PMID 24725397 DOI: 10.1016/J.Cell.2014.03.029 |
0.381 |
|
| 2013 |
Horwich AL. Chaperonin-mediated protein folding. The Journal of Biological Chemistry. 288: 23622-32. PMID 23803606 DOI: 10.1074/Jbc.X113.497321 |
0.384 |
|
| 2013 |
Song Y, Nagy M, Ni W, Tyagi NK, Fenton WA, López-Giráldez F, Overton JD, Horwich AL, Brady ST. Molecular chaperone Hsp110 rescues a vesicle transport defect produced by an ALS-associated mutant SOD1 protein in squid axoplasm. Proceedings of the National Academy of Sciences of the United States of America. 110: 5428-33. PMID 23509252 DOI: 10.1073/Pnas.1303279110 |
0.746 |
|
| 2013 |
Bilguvar K, Tyagi NK, Ozkara C, Tuysuz B, Bakircioglu M, Choi M, Delil S, Caglayan AO, Baranoski JF, Erturk O, Yalcinkaya C, Karacorlu M, Dincer A, Johnson MH, Mane S, ... ... Horwich AL, et al. Recessive loss of function of the neuronal ubiquitin hydrolase UCHL1 leads to early-onset progressive neurodegeneration. Proceedings of the National Academy of Sciences of the United States of America. 110: 3489-94. PMID 23359680 DOI: 10.1073/Pnas.1222732110 |
0.354 |
|
| 2013 |
Saibil HR, Fenton WA, Clare DK, Horwich AL. Structure and allostery of the chaperonin GroEL. Journal of Molecular Biology. 425: 1476-87. PMID 23183375 DOI: 10.1016/J.Jmb.2012.11.028 |
0.44 |
|
| 2012 |
Clare DK, Vasishtan D, Stagg S, Quispe J, Farr GW, Topf M, Horwich AL, Saibil HR. ATP-triggered conformational changes delineate substrate-binding and -folding mechanics of the GroEL chaperonin. Cell. 149: 113-23. PMID 22445172 DOI: 10.1016/J.Cell.2012.02.047 |
0.409 |
|
| 2012 |
Horwich AL, Buchner J, Smock RG, Gierasch LM, Saibil HR. Chaperones and protein folding Comprehensive Biophysics. 3: 212-237. DOI: 10.1016/B978-0-12-374920-8.00313-1 |
0.311 |
|
| 2011 |
Horwich AL. Protein folding in the cell: an inside story. Nature Medicine. 17: 1211-6. PMID 21989012 DOI: 10.1038/Nm.2468 |
0.398 |
|
| 2011 |
Charbon G, Wang J, Brustad E, Schultz PG, Horwich AL, Jacobs-Wagner C, Chapman E. Localization of GroEL determined by in vivo incorporation of a fluorescent amino acid. Bioorganic & Medicinal Chemistry Letters. 21: 6067-70. PMID 21890355 DOI: 10.1016/J.Bmcl.2011.08.057 |
0.461 |
|
| 2011 |
Farr GW, Ying Z, Fenton WA, Horwich AL. Hydrogen-deuterium exchange in vivo to measure turnover of an ALS-associated mutant SOD1 protein in spinal cord of mice. Protein Science : a Publication of the Protein Society. 20: 1692-6. PMID 21780215 DOI: 10.1002/Pro.700 |
0.337 |
|
| 2011 |
Koculi E, Horst R, Horwich AL, Wüthrich K. Nuclear magnetic resonance spectroscopy with the stringent substrate rhodanese bound to the single-ring variant SR1 of the E. coli chaperonin GroEL. Protein Science : a Publication of the Protein Society. 20: 1380-6. PMID 21633984 DOI: 10.1002/Pro.665 |
0.376 |
|
| 2011 |
Tyagi NK, Fenton WA, Deniz AA, Horwich AL. Double mutant MBP refolds at same rate in free solution as inside the GroEL/GroES chaperonin chamber when aggregation in free solution is prevented. Febs Letters. 585: 1969-72. PMID 21609718 DOI: 10.1016/J.Febslet.2011.05.031 |
0.321 |
|
| 2010 |
Tyagi NK, Fenton WA, Horwich AL. ATP-triggered ADP release from the asymmetric chaperonin GroEL/GroES/ADP7 is not the rate-limiting step of the GroEL/GroES reaction cycle. Febs Letters. 584: 951-3. PMID 20083109 DOI: 10.1016/J.Febslet.2010.01.021 |
0.411 |
|
| 2009 |
Tyagi NK, Fenton WA, Horwich AL. GroEL/GroES cycling: ATP binds to an open ring before substrate protein favoring protein binding and production of the native state. Proceedings of the National Academy of Sciences of the United States of America. 106: 20264-9. PMID 19915138 DOI: 10.1073/Pnas.0911556106 |
0.47 |
|
| 2009 |
Horwich AL, Fenton WA. Chaperonin-mediated protein folding: using a central cavity to kinetically assist polypeptide chain folding. Quarterly Reviews of Biophysics. 42: 83-116. PMID 19638247 DOI: 10.1017/S0033583509004764 |
0.513 |
|
| 2009 |
Horwich AL, Apetri AC, Fenton WA. The GroEL/GroES cis cavity as a passive anti-aggregation device. Febs Letters. 583: 2654-62. PMID 19577567 DOI: 10.1016/J.Febslet.2009.06.049 |
0.387 |
|
| 2009 |
Wang J, Farr GW, Zeiss CJ, Rodriguez-Gil DJ, Wilson JH, Furtak K, Rutkowski DT, Kaufman RJ, Ruse CI, Yates JR, Perrin S, Feany MB, Horwich AL. Progressive aggregation despite chaperone associations of a mutant SOD1-YFP in transgenic mice that develop ALS. Proceedings of the National Academy of Sciences of the United States of America. 106: 1392-7. PMID 19171884 DOI: 10.1073/Pnas.0813045106 |
0.469 |
|
| 2009 |
Wang J, Farr GW, Hall DH, Li F, Furtak K, Dreier L, Horwich AL. An ALS-linked mutant SOD1 produces a locomotor defect associated with aggregation and synaptic dysfunction when expressed in neurons of Caenorhabditis elegans. Plos Genetics. 5: e1000350. PMID 19165329 DOI: 10.1371/Journal.Pgen.1000350 |
0.465 |
|
| 2009 |
Chapman E, Farr GW, Furtak K, Horwich AL. A small molecule inhibitor selective for a variant ATP-binding site of the chaperonin GroEL. Bioorganic & Medicinal Chemistry Letters. 19: 811-3. PMID 19110421 DOI: 10.1016/J.Bmcl.2008.12.015 |
0.436 |
|
| 2008 |
Chapman E, Farr GW, Fenton WA, Johnson SM, Horwich AL. Requirement for binding multiple ATPs to convert a GroEL ring to the folding-active state. Proceedings of the National Academy of Sciences of the United States of America. 105: 19205-10. PMID 19050077 DOI: 10.1073/Pnas.0810657105 |
0.453 |
|
| 2008 |
Apetri AC, Horwich AL. Chaperonin chamber accelerates protein folding through passive action of preventing aggregation. Proceedings of the National Academy of Sciences of the United States of America. 105: 17351-5. PMID 18987317 DOI: 10.1073/Pnas.0809794105 |
0.399 |
|
| 2008 |
Clare DK, Stagg S, Quispe J, Farr GW, Horwich AL, Saibil HR. Multiple states of a nucleotide-bound group 2 chaperonin. Structure (London, England : 1993). 16: 528-34. PMID 18400175 DOI: 10.1016/J.Str.2008.01.016 |
0.415 |
|
| 2007 |
Horst R, Fenton WA, Englander SW, Wüthrich K, Horwich AL. Folding trajectories of human dihydrofolate reductase inside the GroEL GroES chaperonin cavity and free in solution. Proceedings of the National Academy of Sciences of the United States of America. 104: 20788-92. PMID 18093916 DOI: 10.1073/Pnas.0710042105 |
0.424 |
|
| 2007 |
Elad N, Farr GW, Clare DK, Orlova EV, Horwich AL, Saibil HR. Topologies of a substrate protein bound to the chaperonin GroEL. Molecular Cell. 26: 415-26. PMID 17499047 DOI: 10.1016/J.Molcel.2007.04.004 |
0.425 |
|
| 2007 |
Horwich AL, Fenton WA, Chapman E, Farr GW. Two families of chaperonin: physiology and mechanism. Annual Review of Cell and Developmental Biology. 23: 115-45. PMID 17489689 DOI: 10.1146/Annurev.Cellbio.23.090506.123555 |
0.466 |
|
| 2007 |
Farr GW, Fenton WA, Horwich AL. Perturbed ATPase activity and not "close confinement" of substrate in the cis cavity affects rates of folding by tail-multiplied GroEL. Proceedings of the National Academy of Sciences of the United States of America. 104: 5342-7. PMID 17372195 DOI: 10.1073/Pnas.0700820104 |
0.493 |
|
| 2007 |
Park ES, Fenton WA, Horwich AL. Disulfide formation as a probe of folding in GroEL-GroES reveals correct formation of long-range bonds and editing of incorrect short-range ones. Proceedings of the National Academy of Sciences of the United States of America. 104: 2145-50. PMID 17283341 DOI: 10.1073/Pnas.0610989104 |
0.431 |
|
| 2006 |
Chapman E, Farr GW, Usaite R, Furtak K, Fenton WA, Chaudhuri TK, Hondorp ER, Matthews RG, Wolf SG, Yates JR, Pypaert M, Horwich AL. Global aggregation of newly translated proteins in an Escherichia coli strain deficient of the chaperonin GroEL. Proceedings of the National Academy of Sciences of the United States of America. 103: 15800-5. PMID 17043235 DOI: 10.1073/Pnas.0607534103 |
0.392 |
|
| 2006 |
Horwich AL, Farr GW, Fenton WA. GroEL-GroES-mediated protein folding. Chemical Reviews. 106: 1917-30. PMID 16683761 DOI: 10.1021/Cr040435V |
0.429 |
|
| 2006 |
Bukau B, Weissman J, Horwich A. Molecular chaperones and protein quality control. Cell. 125: 443-51. PMID 16678092 DOI: 10.1016/J.Cell.2006.04.014 |
0.525 |
|
| 2006 |
Ranson NA, Clare DK, Farr GW, Houldershaw D, Horwich AL, Saibil HR. Allosteric signaling of ATP hydrolysis in GroEL-GroES complexes. Nature Structural & Molecular Biology. 13: 147-52. PMID 16429154 DOI: 10.1038/Nsmb1046 |
0.465 |
|
| 2005 |
Hinnerwisch J, Reid BG, Fenton WA, Horwich AL. Roles of the N-domains of the ClpA unfoldase in binding substrate proteins and in stable complex formation with the ClpP protease. The Journal of Biological Chemistry. 280: 40838-44. PMID 16207718 DOI: 10.1074/Jbc.M507879200 |
0.438 |
|
| 2005 |
Horst R, Bertelsen EB, Fiaux J, Wider G, Horwich AL, Wüthrich K. Direct NMR observation of a substrate protein bound to the chaperonin GroEL. Proceedings of the National Academy of Sciences of the United States of America. 102: 12748-53. PMID 16116078 DOI: 10.1073/Pnas.0505642102 |
0.406 |
|
| 2005 |
Hinnerwisch J, Fenton WA, Furtak KJ, Farr GW, Horwich AL. Loops in the central channel of ClpA chaperone mediate protein binding, unfolding, and translocation. Cell. 121: 1029-41. PMID 15989953 DOI: 10.1016/J.Cell.2005.04.012 |
0.446 |
|
| 2005 |
Park ES, Fenton WA, Horwich AL. No evidence for a forced-unfolding mechanism during ATP/GroES binding to substrate-bound GroEL: no observable protection of metastable Rubisco intermediate or GroEL-bound Rubisco from tritium exchange. Febs Letters. 579: 1183-6. PMID 15710410 DOI: 10.1016/J.Febslet.2005.01.013 |
0.395 |
|
| 2004 |
Horwich AL. Chaperoned protein disaggregation--the ClpB ring uses its central channel. Cell. 119: 579-81. PMID 15550237 DOI: 10.1016/J.Cell.2004.11.018 |
0.427 |
|
| 2004 |
Motojima F, Chaudhry C, Fenton WA, Farr GW, Horwich AL. Substrate polypeptide presents a load on the apical domains of the chaperonin GroEL. Proceedings of the National Academy of Sciences of the United States of America. 101: 15005-12. PMID 15479763 DOI: 10.1073/Pnas.0406132101 |
0.401 |
|
| 2004 |
Sewell BT, Best RB, Chen S, Roseman AM, Farr GW, Horwich AL, Saibil HR. A mutant chaperonin with rearranged inter-ring electrostatic contacts and temperature-sensitive dissociation. Nature Structural & Molecular Biology. 11: 1128-33. PMID 15475965 DOI: 10.1038/Nsmb844 |
0.458 |
|
| 2004 |
Horwich A. Sight at the end of the tunnel Nature. 431: 520-522. PMID 15457244 DOI: 10.1038/431520A |
0.369 |
|
| 2004 |
Chaudhry C, Horwich AL, Brunger AT, Adams PD. Exploring the structural dynamics of the E.coli chaperonin GroEL using translation-libration-screw crystallographic refinement of intermediate states. Journal of Molecular Biology. 342: 229-45. PMID 15313620 DOI: 10.1016/J.Jmb.2004.07.015 |
0.359 |
|
| 2004 |
Fiaux J, Bertelsen EB, Horwich AL, Wüthrich K. Uniform and residue-specific 15N-labeling of proteins on a highly deuterated background. Journal of Biomolecular Nmr. 29: 289-97. PMID 15213427 DOI: 10.1023/B:Jnmr.0000032523.00554.38 |
0.36 |
|
| 2003 |
Fenton WA, Horwich AL. Chaperonin-mediated protein folding: fate of substrate polypeptide. Quarterly Reviews of Biophysics. 36: 229-56. PMID 14686103 DOI: 10.1017/S0033583503003883 |
0.503 |
|
| 2003 |
Chaudhry C, Farr GW, Todd MJ, Rye HS, Brunger AT, Adams PD, Horwich AL, Sigler PB. Role of the gamma-phosphate of ATP in triggering protein folding by GroEL-GroES: function, structure and energetics. The Embo Journal. 22: 4877-87. PMID 14517228 DOI: 10.1093/Emboj/Cdg477 |
0.746 |
|
| 2003 |
Farr GW, Fenton WA, Chaudhuri TK, Clare DK, Saibil HR, Horwich AL. Folding with and without encapsulation by cis- and trans-only GroEL-GroES complexes. The Embo Journal. 22: 3220-30. PMID 12839985 DOI: 10.1093/Emboj/Cdg313 |
0.487 |
|
| 2003 |
Horwich AL, Fenton WA. The Role of ATP in directing chaperonin-mediated polypeptide folding Enzymes. 23: 399-433,IX-XII. DOI: 10.1016/S1874-6047(04)80010-6 |
0.452 |
|
| 2002 |
Horwich A. Protein aggregation in disease: A role for folding intermediates forming specific multimeric interactions Journal of Clinical Investigation. 110: 1221-1232. PMID 12417558 DOI: 10.1172/Jci16781 |
0.33 |
|
| 2002 |
Dougan DA, Reid BG, Horwich AL, Bukau B. ClpS, a substrate modulator of the ClpAP machine. Molecular Cell. 9: 673-83. PMID 11931773 DOI: 10.1016/S1097-2765(02)00485-9 |
0.434 |
|
| 2001 |
Saibil HR, Horwich AL, Fenton WA. Allostery and protein substrate conformational change during GroEL/GroES-mediated protein folding. Advances in Protein Chemistry. 59: 45-72. PMID 11868280 DOI: 10.1016/S0065-3233(01)59002-6 |
0.528 |
|
| 2001 |
Ranson NA, Farr GW, Roseman AM, Gowen B, Fenton WA, Horwich AL, Saibil HR. ATP-bound states of GroEL captured by cryo-electron microscopy. Cell. 107: 869-79. PMID 11779463 DOI: 10.1016/S0092-8674(01)00617-1 |
0.465 |
|
| 2001 |
Horwich AL, Fenton WA, Rapoport TA. Protein folding taking shape. Workshop on molecular chaperones. Embo Reports. 2: 1068-73. PMID 11743017 DOI: 10.1093/Embo-Reports/Kve253 |
0.399 |
|
| 2001 |
Chaudhuri TK, Farr GW, Fenton WA, Rospert S, Horwich AL. GroEL/GroES-mediated folding of a protein too large to be encapsulated. Cell. 107: 235-46. PMID 11672530 DOI: 10.1016/S0092-8674(01)00523-2 |
0.48 |
|
| 2001 |
Chen J, Walter S, Horwich AL, Smith DL. Folding of malate dehydrogenase inside the GroEL-GroES cavity. Nature Structural Biology. 8: 721-8. PMID 11473265 DOI: 10.1038/90443 |
0.468 |
|
| 2001 |
Reid BG, Fenton WA, Horwich AL, Weber-Ban EU. ClpA mediates directional translocation of substrate proteins into the ClpP protease. Proceedings of the National Academy of Sciences of the United States of America. 98: 3768-72. PMID 11259663 DOI: 10.1073/Pnas.071043698 |
0.438 |
|
| 2001 |
Grantcharova V, Alm EJ, Baker D, Horwich AL. Mechanisms of protein folding. Current Opinion in Structural Biology. 11: 70-82. PMID 11179895 DOI: 10.1016/S0959-440X(00)00176-7 |
0.436 |
|
| 2000 |
Farr GW, Furtak K, Rowland MB, Ranson NA, Saibil HR, Kirchhausen T, Horwich AL. Multivalent binding of nonnative substrate proteins by the chaperonin GroEL. Cell. 100: 561-73. PMID 10721993 DOI: 10.1016/S0092-8674(00)80692-3 |
0.44 |
|
| 1999 |
Horwich AL, Weber-Ban EU, Finley D. Chaperone rings in protein folding and degradation. Proceedings of the National Academy of Sciences of the United States of America. 96: 11033-40. PMID 10500119 DOI: 10.1073/Pnas.96.20.11033 |
0.511 |
|
| 1999 |
Weber-Ban EU, Reid BG, Miranker AD, Horwich AL. Global unfolding of a substrate protein by the Hsp100 chaperone ClpA. Nature. 401: 90-3. PMID 10485712 DOI: 10.1038/43481 |
0.491 |
|
| 1999 |
Rye HS, Roseman AM, Chen S, Furtak K, Fenton WA, Saibil HR, Horwich AL. GroEL-GroES cycling: ATP and nonnative polypeptide direct alternation of folding-active rings. Cell. 97: 325-38. PMID 10319813 DOI: 10.1016/S0092-8674(00)80742-4 |
0.745 |
|
| 1998 |
Won KA, Schumacher RJ, Farr GW, Horwich AL, Reed SI. Maturation of human cyclin E requires the function of eukaryotic chaperonin CCT. Molecular and Cellular Biology. 18: 7584-9. PMID 9819444 DOI: 10.1128/Mcb.18.12.7584 |
0.321 |
|
| 1998 |
Kim S, Schilke B, Craig EA, Horwich AL. Folding in vivo of a newly translated yeast cytosolic enzyme is mediated by the SSA class of cytosolic yeast Hsp70 proteins. Proceedings of the National Academy of Sciences of the United States of America. 95: 12860-5. PMID 9789005 DOI: 10.1073/Pnas.95.22.12860 |
0.447 |
|
| 1998 |
Sigler PB, Xu Z, Rye HS, Burston SG, Fenton WA, Horwich AL. Structure and function in GroEL-mediated protein folding. Annual Review of Biochemistry. 67: 581-608. PMID 9759498 DOI: 10.1146/Annurev.Biochem.67.1.581 |
0.759 |
|
| 1998 |
Horwich AL, Burston SG, Rye HS, Weissman JS, Fenton WA. Construction of single-ring and two-ring hybrid versions of bacterial chaperonin GroEL. Methods in Enzymology. 290: 141-6. PMID 9534157 DOI: 10.1016/S0076-6879(98)90013-1 |
0.749 |
|
| 1997 |
Rye HS, Burston SG, Fenton WA, Beechem JM, Xu Z, Sigler PB, Horwich AL. Distinct actions of cis and trans ATP within the double ring of the chaperonin GroEL. Nature. 388: 792-8. PMID 9285593 DOI: 10.1038/42047 |
0.74 |
|
| 1997 |
Xu Z, Horwich AL, Sigler PB. The crystal structure of the asymmetric GroEL-GroES-(ADP)7 chaperonin complex. Nature. 388: 741-50. PMID 9285585 DOI: 10.1038/41944 |
0.504 |
|
| 1997 |
Farr GW, Scharl EC, Schumacher RJ, Sondek S, Horwich AL. Chaperonin-mediated folding in the eukaryotic cytosol proceeds through rounds of release of native and nonnative forms. Cell. 89: 927-37. PMID 9200611 DOI: 10.1016/S0092-8674(00)80278-0 |
0.428 |
|
| 1997 |
Horwich AL, Weissman JS. Deadly conformations--protein misfolding in prion disease. Cell. 89: 499-510. PMID 9160742 DOI: 10.1016/S0092-8674(00)80232-9 |
0.544 |
|
| 1997 |
Fenton WA, Horwich AL. GroEL-mediated protein folding. Protein Science : a Publication of the Protein Society. 6: 743-60. PMID 9098884 DOI: 10.1002/Pro.5560060401 |
0.45 |
|
| 1997 |
Goldberg MS, Zhang J, Sondek S, Matthews CR, Fox RO, Horwich AL. Native-like structure of a protein-folding intermediate bound to the chaperonin GroEL. Proceedings of the National Academy of Sciences of the United States of America. 94: 1080-5. PMID 9037009 DOI: 10.1073/pnas.94.4.1080 |
0.356 |
|
| 1997 |
Xu Z, Horwich AL, Sigler PB. ATP and the editing of protein folding Faseb Journal. 11: A853. |
0.359 |
|
| 1996 |
Fenton WA, Weissman JS, Horwich AL. Putting a lid on protein folding: structure and function of the co-chaperonin, GroES. Chemistry & Biology. 3: 157-61. PMID 8807841 DOI: 10.1016/S1074-5521(96)90257-4 |
0.593 |
|
| 1996 |
Burston SG, Weissman JS, Farr GW, Fenton WA, Horwich AL. Release of both native and non-native proteins from a cis-only GroEL ternary complex. Nature. 383: 96-9. PMID 8779722 DOI: 10.1038/383096A0 |
0.615 |
|
| 1996 |
Weissman JS, Rye HS, Fenton WA, Beechem JM, Horwich AL. Characterization of the active intermediate of a GroEL-GroES-mediated protein folding reaction. Cell. 84: 481-90. PMID 8608602 DOI: 10.1016/S0092-8674(00)81293-3 |
0.775 |
|
| 1996 |
Boisvert DC, Wang J, Otwinowski Z, Horwich AL, Sigler PB. The 2.4 A crystal structure of the bacterial chaperonin GroEL complexed with ATP gamma S. Nature Structural Biology. 3: 170-7. PMID 8564544 DOI: 10.1038/Nsb0296-170 |
0.549 |
|
| 1995 |
Horwich AL, Weissman JS, Fenton WA. Kinesis of polypeptide during GroEL-mediated folding. Cold Spring Harbor Symposia On Quantitative Biology. 60: 435-40. PMID 8824417 DOI: 10.1101/Sqb.1995.060.01.048 |
0.548 |
|
| 1995 |
Sigler PB, Horwich AL. Unliganded GroEL at 2.8 A: structure and functional implications. Philosophical Transactions of the Royal Society of London. Series B, Biological Sciences. 348: 113-9. PMID 7770481 DOI: 10.1098/Rstb.1995.0052 |
0.389 |
|
| 1995 |
Weissman JS, Sigler PB, Horwich AL. From the cradle to the grave: ring complexes in the life of a protein. Science (New York, N.Y.). 268: 523-4. PMID 7725096 DOI: 10.1126/Science.7725096 |
0.551 |
|
| 1995 |
Weissman JS, Hohl CM, Kovalenko O, Kashi Y, Chen S, Braig K, Saibil HR, Fenton WA, Horwich AL. Mechanism of GroEL action: productive release of polypeptide from a sequestered position under GroES. Cell. 83: 577-87. PMID 7585961 DOI: 10.1016/0092-8674(95)90098-5 |
0.57 |
|
| 1995 |
Horwich AL. Molecular chaperones. Resurrection or destruction? Current Biology : Cb. 5: 455-8. PMID 7583086 DOI: 10.1016/S0960-9822(95)00089-3 |
0.311 |
|
| 1994 |
Fenton WA, Kashi Y, Furtak K, Horwich AL. Residues in chaperonin GroEL required for polypeptide binding and release. Nature. 371: 614-9. PMID 7935796 DOI: 10.1038/371614a0 |
0.356 |
|
| 1994 |
Braig K, Otwinowski Z, Hegde R, Boisvert DC, Joachimiak A, Horwich AL, Sigler PB. The crystal structure of the bacterial chaperonin GroEL at 2.8 A. Nature. 371: 578-86. PMID 7935790 DOI: 10.1038/371578A0 |
0.352 |
|
| 1994 |
Weissman JS, Kashi Y, Fenton WA, Horwich AL. GroEL-mediated protein folding proceeds by multiple rounds of binding and release of nonnative forms. Cell. 78: 693-702. PMID 7915201 DOI: 10.1016/0092-8674(94)90533-9 |
0.615 |
|
| 1994 |
Craig EA, Weissman JS, Horwich AL. Heat shock proteins and molecular chaperones: mediators of protein conformation and turnover in the cell. Cell. 78: 365-72. PMID 7914834 DOI: 10.1016/0092-8674(94)90416-2 |
0.556 |
|
| 1994 |
Kim S, Willison KR, Horwich AL. Cystosolic chaperonin subunits have a conserved ATPase domain but diverged polypeptide-binding domains. Trends in Biochemical Sciences. 19: 543-8. PMID 7846767 DOI: 10.1016/0968-0004(94)90058-2 |
0.373 |
|
| 1993 |
Horwich AL, Low KB, Fenton WA, Hirshfield IN, Furtak K. Folding in vivo of bacterial cytoplasmic proteins: role of GroEL. Cell. 74: 909-17. PMID 8104102 DOI: 10.1016/0092-8674(93)90470-B |
0.468 |
|
| 1993 |
Braig K, Simon M, Furuya F, Hainfeld JF, Horwich AL. A polypeptide bound by the chaperonin groEL is localized within a central cavity. Proceedings of the National Academy of Sciences of the United States of America. 90: 3978-82. PMID 8097882 DOI: 10.1073/Pnas.90.9.3978 |
0.46 |
|
| 1992 |
Yaffe MB, Farr GW, Miklos D, Horwich AL, Sternlicht ML, Sternlicht H. TCP1 complex is a molecular chaperone in tubulin biogenesis. Nature. 358: 245-8. PMID 1630491 DOI: 10.1038/358245A0 |
0.424 |
|
| 1992 |
Martin J, Horwich AL, Hartl FU. Prevention of protein denaturation under heat stress by the chaperonin Hsp60. Science (New York, N.Y.). 258: 995-8. PMID 1359644 DOI: 10.1126/Science.1359644 |
0.356 |
|
| 1992 |
Koll H, Guiard B, Rassow J, Ostermann J, Horwich AL, Neupert W, Hartl FU. Antifolding activity of hsp60 couples protein import into the mitochondrial matrix with export to the intermembrane space. Cell. 68: 1163-75. PMID 1347713 DOI: 10.1016/0092-8674(92)90086-R |
0.403 |
|
| 1992 |
Horwich AL, Caplan S, Wall JS, Hartl FU. Chapter 26 Chaperonin-mediated protein folding New Comprehensive Biochemistry. 22: 329-337. DOI: 10.1016/S0167-7306(08)60103-9 |
0.446 |
|
| 1991 |
Trent JD, Nimmesgern E, Wall JS, Hartl FU, Horwich AL. A molecular chaperone from a thermophilic archaebacterium is related to the eukaryotic protein t-complex polypeptide-1. Nature. 354: 490-3. PMID 1836250 DOI: 10.1038/354490A0 |
0.456 |
|
| 1991 |
Horwich AL, Cheng M, West A, Pollock RA. Mitochondrial protein import. Current Topics in Microbiology and Immunology. 170: 1-42. PMID 1760928 |
0.307 |
|
| 1991 |
Wienhues U, Becker K, Schleyer M, Guiard B, Tropschug M, Horwich AL, Pfanner N, Neupert W. Protein folding causes an arrest of preprotein translocation into mitochondria in vivo. The Journal of Cell Biology. 115: 1601-9. PMID 1757464 DOI: 10.1083/Jcb.115.6.1601 |
0.412 |
|
| 1991 |
Martin J, Langer T, Boteva R, Schramel A, Horwich AL, Hartl FU. Chaperonin-mediated protein folding at the surface of groEL through a 'molten globule'-like intermediate. Nature. 352: 36-42. PMID 1676490 DOI: 10.1038/352036A0 |
0.46 |
|
| 1990 |
Mahlke K, Pfanner N, Martin J, Horwich AL, Hartl FU, Neupert W. Sorting pathways of mitochondrial inner membrane proteins. European Journal of Biochemistry / Febs. 192: 551-5. PMID 2145157 DOI: 10.1111/J.1432-1033.1990.Tb19260.X |
0.388 |
|
| 1990 |
Cheng MY, Hartl FU, Horwich AL. The mitochondrial chaperonin hsp60 is required for its own assembly. Nature. 348: 455-8. PMID 1978929 DOI: 10.1038/348455a0 |
0.334 |
|
| 1990 |
Horwich AL, Neupert W, Hartl FU. Protein-catalysed protein folding. Trends in Biotechnology. 8: 126-31. PMID 1369433 DOI: 10.1016/0167-7799(90)90153-O |
0.4 |
|
| 1990 |
HARTL F, MARTIN J, OSTERMANN J, HORWICH A, NEUPERT W. The mitochondrial stress protein HSP60 as a catalyst of protein folding Cell Biology International Reports. 14: 8. DOI: 10.1016/0309-1651(90)90140-T |
0.353 |
|
| 1989 |
Cheng MY, Hartl FU, Martin J, Pollock RA, Kalousek F, Neupert W, Hallberg EM, Hallberg RL, Horwich AL. Mitochondrial heat-shock protein hsp60 is essential for assembly of proteins imported into yeast mitochondria. Nature. 337: 620-5. PMID 2645524 DOI: 10.1038/337620A0 |
0.409 |
|
| 1989 |
Ostermann J, Horwich AL, Neupert W, Hartl FU. Protein folding in mitochondria requires complex formation with hsp60 and ATP hydrolysis. Nature. 341: 125-30. PMID 2528694 DOI: 10.1038/341125A0 |
0.453 |
|
| 1988 |
Pollock RA, Hartl FU, Cheng MY, Ostermann J, Horwich A, Neupert W. The processing peptidase of yeast mitochondria: the two co-operating components MPP and PEP are structurally related. The Embo Journal. 7: 3493-500. PMID 3061797 DOI: 10.1002/J.1460-2075.1988.Tb03225.X |
0.39 |
|
| 1987 |
Cheng MY, Pollock RA, Hendrick JP, Horwich AL. Import and processing of human ornithine transcarbamoylase precursor by mitochondria from Saccharomyces cerevisiae. Proceedings of the National Academy of Sciences of the United States of America. 84: 4063-7. PMID 3295876 DOI: 10.1073/Pnas.84.12.4063 |
0.315 |
|
| 1986 |
Rosenberg LE, Fenton WA, Horwich AL, Kalousek F, Kraus JP. Targeting of nuclear-encoded proteins to the mitochondrial matrix: implications for human genetic defects. Annals of the New York Academy of Sciences. 488: 99-108. PMID 3472484 DOI: 10.1111/J.1749-6632.1986.Tb54396.X |
0.303 |
|
| 1985 |
Horwich AL, Fenton WA, Firgaira FA, Fox JE, Kolansky D, Mellman IS, Rosenberg LE. Expression of amplified DNA sequences for ornithine transcarbamylase in HeLa cells: arginine residues may be required for mitochondrial import of enzyme precursor. The Journal of Cell Biology. 100: 1515-21. PMID 3988798 DOI: 10.1083/Jcb.100.5.1515 |
0.327 |
|
| 1985 |
Horwich AL, Kalousek F, Mellman I, Rosenberg LE. A leader peptide is sufficient to direct mitochondrial import of a chimeric protein. The Embo Journal. 4: 1129-35. PMID 3891325 DOI: 10.1002/J.1460-2075.1985.Tb03750.X |
0.35 |
|
| 1984 |
Horwich AL, Fenton WA, Williams KR, Kalousek F, Kraus JP, Doolittle RF, Konigsberg W, Rosenberg LE. Structure and expression of a complementary DNA for the nuclear coded precursor of human mitochondrial ornithine transcarbamylase. Science (New York, N.Y.). 224: 1068-74. PMID 6372096 DOI: 10.1126/Science.6372096 |
0.335 |
|
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