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Arthur L. Horwich - Publications

Genetics and Pediatrics Yale University, New Haven, CT 

154 high-probability publications. We are testing a new system for linking publications to authors. You can help! If you notice any inaccuracies, please sign in and mark papers as correct or incorrect matches. If you identify any major omissions or other inaccuracies in the publication list, please let us know.

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  1
2019 Taguchi YV, Gorenberg EL, Nagy M, Thrasher D, Fenton WA, Volpicelli-Daley L, Horwich AL, Chandra SS. Hsp110 mitigates α-synuclein pathology in vivo. Proceedings of the National Academy of Sciences of the United States of America. PMID 31685606 DOI: 10.1073/Pnas.1903268116  1
2018 Abdeen S, Kunkle T, Salim N, Ray AM, Mammadova N, Summers C, Stevens M, Ambrose A, Park Y, Schultz PG, Horwich AL, Hoang Q, Chapman E, Johnson SM. Sulfonamido-2-arylbenzoxazole GroEL/ES inhibitors are potent antibacterials against methicillin-resistant Staphylococcus aureus (MRSA). Journal of Medicinal Chemistry. PMID 30060666 DOI: 10.1021/Acs.Jmedchem.8B00989  0.44
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  0.76
2017 Thomas EV, Fenton WA, McGrath J, Horwich AL. Transfer of pathogenic and nonpathogenic cytosolic proteins between spinal cord motor neurons in vivo in chimeric mice. Proceedings of the National Academy of Sciences of the United States of America. PMID 28348221 DOI: 10.1073/Pnas.1701465114  1
2017 Zhang Y, Ni W, Horwich AL, Kaczmarek LK. An ALS-associated mutant SOD1 rapidly suppresses KCNT1 (Slack) Na+-activated K+ channels in Aplysia neurons. The Journal of Neuroscience : the Official Journal of the Society For Neuroscience. PMID 28119399 DOI: 10.1523/Jneurosci.3102-16.2017  0.52
2016 Hadzipasic M, Ni W, Nagy M, Steenrod N, McGinley MJ, Kaushal A, Thomas E, McCormick DA, Horwich AL. Reduced high-frequency motor neuron firing, EMG fractionation, and gait variability in awake walking ALS mice. Proceedings of the National Academy of Sciences of the United States of America. PMID 27821773 DOI: 10.1073/Pnas.1616832113  0.52
2016 Abdeen S, Salim N, Mammadova N, Summers CM, Goldsmith-Pestana K, McMahon-Pratt D, Schultz PG, Horwich AL, Chapman E, Johnson SM. Targeting the HSP60/10 chaperonin systems of Trypanosoma brucei as a strategy for treating African sleeping sickness. Bioorganic & Medicinal Chemistry Letters. PMID 27720295 DOI: 10.1016/J.Bmcl.2016.09.051  0.44
2016 Abdeen S, Salim N, Mammadova N, Summers CM, Frankson R, Ambrose AJ, Anderson GG, Schultz PG, Horwich AL, Chapman E, Johnson SM. GroEL/ES inhibitors as potential antibiotics. Bioorganic & Medicinal Chemistry Letters. 26: 3127-34. PMID 27184767 DOI: 10.1016/J.Bmcl.2016.04.089  1
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  1
2015 Rosenzweig R, Farber P, Velyvis A, Rennella E, Latham MP, Kay LE. ClpB N-terminal domain plays a regulatory role in protein disaggregation. Proceedings of the National Academy of Sciences of the United States of America. PMID 26621746 DOI: 10.1073/Pnas.1512783112  1
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  1
2015 Lang L, Zetterström P, Brännström T, Marklund SL, Danielsson J, Oliveberg M, Horwich AL. SOD1 aggregation in ALS mice shows simplistic test tube behavior Proceedings of the National Academy of Sciences of the United States of America. 112: 9878-9883. DOI: 10.1073/pnas.1503328112  1
2014 Hadzipasic M, Tahvildari B, Nagy M, Bian M, Horwich AL, McCormick DA. Selective degeneration of a physiological subtype of spinal motor neuron in mice with SOD1-linked ALS. Proceedings of the National Academy of Sciences of the United States of America. 111: 16883-8. PMID 25385594 DOI: 10.1073/Pnas.1419497111  1
2014 Bandyopadhyay U, Nagy M, Fenton WA, Horwich AL. Absence of lipofuscin in motor neurons of SOD1-linked ALS mice. Proceedings of the National Academy of Sciences of the United States of America. 111: 11055-60. PMID 25024188 DOI: 10.1073/Pnas.1409314111  1
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  1
2014 Bandyopadhyay U, Fenton WA, Horwich AL, Nagy M. Production of RNA for transcriptomic analysis from mouse spinal cord motor neuron cell bodies by laser capture microdissection. Journal of Visualized Experiments : Jove. e51168. PMID 24457537 DOI: 10.3791/51168  1
2014 Johnson SM, Sharif O, Mak PA, Wang HT, Engels IH, Brinker A, Schultz PG, Horwich AL, Chapman E. A biochemical screen for GroEL/GroES inhibitors. Bioorganic & Medicinal Chemistry Letters. 24: 786-9. PMID 24418775 DOI: 10.1016/J.Bmcl.2013.12.100  1
2013 Horwich AL. Chaperonin-mediated protein folding. The Journal of Biological Chemistry. 288: 23622-32. PMID 23803606 DOI: 10.1074/Jbc.X113.497321  1
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  1
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  1
2013 Bandyopadhyay U, Cotney J, Nagy M, Oh S, Leng J, Mahajan M, Mane S, Fenton WA, Noonan JP, Horwich AL. RNA-Seq profiling of spinal cord motor neurons from a presymptomatic SOD1 ALS mouse. Plos One. 8: e53575. PMID 23301088 DOI: 10.1371/Journal.Pone.0053575  1
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  1
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  1
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  1
2011 Horwich AL. Protein folding in the cell: an inside story. Nature Medicine. 17: 1211-6. PMID 21989012 DOI: 10.1038/Nm.2468  1
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  1
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  1
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  1
2011 Horwich AL, Saibil HR. The GroEL/GroES chaperonin machine Molecular Machines in Biology: Workshop of the Cell. 191-207. DOI: 10.1017/CBO9781139003704.012  1
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  1
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  1
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  1
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  1
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  1
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  1
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  1
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  1
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  1
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  1
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  1
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  1
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  1
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  1
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  1
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  1
2006 Horwich AL, Farr GW, Fenton WA. GroEL-GroES-mediated protein folding. Chemical Reviews. 106: 1917-30. PMID 16683761 DOI: 10.1021/Cr040435V  1
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  1
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  1
2005 Kim SY, Semyonov AN, Twieg RJ, Horwich AL, Frydman J, Moerner WE. Probing the sequence of conformationally induced polarity changes in the molecular chaperonin GroEL with fluorescence spectroscopy. The Journal of Physical Chemistry. B. 109: 24517-25. PMID 16375456 DOI: 10.1021/Jp0534232  1
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  1
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  1
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  1
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  1
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  1
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  1
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  1
2004 Horwich A. Sight at the end of the tunnel Nature. 431: 520-522. PMID 15457244 DOI: 10.1038/431520A  1
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  1
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  1
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  1
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  1
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  1
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  1
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  1
2002 Riek R, Fiaux J, Bertelsen EB, Horwich AL, Wuthrich K. Solution NMR techniques for large molecular and supramolecular structures. Journal of the American Chemical Society. 124: 12144-53. PMID 12371854 DOI: 10.1021/Ja026763Z  1
2002 Fiaux J, Bertelsen EB, Horwich AL, Wüthrich K. NMR analysis of a 900K GroEL GroES complex. Nature. 418: 207-11. PMID 12110894 DOI: 10.1038/Nature00860  1
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  1
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  1
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  1
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  1
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  1
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  1
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  1
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  1
2001 Horwich A. Advances in Protein Chemistry: Preface Advances in Protein Chemistry. 59: xi-xiii. DOI: 10.1016/S0065-3233(01)59000-2  1
2000 Horwich A. Working with Paul Sigler Nature Structural Biology. 7: 269-270. PMID 10798859  1
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  1
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  1
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  1
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  1
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  1
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  1
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  1
1998 Horwich AL, Saibil HR. The thermosome: chaperonin with a built-in lid. Nature Structural Biology. 5: 333-6. PMID 9586988 DOI: 10.1038/Nsb0598-333  1
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  1
1998 Bukau B, Horwich AL. The Hsp70 and Hsp60 chaperone machines. Cell. 92: 351-66. PMID 9476895 DOI: 10.1016/S0092-8674(00)80928-9  1
1998 Horwich AL, Fenton WA, Farr GW, Furtak K, Rye HS. The reaction cycle of groe-assisted protein folding Faseb Journal. 12: A1328.  1
1997 Bergeron JJ, Craig EA, Horwich AL, Langer T, Multhoff G, Smith DF, Hightower LE. Molecular chaperones in biology and medicine at Obernai. Cell Stress & Chaperones. 2: 220-8. PMID 9495279 DOI: 10.1379/1466-1268(1997)002<0220:Mcibam>2.3.Co;2  1
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  1
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  1
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  1
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  1
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  1
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  1
1997 Xu Z, Horwich AL, Sigler PB. ATP and the editing of protein folding Faseb Journal. 11: A853.  1
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  1
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  1
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  1
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  1
1996 Fenton WA, Weissman JS, Horwich AL. Putting a lid on protein folding: Structure and function of the co-chaperon in, GroES Chemistry and Biology. 3: 157-161.  1
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  1
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  1
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  1
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  0.8
1995 Horwich AL. Molecular chaperones. Resurrection or destruction? Current Biology : Cb. 5: 455-8. PMID 7583086 DOI: 10.1016/S0960-9822(95)00089-3  1
1994 Burnett BP, Horwich AL, Low KB. A carboxy-terminal deletion impairs the assembly of GroEL and confers a pleiotropic phenotype in Escherichia coli K-12. Journal of Bacteriology. 176: 6980-5. PMID 7961461  1
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  1
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  1
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  1
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  1
1994 Miklos D, Caplan S, Mertens D, Hynes G, Pitluk Z, Kashi Y, Harrison-Lavoie K, Stevenson S, Brown C, Barrell B. Primary structure and function of a second essential member of the heterooligomeric TCP1 chaperonin complex of yeast, TCP1 beta. Proceedings of the National Academy of Sciences of the United States of America. 91: 2743-7. PMID 7908441  1
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  1
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  1
1993 Horwich AL, Willison KR. Protein folding in the cell: functions of two families of molecular chaperone, hsp 60 and TF55-TCP1. Philosophical Transactions of the Royal Society of London. Series B, Biological Sciences. 339: 313-25; discussion 3. PMID 8098536 DOI: 10.1098/Rstb.1993.0030  1
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  1
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  1
1992 West AH, Clark DJ, Martin J, Neupert W, Hartl FU, Horwich AL. Two related genes encoding extremely hydrophobic proteins suppress a lethal mutation in the yeast mitochondrial processing enhancing protein. The Journal of Biological Chemistry. 267: 24625-33. PMID 1447206  1
1992 McGrath J, Horwich AL, Brueckner M. Duplication/deficiency mapping of situs inversus viscerum (iv), a gene that determines left-right asymmetry in the mouse. Genomics. 14: 643-8. PMID 1427890 DOI: 10.1016/S0888-7543(05)80163-6  1
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  1
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  1
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  1
1991 Horwich AL. Inherited hepatic enzyme defects as candidates for liver-directed gene therapy. Current Topics in Microbiology and Immunology. 168: 185-200. PMID 1893777 DOI: 10.1007/978-3-642-76015-0_9  1
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  1
1991 Brueckner M, McGrath J, D'Eustachio P, Horwich AL. Establishment of left-right asymmetry in vertebrates: genetically distinct steps are involved. Ciba Foundation Symposium. 162: 202-12; discussion 2. PMID 1802643  1
1991 Horwich AL, Cheng M, West A, Pollock RA. Mitochondrial protein import. Current Topics in Microbiology and Immunology. 170: 1-42. PMID 1760928  1
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  1
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  1
1990 Horwich AL, Fenton WA. Precarious balance of nitrogen metabolism in women with a urea-cycle defect. The New England Journal of Medicine. 322: 1668-70. PMID 2342527 DOI: 10.1056/Nejm199006073222310  1
1990 Summers J, Smith PM, Horwich AL. Hepadnavirus envelope proteins regulate covalently closed circular DNA amplification. Journal of Virology. 64: 2819-24. PMID 2335817  1
1990 Horwich AL, Furtak K, Pugh J, Summers J. Synthesis of hepadnavirus particles that contain replication-defective duck hepatitis B virus genomes in cultured HuH7 cells. Journal of Virology. 64: 642-50. PMID 2153230  1
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  1
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  1
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  1
1989 Brueckner M, D'Eustachio P, Horwich AL. Linkage mapping of a mouse gene, iv, that controls left-right asymmetry of the heart and viscera. Proceedings of the National Academy of Sciences of the United States of America. 86: 5035-8. PMID 2740340 DOI: 10.1016/0168-9525(89)90134-0  1
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  1
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  1
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  1
1988 Kelley KA, Chamberlain JW, Nolan JA, Horwich AL, Kalousek F, Eisenstadt J, Herrup K, Rosenberg LE. Meiotic expression of human ornithine transcarbamylase in the testes of transgenic mice. Molecular and Cellular Biology. 8: 1821-5. PMID 2837657 DOI: 10.1128/Mcb.8.4.1821  1
1987 Horwich AL, Kalousek F, Fenton WA, Furtak K, Pollock RA, Rosenberg LE. The ornithine transcarbamylase leader peptide directs mitochondrial import through both its midportion structure and net positive charge. The Journal of Cell Biology. 105: 669-77. PMID 3624306 DOI: 10.1083/Jcb.105.2.669  1
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  1
1986 Horwich AL, Kalousek F, Fenton WA, Pollock RA, Rosenberg LE. Targeting of pre-ornithine transcarbamylase to mitochondria: definition of critical regions and residues in the leader peptide. Cell. 44: 451-9. PMID 3943133 DOI: 10.1016/0092-8674(86)90466-6  1
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  1
1986 Rozen R, Fox JE, Hack AM, Fenton WA, Horwich AL, Rosenberg LE. DNA analysis for ornithine transcarbamylase deficiency. Journal of Inherited Metabolic Disease. 9: 49-57. PMID 2878115 DOI: 10.1007/Bf01800858  1
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  1
1985 Horwich AL, Kalousek F, Rosenberg LE. Arginine in the leader peptide is required for both import and proteolytic cleavage of a mitochondrial precursor. Proceedings of the National Academy of Sciences of the United States of America. 82: 4930-3. PMID 3895227 DOI: 10.1073/Pnas.82.15.4930  1
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  1
1985 Kraus JP, Hodges PE, Williamson CL, Horwich AL, Kalousek F, Williams KR, Rosenberg LE. A cDNA clone for the precursor of rat mitochondrial ornithine transcarbamylase: comparison of rat and human leader sequences and conservation of catalytic sites. Nucleic Acids Research. 13: 943-52. PMID 3839075 DOI: 10.1093/Nar/13.3.943  1
1985 Rozen R, Fox J, Fenton WA, Horwich AL, Rosenberg LE. Gene deletion and restriction fragment length polymorphisms at the human ornithine transcarbamylase locus. Nature. 313: 815-7. PMID 2983225 DOI: 10.1038/313815A0  1
1984 Horwich AL, Seashore MR, Dwyer JM. Overwhelming sepsis in the adult variant of Wiskott-Aldrich syndrome. Archives of Internal Medicine. 144: 1498-500. PMID 6732413 DOI: 10.1001/archinte.1984.00350190208036  1
1984 Lindgren V, de Martinville B, Horwich AL, Rosenberg LE, Francke U. Human ornithine transcarbamylase locus mapped to band Xp21.1 near the Duchenne muscular dystrophy locus. Science (New York, N.Y.). 226: 698-700. PMID 6494904 DOI: 10.1126/Science.6494904  1
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  1
1983 Horwich AL, Kraus JP, Williams K, Kalousek F, Konigsberg W, Rosenberg LE. Molecular cloning of the cDNA coding for rat ornithine transcarbamoylase. Proceedings of the National Academy of Sciences of the United States of America. 80: 4258-62. PMID 6576335 DOI: 10.1073/Pnas.80.14.4258  1
1983 Yamaizumi M, Horwich AL, Ruddle FH. Expression and stabilization of microinjected plasmids containing the herpes simplex virus thymidine kinase gene and polyoma virus DNA in mouse cells. Molecular and Cellular Biology. 3: 511-22. PMID 6304496  1
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