Selected Publications:

Cheng, M.-Y., Hartl, F.-U., Martin, J., Pollock, R.A., Kalousek, F., Neupert, W., Hallberg, E.M., Hallberg, R.L. and Horwich, A.L. (1989) Mitochondrial heat shock  protein HSP60 is essential for assembly of proteins imported into yeast mitochondria. Nature 337, 620-625.

Ostermann, J., Horwich, A.L., Neupert, W., and Hartl, F.-U. (1989) Protein folding in mitochondria requires complex formation with HSP60 and ATP-hydrolysis.  Nature 341, 125-130.

Cheng, M.Y., Hartl, F.-U., and Horwich, A.L. (1990) Hsp60, the mitochondrial  chaperonin, is required for its own assembly. Nature 348, 455-458.

Martin, J., Langer, T., Boteva, R., Schramel, A., Horwich, A.L., and Hartl, F.-U. (1991) Chaperonin-mediated protein folding occurs at the surface of groEL via a molten globule-like intermediate. Nature 352, 36-42.

Trent, J., Wall, J., Furtak, K., Nimmesgern, E., Martin, J., Hartl, F.-U., and Horwich,  A.L. (1991) A molecular chaperone from a thermophilic archaebacterium is related to the eukaryotic protein t-complex polypeptide-1.  Nature 354, 490-493.

Yaffe, M.B., Farr, G.W., Miklos, D., Horwich, A.L., Sternlicht, M.L., and Sternlicht, H. (1992) TCP1 complex is a molecular chaperone in tubnulin biogenesis. Nature 358, 245-248.

Braig, K., Simon, M., Furuya, F., Hainfeld, J.F., and Horwich, A.L. (1993)  A polypeptide bound to the chaperonin groEL is localized within a central cavity. Proc. Natl. Acad. Sci. USA 90, 3978-3982.

Horwich, A.L., Low, K.B., Fenton, W.A., Hirshfield, I.N., and Furtak, K. (1993)  Folding in vivo of bacterial cytoplasmic proteins - role of GroEL.  Cell 74, 909-917.

Weissman, J., Kashi, Y., Fenton, W.A., and Horwich, A.L. (1994) GroEL-mediated protein folding occurs by multiple rounds of release and rebinding of non-native forms.  Cell 78, 693-702.

Braig, K., Otwinowski, Z., Hegde, R., Boisvert, D., Joahimiak, A., Horwich, A.L., and Sigler, P.B. (1994)Crystalstructure of GroEL at 2.8 ?.  Nature 371, 578-586.

Fenton, W.A., Kashi, Y., Furtak, K., and Horwich, A.L. (1994) Functional analysis of the chaperonin GroEL:  identification of residues involved in polypeptide binding and release.  Nature 371, 614-619.

Weissman, J.S., Hohl, C.M., Kovalenko, O., Chen, S., Braig, K., Saibil, H.R., Fenton, W.A., and Horwich, A.L. (1995) Mechanism of GroEL action:  Productive release of polypeptide from a sequestered position under GroES.  Cell 83, 577-587.

Weissman, J.S., Rye, H.S., Fenton, W.A., Beechem, J.M., and Horwich, A.L. (1996) Characterization of the active intermediate of a GroEL-GroES-mediated protein folding reaction.  Cell 84, 481-490.

Burston, S.G., Weissman, J.S., Farr, G.W., Fenton, W.A., and Horwich, A.L. (1996)  Release of both native and non-native proteins from a cis-only GroEL ternary complex.  Nature 383, 96-99.

Goldberg, M.S., Sondek, S., Zhang, J., Matthews, C.R., Fox, R.O., and Horwich, A.L.  (1997) Native-like structure of a protein-folding intermediate bound to the chaperonin GroEL.  Proc. Natl. Acad. Sci. USA 94, 1080-1085.

Farr, G., Scharl, E.C., Schumacher, R.J., Sondek, S., and Horwich, A.L. (1997) Chaperonin-mediated folding in the eukaryotic cytosol proceeds through rounds of release of native and non-native forms. Cell 89, 927-937.

Xu, Z., Horwich, A.L., and Sigler, P.B. (1997) The crystal structure of the asymmetric GroEL-GroES-(ADP)₇ chaperonin complex. Nature 388, 741-751.

Rye, H.S., Burston, S.G., Fenton, W.A., Beechem, J.M., Xu, Z., Sigler, P.B., and Horwich, A.L.  (1997) Distinct actions of cis and trans ATP within the double ring of the chaperonin GroEL.  Nature 388, 792-798.

Bukau, B., and Horwich, A.L. (1998)  The chaperone machines.  Cell 92, 351-366.

Sigler, P.B., Xu, Z.,Rye, H.S., Burston, S.G., Fenton, W.A., and Horwich, A.L. (1998) Structure and function in GroEL-mediated protein folding.Annu. Rev. Biochem. 67, 581-608.

Rye, H.S., Roseman, A.M., Furtak, K., Fenton, W.A., Saibil, H.R., and Horwich, A.L.  (1999) GroEL-GroES cycling: ATP and non-native polypeptide direct alternation of folding-active rings.  Cell 97, 325-338.

Weber-Ban, E.U., Reid, B.G., Miranker, A.D., and Horwich, A.L. (1999) Global unfolding of a substrate protein by the Hsp100 chaperone ClpA.  Nature 401, 90-93.

Farr, G., Furtak, K., Rowland, M.C., Ranson, N.A., Saibil, H.R., Kirchhausen, T., and Horwich, A.L. (2000) Multivalent binding of non-native substrate proteins by the chaperonin GroEL.  Cell 100, 561-573.

Reid, B.G., Fenton, W.A., Horwich, A.L., and Weber-Ban, E.U. (2001) ClpA mediates directional translocation of substrate proteins into the ClpP protease.  Proc NatlAcadSci USA 98, 3768-3772.

Chen, J., Walter, S., Horwich, A.L., and Smith, D.L. (2001) Folding of malate dehydrogenase inside the GroEL-GroES cavity.  Nature StructBiol 8, 721-728.

Ranson, N.A., Farr, G.W., Roseman, A.M., Gowen, B., Fenton, W.A., Horwich, A.L., and Saibil, H.R. (2001) ATP-bound states of GroEL captured by cryo-electron microscopy. Cell 107, 869-879.

Chaudhuri, T.K., Farr, G.W., Fenton, W.A., Rospert, S., and Horwich, A.L. (2001) GroEL/GroES-mediated folding of a protein too large to be encapsulated. Cell 107, 235-246.

Fiaux, J., Bertelsen, E.B., Horwich, A.L., and Wuthrich, K. (2002) NMR analysis of a 900K GroEL GroES complex. Nature 418, 207-211.

Farr, G.W., Fenton, W.A., Chaudhuri, T.K., Clare, D.K., Saibil, H.R., and Horwich, A.L. (2003) Folding with and without encapsulation by cis and trans-only GroEL-GroES complexes.  EMBO J 22, 3220-3230.

Fenton, W.A., Horwich, A.L. (2003) Chaperonin-mediated protein folding: fate of substrate polypeptide.? Q Rev Biophys 36, 229-256.

Motojima, F., Chaudhry, C., Fenton, W.A., Farr, G.W., and Horwich, A.L. (2004) Substrate polypeptide presents a load on the apical domains of the chaperonin GroEL. Proc NatlAcadSci U S A 101, 15005-15012.

Park, E.S., Fenton, W.A., and Horwich, A.L. (2005) 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 Lett 579, 1183-1186.

Hinnerwisch, J., Fenton, W.A., Furtak, K.J., Farr, G.W., and Horwich, A.L. (2005) Loops in the central channel of ClpA chaperone mediate protein binding, unfolding, and translocation. Cell 121, 1029-1041.

Horst, R., Bertelsen, E.B., Fiaux, J., Wider, G., Horwich, A.L., and W?thrich, K. (2005) Direct NMR observation of a substrate protein bound to the chaperonin GroEL. Proc NatlAcadSciUSA102, 12748-12753.

Chapman, E., Farr, G.W., Usaite, R., Furtak, K., Fenton, W.A., Chaudhuri, T.K., Hondorp, E.R., Matthews, R.G., Wolf, S.G., Yates, J.R., Pypaert, M., and Horwich, A.L. (2006) Global aggregation of newly translated proteins in an Escherichia coli strain deficient of the chaperonin GroEL. Proc NatlAcadSci USA 103, 15800-15805.

Park, E.S., Fenton, W.A., and Horwich, A.L. (2007) Disulfide formation as a probe of folding in GroEL-GroES reveals correct formation of long-range bonds and editing of incorrect short-range ones. Pro.NatlAcadSciUSA104, 2145-2150.

Farr, G.W., Fenton, W.A., and Horwich, A.L. (2007) Perturbed ATPase activity and not "close confinement" of substrate in the cis cavity affects rates of folding by tail-multiplied GroEL. Proc NatlAcadSciUSA104, 5342-5347.

Elad, N., Farr, G.W., Clare, D.K., Orlova, E.V., Horwich, A.L., and Saibil, H.R. (2007) Topologies of a substrate protein bound to the chaperonin GroEL. Mol Cell 26, 415-426.

Horst, R., Fenton, W.A., Englander, S.W., W?thrich, K., and Horwich, A.L. (2007) Folding trajectories of human dihydrofolate reductase inside the GroEL GroES chaperonin cavity and free in solution. Proc NatlAcadSci USA 104, 20788-20792.

Apetri, A.C., and Horwich, A.L. (2008) Chaperonin chamber accelerates protein folding through passive action of preventing aggregation. Proc NatlAcadSci USA 105, 17351-17355.

Wang, J., Farr, G.W., Hall, D.H., Li, F., Furtak, K., Dreier, L., and Horwich, A,L. (2009) An ALS-linked mutant SOD1 produces a locomotor defect associated with aggregation and synaptic dysfunction when expressed in neurons of Caenorhabditiselegans. PLoS Genet 5, e1000350. doi:10.1371/journal.pgen.1000350

Wang, J., Farr, G.W., Zeiss, C.J., Rodriguez-Gil, D.J., Wilson, J.H., Furtak, K., Rutkowski, D.T., Kaufman, R.J., Ruse, C.I., Yates, J.R., 3rd, Perrin, S., Feany, M.B., and Horwich, A.L. (2009) Progressive aggregation despite chaperone associations of a mutant SOD1-YFP in transgenic mice that develop ALS. Proc NatlAcadSci USA 106, 1392-1397.

Tyagi, N.K., Fenton, W.A., and Horwich, A.L. (2009) GroEL/GroES cycling: ATP binds to an open ring before substrate protein favoring protein binding and production of the native state. Proc Natl Acad Sci USA 106, 20264-20269.

Tyagi, N.K., Fenton, W.A., and Horwich, A.L. (2010) ATP-triggered ADP release from the asymmetric chaperonin GroEL/GroES/ADP₇ is not the rate-limiting step of the GroEL/GroES reaction cycle. FEBS Lett. 584, 951-953.

Farr, G.W., Ying, Z., Fenton, W.A., and Horwich, A.L. (2011) Hydrogen-deuterium exchange in vivo to measure turnover of an ALS-associated mutant SOD1 protein in spinal cord of mice. Protein Sci. 20, 1692-1696.

Clare, D.K., Vasishtan, D., Stagg, S., Quispe, J., Farr, G.W., Topf, M., Horwich, A.L., and Saibil, H.R. (2012) ATP-triggered conformational changes delineate substrate-binding and -folding mechanics of the GroEL chaperonin.  Cell 149, 113-123.