MeSH Review:
Protein Folding
- In vivo observation of polypeptide flux through the bacterial chaperonin system. Ewalt, K.L., Hendrick, J.P., Houry, W.A., Hartl, F.U. Cell (1997)
- Structural adaptations in the specialized bacteriophage T4 co-chaperonin Gp31 expand the size of the Anfinsen cage. Hunt, J.F., van der Vies, S.M., Henry, L., Deisenhofer, J. Cell (1997)
- A foldable CFTR{Delta}F508 biogenic intermediate accumulates upon inhibition of the Hsc70-CHIP E3 ubiquitin ligase. Younger, J.M., Ren, H.Y., Chen, L., Fan, C.Y., Fields, A., Patterson, C., Cyr, D.M. J. Cell Biol. (2004)
- Structure of human lactoferrin at 3.2-A resolution. Anderson, B.F., Baker, H.M., Dodson, E.J., Norris, G.E., Rumball, S.V., Waters, J.M., Baker, E.N. Proc. Natl. Acad. Sci. U.S.A. (1987)
- Carnitine palmitoyltransferase in cardiac ischemia. A potential site for altered fatty acid metabolism. Pauly, D.F., Kirk, K.A., McMillin, J.B. Circ. Res. (1991)
- Doxycycline and protein folding agents rescue the abnormal phenotype of familial CJD H187R in a cell model. Gu, Y., Singh, N. Brain Res. Mol. Brain Res. (2004)
- Chaperone-mediated protein folding. Fink, A.L. Physiol. Rev. (1999)
- Structure of Ero1p, source of disulfide bonds for oxidative protein folding in the cell. Gross, E., Kastner, D.B., Kaiser, C.A., Fass, D. Cell (2004)
- ATP-bound states of GroEL captured by cryo-electron microscopy. Ranson, N.A., Farr, G.W., Roseman, A.M., Gowen, B., Fenton, W.A., Horwich, A.L., Saibil, H.R. Cell (2001)
- ARSACS, a spastic ataxia common in northeastern Québec, is caused by mutations in a new gene encoding an 11.5-kb ORF. Engert, J.C., Bérubé, P., Mercier, J., Doré, C., Lepage, P., Ge, B., Bouchard, J.P., Mathieu, J., Melançon, S.B., Schalling, M., Lander, E.S., Morgan, K., Hudson, T.J., Richter, A. Nat. Genet. (2000)
- Polypeptide flux through bacterial Hsp70: DnaK cooperates with trigger factor in chaperoning nascent chains. Teter, S.A., Houry, W.A., Ang, D., Tradler, T., Rockabrand, D., Fischer, G., Blum, P., Georgopoulos, C., Hartl, F.U. Cell (1999)
- Cooperation of enzymatic and chaperone functions of trigger factor in the catalysis of protein folding. Scholz, C., Stoller, G., Zarnt, T., Fischer, G., Schmid, F.X. EMBO J. (1997)
- A Bethlem myopathy Gly to Glu mutation in the von Willebrand factor A domain N2 of the collagen alpha3(VI) chain interferes with protein folding. Sasaki, T., Hohenester, E., Zhang, R.Z., Gotta, S., Speer, M.C., Tandan, R., Timpl, R., Chu, M.L. FASEB J. (2000)
- Homogeneous Escherichia coli chaperonin 60 induces IL-1 beta and IL-6 gene expression in human monocytes by a mechanism independent of protein conformation. Tabona, P., Reddi, K., Khan, S., Nair, S.P., Crean, S.J., Meghji, S., Wilson, M., Preuss, M., Miller, A.D., Poole, S., Carne, S., Henderson, B. J. Immunol. (1998)
- Oligomycin sensitivity-conferring protein (OSCP) of mitochondrial ATP synthase. The carboxyl-terminal region of OSCP is essential for the reconstitution of oligomycin-sensitive H(+)-ATPase. Joshi, S., Javed, A.A., Gibbs, L.C. J. Biol. Chem. (1992)
- High salt-induced conversion of Escherichia coli GroEL into a fully functional thermophilic chaperonin. Kusmierczyk, A.R., Martin, J. J. Biol. Chem. (2000)
- Trigger factor and DnaK cooperate in folding of newly synthesized proteins. Deuerling, E., Schulze-Specking, A., Tomoyasu, T., Mogk, A., Bukau, B. Nature (1999)
- Mutants of bovine pancreatic trypsin inhibitor lacking cysteines 14 and 38 can fold properly. Marks, C.B., Naderi, H., Kosen, P.A., Kuntz, I.D., Anderson, S. Science (1987)
- Structure and function of DNA methyltransferases. Cheng, X. Annual review of biophysics and biomolecular structure. (1995)
- Macromolecular crowding perturbs protein refolding kinetics: implications for folding inside the cell. van den Berg, B., Wain, R., Dobson, C.M., Ellis, R.J. EMBO J. (2000)
- Active site mutations in yeast protein disulfide isomerase cause dithiothreitol sensitivity and a reduced rate of protein folding in the endoplasmic reticulum. Holst, B., Tachibana, C., Winther, J.R. J. Cell Biol. (1997)
- A homologue of the bacterial heat-shock gene DnaJ that alters protein sorting in yeast. Blumberg, H., Silver, P.A. Nature (1991)
- Role of the chaperonin cofactor Hsp10 in protein folding and sorting in yeast mitochondria. Höhfeld, J., Hartl, F.U. J. Cell Biol. (1994)
- Complementation of DsbA deficiency with secreted thioredoxin variants reveals the crucial role of an efficient dithiol oxidant for catalyzed protein folding in the bacterial periplasm. Jonda, S., Huber-Wunderlich, M., Glockshuber, R., Mössner, E. EMBO J. (1999)
- The cyclosporin A-binding immunophilin CyP-40 and the FK506-binding immunophilin hsp56 bind to a common site on hsp90 and exist in independent cytosolic heterocomplexes with the untransformed glucocorticoid receptor. Owens-Grillo, J.K., Hoffmann, K., Hutchison, K.A., Yem, A.W., Deibel, M.R., Handschumacher, R.E., Pratt, W.B. J. Biol. Chem. (1995)
- Conformational dynamics underlie the activity of the auxin-binding protein, Nt-abp1. David, K., Carnero-Diaz, E., Leblanc, N., Monestiez, M., Grosclaude, J., Perrot-Rechenmann, C. J. Biol. Chem. (2001)
- Protein-disulphide isomerase and prolyl isomerase act differently and independently as catalysts of protein folding. Lang, K., Schmid, F.X. Nature (1988)
- Isolation and sequence of an FK506-binding protein from N. crassa which catalyses protein folding. Tropschug, M., Wachter, E., Mayer, S., Schönbrunner, E.R., Schmid, F.X. Nature (1990)
- Hybrid hydrogels assembled from synthetic polymers and coiled-coil protein domains. Wang, C., Stewart, R.J., Kopecek, J. Nature (1999)
- Rules for alpha-helix termination by glycine. Aurora, R., Srinivasan, R., Rose, G.D. Science (1994)
- Folding of VSV G protein: sequential interaction with BiP and calnexin. Hammond, C., Helenius, A. Science (1994)
- Association of a 59-kilodalton immunophilin with the glucocorticoid receptor complex. Tai, P.K., Albers, M.W., Chang, H., Faber, L.E., Schreiber, S.L. Science (1992)
- The ERO1 gene of yeast is required for oxidation of protein dithiols in the endoplasmic reticulum. Frand, A.R., Kaiser, C.A. Mol. Cell (1998)
- Presenilin-1 mutations downregulate the signalling pathway of the unfolded-protein response. Katayama, T., Imaizumi, K., Sato, N., Miyoshi, K., Kudo, T., Hitomi, J., Morihara, T., Yoneda, T., Gomi, F., Mori, Y., Nakano, Y., Takeda, J., Tsuda, T., Itoyama, Y., Murayama, O., Takashima, A., St George-Hyslop, P., Takeda, M., Tohyama, M. Nat. Cell Biol. (1999)
- Manipulation of oxidative protein folding and PDI redox state in mammalian cells. Mezghrani, A., Fassio, A., Benham, A., Simmen, T., Braakman, I., Sitia, R. EMBO J. (2001)
- The protein-folding activity of chaperonins correlates with the symmetric GroEL14(GroES7)2 heterooligomer. Azem, A., Diamant, S., Kessel, M., Weiss, C., Goloubinoff, P. Proc. Natl. Acad. Sci. U.S.A. (1995)
- Structural and functional characterization of the CD2 immunoadhesion domain. Evidence for inclusion of CD2 in an alpha-beta protein folding class. Recny, M.A., Neidhardt, E.A., Sayre, P.H., Ciardelli, T.L., Reinherz, E.L. J. Biol. Chem. (1990)
- Prion glycoprotein: structure, dynamics, and roles for the sugars. Rudd, P.M., Wormald, M.R., Wing, D.R., Prusiner, S.B., Dwek, R.A. Biochemistry (2001)
- The molecular basis of cooperativity in protein folding. Thermodynamic dissection of interdomain interactions in phosphoglycerate kinase. Freire, E., Murphy, K.P., Sanchez-Ruiz, J.M., Galisteo, M.L., Privalov, P.L. Biochemistry (1992)
- Alcohol-induced protein folding transitions in platelet factor 4: the O-state. Yang, Y., Mayo, K.H. Biochemistry (1993)