Identification of a second Escherichia coli groE gene whose product is necessary for bacteriophage morphogenesis. Trigger factor is involved in GroEL-dependent protein degradation in Escherichia coli and promotes binding of GroEL to unfolded proteins. Kandror O, Sherman M, Rhode M, Goldberg AL.Binding and hydrolysis of nucleotides in the chaperonin catalytic cycle: implications for the mechanism of assisted protein folding. Jackson GS, Staniforth RA, Halsall DJ, Atkinson T, Holbrook JJ, Clarke AR, Burston SG.Kinetics versus thermodynamics in protein folding. The formation of protein disulphide bonds. Calnexin: a membrane-bound chaperone of the endoplasmic reticulum. Bergeron JJ, Brenner MB, Thomas DY, Williams DB.Identification and structural characterization of the ATP/ADP-binding site in the Hsp90 molecular chaperone. Prodromou C, Roe SM, O'Brien R, Ladbury JE, Piper PW, Pearl LH.Crystal structure of an Hsp90-geldanamycin complex: targeting of a protein chaperone by an antitumor agent. Stebbins CE, Russo AA, Schneider C, Rosen N, Hartl FU, Pavletich NP.Role of the chaperone protein Hsp104 in propagation of the yeast prion-like factor. Chernoff YO, Lindquist SL, Ono B, Inge-Vechtomov SG, Liebman SW.coli homolog of the 20S proteasome, and its ATP-dependent activator, ClpY. Six-fold rotational symmetry of ClpQ, the E.
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