Results 141 to 150 of about 5,379 (199)

Dicarboxylic acids synergize with yeast and human Hsp60/10 systems to mimic GroEL/ES

Gautam D, Aaquib M, Kochar M, Chakraborty K.   +3 more
europepmc   +1 more source

Candidate Interaction Partners of Calpain-5 Suggest Clues to Its Involvement in Neovascular Inflammatory Vitreoretinopathy. [PDF]

Cells
Gal J, Bondada V, Crasta R, Croall DE, Vary CP, Geddes JW.   +5 more
europepmc   +1 more source

Chaperone-mediated remodelling of mutant huntingtin. [PDF]

Philos Trans R Soc Lond B Biol Sci
Gharat K, Kirstein J.
europepmc   +1 more source

On adaptation to a mesophilic environment and the chaperone network in Archaea

Rebeaud ME.
europepmc   +1 more source

Stress resilience in <i>Coffea arabica</i> and <i>Coffea canephora</i> under harsh drought and/or heat conditions: selected genes, proteins, and lipid integrated responses. [PDF]

Front Plant Sci
Ramalho JC, Marques I, Pais IP, Armengaud J, Gouveia D, Rodrigues AP, Dubberstein D, Leitão AE, Rakočević M, Scotti-Campos P, Martins S, Semedo MC, Partelli FL, Lidon FC, DaMatta FM, Ribeiro-Barros AI.   +15 more
europepmc   +1 more source

Hsp90 co-chaperone FKBP4 facilitates CCT8 folding and connects Hsp90 to chaperonin-dependent proteostasis. [PDF]

J Biol Chem
Huang YY, Chang YL, Chen Y, Chiang WY, Chiang AT, Hsu PH, Teng SC.   +6 more
europepmc   +1 more source

The Nuclear Interactome of ATR7 Implicates a Chromatin-Based Repression Mechanism Controlling Oxidative Stress Tolerance and Programmed Cell Death in Arabidopsis. [PDF]

Int J Mol Sci
Qureshi MK, Gechev T.
europepmc   +1 more source

Multiple chaperonins in bacteria--why so many?

FEMS Microbiology Reviews, 2009
A significant proportion of bacteria express two or more chaperonin genes. Chaperonins are a group of molecular chaperones, defined by sequence similarity, required for the folding of some cellular proteins. Chaperonin monomers have a mass of c.
Peter A Lund
exaly   +2 more sources

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Purification of chaperonins

Journal of Chromatography B: Biomedical Sciences and Applications, 1999
The availability of protein samples of sufficient quality and in sufficient quantity is a driving force in biology and biotechnology. Protein samples that are free of critical contaminants are required for specific assays. Large amounts of highly homogeneous and reproducible material are needed for crystallography and nuclear magnetic resonance studies
E, Quaite-Randall, A, Joachimiak
openaire   +2 more sources

Review: Allostery in Chaperonins

Journal of Structural Biology, 2001
Chaperonins mediate protein folding in an ATP-dependent manner. ATP binding and hydrolysis by chaperonins are subject to both homotropic and heterotropic allosteric regulation. In the case of GroEL and CCT, homotropic regulation by ATP is manifested in nested cooperativity, which involves positive intra-ring cooperativity and negative inter-ring ...
Amnon Horovitz, Ofer Yifrach, O Yifrach
exaly   +3 more sources