Results 161 to 170 of about 21,272 (221)

Dissection of <i>in vivo</i> archaeal RNA polymerase assembly reveals a modular pathway and stoichiometric control. [PDF]

mBio
Li J, Qi W, Duan H, Ren D, Liu J, Dong X.   +5 more
europepmc   +1 more source

TRiC-assisted folding of class I HDAC family proteins regulated by distinct co-chaperone and cofactor networks. [PDF]

Sci Adv
Li Z, Zhao Q, Jiang W, Song Q, Zhou X, Shi X, Zhang Q, Wang Y, Lin Y, Yin Y, Pan C, Cong Y.   +11 more
europepmc   +1 more source

The TRiC/CCT Complex at the Crossroads of Metabolism and Hypoxia in GBM: Implications for IDH-Dependent Therapeutic Targeting. [PDF]

Int J Mol Sci
Alberti G, D'Amico G, Augello MA, Cappello F, Szychlinska MA, Caruso Bavisotto C, Scalia F.   +6 more
europepmc   +1 more source

Genetic and structural insights into the functional importance of the conserved gly-met-rich C-terminal tails in bacterial chaperonins. [PDF]

Commun Biol
Kumar CMS, Mai AM, Mande SC, Lund PA.
europepmc   +1 more source

Rearrangement of the Cell Chaperone Machinery in Human Fibrosarcoma HT1080 Cells With the Knocked-Out HSP90AA1 Gene Encoding Hsp90α. [PDF]

Biol Cell
Petrenko V, Vrublevskaya V, Skarga Y, Zhmurina M, Morenkov O.   +4 more
europepmc   +1 more source

Chaperonin-containing tailless complex polypeptide 1 subunit 6A negatively regulates autophagy and protects colorectal cancer cells from cisplatin-induced cytotoxicity. [PDF]

World J Gastroenterol
Ma JX, Li XJ, Li YL, Liu MC, Du RH, Cheng Y, Li LJ, Ai ZY, Jiang JT, Yan SY.   +9 more
europepmc   +1 more source

Pathway of Actin Folding Directed by the Eukaryotic Chaperonin TRiC

Cell, 2018
The hetero-oligomeric chaperonin of eukarya, TRiC, is required to fold the cytoskeletal protein actin. The simpler bacterial chaperonin system, GroEL/GroES, is unable to mediate actin folding.
Manajit Hayer-Hartl, Mike Strauss, David Balchin   +2 more
exaly   +2 more sources

Some of the next articles are maybe not open access.

Related searches:

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

On the oligomeric state of chloroplast chaperonin 10 and chaperonin 20

Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics, 2003
Type I chaperonins are fundamental protein folding machineries that function in eubacteria, mitochondria and chloroplasts. Eubacteria and mitochondria contain chaperonin systems comprised of homo-oligomeric chaperonin 60 tetradecamers and co-chaperonin 10 heptamers.
Rajach, Sharkia, Anat L, Bonshtien, Itzhak, Mizrahi, Celeste, Weiss, Adina, Niv, Ariel, Lustig, Paul V, Viitanen, Abdussalam, Azem   +7 more
openaire   +2 more sources

Chaperonin: Co-chaperonin Interactions

2014
Co-chaperonins function together with chaperonins to mediate ATP-dependent protein folding in a variety of cellular compartments. Chaperonins are evolutionarily conserved and form two distinct classes, namely, group I and group II chaperonins. GroEL and its co-chaperonin GroES form part of group I and are the archetypal members of this family of ...
openaire   +3 more sources