Results 121 to 130 of about 4,302 (172)

mRNA therapy as primary and bridge therapy for inborn errors of metabolism. [PDF]

Mol Ther
Vockley J.
europepmc   +1 more source

Homozygous Frameshift Mutation in the BBS10 Gene Causing Bardet-Biedl Syndrome with Rod-Cone Dystrophy: A Case Report. [PDF]

Korean J Ophthalmol
Heo J, Jeong YH, Park SW, Byon I, Kwon HJ.   +4 more
europepmc   +1 more source

External Force Field for Protein Folding in ChaperoninsPotential Application in In Silico Protein Folding

ACS Omega
Irena Roterman, Katarzyna Stapor, Dawid Dułak, Leszek Konieczny   +3 more
doaj   +1 more source

Asymmetric apical domain states of mitochondrial Hsp60 coordinate substrate engagement and chaperonin assembly. [PDF]

Nat Struct Mol Biol
Braxton JR, Shao H, Tse E, Gestwicki JE, Southworth DR.   +4 more
europepmc   +1 more source

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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
exaly   +3 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 FUNCTION DEPENDS ON STRUCTURE AND DISORDER IN CO-CHAPERONIN MOBILE LOOPS [PDF]

Biocomputing '99, 1998
Co-chaperonins from diverse organisms exhibit mobile loops which fold into a beta hairpin conformation upon binding to the chaperonin. GroES, Gp31, and human Hsp10 mobile loops exhibit a preference for the beta hairpin conformation in the free co-chaperonins, and the conformational dynamics of the human Hsp10 mobile loop appear to be restricted by ...
S. J. Landry, N. K. Steede, A. M. Garaudy, K. Maskos, P. V. Viitanen   +4 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

On the evolutionary origin of the chaperonins

Proteins: Structure, Function, and Bioinformatics, 2011
AbstractAn analysis of the apical domain of the Group‐I and Group‐II chaperonins shows that they have structural similarities to two different protein folds: a “swivel‐domain” phosphotransferase and a thioredoxin‐like peroxiredoxin. There is no significant sequence similarity that supports either similarity and the degree of similarity based on ...
Dekker, C, Willison, KR, Taylor, WR
openaire   +3 more sources