Results 161 to 170 of about 8,360 (214)

A chaperonin complex regulates organelle proteostasis in malaria parasites. [PDF]

PLoS Pathog
Tissawak A, Rosin Y, Katz Galay S, Qasem A, Shahar M, Trabelsi N, Furman-Schueler O, Johnson SM, Florentin A.   +8 more
europepmc   +1 more source

The Role of <i>Helicobacter pylori</i> Heat Shock Proteins in Gastric Diseases' Pathogenesis. [PDF]

Int J Mol Sci
Manna OM, Caruso Bavisotto C, Gratie MI, Damiani P, Tomasello G, Cappello F.   +5 more
europepmc   +1 more source

Molecular, structural, and functional characterization of delta subunit of T-complex protein-1 from <i>Leishmania donovani</i>. [PDF]

Infect Immun
Anand A, Gautam G, Srivastava G, Yadav S, Ramalingam K, Siddiqi MI, Goyal N.   +6 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

The structural basis of eukaryotic chaperonin TRiC/CCT: Action and folding. [PDF]

Mol Cells
Kim H, Park J, Roh SH.
europepmc   +1 more source

Origin of chaperone dependence and assembly complexity in Rubisco’s biogenesis

Ng JZY, Wiens D, Schulz L, Hergenröder A, Küffner AM, Geil C, Erb TJ, Hochberg GKA.   +7 more
europepmc   +1 more source

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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

Allostery in chaperonins

Rendiconti Lincei, 2006
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   +2 more sources

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