Results 101 to 110 of about 21,272 (221)

Seryl phosphorylation modulates chaperonin function of Mycobacterial chaperonin, Cpn60.1

Cell Stress & Chaperones
The GroEL chaperonin forms a 14‑subunit double ring that encapsulates client proteins for folding with the aid of the cochaperonin GroES. Mycobacteria encode two GroEL homologs: Cpn60.2 (which is essential) and Cpn60.1 (which is non-essential but which ...
C. M. Santosh Kumar, Monika Singh, Shekhar C. Mande, Peter A. Lund   +3 more
doaj   +1 more source

The essential role of CCT2 in the regulation of aggrephagy

Frontiers in Aging Neuroscience
Protein aggregation, a defining characteristic of numerous human diseases, poses a significant challenge to cellular health. Autophagy, an essential cellular recycling process, specifically targets and degrades these harmful protein aggregates through a ...
Jie Luo, Ze-Sen Feng, Ji-Xin Tang
doaj   +1 more source

Characterization of Archaeal Group II Chaperonin-ADP-Metal Fluoride Complexes

, 2005
Group II chaperonins, found in Archaea and in the eukaryotic cytosol, act independently of a cofactor corresponding to GroES of group I chaperonins.
桑島, 邦博, et, al., IIZUKA, Ryo, KUWAJIMA, Kunihiro   +3 more
core   +1 more source

Chaperonins [PDF]

Current Biology, 1996
openaire   +2 more sources

A Role for Confined Water in Chaperonin Function

, 2015
A Role for Confined Water in Chaperonin ...
Del Lucent (239216), Vijay S. Pande (187500), Jeremy L. England (1265178)   +2 more
core   +1 more source

Los complejos Chaperonina(MSP63)inducen anticuerpos de reacciones cruzadas, bactericidas y opsonofagocítica.

VacciMonitor, 2009
Alteration of the native structure of antigens can lead to the loss of protective epitopes. Our previous results showed that separation of the meningococcal outer membrane proteins in native conditions revealed the existence of protein complexes that ...
Juan Marzoa, Sandra Sánchez, Charlotte Brookes, Stephen Taylor, Andrew Gorringe, M. Teresa Criado, Carlos M. Ferreirós   +6 more
doaj  

Visualizing chaperonin function in situ by cryo-electron tomography

Chaperonins are large barrel-shaped complexes that mediate ATP-dependent protein folding 1–3 . The bacterial chaperonin GroEL forms juxtaposed rings that bind unfolded protein and the lid-shaped cofactor GroES at their apertures. In vitro analyses of the
Baumeister, Wolfgang, Hartl, F. Ulrich, Beck, Florian, Bohn, Stefan, Wan, William, Wagner, Jonathan, Bracher, Andreas, Körner, Roman, Fernandez-Busnadiego, Ruben, Carvajal, Alonso I.   +9 more
core   +2 more sources

The chaperonin from the archaeon Sulfolobus solfataricus promotes correct refolding and prevents thermal denaturation in vitro.

, 1994
We have isolated a chaperonin from the hyperthermophilic archaeon Sulfolobus solfataricus based on its ability to inhibit the spontaneous refolding 5a0t "C of dimeric S. solfataricus malic enzyme.
ROSSI M., CERCHIA L., BARTOLUCCI, SIMONETTA, GUAGLIARDI A.   +3 more
core   +1 more source

Versatile platform for nanotechnology based on circular permutations of chaperonin protein [PDF]

, 2010
The present invention provides chaperonin polypeptides which are modified to include N-terminal and C-terminal ends that are relocated from the central pore region to various different positions in the polypeptide which are located on the exterior of the
Trent, Jonathan D., Paavola, Chad D., Chan, Suzanne L., Li, Yi-Fen, McMillan, R. Andrew, Kagawa, Hiromi   +5 more
core  

Crystal Structure of the 65 Kilodalton Heat Shock Protein, Chaperonin 60.2, of Mycobacterium tuberculosis

, 2004
Chaperonin 60s are a ubiquitous class of proteins that promote folding and assembly of other cellular polypeptides in an ATP dependent manner. The oligomeric state of chaperonin 60s has been shown to be crucial to their role as molecular chaperones ...
Qamra, R., Mande, S.C.
core   +1 more source