Results 41 to 50 of about 23,956 (223)

Friends in need: How chaperonins recognize and remodel proteins that require folding assistance

Frontiers in Molecular Biosciences, 2022
Chaperonins are biological nanomachines that help newly translated proteins to fold by rescuing them from kinetically trapped misfolded states. Protein folding assistance by the chaperonin machinery is obligatory in vivo for a subset of proteins in the ...
George Stan, George H. Lorimer, D. Thirumalai, D. Thirumalai   +3 more
doaj   +1 more source

Emerging themes in the Identifying Successful STARTS Methodologies project and exhibition

Artnodes, 2023
In 2019 a team of multi-disciplinary researchers undertook a research project entitled Identifying Successful STARTS Methodologies (ISSM) (2019-2021) in order to analyze the innovative and collaborative strategies utilized by the global Science ...
Denise Doyle, Richard Glover, Martin Khechara, Sebastian Groes   +3 more
doaj   +1 more source

Refolding of yeast enolase in the presence of the chaperonin GroE. The nucleotide specificity of GroE and the role of GroES.

Journal of Biological Chemistry, 1993
GroE, a chaperonin protein from Escherichia coli, facilitates the folding of numerous proteins by binding to protein-folding intermediates and suppressing aggregation (Gething, M., and Sambrook, J. (1992) Nature 355, 33-45). The specific mechanism of GroE-facilitated folding involves numerous interactions between GroEL, GroES, the refolding protein ...
T, Kubo, T, Mizobata, Y, Kawata
openaire   +2 more sources

Hsp70 in mitochondrial biogenesis [PDF]

, 1994
The family of hsp70 (70 kilodalton heat shock protein) molecular chaperones plays an essential and diverse role in cellular physiology, Hsp70 proteins appear to elicit their effects by interacting with polypeptides that present domains which exhibit non ...
A. Tzagoloff, A. Tzagoloff, A.J. Caplan, A.J. Caplan, B.D. Gambill, B.S. Glick, C.K. Suzuki, D. Ang, D. M. Cyr, D.M. Cyr, D.M. Cyr, D.M. Cyr, D.M. Cyr, D.P. Atencio, E. Ikeda, E. Kutejová, E.A. Craig, E.A. Craig, F.-U. Hartl, G.S.P. Groot, H.R.B. Pelham, J. Ostermann, J. Rassow, J.F. Dice, J.P. Hendrick, K. Liberek, L. Dyck van, M. Eilers, M. Kiebler, M. Schleyer, M.-J. Gething, M.Y. Cheng, N. Rowley, N. Wang, P. Borst, P. Terpstra, P.-J. Kang, R. A. Stuart, R.A. Stuart, R.A. Stuart, R.B. Deshaies, R.G. Hadikusumo, R.J. Nelson, R.P. Beckman, S. Lindquist, S. Rospert, S.T. Hwang, T. Langer, U.C. Manning-Krieg, W. Neupert, W. Neupert, W. Voos, W.J. Chirico, Z. Xia   +53 more
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Catalysis, Commitment and Encapsulation during GroE-mediated Folding [PDF]

Journal of Molecular Biology, 1999
The Escherichia coli GroE chaperones assist protein folding under conditions where no spontaneous folding occurs. To achieve this, the cooperation of GroEL and GroES, the two protein components of the chaperone system, is an essential requirement. While in many cases GroE simply suppresses unspecific aggregation of non-native proteins by encapsulation,
M, Beissinger, K, Rutkat, J, Buchner
openaire   +2 more sources

Bridging between NMA and Elastic Network Models: Preserving All-Atom Accuracy in Coarse-Grained Models. [PDF]

PLoS Computational Biology, 2015
Dynamics can provide deep insights into the functional mechanisms of proteins and protein complexes. For large protein complexes such as GroEL/GroES with more than 8,000 residues, obtaining a fine-grained all-atom description of its normal mode motions ...
Hyuntae Na, Robert L Jernigan, Guang Song   +2 more
doaj   +1 more source

Enhanced Production of (R)-3-Hydroxybutyrate Oligomers by Coexpression of Molecular Chaperones in Recombinant Escherichia coli Harboring a Polyhydroxyalkanoate Synthase Derived from Bacillus cereus YB-4

Microorganisms, 2022
The biodegradable polyester poly-(R)-3-hydroxybutyrate [P(3HB)] is synthesized by a polymerizing enzyme called polyhydroxyalkanoate (PHA) synthase and accumulates in a wide variety of bacterial cells. Recently, we demonstrated the secretory production of
Saki Goto, Yuki Miyahara, Seiichi Taguchi, Takeharu Tsuge, Ayaka Hiroe   +4 more
doaj   +1 more source

Necrotrophic growth of periodontopathogens is a novel virulence factor in oral biofilms [PDF]

, 2017
The oral use of antimicrobial agents embedded in toothpastes and mouth rinses results in an oral microbial massacre with high amounts of dead bacteria in close proximity to few surviving bacteria.
Bernaerts, Kristel, Boon, Nico, Pauwels, Martine, Quirynen, Marc, Rodriguez Herrero, Esteban, Slomka, Vera, Teughels, Wim   +6 more
core   +1 more source

GroEL‐GroES‐mediated protein folding

The FASEB Journal, 2008
The chaperonin system assists the folding of a large variety of proteins by two actions: binding in the hydrophobic central cavity of an open ring and folding mediated in a subsequently GroES‐encapsulated hydrophilic chamber. We have been studying the GroEL system both in vivo and in vitro, and report on recent results.
Arthur Horwich, Eli Chapman, Eda Koculi, Adrian Apetri, Wayne A. Fenton, George Farr, Reto Horst, Kurt Wüthrich   +7 more
openaire   +1 more source

Environmental stress responses in Lactococcus lactis [PDF]

, 1999
Bacteria can encounter a variety of physical conditions during their life. Bacterial cells are able to survive these (often adverse) conditions by the induction of specific or general protection mechanisms. The lactic acid bacterium Lactococcus lactis is
Kok, Jan,, Sanders, Jan Willem,, Venema, Gerard,   +2 more
core   +3 more sources