Results 161 to 170 of about 9,153 (190)

Co‐chaperonin GroES as a modulator of proteasomal activity

Journal of Molecular Recognition, 2008
AbstractThe proteasome has a crucial part in the degradation of normal, damaged, mutant or misfolded proteins within both the ubiquitin ATP‐dependent and the ubiquitin ATP‐independent pathways. Proteasome‐mediated proteolysis is modulated by diverse factors, and in this regard, chaperonins have been attracting great interest.
CUCCIOLONI, Massimiliano, MONTECCHIA F, AMICI M, MOZZICAFREDDO, MATTEO, ELEUTERI, Anna Maria, ANGELETTI, Mauro   +5 more
openaire   +3 more sources

Prediction of the structure of GroES and its interaction with GroEL

Proteins: Structure, Function, and Bioinformatics, 1995
AbstractThe three‐dimensional structure of the GroES monomer and its interaction with GroEL has been predicted using a combination of prediction tools and experimental data obtained by biophysical [electron microscope (EM), Fourier transform infrared (FTIR), and nuclear magnetic resonance (NMR)] and biochemical techniques.
Valencia, A, Hubbard, T J, Muga, A, Bañuelos, S, Llorca, O, Carrascosa, J L, Valpuesta, J M   +6 more
openaire   +3 more sources

Dissociation of the GroEL−GroES Asymmetric Complex Is Accelerated by Increased Cooperativity in ATP Binding to the GroEL Ring Distal to GroES

Biochemistry, 2002
A kinetic analysis of the ATP-dependent dissociation of wild-type GroEL and mutants from immobilized GroES was carried out using surface plasmon resonance. Excellent fits of the data were obtained using a double-exponential equation with a linear drift. Both the fast and slow observed dissociation rate constants are found to have a sigmoidal dependence
Yael, Fridmann, Galit, Kafri, Oded, Danziger, Amnon, Horovitz   +3 more
openaire   +2 more sources

The Escherichia coli groE chaperonins.

Seminars in cell biology, 1991
The E.coli groES and groEL genes have been shown to form an operon, to be essential for E. coli viability, and to belong to the so-called heat-shock class of genes whose expression is regulated by the intracellular levels of sigma factor sigma 32.
C, Georgopoulos, D, Ang
openaire   +1 more source

Nucleotide sequence of the Escherichia coli groE promoter

Gene, 1994
The promoter region of the Escherichia coli groE operon was cloned using the polymerase chain reaction (PCR). The 118-bp nucleotide sequence of the cloned groE promoter was determined on both strands of DNA. Two bp were found between the -10 and -35 regions of this promoter that have not been reported in previous publications of this sequence.
openaire   +2 more sources

Entering deeper into the mysteries of the GroEL–GroES nanomachine

Current Opinion in Microbiology
In the densely populated intracellular milieu, polypeptides are at constant risk of nonspecific interactions and aggregation, posing a threat to essential cellular functions. Cells rely on a network of protein folding factors to deal with this challenge.
Emile, Dupuy, Jean-François, Collet
openaire   +2 more sources

GroEL−GroES-Mediated Protein Folding

Chemical Reviews, 2006
Arthur L, Horwich, George W, Farr, Wayne A, Fenton   +2 more
openaire   +2 more sources

A risk management framework for Gentle Remediation Options (GRO)

Science of the Total Environment, 2022
Yevheniya Volchko, Shaswati Chowdhury, Yvonne Andersson-Sköld   +2 more
exaly  

Accretion torque reversals in GRO J1008-57 revealed by

Journal of High Energy Astrophysics, 2021
Gang Li, Shuang-Nan Zhang, Prahlad R Epili   +2 more
exaly  

Enhanced separation performance of a novel composite material GrO@MIL-101 for CO/CH binary mixture

Chemical Engineering Journal, 2015
Yufang Wu, Haihui Wang, Xin Zhou
exaly