Results 11 to 20 of about 27,570 (293)

In vivo client proteins of the chaperonin GroEL-GroES provide insight into the role of chaperones in protein evolution

Frontiers in Molecular Biosciences, 2023
Protein folding is often hampered by intermolecular protein aggregation, which can be prevented by a variety of chaperones in the cell. Bacterial chaperonin GroEL is a ring-shaped chaperone that forms complexes with its cochaperonin GroES, creating ...
Hideki Taguchi, Ayumi Koike-Takeshita
doaj   +2 more sources

Back to GroEL-Assisted Protein Folding: GroES Binding-Induced Displacement of Denatured Proteins from GroEL to Bulk Solution

Biomolecules, 2020
The main events in chaperone-assisted protein folding are the binding and ligand-induced release of substrate proteins. Here, we studied the location of denatured proteins previously bound to the GroEL chaperonin resulting from the action of the GroES co-
Victor Marchenkov, Andrey Gorokhovatsky, Natalia Marchenko, Tanya Ivashina, Gennady Semisotnov   +4 more
doaj   +2 more sources

Novel cryo-EM structure of an ADP-bound GroEL–GroES complex

Scientific Reports, 2021
The GroEL–GroES chaperonin complex is a bacterial protein folding system, functioning in an ATP-dependent manner. Upon ATP binding and hydrolysis, it undergoes multiple stages linked to substrate protein binding, folding and release.
Sofia S. Kudryavtseva, Evgeny B. Pichkur, Igor A. Yaroshevich, Aleksandra A. Mamchur, Irina S. Panina, Andrei V. Moiseenko, Olga S. Sokolova, Vladimir I. Muronetz, Tatiana B. Stanishneva-Konovalova   +8 more
doaj   +2 more sources

Creating the Functional Single-Ring GroEL-GroES Chaperonin Systems via Modulating GroEL-GroES Interaction [PDF]

Scientific Reports, 2017
AbstractChaperonin and cochaperonin, represented by E. coli GroEL and GroES, are essential molecular chaperones for protein folding. The double-ring assembly of GroEL is required to function with GroES, and a single-ring GroEL variant GroELSR forms a stable complex with GroES, arresting the chaperoning reaction cycle.
Illingworth, Melissa, Ellis, Holly, Chen, Lingling   +2 more
openaire   +3 more sources

Temperature Regulates Stability, Ligand Binding (Mg2+ and ATP) and Stoichiometry of GroEL/GroES Complexes [PDF]

Journal of the American Chemical Society, 2021
Chaperonins are nanomachines that harness ATP hydrolysis to power and catalyze protein folding, a chemical action that is directly linked to the maintenance of cell function through protein folding/refolding and assembly.
T.G. Walker, Mehdi Shirzadeh, He Mirabel Sun, Jacob W. McCabe, Andrew Roth, Zahra Moghadamchargari, David E. Clemmer, Arthur Laganowsky, Hays S. Rye, David H. Russell   +9 more
openalex   +2 more sources

GroEL-GroES Cycling [PDF]

Cell, 1999
Hays S Rye, Alan M Roseman, Wayne A Fenton   +2 more
exaly   +2 more sources

Stimulating the Substrate Folding Activity of a Single Ring GroEL Variant by Modulating the Cochaperonin GroES [PDF]

Journal of Biological Chemistry, 2011
In mediating protein folding, chaperonin GroEL and cochaperonin GroES form an enclosed chamber for substrate proteins in an ATP-dependent manner. The essential role of the double ring assembly of GroEL is demonstrated by the functional deficiency of the ...
Melissa Illingworth, Andrew J. Ramsey, Zhida Zheng, Ling‐Ling Chen   +3 more
openalex   +2 more sources

Substrate protein dependence of GroEL–GroES interaction cycle revealed by high-speed atomic force microscopy imaging [PDF]

Philosophical Transactions of the Royal Society B: Biological Sciences, 2018
A double-ring-shaped tetradecameric GroEL complex assists proper protein folding in cooperation with the cochaperonin GroES. The dynamic GroEL–GroES interaction reflects the allosteric intra- and inter-ring communications and the chaperonin reaction ...
Daisuke Noshiro, Toshio Ando
openalex   +2 more sources

GroEL/GroES-Mediated Folding of a Protein Too Large to Be Encapsulated [PDF]

Cell, 2001
Tapan K Chaudhuri, Wayne A Fenton, Arthur L Horwich   +2 more
exaly   +2 more sources

Landmarks to guide femoral insertion in lateral patellofemoral ligament reconstruction: An in vivo assessment of isometry. [PDF]

Knee Surg Sports Traumatol Arthrosc
Abstract Purpose Lateral patellofemoral ligament (LPFL) reconstruction addresses medial patellar instability, but uncertainty regarding the optimal femoral attachment site may affect isometry and increase complication rates. This study aimed to establish landmarks for the femoral attachment of the LPFL graft based on in vivo isometry during active knee
Boot MR, van de Groes SAW, Tanck E, Janssen D.   +3 more
europepmc   +2 more sources