Results 21 to 30 of about 9,153 (190)

GroE is vital for cell-wall synthesis [PDF]

Nature, 1998
Chaperone proteins help other proteins to fold. GroEL, the Escherichia coli form of the ubiquitous Cpn60 chaperonins, has a multimeric barrel-shaped structure with a central cavity, within which almost any protein can fold in vitro1. But what does GroE (GroEL plus its co-chaperone GroES) fold in the cell? Why is it needed for cell survival2?
N, McLennan, M, Masters
openaire   +2 more sources

Chaperonin GroEL Reassembly: An Effect of Protein Ligands and Solvent Composition

Biomolecules, 2014
Chaperonin GroEL is a complex oligomeric heat shock protein (Hsp60) assisting the correct folding and assembly of other proteins in the cell. An intriguing question is how GroEL folds itself.
Nataliya Ryabova, Victor Marchenkov, Nina Kotova, Gennady Semisotnov   +3 more
doaj   +1 more source

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   +1 more source

Novel Chaperones RrGroEL and RrGroES for Activity and Stability Enhancement of Nitrilase in Escherichia coli and Rhodococcus ruber

Molecules, 2020
For large-scale bioproduction, thermal stability is a crucial property for most industrial enzymes. A new method to improve both the thermal stability and activity of enzymes is of great significance.
Chunmeng Xu, Lingjun Tang, Youxiang Liang, Song Jiao, Huimin Yu, Hui Luo   +5 more
doaj   +1 more source

Chaperonin GroEL/GroES over-expression promotes multi-drug resistance in E. coli following exposure to aminoglycoside antibiotics

Frontiers in Microbiology, 2016
Antibiotic resistance is an increasing challenge to modern healthcare. Aminoglycoside antiobiotics cause translation corruption and protein misfolding and aggregation in Escherichia coli.
Lise eGoltermann, Menachem Viktor Sarusie, Thomas eBentin   +2 more
doaj   +1 more source

The Mycobacterium tuberculosis sRNA F6 Modifies Expression of Essential Chaperonins, GroEL2 and GroES

Microbiology Spectrum, 2021
Almost 140 years after the identification of Mycobacterium tuberculosis as the etiological agent of tuberculosis, important aspects of its biology remain poorly described.
Joanna Houghton, Angela Rodgers, Graham Rose, Alexandre D’Halluin, Terry Kipkorir, Declan Barker, Simon J. Waddell, Kristine B. Arnvig   +7 more
doaj   +1 more source

Stress-related genes promote Edwardsiella ictaluri pathogenesis. [PDF]

PLoS ONE, 2018
Edwardsiella ictaluri is a Gram-negative facultative anaerobic rod and the causative agent of enteric septicemia of channel catfish (ESC), which is one of the most prevalent diseases of catfish, causing significant economic losses in the catfish industry.
Ali Akgul, Ayfer Akgul, Mark L Lawrence, Attila Karsi   +3 more
doaj   +1 more source

Hegemonic and Subordinated Masculinities

Nordic Journal of African Studies, 2009
The article explores theoretical implications of sexual and violent practices among disenfranchised young men in Southern Africa. Ethnographic findings from Maputo, Mozambique indicate that massive unemployment caused by neo-liberal reforms have led to ...
Christian Groes-Green
doaj   +1 more source

Proteome-Wide Analyis of Chaperonin-Dependent Protein Folding in Escherichia coli [PDF]

, 2006
In Escherichia coli, the cylindrical chaperonin GroEL and its cofactor GroES promote the folding of a fraction of newly synthesized polypeptide chains by acting as an Anfinsen cage.
Maier, Tobias
core   +1 more source

Characterization of multifunctional proteins from Helicobacter pylori [PDF]

, 2010
This thesis reports the cloning, overexpression and characterization of two interesting proteins from Helicobacter pylori: Heat Shock protein A (HspA), and CoaX (Type III Pantothenate kinase).
Scannella, Alessandra
core   +1 more source