Results 21 to 30 of about 23,956 (223)
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 +8 more
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HSP10 as a Chaperone for Neurodegenerative Amyloid Fibrils
Frontiers in Neuroscience, 2022 Neurodegenerative diseases (NDs) are associated with accumulated misfolded proteins (MPs). MPs oligomerize and form multiple forms of amyloid fibril polymorphs that dictate fibril propagation and cellular dysfunction.
Johan N. K. Larsson +2 more
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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 +5 more
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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 +3 more
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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 +7 more
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The Proteome of Biologically Active Membrane Vesicles from Piscirickettsia salmonis LF-89 Type Strain Identifies Plasmid-Encoded Putative Toxins [PDF]
, 2017 Indexación: Scopus.Piscirickettsia salmonis is the predominant bacterial pathogen affecting the Chilean salmonid industry. This bacterium is the etiological agent of piscirickettsiosis, a significant fish disease.
Artigues, A. +14 more
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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
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 +2 more
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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 +3 more
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