Results 41 to 50 of about 31,985 (221)
Reconstitution of Pure Chaperonin Hetero-Oligomer Preparations in Vitro by Temperature Modulation
Frontiers in Molecular Biosciences, 2018 Chaperonins are large, essential, oligomers that facilitate protein folding in chloroplasts, mitochondria, and eubacteria. Plant chloroplast chaperonins are comprised of multiple homologous subunits that exhibit unique properties.
Anna Vitlin Gruber +3 more
doaj +1 more source
Extragenic Suppression analysis of TS mutations using Sec61p [PDF]
, 2007 During synthesis, secretory and membrane proteins are cotranslationally translocated into the lumen of the endoplasmic reticulum through an aqueous gated channel.
Sterling Smith
core +2 more sources
Molecules, 2022 The Escherichia coli chaperonin GroEL/ES (GroE) is one of the most extensively studied molecular chaperones. So far, ~80 proteins in E. coli are identified as GroE substrates that obligately require GroE for folding in vivo. In GroE-depleted cells, these
Tatsuya Niwa +2 more
doaj +1 more source
ATP binding to a multisubunit enzyme: statistical thermodynamics analysis
, 2012 Due to inter-subunit communication, multisubunit enzymes usually hydrolyze ATP in a concerted fashion. However, so far the principle of this process remains poorly understood.
A. Fersht +3 more
core +1 more source
Pb2+ tolerance by Frankia sp. strain EAN1pec involves surface-binding [PDF]
, 2017 Several Frankia strains have been shown to be lead-resistant. The mechanism of lead resistance was investigated for Frankia sp. strain EAN1pec. Analysis of the cultures by scanning electron microscopy (SEM), energy dispersive X-ray spectroscopy (EDAX ...
Furnholm, Teal +3 more
core +2 more sources
Rubisco Assembly in the Chloroplast
Frontiers in Molecular Biosciences, 2018 Ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco) catalyzes the rate-limiting step in the Calvin-Benson cycle, which transforms atmospheric carbon into a biologically useful carbon source.
Anna Vitlin Gruber, Leila Feiz
doaj +1 more source
Biomedical and Biotechnology Research Journal, 2021 Background: The role of Lactobacillus casei on human health is well documented. However, little is known about their protein effects on food digestion. Therefore, in the present study, we aimed to investigate the efficacy of three proteins of L. casei on
Golgis Karimi +4 more
doaj +1 more source
ATP dependent rotational motion of group II chaperonin observed by X-ray single molecule tracking. [PDF]
PLoS ONE, 2013 Group II chaperonins play important roles in protein homeostasis in the eukaryotic cytosol and in Archaea. These proteins assist in the folding of nascent polypeptides and also refold unfolded proteins in an ATP-dependent manner.
Hiroshi Sekiguchi +10 more
doaj +1 more source
Frontiers in Immunology, 2021 Recombinant human factor H (hFH) has potential for treating diseases linked to aberrant complement regulation including C3 glomerulopathy (C3G) and dry age-related macular degeneration.
Heather Kerr +18 more
doaj +1 more source
Chaperonin-mediated Protein Folding [PDF]
Journal of Biological Chemistry, 2011 We have been studying chaperonins these past twenty years through an initial discovery of an action in protein folding, analysis of structure, and elucidation of mechanism. Some of the highlights of these studies were presented recently upon sharing the honor of the 2013 Herbert Tabor Award with my early collaborator, Ulrich Hartl, at the annual ...
openaire +3 more sources