Results 21 to 30 of about 5,379 (199)
The BBS/CCT chaperonin complex ensures the localization of the adhesion G protein-coupled receptor ADGRV1 to the base of primary cilia [PDF]
Frontiers in Cell and Developmental BiologyPrimary cilia are antenna-like sensory organelles present on almost all eukaryotic cells. Their sensory capacity relies on receptors, in particular G-protein-coupled receptors (GPCRs) which localize to the ciliary membrane.
Joshua Linnert +6 more
doaj +2 more sources
Functional and structural characterisation of Mycobacterial Chaperonins [PDF]
, 2010 In Mycobacterium tuberculosis there are 2 distinct groEL homologues which encode the chaperonins Cpn60.1 and Cpn60.2, with the latter predicted to be the main house-keeping chaperonin.
Ahmed, Mohammad Tabish
core +7 more sources
Current Opinion in Structural Biology, 1998 Molecular chaperones are essential to all living organisms. Their key role consists of mediating protein folding within the cell. Recent functional studies have provided more detailed information about the function and regulation of the chaperone network.
N A, Ranson, H E, White, H R, Saibil
openaire +4 more sources
Chaperonins – keeping a lid on folding proteins [PDF]
, 2001 Two classes of chaperonins are known in all groups of organisms to participate in the folding of newly synthesized proteins. Whereas bacterial type I chaperonins use a reversibly binding cofactor to temporarily sequester folding substrate proteins within
Andrew R Kusmierczyk +3 more
core +3 more sources
Local Flexibility of a New Single-Ring Chaperonin Encoded by Bacteriophage AR9 Bacillus subtilis
Biomedicines, 2022 Chaperonins, a family of molecular chaperones, assist protein folding in all domains of life. They are classified into two groups: bacterial variants and those present in endosymbiotic organelles of eukaryotes belong to group I, while group II includes ...
Olga S. Sokolova +7 more
doaj +1 more source
The Possible Role of the Type I Chaperonins in Human Insulin Self-Association
Life, 2022 Insulin is a hormone that attends to energy metabolism by regulating glucose levels in the bloodstream. It is synthesised within pancreas beta-cells where, before being released into the serum, it is stored in granules as hexamers coordinated by Zn2+ and
Federica Pizzo +6 more
doaj +1 more source
Identification of elements that dictate the specificity of mitochondrial Hsp60 for its co-chaperonin. [PDF]
PLoS ONE, 2012 Type I chaperonins (cpn60/Hsp60) are essential proteins that mediate the folding of proteins in bacteria, chloroplast and mitochondria. Despite the high sequence homology among chaperonins, the mitochondrial chaperonin system has developed unique ...
Avital Parnas +8 more
doaj +1 more source
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 +4 more
doaj +1 more source
Microbiology Research, 2023 This review discusses a few examples of specific mechanisms mediating the contribution of the GIT microbiota to the development of amyloid neurodegenerative diseases caused by the pathologic transformation of prion protein, or alpha-synuclein. The effect
Vladimir I. Muronetz +3 more
doaj +1 more source
Cell Reports, 2020 Summary: Global warming and emerging plant diseases challenge agricultural food/feed production. We identify mechanism(s) regulating both plant thermotolerance and disease resistance.
Bikram Datt Pant +4 more
doaj +1 more source