Search Results - "chaperonin"

Mitochondrial chaperonin Hsp60 locations, functions and pathology /

Table of Contents: “…Contents: Chaperonology: the study of molecular chaperones in all their aspects, normal and pathological -- The chaperoning system: the entire complement of chaperones in an organism, including co-chaperones and co-factors -- Chaperonopathies: diseases in which abnormal chaperones play a pathogenic role -- Hsp60: the mitochondrial chaperonin Cpn60 -- Genetic Hsp60 chaperonopathies: pathologic conditions in which Hsp60 mutations are involved as etiologic-pathogenic factors -- Hsp60 in cancer: Hsp60 chaperonopathies by mistake, in which the chaperonin helps the tumour rather than the patient.…”
Get full text
Series

Chaperonin-mediated protein folding part 1 /

Table of Contents: “…Contents: Chaperonin-mediated protein folding by GroEL/GroES -- Folding of newly-translated protein -- Currently known Molecular chaperones (including the Heat shock protein Hsp group) -- Recognition of non native proteins by Hsps and formation of aggregates -- Aggregates and neurodegenerative disease -The discovery of the chaperonin-mediated folding -- The structure of the GroES/GroeEL chaperonin class of molecular chaperones -- The steps of polypeptide binding and folding -- The action of ATP binding and hydrolysis in driving the rings of the machine through cycles of binding and release cycle.…”
Get full text

Chaperonin-mediated protein folding part 2 /

Table of Contents: “…Contents: Chaperonin-mediated protein folding by GroEL/GroES -- Folding of newly-translated protein -- Currently known Molecular chaperones (including the Heat shock protein Hsp group) -- Recognition of non native proteins by Hsps and formation of aggregates -- Aggregates and neurodegenerative disease -The discovery of the chaperonin-mediated folding -- The structure of the GroES/GroeEL chaperonin class of molecular chaperones -- The steps of polypeptide binding and folding -- The action of ATP binding and hydrolysis in driving the rings of the machine through cycles of binding and release cycle.…”
Get full text

The interaction network of the GroEL chaperonin

Table of Contents: “…-- Identification of the GroEL interaction proteome -- Class III substrates are of relatively low cellular abundance but occupy most of the GroEL capacity -- Chaperonins provide a specialized folding environment with two functional elements: sequestration and steric confinement in a hydrophilic cage -- GroEL as part of the cytosolic chaperone network.…”
Get full text
Series

Mechanistic aspects of chaperonin GroEL/ES function

Table of Contents: “…Contents: Chaperonin structure -- The allosteric mechanism of GroEL coupling between GroEL allostery and folding -- The unfoldase activity of GroEL -- The GroE reaction cycle.…”
Get full text
Series