Search Results - "chaperonin"

The roles of chaperonins in bacteria

Table of Contents: “…Contents: The discovery of the GroEL chaperonin in E. coli -- Organization of the GroEL and GroES genes -- Oligomeric structure of GroEL and GroES proteins -- Key roles of GroEL -- The substrates of GroEL -- Chaperonins in other bacteria and their roles.…”
Get full text
Series

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

Role of chaperonin-like proteins in Bardet-Biedl syndrome

Table of Contents: “…Contents: Introduction to chaperonins -- Evolution of chaperonins -- Introduction to Bardet-Biedl syndrome (BBS) and ciliopathies -- Cloning of BBS disease genes -- Role of chaperonins in Bardet-Biedl syndrome.…”
Get full text
Series

Chaperonin-containing TCP-1 (CCT), actin springs, and protein folding fluxes

Table of Contents: “…Contents: Chaperonins -- Chaperonin containing TCP-1 (CCT) -- Evolution of CCT -- Structure of CCT -- Genetic and proteomic analysis of the CCT interactome in S. cerevisiae -- Substrates of CCT -- Proposed energy landscape of actin folding.…”
Get full text
Series

Overview of eukaryotic molecular chaperones in the cytosol

Table of Contents: “…Contents: Protein folding and molecular chaperones -- Hsp70/Hsc70 -- Co-chaperones of Hsc70 -- Chaperonin TRiC/CCT -- Prefoldin -- Hsp90 -- Co-chaperones of Hsp90 -- Specialized co-chaperones -- Heat shock protein chaperones.…”
Get full text
Series

History of the molecular chaperone concept roles in assembly processes /

Table of Contents: “…Contents: Definition of protein self-assembly and aggregation -- First use of the term 'molecular chaperone' -- Nucleoplasmin -- Chloroplast rubisco aggregation -- The chaperonins -- The general chaperone concept -- Definition of 'molecular chaperone' -- The chaperone function -- Protein folding on polysomes -- Macromolecular crowding -- Folding and assembly chaperones -- Nuclear chaperones -- Nucleosome assembly -- Mechanism of nucleoplasmin action -- The rubisco assembly chaperone RbcX.…”
Get full text
Series

Protein folding inside the cell macromolecular crowding and protein aggregation /

Table of Contents: “…Contents: The principle of protein self-assembly -- Discovery of proteins binding to newly synthesized polypeptides -- Discovery of the chaperonins -- Origins of the molecular chaperone concept -- Replacement of spontaneous self-assembly by assisted self-assembly -- Protein aggregation as a universal cellular problem -- Macromolecular crowding and its effects on reaction rates and association constants -- Stimulation of aggregation by crowding -- How chaperones combat aggregation -- Definition of molecular chaperones -- The chaperone function.…”
Get full text
Series

Chaperone mechanisms in cellular protein folding

Table of Contents: “…Contents: The effect of protein aggregation on productive protein folding -- The function of GroEL and GroES as a folding cage for proteins -- Changes in energy landscape within the folding cage -- Cooperation of different chaperone systems in folding pathways: Hsp70 and chaperonins -- Binding of the Hsp70 homologue protein, DnaK, to newly-synthesized polypeptides -- The role of chaperone mechanisms in toxicity suppression of misfolded disease causing proteins -- Potential uses of the chaperone mechanisms in disease therapeutics.…”
Get full text
Series (Molecular chaperones)
Series (Protein folding)