- Chaperonin-mediated protein folding, organism-specific biosystem (from REACTOME)
Chaperonin-mediated protein folding, organism-specific biosystemThe eukaryotic chaperonin TCP-1 ring complex (TRiC/ CCT) plays an essential role in the folding of a subset of proteins prominent among which are the actins and tubulins (reviewed in Altschuler and...
- Cooperation of Prefoldin and TriC/CCT in actin and tubulin folding, organism-specific biosystem (from REACTOME)
Cooperation of Prefoldin and TriC/CCT in actin and tubulin folding, organism-specific biosystemIn the case of actin and tubulin folding, and perhaps other substrates, the emerging polypeptide chain is transferred from the ribosome to TRiC via Prefoldin (Vainberg et al., 1998).
- Formation of tubulin folding intermediates by CCT/TriC, organism-specific biosystem (from REACTOME)
Formation of tubulin folding intermediates by CCT/TriC, organism-specific biosystemTriC/CCT forms a binary complex with unfolded alpha- or beta-tubulin (Frydman et al., 1992; Gao et al., 1993). The tubulin folding intermediates produced by TriC are unstable (Gao et al., 1993). Fiv...
- Gap junction, organism-specific biosystem (from KEGG)
Gap junction, organism-specific biosystemGap junctions contain intercellular channels that allow direct communication between the cytosolic compartments of adjacent cells. Each gap junction channel is formed by docking of two 'hemichannels'...
- Gap junction, conserved biosystem (from KEGG)
Gap junction, conserved biosystemGap junctions contain intercellular channels that allow direct communication between the cytosolic compartments of adjacent cells. Each gap junction channel is formed by docking of two 'hemichannels'...
- Metabolism of proteins, organism-specific biosystem (from REACTOME)
Metabolism of proteins, organism-specific biosystemProtein metabolism comprises the pathways of translation, post-translational modification and protein folding.
- Pathogenic Escherichia coli infection, organism-specific biosystem (from KEGG)
Pathogenic Escherichia coli infection, organism-specific biosystemEnteropathogenic E. coli (EPEC) and enterohemorrhagic E. coli (EHEC) are closely related pathogenic strains of Escherichia coli. The hallmark of EPEC/EHEC infections [DS:H00278 H00277] is induction o...
- Pathogenic Escherichia coli infection, conserved biosystem (from KEGG)
Pathogenic Escherichia coli infection, conserved biosystemEnteropathogenic E. coli (EPEC) and enterohemorrhagic E. coli (EHEC) are closely related pathogenic strains of Escherichia coli. The hallmark of EPEC/EHEC infections [DS:H00278 H00277] is induction o...
- Phagosome, organism-specific biosystem (from KEGG)
Phagosome, organism-specific biosystemPhagocytosis is the process of taking in relatively large particles by a cell, and is a central mechanism in the tissue remodeling, inflammation, and defense against infectious agents. A phagosome is...
- Phagosome, conserved biosystem (from KEGG)
Phagosome, conserved biosystemPhagocytosis is the process of taking in relatively large particles by a cell, and is a central mechanism in the tissue remodeling, inflammation, and defense against infectious agents. A phagosome is...
- Post-chaperonin tubulin folding pathway, organism-specific biosystem (from REACTOME)
Post-chaperonin tubulin folding pathway, organism-specific biosystemAlpha and beta tubulin folding intermediates are formed through ATPâ??dependent interaction with TriC/CCT. In order to form a functional heterodimer, these folding intermediates undergo a series of...
- Prefoldin mediated transfer of substrate to CCT/TriC, organism-specific biosystem (from REACTOME)
Prefoldin mediated transfer of substrate to CCT/TriC, organism-specific biosystemUnfolded actins and tubulins bound to prefoldin are transferred to CCT via a docking mechanism (McCormack and Willison, 2001).
- Protein folding, organism-specific biosystem (from REACTOME)
Protein folding, organism-specific biosystemDue to the crowded envirnoment within the cell, many proteins must interact with molecular chaperones to attain their native conformation (reviewed in Young et al., 2004). Chaperones recognize and...