The covalent attachment of one or more ribosyl groups to a molecule (usually a macromolecule).
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12-19,24,25 These chaperones with the translocated Cx43 impair the nascent polypeptide chain structure of Cx43 with post- translational modifications such as glycosylation, phosphorylation, sulfation, acetylation, ubiquitination, ribosylation, C-terminal (glycosyl phosphatidyl inositol [GPI] membrane anchors) methylation.
Seluanov, "Repairing split ends: SIRT6, mono-ADP ribosylation and DNA repair," Aging, vol.
The increase in GAPD (glyceraldehyde 3 phosphate dehydrogenase) can contribute to its ADP ribosylation and nuclear cell death.
Protection by thymidine, an inhibitor of polyadenosine diphosphate ribosylation, of streptozotocin inhibition of insulin secretion.
Brain homogenates (10% wt/vol for murine samples and 20% wt/vol for ruminant controls) were prepared by using ribosylation tubes (Bio-Rad Laboratories, Hercules, CA, USA).
The entry of CTA1 to the cell cytosol is the key step for intoxication because CTA1 catalyzes the ADP ribosylation of the trimeric Gsa component of AC.
Detection of residual pertussis toxin in vaccines using a modified ribosylation assay.
These covalent modifications, found in the tails of the histone chains, influence many fundamental biological processes including acetylation, methylation, phosphorylation, citrullination, ubiquitination, sumoylation, ADP ribosylation, deimination, and proline isomerization (Kouzarides 2007) (Figure 2).
The ribosylation of PARP-1 serves to regulate this process and down-regulates PARP-1 activity.
Pertussis toxin-mediated ribosylation of G proteins blocks the hypnotic response to an [[alpha].
The SS1P molecule is an ingenious example of protein engineering: the native Pseudomonas exotoxin protein consists of three domains: domain I targets cell surface receptors, domain II functions to translocate the molecule across a cell membrane and into the cell interior, and domain III catalyzes irreversible ADP ribosylation and inactivation of elongation factor 2 (EF2).
Gi was purified from rabbit liver as a substrate of ADP ribosylation by pertussis toxin.