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ADP-ribosylation


'ADP-ribosylation' can also refer to...

ADP‐ribosylation

ADP‐ribosylation factor

ADP-ribosylation factor

ADP-ribosylation

Localization and function of ADP ribosylation factor A in Aspergillus nidulans

ADP-Ribosylation Factor-1 Is Sensitive to N-Ethylmaleimide

Genes encoding ADP-ribosylation factors in Arabidopsis thaliana L. Heyn.; genome analysis and antisense suppression

The NarE protein of Neisseria gonorrhoeae catalyzes ADP-ribosylation of several ADP-ribose acceptors despite an N-terminal deletion

Light inhibits rifampicin inactivation and reduces rifampicin resistance due to a cloned mycobacterial ADP-ribosylation gene

ADP-ribosylation by exoenzyme T of Pseudomonas aeruginosa induces an irreversible effect on the host cell cytoskeleton in vivo

ADP-ribosylation factor-like 3, a manchette-associated protein, is essential for mouse spermiogenesis

The effect of carvedilol on enhanced ADP-ribosylation and red blood cell membrane damage caused by free radicals

Nitric Oxide–Induced Modification of Glyceraldehyde-3-Phosphate Dehydrogenase with NAD+ Is Not ADP-Ribosylation

Purification of Bovine Soluble Guanylate Cyclase and ADP-Ribosylation on its Small Subunit by Bacterial Toxins

Activation of Clostridium botulinum C3 Exoenzyme-Catalyzed ADP-Ribosylation of RhoA by K+in a Mg2+-Dependent Manner

The pioneering spirit of Takashi Sugimura: his studies of the biochemistry of poly(ADP-ribosylation) and of cancer

Structure and Intracellular Localization of Mouse ADP-Ribosylation Factors Type 1 to Type 6 (ARF1–ARF6)

 

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A post-translational modification of proteins by the addition of the ADP-ribosyl moiety of NAD. It is a normal regulatory mechanism but is also the way in which several AB toxins have their effects. ADP-ribosylation factor (ARF) is an ubiquitous GTP-binding protein (181 aa) that mediates the binding of non-clathrin coated vesicles and AP1 (adaptor-protein 1) of clathrin-coated vesicles to Golgi membranes. At least six isoforms have been identified. It is also an allosteric activator of the cholera toxin catalytic subunit. ADP-ribosylation factor-binding proteins (Golgi-associated γ-adaptin ear containing ARF-binding proteins, GGAs 1–3, 639 aa, 613 aa, and 723 aa respectively) mediate the ARF-dependent recruitment of clathrin to the trans-Golgi network.

Subjects: Chemistry — Medicine and Health.


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