"ADP Ribose Transferases" is a descriptor in the National Library of Medicine's controlled vocabulary thesaurus,
MeSH (Medical Subject Headings). Descriptors are arranged in a hierarchical structure,
which enables searching at various levels of specificity.
Enzymes that transfer the ADP-RIBOSE group of NAD or NADP to proteins or other small molecules. Transfer of ADP-ribose to water (i.e., hydrolysis) is catalyzed by the NADASES. The mono(ADP-ribose)transferases transfer a single ADP-ribose. POLY(ADP-RIBOSE) POLYMERASES transfer multiple units of ADP-ribose to protein targets, building POLY ADENOSINE DIPHOSPHATE RIBOSE in linear or branched chains.
| Descriptor ID |
D036002
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| MeSH Number(s) |
D08.811.913.400.725.115
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| Concept/Terms |
ADP Ribose Transferases- ADP Ribose Transferases
- Ribose Transferases, ADP
- Transferases, ADP Ribose
- ADP Ribose Transferase
- Ribose Transferase, ADP
- Transferase, ADP Ribose
- ARTase
- ART Transferase
- Transferase, ART
- ADPRTs
- ART Transferases
- Transferases, ART
- ARTases
- ADPRT
- ADP-Ribosyltransferase
- ADP Ribosyltransferase
Mono(ADP-Ribose) Transferases- Mono(ADP-Ribose) Transferases
- Mono(ADP-Ribose) Transferase
- Mono ADPribose Transferases
- ADPribose Transferases, Mono
- Transferases, Mono ADPribose
- MonoADPribosyltransferase
- Mono ADP-ribose Transferases
- ADP-ribose Transferases, Mono
- Mono ADP ribose Transferases
- Transferases, Mono ADP-ribose
- Mono(ADP-Ribosyl)transferase
- Mono(ADPribosyl)transferase
- Mono-ADP-Ribosyltransferase
- Mono ADP Ribosyltransferase
- Mono ADPribose Transferase
- ADPribose Transferase, Mono
- Transferase, Mono ADPribose
NAD(P)(+)-Arginine ADP-Ribosyltransferase- NAD(P)(+)-Arginine ADP-Ribosyltransferase
- NADP-ADPRTase
- NADP ADPRTase
- NAD(+)-L-arginine ADP-D-ribosyltransferase
- NAD-Agmatine ADP-Ribosyltransferase
- ADP-Ribosyltransferase, NAD-Agmatine
- NAD Agmatine ADP Ribosyltransferase
- NADP-Arginine ADP-Ribosyltransferase
- ADP-Ribosyltransferase, NADP-Arginine
- NADP Arginine ADP Ribosyltransferase
- NAD-Arginine ADP-Ribosyltransferase
- ADP-Ribosyltransferase, NAD-Arginine
- NAD Arginine ADP Ribosyltransferase
NAD+ ADP-Ribosyltransferase- NAD+ ADP-Ribosyltransferase
- ADP-Ribosyltransferase, NAD+
- NAD+ ADP Ribosyltransferase
- NAD ADP-Ribosyltransferase
- ADP-Ribosyltransferase, NAD
- NAD ADP Ribosyltransferase
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Below are MeSH descriptors whose meaning is more general than "ADP Ribose Transferases".
Below are MeSH descriptors whose meaning is more specific than "ADP Ribose Transferases".
This graph shows the total number of publications written about "ADP Ribose Transferases" by people in this website by year, and whether "ADP Ribose Transferases" was a major or minor topic of these publications.
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Below are the most recent publications written about "ADP Ribose Transferases" by people in Profiles.
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CrkII/Abl phosphorylation cascade is critical for NLRC4 inflammasome activity and is blocked by Pseudomonas aeruginosa ExoT. Nat Commun. 2022 03 11; 13(1):1295.
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Pseudomonas aeruginosa ExoT induces G1 cell cycle arrest in melanoma cells. Cell Microbiol. 2021 08; 23(8):e13339.
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Pseudomonas aeruginosa ExoS Induces Intrinsic Apoptosis in Target Host Cells in a Manner That is Dependent on its GAP Domain Activity. Sci Rep. 2018 09 19; 8(1):14047.
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Pseudomonas aeruginosa ExoT Induces Mitochondrial Apoptosis in Target Host Cells in a Manner That Depends on Its GTPase-activating Protein (GAP) Domain Activity. J Biol Chem. 2015 Nov 27; 290(48):29063-73.
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Pseudomonas aeruginosa ExoT Induces Atypical Anoikis Apoptosis in Target Host Cells by Transforming Crk Adaptor Protein into a Cytotoxin. PLoS Pathog. 2015 May; 11(5):e1004934.
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Pseudomonas aeruginosa exotoxin T induces potent cytotoxicity against a variety of murine and human cancer cell lines. J Med Microbiol. 2015 Feb; 64(Pt 2):164-73.
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The ADP-ribosyltransferase domain of the effector protein ExoS inhibits phagocytosis of Pseudomonas aeruginosa during pneumonia. mBio. 2014 Jun 10; 5(3):e01080-14.
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The Pseudomonas aeruginosa type III secreted toxin ExoT is necessary and sufficient to induce apoptosis in epithelial cells. Cell Microbiol. 2008 Apr; 10(4):994-1007.
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Use of a novel coinfection system reveals a role for Rac1, H-Ras, and CrkII phosphorylation in Helicobacter pylori-induced host cell actin cytoskeletal rearrangements. FEMS Immunol Med Microbiol. 2007 Jul; 50(2):190-205.
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Pseudomonas aeruginosa type III-secreted toxin ExoT inhibits host-cell division by targeting cytokinesis at multiple steps. Proc Natl Acad Sci U S A. 2006 Oct 17; 103(42):15605-10.