Skip to search formSkip to main content
You are currently offline. Some features of the site may not work correctly.

ADP Ribose Transferases

Known as: ARTases, Transferases, ART, ADPRTs 
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… Expand
National Institutes of Health

Related topics

Related topics

24 relations
ART3 geneIn BloodPARP1 genePARP1 wt Allele
Expand

Narrower (11)

ART5 protein, mouseArt2b protein, ratBMS-191352 protein, recombinantExoT protein, Pseudomonas aeruginosa
Expand

Papers overview

Semantic Scholar uses AI to extract papers important to this topic.
Highly Cited
2012
Highly Cited
2012
ExoS and ExoT ADP Ribosyltransferase Activities Mediate Pseudomonas aeruginosa Keratitis by Promoting Neutrophil Apoptosis and Bacterial Survival
Pseudomonas aeruginosa is a leading cause of blinding corneal ulcers worldwide. To determine the role of type III secretion in… Expand
  • table I
  • table II
  • figure 1
  • table III
  • figure 2
Highly Cited
2008
Highly Cited
2008
Structural basis of actin recognition and arginine ADP-ribosylation by Clostridium perfringens ι-toxin
The ADP-ribosylating toxins (ADPRTs) produced by pathogenic bacteria modify intracellular protein and affect eukaryotic cell… Expand
  • figure 1
  • figure 2
  • table 1
  • figure 3
  • figure 4
Highly Cited
2008
Highly Cited
2008
Association between Polymorphisms in DNA Base Excision Repair Genes XRCC1, APE1, and ADPRT and Differentiated Thyroid Carcinoma
Purpose: DNA BER pathway is related with carcinogenesis. We hypothesized that functional polymorphisms of three BER genes, XRCC1… Expand
  • table 1
  • table 2
  • table 3
  • table 4
  • table 5
Highly Cited
2004
Highly Cited
2004
The ADP Ribosyltransferase Domain of Pseudomonas aeruginosa ExoT Contributes to Its Biological Activities
ABSTRACT ExoT is a type III secreted effector protein found in almost all strains of Pseudomonas aeruginosa and is required for… Expand
  • table 1
  • table 2
  • figure 1
  • figure 2
  • figure 3
Highly Cited
2003
Highly Cited
2003
Crystal structure and site-directed mutagenesis of enzymatic components from Clostridium perfringens iota-toxin.
Iota-toxin from Clostridium perfringens type E is an ADP-ribosylating toxin (ADPRT) that ADP-ribosylates actin, which is lethal… Expand
2003
2003
NarE: a novel ADP‐ribosyltransferase from Neisseria meningitidis
Mono ADP‐ribosyltransferases (ADPRTs) are a class of functionally conserved enzymes present in prokaryotic and eukaryotic… Expand
Highly Cited
2001
Highly Cited
2001
Vibrio fischeri genes hvnA and hvnB encode secreted NAD(+)-glycohydrolases.
HvnA and HvnB are proteins secreted by Vibrio fischeri ES114, an extracellular light organ symbiont of the squid Euprymna… Expand
  • figure 1
  • figure 2
  • figure 3
  • figure 4
  • figure 5
Highly Cited
2000
Highly Cited
2000
Interaction of Two Classes of ADP-ribose Transfer Reactions in Immune Signaling*
  • Myung-Kwan Han, Yee-Sook Cho, Young Saeng Kim, C. Yim, U. Kim
  • The Journal of Biological Chemistry
  • 2000
    • Corpus ID: 37571240
CD38 is a bifunctional ectoenzyme predominantly expressed on hematopoietic cells where its expression correlates with… Expand
  • figure 1
  • figure 3
  • figure 4
  • figure 5
Highly Cited
2000
Highly Cited
2000
Characterization of the enzymatic component of Clostridium perfringens iota-toxin.
The iota(a) component (i(a)) of Clostridium perfringens ADP ribosylates nonmuscle beta/gamma actin and skeletal muscle alpha… Expand
  • figure 1
  • figure 2
  • table 1
  • table 2
  • table 3
Highly Cited
1995
Highly Cited
1995
Mice lacking ADPRT and poly(ADP-ribosyl)ation develop normally but are susceptible to skin disease.
Poly(ADP-ribosyl)ation is catalyzed by NAD+: protein(ADP-ribosyl) transferase (ADPRT), a chromatin-associated enzyme which, in… Expand
By clicking accept or continuing to use the site, you agree to the terms outlined in our Privacy Policy, Terms of Service, and Dataset License
ACCEPT & CONTINUE