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ADP Ribose Transferases
Known as:
ARTases
, Transferases, ART
, ADPRTs
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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…
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National Institutes of Health
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Related topics
Related topics
24 relations
ART3 gene
In Blood
PARP1 gene
PARP1 wt Allele
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Narrower (11)
ART5 protein, mouse
Art2b protein, rat
BMS-191352 protein, recombinant
ExoT protein, Pseudomonas aeruginosa
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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
Yan Sun
,
Mausita Karmakar
,
Patricia R. Taylor
,
A. Rietsch
,
E. Pearlman
The Journal of Immunology
2012
Corpus ID: 1572379
Pseudomonas aeruginosa is a leading cause of blinding corneal ulcers worldwide. To determine the role of type III secretion in…
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Highly Cited
2008
Highly Cited
2008
Structural basis of actin recognition and arginine ADP-ribosylation by Clostridium perfringens ι-toxin
H. Tsuge
,
M. Nagahama
,
+6 authors
J. Sakurai
Proceedings of the National Academy of Sciences
2008
Corpus ID: 12706750
The ADP-ribosylating toxins (ADPRTs) produced by pathogenic bacteria modify intracellular protein and affect eukaryotic cell…
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Highly Cited
2008
Highly Cited
2008
Association between Polymorphisms in DNA Base Excision Repair Genes XRCC1, APE1, and ADPRT and Differentiated Thyroid Carcinoma
F. Chiang
,
Che‐Wei Wu
,
+5 authors
S. Juo
Clinical Cancer Research
2008
Corpus ID: 11382362
Purpose: DNA BER pathway is related with carcinogenesis. We hypothesized that functional polymorphisms of three BER genes, XRCC1…
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Review
2006
Review
2006
A family of killer toxins
Kenneth P. Holbourn
,
C. Shone
,
K. Acharya
The FEBS journal
2006
Corpus ID: 40379655
The ADP‐ribosylating toxins (ADPRTs) are a family of toxins that catalyse the hydrolysis of NAD and the transfer of the ADP…
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Highly Cited
2004
Highly Cited
2004
The ADP Ribosyltransferase Domain of Pseudomonas aeruginosa ExoT Contributes to Its Biological Activities
L. Garrity-Ryan
,
S. Shafikhani
,
+8 authors
J. Engel
Infection and Immunity
2004
Corpus ID: 21038353
ABSTRACT ExoT is a type III secreted effector protein found in almost all strains of Pseudomonas aeruginosa and is required for…
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Highly Cited
2003
Highly Cited
2003
Crystal structure and site-directed mutagenesis of enzymatic components from Clostridium perfringens iota-toxin.
H. Tsuge
,
M. Nagahama
,
+5 authors
J. Sakurai
Journal of molecular biology
2003
Corpus ID: 25705418
Highly Cited
2001
Highly Cited
2001
Vibrio fischeri Genes hvnA andhvnB Encode Secreted NAD+-Glycohydrolases
E. Stabb
,
K. Reich
,
E. Ruby
Journal of bacteriology
2001
Corpus ID: 14225168
ABSTRACT HvnA and HvnB are proteins secreted by Vibrio fischeriES114, an extracellular light organ symbiont of the squidEuprymna…
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Highly Cited
2000
Highly Cited
2000
Characterization of the Enzymatic Component of Clostridium perfringens Iota-Toxin
M. Nagahama
,
Yoshihiko Sakaguchi
,
Keiko Kobayashi
,
S. Ochi
,
J. Sakurai
Journal of bacteriology
2000
Corpus ID: 22500540
ABSTRACT The iotaa component (ia) ofClostridium perfringens ADP ribosylates nonmuscle β/γ actin and skeletal muscle α-actin…
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Highly Cited
2000
Highly Cited
2000
Interaction of Two Classes of ADP-ribose Transfer Reactions in Immune Signaling*
Myung-Kwan Han
,
Y. Cho
,
Young S. 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…
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Highly Cited
1995
Highly Cited
1995
Mice lacking ADPRT and poly(ADP-ribosyl)ation develop normally but are susceptible to skin disease.
Z. Wang
,
B. Auer
,
+4 authors
E. Wagner
Genes & development
1995
Corpus ID: 32338147
Poly(ADP-ribosyl)ation is catalyzed by NAD+: protein(ADP-ribosyl) transferase (ADPRT), a chromatin-associated enzyme which, in…
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