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ADO gene
Known as:
CYSTEAMINE DIOXYGENASE
, 2-AMINOETHANETHIOL DIOXYGENASE
, CHROMOSOME 10 OPEN READING FRAME 22
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National Institutes of Health
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Related topics
Related topics
1 relation
cysteamine dioxygenase
Papers overview
Semantic Scholar uses AI to extract papers important to this topic.
Highly Cited
2018
Highly Cited
2018
Tumor immune evasion arises through loss of TNF sensitivity
C. Kearney
,
S. Vervoort
,
+15 authors
J. Oliaro
Science Immunology
2018
Corpus ID: 21698210
Whole-genome CRISPR screens identify resistance to TNF-mediated killing by T and NK cells as a tumor immune evasion mechanism…
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2018
2018
Cofactor Biogenesis in Cysteamine Dioxygenase: C-F Bond Cleavage with Genetically Incorporated Unnatural Tyrosine.
Yifan Wang
,
W. Griffith
,
+4 authors
Aimin Liu
Angewandte Chemie
2018
Corpus ID: 21663353
Cysteamine dioxygenase (ADO) is a thiol dioxygenase whose study has been stagnated by the ambiguity as to whether or not it…
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Highly Cited
2017
Highly Cited
2017
Dense genotyping of immune-related loci implicates host responses to microbial exposure in Behçet’s disease susceptibility
M. Takeuchi
,
N. Mizuki
,
+27 authors
E. Remmers
Nature Genetics
2017
Corpus ID: 20961399
We analyzed 1,900 Turkish Behçet's disease cases and 1,779 controls genotyped with the Immunochip. The most significantly…
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Review
2017
Review
2017
Understanding human thiol dioxygenase enzymes: structure to function, and biology to pathology
Bibekananda Sarkar
,
Mahesh Kulharia
,
A. Mantha
International journal of experimental pathology
2017
Corpus ID: 4519624
Amino acid metabolism is a significant metabolic activity in humans, especially of sulphur‐containing amino acids, methionine and…
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2016
2016
Synthesis, X-ray Structures, Electronic Properties, and O2/NO Reactivities of Thiol Dioxygenase Active-Site Models.
Anne A. Fischer
,
Nuru G. Stracey
,
S. Lindeman
,
T. Brunold
,
Adam T. Fiedler
Inorganic chemistry
2016
Corpus ID: 29024806
Mononuclear non-heme iron complexes that serve as structural and functional mimics of the thiol dioxygenases (TDOs), cysteine…
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2015
2015
Utilizing the Trispyrazolyl Borate Ligand for the Mimicking of O2-Activating Mononuclear Nonheme Iron Enzymes.
M. Sallmann
,
C. Limberg
Accounts of chemical research
2015
Corpus ID: 28167723
Mononuclear, O2-activating nonheme iron enzymes are a fascinating class of metalloproteines, capable of realizing the most…
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Review
2010
Review
2010
Thiol dioxygenases: unique families of cupin proteins
M. Stipanuk
,
C. Simmons
,
P. Andrew Karplus
,
J. Dominy
Amino Acids
2010
Corpus ID: 23324487
Proteins in the cupin superfamily have a wide range of biological functions in archaea, bacteria and eukaryotes. Although…
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Highly Cited
2009
Highly Cited
2009
3-Mercaptopropionate Dioxygenase, a Cysteine Dioxygenase Homologue, Catalyzes the Initial Step of 3-Mercaptopropionate Catabolism in the 3,3-Thiodipropionic Acid-degrading Bacterium Variovorax…
N. Bruland
,
J. H. Wübbeler
,
A. Steinbüchel
Journal of Biological Chemistry
2009
Corpus ID: 22884664
The thioether 3,3-thiodipropionic acid can be used as precursor substrate for biotechnological synthesis of 3-mercaptopropionic…
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Highly Cited
2007
Highly Cited
2007
Discovery and Characterization of a Second Mammalian Thiol Dioxygenase, Cysteamine Dioxygenase*
J. Dominy
,
C. Simmons
,
L. Hirschberger
,
Jesse Hwang
,
R. Coloso
,
M. Stipanuk
Journal of Biological Chemistry
2007
Corpus ID: 33471230
There are only two known thiol dioxygenase activities in mammals, and they are ascribed to the enzymes cysteine dioxygenase (CDO…
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Highly Cited
2006
Highly Cited
2006
Cysteamine dioxygenase: evidence for the physiological conversion of cysteamine to hypotaurine in rat and mouse tissues.
R. Coloso
,
L. Hirschberger
,
J. Dominy
,
Jeong‐In Lee
,
M. Stipanuk
Advances in experimental medicine and biology
2006
Corpus ID: 36875148
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