Enhanced proteolysis of thiopurine S-methyltransferase (TPMT) encoded by mutant alleles in humans (TPMT3A, TPMT2): mechanisms for the genetic polymorphism of TPMT activity (Q24682894)

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English	Enhanced proteolysis of thiopurine S-methyltransferase (TPMT) encoded by mutant alleles in humans (TPMT3A, TPMT2): mechanisms for the genetic polymorphism of TPMT activity	scientific article

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scholarly article

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Enhanced proteolysis of thiopurine S-methyltransferase (TPMT) encoded by mutant alleles in humans (TPMT*3A, TPMT*2): mechanisms for the genetic polymorphism of TPMT activity (English)

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author name string

H L Tai

1

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E Y Krynetski

2

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E G Schuetz

3

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Y Yanishevski

4

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W E Evans

5

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language of work or name

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publication date

10 June 1997

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Proceedings of the National Academy of Sciences of the United States of America

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94

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12

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6444-9

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Thiopurine S-methyltransferase deficiency: two nucleotide transitions define the most prevalent mutant allele associated with loss of catalytic activity in Caucasians

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Human thiopurine methyltransferase: molecular cloning and expression of T84 colon carcinoma cell cDNA

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7 April 2017

A single point mutation leading to loss of catalytic activity in human thiopurine S-methyltransferase

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7 April 2017

Mercaptopurine pharmacogenetics: monogenic inheritance of erythrocyte thiopurine methyltransferase activity

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Molecular diagnosis of thiopurine S-methyltransferase deficiency: genetic basis for azathioprine and mercaptopurine intolerance

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7 April 2017

Thiopurine methyltransferase pharmacogenetics: human gene cloning and characterization of a common polymorphism

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In vivo half-life of a protein is a function of its amino-terminal residue

1 reference

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Selective protein degradation in the yeast exocytic pathway

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Congenital thiopurine methyltransferase deficiency and 6-mercaptopurine toxicity during treatment for acute lymphoblastic leukaemia

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The ubiquitin-mediated proteolytic pathway: mechanisms of recognition of the proteolytic substrate and involvement in the degradation of native cellular proteins.

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Regulation of protein degradation rates in eukaryotes

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Proteinase yscE, the yeast proteasome/multicatalytic-multifunctional proteinase: mutants unravel its function in stress induced proteolysis and uncover its necessity for cell survival

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Natural substrates of the ubiquitin proteolytic pathway

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Metabolism of alpha-factor by a mating type cells of Saccharomyces cerevisiae

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Degradation of fluorescent and radiolabelled sphingomyelins in intact cells by a non-lysosomal pathway

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28 September 2017

Control of the yeast cell cycle is associated with assembly/disassembly of the Cdc28 protein kinase complex

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30 May 2018

Pharmacogenetics of acute azathioprine toxicity: relationship to thiopurine methyltransferase genetic polymorphism

1 reference

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Altered mercaptopurine metabolism, toxic effects, and dosage requirement in a thiopurine methyltransferase-deficient child with acute lymphocytic leukemia

1 reference

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30 May 2018

In vivo function of the proteasome in the ubiquitin pathway

1 reference

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1 reference

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Azathioprine-induced myelosuppression in thiopurine methyltransferase deficient heart transplant recipient.

1 reference

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Methotrexate inhibits proteolysis of dihydrofolate reductase by the N-end rule pathway.

1 reference

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Turnover of excess hemoglobin alpha chains in beta-thalassemic cells is ATP-dependent

1 reference

https://pubmed.ncbi.nlm.nih.gov/9177237

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Azathioprine-induced myelosuppression in thiopurine methyltransferase deficient heart transplant recipient

1 reference

https://pubmed.ncbi.nlm.nih.gov/9177237

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Thiopurine methyltransferase activity in American white subjects and black subjects

1 reference

https://pubmed.ncbi.nlm.nih.gov/9177237

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Quantification of proteins dissolved in an electrophoresis sample buffer

1 reference

https://pubmed.ncbi.nlm.nih.gov/9177237

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Immunochemical analysis of the turnover of ubiquitin-protein conjugates in intact cells. Relationship to the breakdown of abnormal proteins

1 reference

https://pubmed.ncbi.nlm.nih.gov/9177237

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Identifiers

10.1073/PNAS.94.12.6444

1 reference

Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

1997PNAS...94.6444T

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OpenCitations bibliographic resource ID

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Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

PMC publication ID

1 reference

Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

PubMed publication ID

1 reference

Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

ResearchGate publication ID

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