Cloning of three human multifunctional de novo purine biosynthetic genes by functional complementation of yeast mutations (Q24558712)

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A J Brake

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M C Kiefer

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D Young

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P J Barr

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

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language of work or name

English

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publication date

April 1990

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published in

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volume

87

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issue

8

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page(s)

2916-20

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cites work

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Primary structure of a human trifunctional enzyme. Isolation of a cDNA encoding methylenetetrahydrofolate dehydrogenase-methenyltetrahydrofolate cyclohydrolase-formyltetrahydrofolate synthetase

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27 September 2017

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Structural and mechanistic studies on the HeLa and chicken liver proteins that catalyze glycinamide ribonucleotide synthesis and formylation and aminoimidazole ribonucleotide synthesis

27 September 2017

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Cloning and characterization of a 12-gene cluster from Bacillus subtilis encoding nine enzymes for de novo purine nucleotide synthesis.

27 September 2017

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27 September 2017

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27 September 2017

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27 September 2017

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27 September 2017

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Purification and properties of an enzyme duet, phosphoribosylaminoimidazole carboxylase and phosphoribosylaminoimidazolesuccinocarboxamide synthetase, involved in the biosynthesis of purine nucleotides de novo

30 May 2018

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A somatic cell hybrid with a single human chromosome 22 corrects the defect in the CHO mutant (Ade-I) lacking adenylosuccinase activity.

30 May 2018

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30 May 2018

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30 May 2018

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Isolation and characterization of cDNA clones encoding the murine NAD-dependent methylenetetrahydrofolate dehydrogenase-methenyltetrahydrofolate cyclohydrolase.

30 May 2018

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Isolation of a gene from Drosophila by complementation in yeast.

30 May 2018

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Identification and nucleotide sequence of a gene encoding 5'-phosphoribosylglycinamide transformylase in Escherichia coli K12.

28 November 2018

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Antifolate metabolism and sites of action: implications for the design of new antifolates

28 November 2018

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inferred from PubMed ID database lookup

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based on heuristic

NAD-dependent methylenetetrahydrofolate dehydrogenase-methenyltetrahydrofolate cyclohydrolase in transformed cells is a mitochondrial enzyme

1 reference

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