Evidence for X-linkage of human phosphoribosylpyrophosphate synthetase. - Wikidata - wikimedia - TriplyDB

Evidence for X-linkage of human phosphoribosylpyrophosphate synthetase.

Evidence for X-linkage of human phosphoribosylpyrophosphate synthetase.

http://www.wikidata.org/entity/Q33958008

about

Crystal structure of human phosphoribosylpyrophosphate synthetase 1 reveals a novel allosteric site Phosphoribosylpyrophosphate synthetase overactivity as a cause of uric acid overproduction in a young woman The genetic and functional basis of purine nucleotide feedback-resistant phosphoribosylpyrophosphate synthetase superactivity Structural features of the phosphoribosyltransferases and their relationship to the human deficiency disorders of purine and pyrimidine metabolism Heberden oration 1979: human aberrations of purine metabolism and their significance for rheumatology.Selective expression of phosphoribosylpyrophosphate synthetase superactivity in human lymphoblast lines.Variant human phosphoribosylpyrophosphate synthetase altered in regulatory and catalytic functions Phosphoribosylpyrophosphate synthetase (PrsA) variants alter cellular pools of ribose 5-phosphate and influence thiamine synthesis in Salmonella enterica Overexpression of the normal phosphoribosylpyrophosphate synthetase 1 isoform underlies catalytic superactivity of human phosphoribosylpyrophosphate synthetase.Accelerated transcription of PRPS1 in X-linked overactivity of normal human phosphoribosylpyrophosphate synthetase.

P2860

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P2860

Evidence for X-linkage of human phosphoribosylpyrophosphate synthetase.

http://www.wikidata.org/entity/Q33958008

description

1978 nî lūn-bûn

@nan

1978 թուականի Յունուարին հրատարակուած գիտական յօդուած

@hyw

1978 թվականի հունվարին հրատարակված գիտական հոդված

@hy

1978年の論文

@ja

1978年論文

@yue

1978年論文

@zh-hant

1978年論文

@zh-hk

1978年論文

@zh-mo

1978年論文

@zh-tw

1978年论文

@wuu

name

Evidence for X-linkage of human phosphoribosylpyrophosphate synthetase.

@ast

Evidence for X-linkage of human phosphoribosylpyrophosphate synthetase.

@en

type

label

Evidence for X-linkage of human phosphoribosylpyrophosphate synthetase.

@ast

Evidence for X-linkage of human phosphoribosylpyrophosphate synthetase.

@en

prefLabel

Evidence for X-linkage of human phosphoribosylpyrophosphate synthetase.

@ast

Evidence for X-linkage of human phosphoribosylpyrophosphate synthetase.

@en

P1433

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P1433

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

P1476

Evidence for X-linkage of human phosphoribosylpyrophosphate synthetase.

@en

P2093

Adams WB

http://www.w3.org/2001/XMLSchema#string

Becker MA

http://www.w3.org/2001/XMLSchema#string

Lazar C

http://www.w3.org/2001/XMLSchema#string

Yen RC

http://www.w3.org/2001/XMLSchema#string

P2860

Protein measurement with the Folin phenol reagent

Mutant feedback-resistant phosphoribosylpyrophosphate synthetase associated with purine overproduction and gout. Phosphoribosylpyrophosphate and purine metabolism in cultured fibroblasts

Human glutamine phosphoribosylpyrophosphate amidotransferase. Kinetic and regulatory properties

Gene action in the X-chromosome of the mouse (Mus musculus L.)

Hemizygous expression of glucose-6-phosphate dehydrogenase in erythrocytes of heterozygotes for the Lesch-Nyhan syndrome.

Human phosphoribosylpyrophosphate synthetase: increased enzyme specific activity in a family with gout and excessive purine synthesis.

Patterns of phosphoribosylpyrophosphate and ribose-5-phosphate concentration and generation in fibroblasts from patients with gout and purine overproduction

DEMONSTRATION OF TWO POPULATIONS OF CELLS IN THE HUMAN FEMALE HETEROZYGOUS FOR GLUCOSE-6-PHOSPHATE DEHYDROGENASE VARIANTS.

An improved method for the electrophoretic separation and histochemical identification of 5-phosphoribosyl-1-pyrophosphate synthetase using microgram quantities of crude cell extracts.

Human phosphoribosylpyrophosphate synthetase. Comparison of purified normal and mutant enzymes.

P304

482-485

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P31

scholarly article

P356

10.1073/PNAS.75.1.482

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P433

1

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75

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1978-01-01T00:00:00Z

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22932943

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P698

203941

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P932

411274

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