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Article

The Q188R mutation in human galactose-1-phosphate uridylyltransferase acts as a partial dominant negative.

The Journal of biological chemistry - 13 Dec 1996

Elsevier J P, Fridovich-Keil J L

Abstract excerpt

A longstanding goal in the fields of molecular genetics and biochemistry has been to explain how naturally occurring mutations associated with human metabolic disease impair activity of the enzymes involved. This goal is particularly complex for enzymes composed of multiple subunits, because sing...

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Identifiers

PMID: 8943248
DOI: 10.1074/jbc.271.50.32002

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 1 Sept 2026. Prepared record publication-8943248-2026-09-01.1. Manifest publication-graph-cohort-2026-09-01.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 1 Sept 2026.

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The Q188R mutation in human galactose-1-phosphate uridylyltransferase acts as a partial dominant negative.PMID 8943248Read ↗

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Impact of patient mutations on heterodimer formation and function in human galactose-1-P uridylyltransferase.Semantic proximity Read ↗

Structural and molecular biology of type I galactosemia: disease-associated mutations.Semantic proximity Read ↗

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Homology modeling studies on human galactose-1-phosphate uridylyltransferase and on its galactosemia-related mutant Q188R provide an explanation of molecular effects of the mutation on homo- and heterodimers.Semantic proximity Read ↗

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Characterization of the N314D allele of human galactose-1-phosphate uridylyltransferase using a yeast expression system.Semantic proximity Read ↗

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