Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

A single amino acid substitution in the putative redox partner-binding site of P450c17 as cause of isolated 17,20-lyase deficiency.

The Journal of clinical endocrinology and metabolism - 1 Nov 1997

Biason-Lauber A, Leiberman E, Zachmann M

Abstract excerpt

The molecular basis of isolated 17,20-lyase deficiency was clarified in a newborn male patient from Israel with micropenis, undescended testes, and hormonal pattern consistent with isolated 17,20-lyase deficiency. Analysis of the CYP17 gene revealed the presence of a compound heterozygosity. One allele carries a single base pair deletion (T at position 198 in exon 1) leading to a frame shift with the introduction...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Alleles
Share to Binding Sites
Share to Blotting, Southern

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Heterozygote

Share to Mutation

Share to Pedigree

Share to Sequence Analysis, DNA

Share to Transfection

Source

Identifiers

PMID: 9360545
DOI: 10.1210/jcem.82.11.4380

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

A single amino acid substitution in the putative redox partner-binding site of P450c17 as cause of isolated 17,20-lyase deficiency.PMID 9360545Read ↗

The genetic and functional basis of isolated 17,20-lyase deficiency.Semantic proximity Read ↗

Towards a unifying mechanism for CYP17 mutations that cause isolated 17,20-lyase deficiency.Semantic proximity Read ↗

Homozygous Mutation G539R in the Gene for P450 Oxidoreductase in a Family Previously Diagnosed as Having 17,20-Lyase DeficiencySemantic proximity Read ↗

Pitfalls in characterizing P450c17 mutations associated with isolated 17,20-lyase deficiency.Semantic proximity Read ↗

The molecular basis of isolated 17,20 lyase deficiency.Semantic proximity Read ↗

A Missense Mutation in the Human Cytochrome b5 Gene causes 46,XY Disorder of Sex Development due to True Isolated 17,20 Lyase DeficiencySemantic proximity Read ↗

The regulation of 17,20 lyase activity.Semantic proximity Read ↗

[Clinical and genetic analysis of an infant with isolated 17, 20-lyase deficiency].Semantic proximity Read ↗

Novel mutation of the CYP17 gene in two unrelated patients with combined 17alpha-hydroxylase/17,20-lyase deficiency: demonstration of absent enzyme activity by expressing the mutant CYP17 gene and by three-dimensional modeling.Semantic proximity Read ↗

Metabolic evidence for impaired 17alpha-hydroxylase activity in a kindred bearing the E305G mutation for isolate 17,20-lyase activity.Semantic proximity Read ↗

Molecular basis of apparent isolated 17,20-lyase deficiency: compound heterozygous mutations in the C-terminal region (Arg(496)----Cys, Gln(461)----Stop) actually cause combined 17 alpha-hydroxylase/17,20-lyase deficiency.Semantic proximity Read ↗

Mutation of histidine 373 to leucine in cytochrome P450c17 causes 17 alpha-hydroxylase deficiency.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.