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

γ-Glutamyl carboxylase mutations differentially affect the biological function of vitamin K-dependent proteins.

Blood - 28 Jan 2021

Hao Zhenyu, Jin Da-Yun, Chen Xuejie, Schurgers Leon J, Stafford Darrel W, Tie Jian-Ke

Abstract excerpt

γ-Glutamyl carboxylase (GGCX) is an integral membrane protein that catalyzes posttranslational carboxylation of a number of vitamin K-dependent (VKD) proteins involved in a wide variety of physiologic processes, including blood coagulation, vascular calcification, and bone metabolism. Naturally occurring GGCX mutations are associated with multiple distinct clinical phenotypes. However, the genotype-phenotype...

Read the complete abstract on PubMed

Topics

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

Share to Carbon-Carbon Ligases
Share to Carboxy-Lyases

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Genetic Pleiotropy

Share to Hemorrhagic Disorders

Share to Osteocalcin

Share to Protein C

Share to RNA Precursors

Share to Vitamin K

Source

Open in PubMed Open full text

Identifiers

PMID: 33507293
DOI: 10.1182/blood.2020006329
PMCID: PMC7845004

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 1 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

γ-Glutamyl carboxylase mutations differentially affect the biological function of vitamin K-dependent proteins.PMID 33507293Read ↗

Cellular and biochemical approaches to define GGCX carboxylation of vitamin K-dependent proteins.Semantic proximity Read ↗

Molecular insights into the comorbidity of vitamin K-dependent clotting factor deficiency and chondrodysplasia punctata.Semantic proximity Read ↗

Characterization of vitamin K-dependent carboxylase mutations that cause bleeding and nonbleeding disorders.Semantic proximity Read ↗

Structural and Functional Insights into GGCX-FIX Interaction: Implications for Vitamin K-Dependent Bleeding DisordersSemantic proximity Read ↗

The Role of GRP and MGP in the Development of Non-Hemorrhagic VKCFD1 Phenotypes.Semantic proximity Read ↗

GGCX variants leading to biallelic deficiency to γ-carboxylate GRP cause skin laxity in VKCFD1 patients.Semantic proximity Read ↗

GGCX variants leading to biallelic deficiency to γ-carboxylate GRP cause skin laxity in VKCFD1 patientsSemantic proximity Read ↗

GGCX-Associated Phenotypes: An Overview in Search of Genotype-Phenotype Correlations.Semantic proximity Read ↗

[Partial research progress of GGCX pathogenic variation associated phenotypes].Semantic proximity Read ↗

Structural and functional insights into enzymes of the vitamin K cycle.Semantic proximity Read ↗

Vitamin K-dependent coagulation factors deficiency.Semantic proximity Read ↗

Familial deficiency of vitamin K‐dependent clotting factorsSemantic proximity Read ↗

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