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

Biochemical characterization of human prolyl hydroxylase domain protein 2 variants associated with erythrocytosis.

Biochemistry - 28 Oct 2008

Pappalardi Melissa B, Martin John D, Jiang Yong, Burns Matthew C, Zhao Huizhen, Ho Thau, Sweitzer Sharon, Lor Leng, Schwartz Benjamin, Duffy Kevin, Gontarek Richard, Tummino Peter J, Copeland Robert A, Luo Lusong

Abstract excerpt

Prolyl hydroxylase domain proteins (PHD isozymes 1-3) regulate levels of the alpha-subunit of the hypoxia inducible factor (HIF) through proline hydroxylation, earmarking HIFalpha for proteosome-mediated degradation. Under hypoxic conditions, HIF stabilization leads to enhanced transcription and regulation of a multitude of processes, including erythropoiesis. Herein, we examine the biochemical characterization...

Read the complete abstract on PubMed

Topics

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

Share to Arginine
Share to Histidine

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Hydrogen Bonding

Share to Hydroxylation

Share to Hypoxia-Inducible Factor 1, alpha Subunit

Share to Polycythemia

Share to Procollagen-Proline Dioxygenase

Share to Proline

Source

Identifiers

PMID: 18834144
DOI: 10.1021/bi801624f

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

Biochemical characterization of human prolyl hydroxylase domain protein 2 variants associated with erythrocytosis.PMID 18834144Read ↗

A novel erythrocytosis-associated PHD2 mutation suggests the location of a HIF binding groove.Semantic proximity Read ↗

Isolated erythrocytosis: study of 67 patients and identification of three novel germ-line mutations in the prolyl hydroxylase domain protein 2 (PHD2) geneSemantic proximity Read ↗

Novel <i>EGLN1</i> variants identified in patients with erythrocytosis: a functional studySemantic proximity Read ↗

Characterization of genetic variants in the EGLN1/PHD2 gene identified in a European collection of patients with erythrocytosisSemantic proximity Read ↗

Cardiopulmonary phenotype associated with human PHD2 mutation.Semantic proximity Read ↗

Erythrocytosis-associated HIF-2alpha mutations demonstrate a critical role for residues C-terminal to the hydroxylacceptor proline.Semantic proximity Read ↗

Erythrocytosis-inducing PHD2 mutations implicate biological role for N-terminal prolyl-hydroxylation in HIF1α oxygen-dependent degradation domainSemantic proximity Read ↗

Computational analysis of prolyl hydroxylase domain-containing protein 2 (PHD2) mutations promoting polycythemia insurgence in humans.Semantic proximity Read ↗

The role of PHD2 mutations in the pathogenesis of erythrocytosisSemantic proximity Read ↗

Deficiency in PHD2-mediated hydroxylation of HIF2α underlies Pacak-Zhuang syndrome.Semantic proximity Read ↗

Somatic inactivation of the PHD2 prolyl hydroxylase causes polycythemia and congestive heart failure.Semantic proximity Read ↗

Involvement of oxygen-sensing pathways in physiologic and pathologic erythropoiesis.Semantic proximity Read ↗

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