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

Structural insights into lethal contractural syndrome type 3 (LCCS3) caused by a missense mutation of PIP5Kγ.

The Biochemical journal - 26 Jul 2018

Zeng Xuankun, Uyar Arzu, Sui Dexin, Donyapour Nazanin, Wu Dianqing, Dickson Alex, Hu Jian

Abstract excerpt

Signaling molecule phosphatidylinositol 4,5-bisphosphate is produced primarily by phosphatidylinositol 4-phosphate 5-kinase (PIP5K). PIP5K is essential for the development of the human neuronal system, which has been exemplified by a recessive genetic disorder, lethal congenital contractural syndrome type 3, caused by a single aspartate-to-asparagine mutation in the kinase domain of PIP5Kγ. So far, the exact role...

Read the complete abstract on PubMed

Topics

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

Share to Adenosine Triphosphate
Share to Contracture

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Molecular Dynamics Simulation

Share to Muscular Atrophy

Share to Phosphotransferases (Alcohol Group Acceptor)

Share to Protein Domains

Share to Zebrafish

Share to Zebrafish Proteins

Source

Open in PubMed Open full text

Identifiers

PMID: 29959184
DOI: 10.1042/BCJ20180326
PMCID: PMC6434533

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Structural insights into lethal contractural syndrome type 3 (LCCS3) caused by a missense mutation of PIP5Kγ.PMID 29959184Read ↗

Decoding the Interactions Regulating the Active State Mechanics of Eukaryotic Protein Kinases.Semantic proximity Read ↗

Redistribution of sidechain-sidechain interactions govern ligand-specific binding affinity changes in missense Shank1 PDZ variantsSemantic proximity Read ↗

Structural insights and activating mutations in diverse pathologies define mechanisms of deregulation for phospholipase C gamma enzymes.Semantic proximity Read ↗

CDKL5 Deficiency Disorder: Revealing the Molecular Mechanism of Pathogenic VariantsSemantic proximity Read ↗

Molecular insights into MYO3A kinase domain variants explain variability in both severity and progression of DFNB30 hearing impairment.Semantic proximity Read ↗

B56δ long-disordered arms form a dynamic PP2A regulation interface coupled with global allostery and Jordan's syndrome mutations.Semantic proximity Read ↗

Molecular Dynamics of CYFIP2 Protein and Its R87C Variant Related to Early Infantile Epileptic Encephalopathy.Semantic proximity Read ↗

Molecular mechanics and dynamic simulations of well-known Kabuki syndrome-associated KDM6A variants reveal putative mechanisms of dysfunction.Semantic proximity Read ↗

Functional impact of the ATP1A3-p.A813V variant: insights into a calcium-driven hyperexcitability cascade in rapid-onset dystonia-Parkinsonism.Semantic proximity Read ↗

Extended regulation interface coupled to the allosteric network and disease mutations in the PP2A-B56δ holoenzymeSemantic proximity Read ↗

The second PI(3,5)P2 binding site in the S0 helix of KCNQ1 stabilizes PIP2-at the primary PI1 site with potential consequences on intermediate-to-open state transition.Semantic proximity Read ↗

Exploring the structural insights on human laforin mutation K87A in Lafora disease--a molecular dynamics study.Semantic proximity Read ↗

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