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

Characterization of the SAM domain of the PKD-related protein ANKS6 and its interaction with ANKS3.

BMC structural biology - 7 Jul 2014

Leettola Catherine N, Knight Mary Jane, Cascio Duilio, Hoffman Sigrid, Bowie James U

Abstract excerpt

BACKGROUND: Autosomal dominant polycystic kidney disease (ADPKD) is the most common genetic disorder leading to end-stage renal failure in humans. In the PKD/Mhm(cy/+) rat model of ADPKD, the point mutation R823W in the sterile alpha motif (SAM) domain of the protein ANKS6 is responsible for disease. SAM domains are known protein-protein interaction domains, capable of binding each other to form polymers and...

Read the complete abstract on PubMed

Topics

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

Share to Ankyrin Repeat
Share to Carrier Proteins
Share to Circular Dichroism

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Nuclear Proteins

Share to Protein Conformation

Share to Protein Structure, Secondary

Share to Protein Structure, Tertiary

Share to Surface Plasmon Resonance

Source

Open in PubMed Open full text

Identifiers

PMID: 24998259
DOI: 10.1186/1472-6807-14-17
PMCID: PMC4105859

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

Characterization of the SAM domain of the PKD-related protein ANKS6 and its interaction with ANKS3.PMID 24998259Read ↗

The SAM domain of ANKS6 has different interacting partners and mutations can induce different cystic phenotypes.Semantic proximity Read ↗

ANKS3 Co-Localises with ANKS6 in Mouse Renal Cilia and Is Associated with Vasopressin Signaling and Apoptosis In Vivo in Mice.Semantic proximity Read ↗

Influence of the R823W mutation on the interaction of the ANKS6-ANKS3: insights from molecular dynamics simulation and free energy analysis.Semantic proximity Read ↗

Polycystic kidney disease in Han:SPRD Cy rats is associated with elevated expression and mislocalization of SamCystin.Semantic proximity Read ↗

Unique structural features govern the activity of a human mitochondrial AAA+ disaggregase, Skd3Semantic proximity Read ↗

Atmin modulates Pkhd1 expression and may mediate Autosomal Recessive Polycystic Kidney Disease (ARPKD) through altered non-canonical Wnt/Planar Cell Polarity (PCP) signallingSemantic proximity Read ↗

Missense mutation in sterile alpha motif of novel protein SamCystin is associated with polycystic kidney disease in (cy/+) rat.Semantic proximity Read ↗

Anks3 alters the sub-cellular localization of the Nek7 kinase.Semantic proximity Read ↗

Transgenic overexpression of Anks6(p.R823W) causes polycystic kidney disease in rats.Semantic proximity Read ↗

The Role of ANK in Calcium Pyrophosphate Deposition Disease.Semantic proximity Read ↗

The Inv compartment of renal cilia is an intraciliary signal-activating center to phosphorylate ANKS6.Semantic proximity Read ↗

The polycystic kidney disease-related proteins Bicc1 and SamCystin interact.Semantic proximity Read ↗

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