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

Wiskott-Aldrich Syndrome causing mutation, Pro373Ser restricts conformational changes essential for WASP activity in T-cells.

Biochimica et biophysica acta - 1 Apr 2014

Jain Neeraj, George Bhawana, Thanabalu Thirumaran

Abstract excerpt

Wiskott-Aldrich Syndrome (WAS) is caused by mutations in Wiskott-Aldrich Syndrome Protein (WASP) and majority of the mutations are found in the WASP Homology 1 (WH1) domain which mediates interaction with WIP (WASP Interacting Protein), a WASP chaperone. Two point mutations together in the proline rich region (PRR) domain of WASP (S339Y/P373S) have been reported to cause WAS however the molecular defect has not...

Read the complete abstract on PubMed

Topics

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

Share to Carrier Proteins
Share to Chemotaxis, Leukocyte

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Interleukin-2

Share to Jurkat Cells

Share to Lymphocyte Activation

Share to T-Lymphocytes

Share to Wiskott-Aldrich Syndrome

Share to Wiskott-Aldrich Syndrome Protein

Source

Identifiers

PMID: 24440360
DOI: 10.1016/j.bbadis.2014.01.006

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 3 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Wiskott-Aldrich Syndrome causing mutation, Pro373Ser restricts conformational changes essential for WASP activity in T-cells.PMID 24440360Read ↗

A second-site mutation in the initiation codon of WAS (WASP) results in expansion of subsets of lymphocytes in an Wiskott-Aldrich syndrome patient.Semantic proximity Read ↗

The role of Wiskott-Aldrich Syndrome protein in activation and function of human T cellsSemantic proximity Read ↗

The expression of Wiskott-Aldrich syndrome protein (WASP) is dependent on WASP-interacting protein (WIP)Semantic proximity Read ↗

Ubiquitylation-Dependent Negative Regulation of WASp Is Essential for Actin Cytoskeleton DynamicsSemantic proximity Read ↗

Two novel mutations of Wiskott-Aldrich syndrome: the molecular prediction of interaction between the mutated WASP L101P with WASP-interacting protein by molecular modeling.Semantic proximity Read ↗

WASP family proteins: Molecular mechanisms and implications in human diseaseSemantic proximity Read ↗

WASP suppresses the growth defect of Saccharomyces cerevisiae las17Delta strain in the presence of WIP.Semantic proximity Read ↗

Analysis of clinical and molecular characteristics of Wiskott-Aldrich syndrome in 24 patients from 23 unrelated Chinese families.Semantic proximity Read ↗

Wiskott-Aldrich Syndrome Protein-Deficient Mice Reveal a Role for WASP in T but Not B Cell ActivationSemantic proximity Read ↗

Structural basis of Wiskott-Aldrich syndrome causing mutations in the WH1 domain.Semantic proximity Read ↗

Phosphorylation of tyrosine 291 enhances the ability of WASp to stimulate actin polymerization and filopodium formation. Wiskott-Aldrich Syndrome protein.Semantic proximity Read ↗

A Complex of Wiskott-Aldrich Syndrome Protein with Mammalian Verprolins Plays an Important Role in Monocyte ChemotaxisSemantic proximity Read ↗

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