Gathering STYX: phosphatase-like form predicts functions for unique protein-interaction domains.

doi:10.1016/s0968-0004(98)01241-9

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

Back to search

Article

Gathering STYX: phosphatase-like form predicts functions for unique protein-interaction domains.

Trends in biochemical sciences - 1 Aug 1998

Wishart M J, Dixon J E

Abstract excerpt

The effects of tyrosine phosphorylation are manifested and regulated through protein domains that bind to specific phosphotyrosine motifs. STYX is a unique modular domain found within proteins implicated in mediating the effects of tyrosine phosphorylation in vivo. Individual STYX domains are not...

Topics

Amino Acid Sequence
Animals
Autoantigens
Binding Sites
Carrier Proteins
Databases, Factual
Fungal Proteins
Intracellular Signaling Peptides and Proteins
Membrane Proteins
Molecular Sequence Data
Mutation
Phosphorylation

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Protein Tyrosine Phosphatases

Protein-Tyrosine Kinases

Proteins

Receptor-Like Protein Tyrosine Phosphatases, Class 8

Sequence Homology, Amino Acid

Viral Proteins

Source

Open in PubMed

Identifiers

PMID: 9757831
DOI: 10.1016/s0968-0004(98)01241-9

Genes

STYX

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 30 Aug 2026. Prepared record publication-9757831-2026-08-30.1. Manifest publication-graph-cohort-2026-08-30.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 30 Aug 2026.

Community interpretation

Discuss the evidence

Ask a question, add context or challenge an interpretation. Community activity is separate from scientific evidence strength.

discussions

replies

Citations encouraged

Claims remain attributable.

No discussion yet

Be the first to add a careful, cited interpretation.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Gathering STYX: phosphatase-like form predicts functions for unique protein-interaction domains.PMID 9757831Read ↗

A Systematic Compilation of Human SH3 Domains: A Versatile Superfamily in Cellular SignalingSemantic proximity Read ↗

A Drosophila-centric view of protein tyrosine phosphatases.Semantic proximity Read ↗

The Src module: an ancient scaffold in the evolution of cytoplasmic tyrosine kinases.Semantic proximity Read ↗

Deep mutational scanning of a multi-domain signaling protein reveals mechanisms of regulation and pathogenicitySemantic proximity Read ↗

[The Biological Function of SHP2 in Human Disease].Semantic proximity Read ↗

Multifunctional proteins: examples of gene sharingSemantic proximity Read ↗

Use of Dominant-Negative/Substrate Trapping PTP Mutations to Search for PTP Interactors/Substrates.Semantic proximity Read ↗

The tyrosine phosphatase Shp2 (PTPN11) in cancer.Semantic proximity Read ↗

The Landscape of Protein Tyrosine Phosphatase (Shp2) and CancerSemantic proximity Read ↗

Structural analysis of the protein phosphatase 1 docking motif: molecular description of binding specificities identifies interacting proteins.Semantic proximity Read ↗

A brief introduction to the protein phosphatase families.Semantic proximity Read ↗

Protein tyrosine phosphatases in health and disease.Semantic proximity Read ↗

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