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

SHP2 clinical phenotype, cancer, or RASopathies, can be predicted by mutant conformational propensities.

Cellular and molecular life sciences : CMLS - 12 Dec 2023

Liu Yonglan, Zhang Wengang, Jang Hyunbum, Nussinov Ruth

Abstract excerpt

SHP2 phosphatase promotes full activation of the RTK-dependent Ras/MAPK pathway. Its mutations can drive cancer and RASopathies, a group of neurodevelopmental disorders (NDDs). Here we ask how same residue mutations in SHP2 can lead to both cancer and NDD phenotypes, and whether we can predict what the outcome will be. We collected and analyzed mutation data from the literature and cancer databases and performed...

Read the complete abstract on PubMed

Topics

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

Share to Mutation
Share to Neoplasms
Share to Noonan Syndrome

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Phenotype

Share to Protein Tyrosine Phosphatase, Non-Receptor Type 11

Share to src Homology Domains

Source

Open in PubMed Open full text

Identifiers

PMID: 38085330
DOI: 10.1007/s00018-023-05052-8
PMCID: PMC11072105

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

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

SHP2 clinical phenotype, cancer, or RASopathies, can be predicted by mutant conformational propensities.PMID 38085330Read ↗

Structural and mechanistic insights into LEOPARD syndrome-associated SHP2 mutations.Semantic proximity Read ↗

The pathogenic T42A mutation in SHP2 rewires the interaction specificity of its N-terminal regulatory domainSemantic proximity Read ↗

Diverse biochemical properties of Shp2 mutants. Implications for disease phenotypes.Semantic proximity Read ↗

Multiplexed single-cell transcriptomics reveals diverse phenotypic outcomes for pathogenic SHP2 variantsSemantic proximity Read ↗

Multiplexed single-cell transcriptomics reveals diverse phenotypic outcomes for pathogenic SHP2 variants.Semantic proximity Read ↗

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

SHP2 binds directly to SOS1 to enable RAS activationSemantic proximity Read ↗

An allosteric interaction controls the activation mechanism of SHP2 tyrosine phosphataseSemantic proximity Read ↗

Molecular basis of gain-of-function LEOPARD syndrome-associated SHP2 mutations.Semantic proximity Read ↗

Structural insights into Noonan/LEOPARD syndrome-related mutants of protein-tyrosine phosphatase SHP2 (PTPN11).Semantic proximity Read ↗

The pathogenic T42A mutation in SHP2 rewires the interaction specificity of its N-terminal regulatory domain.Semantic proximity Read ↗

Phase Separation of Disease-Associated SHP2 Mutants Underlies MAPK Hyperactivation.Semantic proximity Read ↗

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