Evidence map›Paper›PMID 32188694›Full record

ArticleThe Journal of biological chemistry2020

Mechanistic insights explain the transforming potential of the T507K substitution in the protein-tyrosine phosphatase SHP2.

Ruo-Yu Zhang, Zhi-Hong Yu, Lan Chen, Chad D Walls, Sheng Zhang, Li Wu, Zhong-Yin Zhang

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
0.9field-weighted citation impact, top 27% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

16 citing papers in PubMed, 22 citations in OpenAlex.

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  9. Review
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  13. A comprehensive review of SHP2 and its role in cancer.Cellular oncology (Dordrecht, Netherlands) · 2022
    Review
  14. Article
  15. Article
  16. Review
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

7 authors at 1 institution in 1 country.

Ruo-Yu ZhangDepartments of Medicinal Chemistry and Molecular Pharmacology and of Chemistry, Center for Cancer Research, and Institute for Drug Discovery, Purdue University, West Lafayette, Indiana 47907.
Zhi-Hong YuDepartments of Medicinal Chemistry and Molecular Pharmacology and of Chemistry, Center for Cancer Research, and Institute for Drug Discovery, Purdue University, West Lafayette, Indiana 47907.
Lan ChenDepartments of Medicinal Chemistry and Molecular Pharmacology and of Chemistry, Center for Cancer Research, and Institute for Drug Discovery, Purdue University, West Lafayette, Indiana 47907.
Chad D WallsDepartments of Medicinal Chemistry and Molecular Pharmacology and of Chemistry, Center for Cancer Research, and Institute for Drug Discovery, Purdue University, West Lafayette, Indiana 47907.
Sheng ZhangDepartments of Medicinal Chemistry and Molecular Pharmacology and of Chemistry, Center for Cancer Research, and Institute for Drug Discovery, Purdue University, West Lafayette, Indiana 47907.
Li WuDepartments of Medicinal Chemistry and Molecular Pharmacology and of Chemistry, Center for Cancer Research, and Institute for Drug Discovery, Purdue University, West Lafayette, Indiana 47907.
Zhong-Yin ZhangDepartments of Medicinal Chemistry and Molecular Pharmacology and of Chemistry, Center for Cancer Research, and Institute for Drug Discovery, Purdue University, West Lafayette, Indiana 47907. Electronic address: zhang-zy@purdue.edu.
Purdue University West Lafayette · US

Funding

Structure/Function of Protein Tyrosine PhosphatasesR01CA069202 · NCI · YESHIVA UNIVERSITY · PI Zhong-Yin Zhang · 1996 to 2026
$7.3M
Development of SHP2 inhibitors for targeted anti-cancer therapyR01CA207288 · NCI · PURDUE UNIVERSITY · PI ZHANG, ZHONG-YIN · 2017 to 2021
$2.3M
NCI NIH HHS R01 CA069202NCI NIH HHS R01 CA207288
6 · The paper itself

Abstract

The protein-tyrosine phosphatase SHP2 is an allosteric enzyme critical for cellular events downstream of growth factor receptors. Mutations in the

Indexed as

Amino Acid SubstitutionAmino Acid SequenceCatalytic DomainCrystallography, X-RayHumansModels, MolecularProtein Tyrosine Phosphatase, Non-Receptor Type 11Protein Tyrosine Phosphatase, Non-Receptor Type 11cancerkineticsmutationphosphataseSHP2signalingstructure–functiontransformation

Identifiers

PMID32188694
PMCPMC7196634
OpenAlexW3012220809

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.