Evidence map›Paper›PMID 28855209›Full record

ReviewCancer research2017

Therapeutic Targeting of Oncogenic Tyrosine Phosphatases.

Rochelle Frankson, Zhi-Hong Yu, Yunpeng Bai, Qinglin Li, Ruo-Yu Zhang, Zhong-Yin Zhang

Open access · bronzeAbstract readReview
In one paragraph

Review in Cancer research, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 99 papers.

0numbers the graph read from it
0cells of the map it votes in
99citing papers in PubMed
7.2field-weighted citation impact, top 2% 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

99 citing papers in PubMed, 187 citations in OpenAlex.

  1. Review
  2. RBM15/IGF2BP2-PTPRH m6A regulatory axis in non-small cell lung cancer.Cellular oncology (Dordrecht, Netherlands) · 2026
    Article
  3. Article
  4. Review
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  6. Article
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  9. Article
  10. Review
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  12. Review
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  14. JAK-STAT Signaling in Autoimmunity and Cancer.ImmunoTargets and therapy · 2025
    Review
  15. Review
  16. Article
  17. Article
  18. Article
  19. Article
  20. Article

39 more citing papers are in PubMed but not listed here.

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

6 authors at 1 institution in 1 country.

Rochelle FranksonDepartments of Medicinal Chemistry and Molecular Pharmacology and Chemistry, Center for Cancer Research and Institute for Drug Discovery, Purdue University, West Lafayette, Indiana.
Zhi-Hong YuDepartments of Medicinal Chemistry and Molecular Pharmacology and Chemistry, Center for Cancer Research and Institute for Drug Discovery, Purdue University, West Lafayette, Indiana.
Yunpeng BaiDepartments of Medicinal Chemistry and Molecular Pharmacology and Chemistry, Center for Cancer Research and Institute for Drug Discovery, Purdue University, West Lafayette, Indiana.
Qinglin LiDepartments of Medicinal Chemistry and Molecular Pharmacology and Chemistry, Center for Cancer Research and Institute for Drug Discovery, Purdue University, West Lafayette, Indiana.
Ruo-Yu ZhangDepartments of Medicinal Chemistry and Molecular Pharmacology and Chemistry, Center for Cancer Research and Institute for Drug Discovery, Purdue University, West Lafayette, Indiana.
Zhong-Yin ZhangDepartments of Medicinal Chemistry and Molecular Pharmacology and Chemistry, Center for Cancer Research and Institute for Drug Discovery, Purdue University, West Lafayette, Indiana. 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

Protein tyrosine phosphatases (PTP) are exciting and novel targets for cancer drug discovery that work in concert with protein tyrosine kinases (PTK) in controlling cellular homeostasis. Given the activating role that some PTKs play in initiating growth factor-mediated cellular processes, PTPs are usually perceived as the negative regulators of these events and therefore tumor suppressive in nature. However, mounting evidence indicate that PTPs do not always antagonize the activity of PTKs in regulating tyrosine phosphorylation, but can also play dominant roles in the initiation and progression of signaling cascades that regulate cell functions. It follows, therefore, that PTP malfunction can actively contribute to a host of human disorders, in particular, cancer, metabolic syndromes, and autoimmune diseases. The Src homology domain containing phosphatase 2 (SHP2) and the three-membered family of phosphatases of regenerating liver (PRL) are infamously oncogenic members of the PTP superfamily. Both are established regulators of major cancer pathways such as Ras/ERK1/2, Src, JAK/STAT, JNK, NF-κB, and PTEN/PI3K/AKT. Furthermore, upregulation, mutation, or other dysregulation of these PTPs has been positively correlated with cancer initiation and progression. This review will provide topical coverage of target validation and drug discovery efforts made in targeting these oncogenic PTPs as compelling candidates for cancer therapy.

Indexed as

AnimalsAntineoplastic AgentsCarcinogenesisHumansMolecular Targeted TherapyMutationNeoplasmsOncogenesProtein Tyrosine PhosphatasesSignal TransductionAntineoplastic AgentsProtein Tyrosine Phosphatases

Identifiers

PMID28855209
PMCPMC5827927
OpenAlexW2751912697

What Socratic holds

Textmetadata
LicenceTDM
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 Socratic graph.