Evidence map›Paper›PMID 36197449›Full record

ArticleJournal of medicinal chemistry2022

Structure-Based Design of Active-Site-Directed, Highly Potent, Selective, and Orally Bioavailable Low-Molecular-Weight Protein Tyrosine Phosphatase Inhibitors.

Rongjun He, Jifeng Wang, Zhi-Hong Yu, Julie S Moyers, M Dodson Michael, Timothy B Durham, Jeff W Cramer, Yuewei Qian, Amy Lin, Li Wu and 3 more

Open access · greenAbstract read
In one paragraph

Article in Journal of medicinal chemistry, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing papers in PubMed
1.0field-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

7 citing papers in PubMed, 11 citations in OpenAlex.

  1. Review
  2. Au Nanoparticle Synthesis in the Presence of Thiolated Hyaluronic Acid.International journal of molecular sciences · 2025
    Article
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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

13 authors at 3 institutions in 2 countries.

Rongjun HeLilly Research Laboratories, Eli Lilly and Company, 307 E Merrill Street, Indianapolis, Indiana 46225, United States.
Jifeng WangDepartment of Biochemistry and Molecular Biology, Indiana University School of Medicine, 635 Barnhill Drive, Indianapolis, Indiana 46202, United States.
Zhi-Hong YuDepartment of Medicinal Chemistry and Molecular Pharmacology and Institute for Drug Discovery, Purdue University, 720 Clinic Drive, West Lafayette, Indiana 47907, United States.
Julie S MoyersLilly Research Laboratories, Eli Lilly and Company, 307 E Merrill Street, Indianapolis, Indiana 46225, United States.
M Dodson MichaelLilly Research Laboratories, Eli Lilly and Company, 307 E Merrill Street, Indianapolis, Indiana 46225, United States.
Timothy B DurhamLilly Research Laboratories, Eli Lilly and Company, 307 E Merrill Street, Indianapolis, Indiana 46225, United States.
Jeff W CramerLilly Research Laboratories, Eli Lilly and Company, 307 E Merrill Street, Indianapolis, Indiana 46225, United States.
Yuewei QianLilly Research Laboratories, Eli Lilly and Company, 307 E Merrill Street, Indianapolis, Indiana 46225, United States.
Amy LinLilly Research Laboratories, Eli Lilly and Company, 307 E Merrill Street, Indianapolis, Indiana 46225, United States.
Li WuDepartment of Medicinal Chemistry and Molecular Pharmacology and Institute for Drug Discovery, Purdue University, 720 Clinic Drive, West Lafayette, Indiana 47907, United States.
Nicholas NoinajDepartment of Biological Sciences, Purdue University, 240 S. Martin Jischke Drive, West Lafayette, Indiana 47907, United States.
David G BarrettLilly Research Laboratories, Eli Lilly and Company, 307 E Merrill Street, Indianapolis, Indiana 46225, United States.
Zhong-Yin ZhangDepartment of Biochemistry and Molecular Biology, Indiana University School of Medicine, 635 Barnhill Drive, Indianapolis, Indiana 46202, United States.ORCID 0000-0001-5527-7910
Eli Lilly (United States) · USPurdue University West Lafayette · USUniversité Bourgogne Franche-Comté · FR

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 constitute an important class of drug targets whose potential has been limited by the paucity of drug-like small-molecule inhibitors. We recently described a class of active-site-directed, moderately selective, and potent inhibitors of the low-molecular-weight protein tyrosine phosphatase (LMW-PTP). Here, we report our extensive structure-based design and optimization effort that afforded inhibitors with vastly improved potency and specificity. The leading compound inhibits LMW-PTP potently and selectively (

Indexed as

Enzyme InhibitorsProtein Tyrosine PhosphatasesAnimalsCatalytic DomainMiceMolecular WeightEnzyme InhibitorsProtein Tyrosine Phosphatases

Identifiers

PMID36197449
PMCPMC10128051
OpenAlexW4302007875

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.