High-Throughput Discovery and Characterization of Covalent Inhibitors for Protein Tyrosine Phosphatases.

Zihan Qu, Aaron D Krabill, Zhong-Yin Zhang

Abstract read

In one paragraph

Article in Methods in molecular biology (Clifton, N.J.), 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it

0cells of the map it votes in

1citing papers in PubMed

–field-weighted citation impact

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

1 citing paper in PubMed.

False Friends in Fluorescence - Simple HPLC Evaluation of False Positive Fragment Hits in a DiFMUP Assay for Protein Tyrosine Phosphatase 1B.Drug design, development and therapy · 2026
Article

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

3 authors.

Zihan QuDepartment of Chemistry, Purdue University, West Lafayette, IN, USA.

Aaron D KrabillDepartment of Medicinal Chemistry and Molecular Pharmacology, Purdue University, West Lafayette, IN, USA.

Zhong-Yin ZhangDepartment of Chemistry, Purdue University, West Lafayette, IN, USA. zhang-zy@purdue.edu.

Funding

Structural Biology CoreU54AG065181 · NIA · INDIANA UNIVERSITY INDIANAPOLIS · PI Timothy I Richardson · 2019 to 2026

$61.3M

Structure/Function of Protein Tyrosine PhosphatasesR01CA069202 · NCI · YESHIVA UNIVERSITY · PI Zhong-Yin Zhang · 1996 to 2026

$7.3M

NCI NIH HHS R01 CA069202NIA NIH HHS U54 AG065181

6 · The paper itself

Abstract

Covalent inhibition has gained increasing interest in targeting the undruggable protein tyrosine phosphatases (PTPs). However, a systematic method for discovering and characterizing covalent PTP inhibitors has yet to be established. Here, we describe a workflow involving high-throughput screening of covalent fragment libraries and a novel biochemical assay that enables the acquisition of kinetics parameters of PTP inhibition by covalent inhibitors with higher throughput.

Indexed as

Biological AssayHigh-Throughput Screening AssaysKineticsPhysicsProtein Tyrosine PhosphatasesProtein Tyrosine PhosphatasesCovalent inhibitionHigh-throughput screeningKinetics of covalent inhibitionpNPP assayProtein tyrosine phosphatase

Identifiers

PMID38147223

DOI10.1007/978-1-0716-3569-8_19

PMCPMC12962263

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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.