Evidence map›Paper›PMID 37673461›Full record

ArticleGenes & development2023

Advancing therapeutics using antibody-induced dimerization of receptor tyrosine phosphatases.

Michel L Tremblay

Open access · diamondAbstract readComment
In one paragraph

Article in Genes & development, 2023. 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, 2 citations in OpenAlex.

  1. Review
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

1 author at 1 institution in 1 country.

Michel L TremblayDepartment of Biochemistry, Goodman Cancer Institute, Faculty of Medicine, McGill University, Montreal, Quebec H3A1A3, Canada michel.tremblay@mcgill.ca.
McGill University · CA

Funding

CIHR FDN-159923
6 · The paper itself

Abstract

Receptor protein tyrosine phosphatases (RPTPs) are involved in a broad list of cellular, developmental, and physiological functions. Altering their expression leads to significant changes in protein phosphorylation linked to a growing list of human diseases, including cancers and neurological disorders. In this issue of

Indexed as

ImmunoglobulinsProtein Tyrosine PhosphatasesCell DifferentiationDimerizationHumansTyrosineImmunoglobulinsProtein Tyrosine PhosphatasesTyrosinebivalent antibodydimerizationprotein tyrosine phosphorylationPTPRDreceptor protein tyrosine phosphataseSRC

Identifiers

PMID37673461
PMCPMC10546972
OpenAlexW4386475323

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.