Evidence map›Paper›PMID 38147214›Full record

ArticleMethods in molecular biology (Clifton, N.J.)2024

System-Level Analysis of the Effects of RPTPs on Cellular Signaling Networks.

Jacqueline Gerritsen, Sophie Rizzo, Damien Thévenin, Forest M White

Open access · greenAbstract read
PubMed Full text at PMC Publisher
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. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing papers in PubMed
–field-weighted citation impact, top 46% 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

0 citing papers in PubMed, 0 citations in OpenAlex.

No citing paper in PubMed yet.

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

4 authors at 2 institutions in 1 country.

Jacqueline GerritsenDepartment of Biological Engineering, Massachusetts Institute of Technology, Cambridge, MA, USA.
Sophie RizzoDepartment of Chemistry, Lehigh University, Bethlehem, PA, USA.
Damien ThéveninDepartment of Chemistry, Lehigh University, Bethlehem, PA, USA.
Forest M WhiteDepartment of Biological Engineering, Massachusetts Institute of Technology, Cambridge, MA, USA. fwhite@mit.edu.
Lehigh University · USMassachusetts Institute of Technology · US

Funding

Identification of adaptive response mechanisms in breast cancer by information theory and proteomicsU01CA238720 · NCI · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI KRAVCHENKO-BALASHA, NATALY, WHITE, FOREST M · 2019 to 2023
$2.0M
Promoting Receptor Protein Tyrosine Phosphatase Activity by TargetingTransmembrane Domain InteractionsR01GM139998 · NIGMS · LEHIGH UNIVERSITY · PI LAZZARA, MATTHEW J, THEVENIN, DAMIEN · 2020 to 2023
$1.7M
NCI NIH HHS U01 CA238720NIGMS NIH HHS R01 GM139998
6 · The paper itself

Abstract

Tyrosine phosphorylation regulates signaling network activity downstream of receptor tyrosine kinase (RTK) activation. Receptor protein tyrosine phosphatases (RPTPs) serve to dephosphorylate RTKs and their proximal adaptor proteins, thus serving to modulate RTK activity. While the general function of RPTPs is well understood, the direct and indirect substrates for each RPTP are poorly characterized. Here we describe a method, quantitative phosphotyrosine phosphoproteomics, that enables the identification of specific phosphorylation sites whose phosphorylation levels are altered by the expression and activity of a given RPTP. In a proof-of-concept application, we use this method to highlight several direct or indirect substrate phosphorylation sites for PTPRJ, also known as DEP1, and show their quantitative phosphorylation in the context of wild-type PTPRJ compared to a mutant form of PTPRJ with increased activity, in EGF-stimulated cells. This method is generally applicable to define the signaling network effects of each RPTP in cells or tissues under different physiological conditions.

Indexed as

Protein Tyrosine PhosphatasesSignal TransductionAdaptor Proteins, Signal TransducingPhosphorylationProtein Processing, Post-TranslationalAdaptor Proteins, Signal TransducingProtein Tyrosine PhosphatasesPhosphatase activitySignaling networksTyrosine phosphorylation

Identifiers

PMID38147214
PMCPMC10787581
OpenAlexW4390232135

What OpenQuestion 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 OpenQuestion graph.