Evidence map›Paper›PMID 38540680›Full record

ReviewBiomolecules2024

The Configuration of GRB2 in Protein Interaction and Signal Transduction.

Dingyi Wang, Guoxia Liu, Yuxin Meng, Hongjie Chen, Zu Ye, Ji Jing

Open access · goldAbstract readReview
In one paragraph

Review in Biomolecules, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
8.2field-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

26 citing papers in PubMed, 35 citations in OpenAlex.

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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

6 authors at 4 institutions in 1 country.

Dingyi WangCollege of Pharmaceutical Science, Zhejiang University of Technology, Hangzhou 310014, China.
Guoxia LiuHangzhou Institute of Medicine, Chinese Academy of Sciences, Zhejiang Cancer Hospital, Hangzhou 310022, China.
Yuxin MengCollege of Pharmaceutical Science, Zhejiang University of Technology, Hangzhou 310014, China.
Hongjie ChenCollege of Pharmaceutical Science, Zhejiang University of Technology, Hangzhou 310014, China.
Zu YeHangzhou Institute of Medicine, Chinese Academy of Sciences, Zhejiang Cancer Hospital, Hangzhou 310022, China.
Ji JingHangzhou Institute of Medicine, Chinese Academy of Sciences, Zhejiang Cancer Hospital, Hangzhou 310022, China.
Zhejiang Cancer Hospital · CNChinese Academy of Sciences · CNTianjin University · CNZhejiang University of Technology · CN

Funding

Key Laboratory of Prevention, Diagnosis and Therapy of Upper Gastrointestinal Cancer of Zhejiang Province 2022E10021National Natural Science Foundation of China 32271485National R&D Program of China 2023YFC3403400Natural Science Foundation of Zhejiang Province YXD23H0302Natural Science Foundation of Zhejiang Province of China LTGY23H160018Zhejiang Medical and Health Science and Technology Program 2024KY789
6 · The paper itself

Abstract

Growth-factor-receptor-binding protein 2 (GRB2) is a non-enzymatic adaptor protein that plays a pivotal role in precisely regulated signaling cascades from cell surface receptors to cellular responses, including signaling transduction and gene expression. GRB2 binds to numerous target molecules, thereby modulating a complex cell signaling network with diverse functions. The structural characteristics of GRB2 are essential for its functionality, as its multiple domains and interaction mechanisms underpin its role in cellular biology. The typical signaling pathway involving GRB2 is initiated by the ligand stimulation to its receptor tyrosine kinases (RTKs). The activation of RTKs leads to the recruitment of GRB2 through its SH2 domain to the phosphorylated tyrosine residues on the receptor. GRB2, in turn, binds to the Son of Sevenless (SOS) protein through its SH3 domain. This binding facilitates the activation of Ras, a small GTPase, which triggers a cascade of downstream signaling events, ultimately leading to cell proliferation, survival, and differentiation. Further research and exploration into the structure and function of GRB2 hold great potential for providing novel insights and strategies to enhance medical approaches for related diseases. In this review, we provide an outline of the proteins that engage with domains of GRB2, along with the function of different GRB2 domains in governing cellular signaling pathways. This furnishes essential points of current studies for the forthcoming advancement of therapeutic medications aimed at GRB2.

Indexed as

Receptor Protein-Tyrosine KinasesSignal TransductionGRB2 Adaptor ProteinPhosphorylationProtein BindingReceptors, Cell SurfaceSon of Sevenless ProteinsTyrosineGRB2 Adaptor ProteinReceptor Protein-Tyrosine KinasesReceptors, Cell SurfaceSon of Sevenless ProteinsTyrosineGRB2SH2 domainSH3 domainsignal transduction

Identifiers

PMID38540680
PMCPMC10968029
OpenAlexW4392050246

What Socratic holds

Textmetadata
LicenceCC BY
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.