ReviewBiochemistry and biophysics reports2024
GRB2: A dynamic adaptor protein orchestrating cellular signaling in health and disease.
Review in Biochemistry and biophysics reports, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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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.
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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.
Who cites it
14 citing papers in PubMed.
- Amino acid balancing and microalgal proteins (Spirulina) improve production performance and milk quality in dairy cows under low-protein diets.NPJ science of food · 2026Article
- Efficacy of Disitamab Vedotin in Treating HER2 2+/FISH-Bladder Cancer: A Case Report.Clinical case reports · 2026Article
- Establishment and characterization of NKMS-1, a novel mouse NK cell line.Scientific reports · 2026Article
- Jinshui Chenfei formula alleviates SiOChinese medicine · 2026Article
- Exploring the Anti-Cervical Cancer Effect and Hepatotoxicity Risk of Gossypol Based on Untargeted Metabolomics and Network Toxicology.Pharmaceuticals (Basel, Switzerland) · 2026Article
- Robust SH2 binding affinity indicates minimal SH3-to-SH2 communication in Grb2.Biology direct · 2026Article
- Adaptor proteins regulating tumor-associated macrophage polarization during cancer progression.Oncoscience · 2026Review
- Unravelling chemotherapeutic activity of fisetin ruthenium-p-cymene complex in lung cancer treatment by the modulation of GRB2/RAS/MEK/DNMT1 signaling pathway.Naunyn-Schmiedeberg's archives of pharmacology · 2025Article
- Under ONIOM Layers: Analysis of BCR-ABL Enzyme Inhibitors Through Bond-Critical Points and Natural Orbitals.Molecules (Basel, Switzerland) · 2025Article
- Targeting Kinase Suppressor of Ras 1 (KSR1) for Cancer Therapy.Pharmaceutics · 2025Review
- Allosteric modulation of Grb2 drives ligand-dependent signal responses.Biology direct · 2025Article
- Relation between Common Carotid Intima-Media Thickness and Molecular Markers in Patients with Newly Diagnosed versus Established Diabetes Mellitus: A Retrospective Study.Medical journal of the Islamic Republic of Iran · 2025Article
- Exploring chamazulene as a novel therapeutic agent for breast cancerFrontiers in pharmacology · 2025Article
- RNA Editing Signatures Powered by Artificial Intelligence: A New Frontier in Differentiating Schizophrenia, Bipolar, and Schizoaffective Disorders.International journal of molecular sciences · 2024Article
Corrections and comments
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Authors and funding
5 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
GRB2, or Growth Factor Receptor-Bound Protein 2, is a pivotal adaptor protein in intracellular signal transduction pathways, particularly within receptor tyrosine kinase (RTK) signaling cascades. Its crystal structure reveals a modular architecture comprising a single Src homology 2 (SH2) domain flanked by two Src homology 3 (SH3) domains, facilitating dynamic interactions critical for cellular signaling. While SH2 domains recognize phosphorylated tyrosines, SH3 domains bind proline-rich sequences, enabling GRB2 to engage with various downstream effectors. Folding and binding studies of GRB2 in its full-length form and isolated domains highlight a complex interplay between its protein-protein interaction domains on the folding energy landscape and in driving its function. Being at the crosslink of many key molecular pathways in the cell, GRB2 possesses a role in cancer pathogenesis, particularly in mediating the Ras-mitogen activated protein kinase (MAPK) pathway. Thus, pharmacological targeting of GRB2 domains is a promising field in cancer therapy, with efforts focused on disrupting protein-protein interactions. However, the dynamic interplay driving GRB2 function suggests the presence of allosteric sites at the interface between domains that could be targeted to modulate the binding properties of its constituent domains. We propose that the analysis of GRB2 proteins from other species may provide additional insights to make the allosteric pharmacological targeting of GRB2 a more feasible strategy.
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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.