ReviewInternational journal of molecular medicine2022
Talin‑1 interaction network in cellular mechanotransduction (Review).
Review in International journal of molecular medicine, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.
What it found
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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.
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.
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Who cites it
32 citing papers in PubMed, 47 citations in OpenAlex.
- Systematic Analysis of MRTFB Phosphoproteomic Datasets Reveals Co-Regulated Kinase Networks and Co-Occurring Phosphosites Associated with the Actin Cytoskeleton Pathway.Current issues in molecular biology · 2026Article
- Role of Mechanotransduction in Cancer: A Complex Problem Involving Gene Mutations and Altered Levels of Connection Components.Biomolecules · 2026Review
- Integrative Proteomics and Phosphoproteomics Profiling of Chronic Enteropathy Associated withBiomedicines · 2026Article
- Conformational flexibility of talin enables force-free sampling of activation-competent states.Communications chemistry · 2026Article
- Reconstituted nascent adhesion condensates drive actin polymerization on supported lipid bilayers.Science advances · 2026Article
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- Clusterin Promotes the Migration and Invasion of Highly Aggressive Breast Cancer Cells Through Molecular Mechanisms That Affect the Cell Cytoskeleton and Extracellular Matrix Dynamics.International journal of molecular sciences · 2026Article
- An Opto-Actuated Hydrogel for Cell Mechanoactuation and Real-Time Force Monitoring.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Article
- Integrating Mechanical Loading, Mechanotransduction, and Biological Responses in Musculoskeletal Tissues Across the Lifespan: Regulation Influenced by Cells, Extracellular Matrix, and Sex.Results and problems in cell differentiation · 2026Review
- Talin1 Mediates Tumor-Nerve Interactions in Prostate and Breast Cancer Cells.Journal of Cancer · 2026Article
- DIA-based serum proteomics of the complement-coagulation cascade identifies candidate biomarkers for myasthenia gravis.Frontiers in neuroscience · 2026Article
- Peptidomics analysis of serum in patients suffered from generalized anxiety disorder.Scientific reports · 2025Article
- Molecular flexibility of hyaluronic acid has a profound effect on invasion of cancer cells.Royal Society open science · 2025Article
- Monensin suppresses EMT-driven cancer cell motility by inducing Golgi pH-dependent exocytosis of GOLIM4.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Phosphoinositide signalling in cell motility and adhesion.Nature cell biology · 2025Review
- Focal adhesion in the tumour metastasis: from molecular mechanisms to therapeutic targets.Biomarker research · 2025Review
- ECM-dependent regulation of septin 7 in focal adhesions promotes mechanosensing and functional response in fibroblasts.iScience · 2024Article
- Physiological Responses to Acute Heat Stress in Rohu, Labeo rohita: Insights from Liver Proteomics.Marine biotechnology (New York, N.Y.) · 2024Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The mechanical signals within the extracellular matrix (ECM) regulate cell growth, proliferation and differentiation, and integrins function as the hub between the ECM and cellular actin. Focal adhesions (FAs) are multi‑protein, integrin‑containing complexes, acting as tension‑sensing anchoring points that bond cells to the extracellular microenvironment. Talin‑1 serves as the central protein of FAs that participates in the activation of integrins and connects them with the actin cytoskeleton. As a cytoplasmic protein, Talin‑1 consists of a globular head domain and a long rod comprised of a series of α‑helical bundles. The unique structure of the Talin‑1 rod domain permits folding and unfolding in response to the mechanical stress, revealing various binding sites. Thus, conformation changes of the Talin‑1 rod domain enable the cell to convert mechanical signals into chemical through multiple signaling pathways. The present review discusses the binding partners of Talin‑1, their interactions, effects on the cellular processes, and their possible roles in diseases.
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Registered trials
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.