The DOI matches its Crossref record; 35 of the 35 references it cites were found in a registry or an index.
Integrin-linked kinase (ILK) and its interactors
Open accessAbstract
How intracellular cytoskeletal and signaling proteins connect and communicate with the extracellular matrix (ECM) is a fundamental question in cell biology. Recent biochemical, cell biological, and genetic studies have revealed important roles of cytoplasmic integrin-linked kinase (ILK) and its interactive proteins in these processes. Cell adhesion to ECM is an important process that controls cell shape change, migration, proliferation, survival, and differentiation. Upon adhesion to ECM, integrins and a selective group of cytoskeletal and signaling proteins are recruited to cell matrix contact sites where they link the actin cytoskeleton to the ECM and mediate signal transduction between the intracellular and extracellular compartments. In this review, we discuss the molecular activities and cellular functions of ILK, a protein that is emerging as a key component of the cell–ECM adhesion structures.
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Self-citationRegulation of Protein Kinase B/Akt-Serine 473 Phosphorylation by Integrin-linked Kinase
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Self-citationMolecular diversity of cell-matrix adhesions
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Self-citationCa2+-independent Smooth Muscle Contraction
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Mechanisms of Vascular Smooth Muscle Cell Migration
Gerthoffer, W. T. (2007) · Circulation Research · doi:10.1161/01.res.0000258492.96097.47 · Cited by 455
Clinging to life: cell to matrix adhesion and cell survival
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Self-citationSignalling via integrins: Implications for cell survival and anticancer strategies
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Metadata
- Authors
- Wu, C., & Dedhar, S.
- Venue
- The Journal of Cell Biology
- Publisher
- Rockefeller University Press
- Published
- 2001-11-05
- Volume
- 155
- Issue
- 4
- Pages
- 505-510
- ISSN
- 0021-9525 (ISSN-L)
- 1540-8140
- OpenAlex
- W2122835088
- Cited by
- 447
- References
- 35
- FWCI
- 11.45
- Type
- journal article
- Language
- en
- Open access
- bronze
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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