Integrin-mediated Cell Adhesion to Type I Collagen Fibrils*
- J. Jokinen, Elina Dadu, J. Heino
- Biology, ChemistryJournal of Biological Chemistry
- 23 July 2004
It is suggested that α2β1 integrin is a functional cellular receptor for type I collagen fibrils, whereas α1β1 Integrin may only effectively bind type I gelatin monomers.
Selective binding of collagen subtypes by integrin alpha 1I, alpha 2I, and alpha 10I domains.
- M. Tulla, O. Pentikäinen, J. Heino
- Biology, Computer ScienceJournal of Biological Chemistry
- 2001
All three collagen receptors appear to differ in their ability to recognize distinct collagen subtypes, and the relatively small structural differences on their collagen binding surfaces may explain the functional specifics.
Structural and Functional Analysis of Integrin α2I Domain Interaction with Echovirus 1*
- L. Xing, M. Huhtala, R. Cheng
- BiologyJournal of Biological Chemistry
- 19 March 2004
Virus attachment to α2β1 integrin on the cell surface was found to result in integrin clustering, which can give rise to signaling and facilitate the initiation of the viral entry process that takes place via caveolae-mediated endocytosis.
Evolution of collagen-based adhesion systems.
- J. Heino, M. Huhtala, J. Käpylä, Mark S. Johnson
- BiologyInternational Journal of Biochemistry and Cell…
- 1 February 2009
Molecular mechanism of α2β1 integrin interaction with human echovirus 1
- J. Jokinen, Daniel J White, J. Heino
- Biology, ChemistryEMBO Journal
- 6 January 2010
Human echovirus 1 seems to rely on the activation of signalling pathways that are dependent on α2β1 clustering, but do not require the conformational regulation of the receptor, which is supported by the fact that the integrin clustering by EV1 did not activate the p38 MAP kinase pathway.
Structure of Collagen Receptor Integrin α1I Domain Carrying the Activating Mutation E317A*
- Matti Lahti, Eva Bligt, T. Salminen
- Biology, ChemistryJournal of Biological Chemistry
- 26 October 2011
The activated α1I domain represents a novel conformation of the αI domain, mimicking the structural state where the Arg287-Glu317 ion pair has just broken during the integrin activation.
Selective Binding of Collagen Subtypes by Integrin α1I, α2I, and α10I Domains*
- M. Tulla, O. Pentikäinen, J. Heino
- Biology, ChemistryJournal of Biological Chemistry
- 21 December 2001
All three collagen receptors appear to differ in their ability to recognize distinct collagen subtypes, and the relatively small structural differences on their collagen binding surfaces may explain the functional specifics.
Structure and function analysis of Escherichia coli inorganic pyrophosphatase: is a hydroxide ion the key to catalysis?
- T. Salminen, J. Käpylä, R. Lahti
- BiologyBiochemistry
- 24 January 1995
Results suggest that the most likely candidate for the essential basic group affected by all mutations in the active site is a hydroxide ion stabilized by coordination to the essential Mg2+ ions.
A Peptide Inhibiting the Collagen Binding Function of Integrin α2I Domain*
- J. Ivaska, J. Käpylä, J. Heino
- Biology, ChemistryJournal of Biological Chemistry
- 5 February 1999
Synthetic peptides representing hydrophilic and charged sequences of jararhagin, including the RSECD sequence replacing the well known RGD motif in the disintegrin-like domain, were synthesized and a basic peptide from the metalloproteinase domain proved to be functional.
Cellular receptors of extracellular matrix molecules.
- J. Heino, J. Käpylä
- BiologyCurrent pharmaceutical design
- 31 March 2009
The largest family of receptors, which mediates cell adhesion to fibronectin, laminins and collagens is called the integrins and their role in human diseases, including cancer and inflammation is described.
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