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dc.contributor.authorMarg, Susanna
dc.contributor.authorWinkler, Ulrike
dc.contributor.authorSestu, Marcello
dc.contributor.authorHimmel, Mirko
dc.contributor.authorSchönherr, Madeleine
dc.contributor.authorBär, Janina
dc.contributor.authorMann, Amrit
dc.contributor.authorMoser, Markus
dc.contributor.authorMierke, Claudia T
dc.contributor.authorRottner, Klemens
dc.contributor.authorBlessing, Manfred
dc.contributor.authorHirrlinger, Johannes
dc.contributor.authorZiegler, Wolfgang H
dc.date.accessioned2011-02-03T10:37:55Z
dc.date.available2011-02-03T10:37:55Z
dc.date.issued2010
dc.identifier.citationThe vinculin-DeltaIn20/21 mouse: characteristics of a constitutive, actin-binding deficient splice variant of vinculin. 2010, 5 (7):e11530 PLoS ONEen
dc.identifier.issn1932-6203
dc.identifier.pmid20644727
dc.identifier.doi10.1371/journal.pone.0011530
dc.identifier.urihttp://hdl.handle.net/10033/121048
dc.description.abstractThe cytoskeletal adaptor protein vinculin plays a fundamental role in cell contact regulation and affects central aspects of cell motility, which are essential to both embryonal development and tissue homeostasis. Functional regulation of this evolutionarily conserved and ubiquitously expressed protein is dominated by a high-affinity, autoinhibitory head-to-tail interaction that spatially restricts ligand interactions to cell adhesion sites and, furthermore, limits the residency time of vinculin at these sites. To date, no mutants of the vinculin protein have been characterized in animal models.
dc.language.isoenen
dc.subject.meshActinsen
dc.subject.meshAnimalsen
dc.subject.meshCells, Cultureden
dc.subject.meshEmbryo, Mammalianen
dc.subject.meshFibroblastsen
dc.subject.meshImmunoblottingen
dc.subject.meshMiceen
dc.subject.meshProtein Bindingen
dc.subject.meshProtein Isoformsen
dc.subject.meshReverse Transcriptase Polymerase Chain Reactionen
dc.subject.meshVinculinen
dc.titleThe vinculin-DeltaIn20/21 mouse: characteristics of a constitutive, actin-binding deficient splice variant of vinculin.en
dc.typeArticleen
dc.contributor.departmentFaculty of Medicine, Interdisciplinary Centre for Clinical Research (IZKF) Leipzig, University of Leipzig, Leipzig, Germany.en
dc.identifier.journalPloS oneen
refterms.dateFOA2018-06-13T01:11:43Z
html.description.abstractThe cytoskeletal adaptor protein vinculin plays a fundamental role in cell contact regulation and affects central aspects of cell motility, which are essential to both embryonal development and tissue homeostasis. Functional regulation of this evolutionarily conserved and ubiquitously expressed protein is dominated by a high-affinity, autoinhibitory head-to-tail interaction that spatially restricts ligand interactions to cell adhesion sites and, furthermore, limits the residency time of vinculin at these sites. To date, no mutants of the vinculin protein have been characterized in animal models.


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