VCL

(redirected from Vinculin)
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AcronymDefinition
VCLVisual Component Library
VCLVioloncello (Cello)
VCLVideo Coding Layer (digital television)
VCLVinculin
VCLVegetation Canopy LIDAR
VCLCurvilinear Velocity
VCLVirus Creation Laboratory
VCLVirtual Channel Link
VCLVixen Controlled Library (Art; Furry Art Website)
VCLVixen Controlled Library (anthro art site)
VCLVrijzinnig-Christelijk Lyceum (Den Haag)
VCLVirtual Computer Library (University of Texas at Austin)
VCLVisual Control Library
VCLVertical-Cavity Laser
VCLVoluntary Committee of Lawyers
VCLVirtual Circuit Link
VCLVoluntary Compliance Level
VCLViscoelastic Control Layer
VCLVice Chairman for Liaison
VCLValidated Compilers List
VCLVector Control Language (ICT In-Circuit Test)
VCLVoluntary Collective License/Licensing
VCLVirtual Coding Layer
VCLVariant Configuration Language (Extensible Markup Language)
VCLVertical Control Line
VCLVisual Communication Lab
References in periodicals archive ?
Furthermore, gin-senoside Rd induced focal adhesion formation and modulating vinculin localization and expression.
Western blot analysis showed that treatment with ginseno-side Rd for 1 or 12 h induced vinculin expression in the presence and absence of PMA (Fig.
Although emerging as a conceivable VPA target from a mechanistic point of view, vinculin might be less straightforward to exploit as a biomarker of VPA effects given the weak response in our cell model (Figure 3).
Vinculin knockout results in heart and brain defects during embryonic development.
For Vinculin, indirect immunofluorescent staining was employed using primary antibody of mouse anti vinculin and secondary antibody of FITC conjugated rabbit anti mouse immunoglobulin.
Vinculin staining of cells seeded on coverslip showed diffused cytoplasmic distribution with circumfrential labeling at the borders of the cells (Fig5a&b).
Recently, N-WASP was shown to be required for Shigella motility (62); like vinculin, it can bind IcsA directly.
Intercellular spread of Shigella flexneri through a monolayer mediated by membranous protrusions and associated with reorganization of the cytoskeletal protein vinculin.
This was not a general decrease in total cellular protein levels or discrepancy between the samples because vinculin levels were virtually unchanged in these samples (Figure 6).
This triggers vinculin to partly unravel as well, freeing several molecular "fingers" that assume a shape that allows alpha- actinin to bind to its partner.
Strong vinculin immunoreactivity was observed in the circular and longitudinal smooth muscle layer of the normal and ganglionic bowel specimens (Figure 3, A).
The newly recognized way that this protein can change its shape is important because slight changes in the shape of vinculin completely change its role in the cell, making the protein a versatile tool for completing different tasks, according to the researchers.