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Human Vimentin Protein expressed in Wheat germ - ABIN1325010
Kim, Nakamura, Lee, Hong, Pérez-Sala, McCulloch: Regulation of cell adhesion to collagen via beta1 integrins is dependent on interactions of filamin A with vimentin and protein kinase C epsilon. in Experimental cell research 2010
Vimentin and its interaction with Shigella flexneri IpaC are dispensable for effector translocation pore formation, but are required for stable docking of Shigella flexneri to cells; moreover, stable docking triggers effector secretion.
the elongation reaction of vimentin in solution and in situ by time-resolved static and dynamic light scattering, is reported.
Vimentin induced by exosomes is necessary for lung cancer to induce mesenchymal transition (EMT (show ITK Proteins)) in recipient bronchial epithelial cells (HBECs).
our results demonstrate that vimentin silencing in ovarian cancer cells upregulates proteins of the exocytotic process to decrease cellular cisplatin accumulation
The combined biomarkers E-cadherin (show CDH1 Proteins), membranous epidermal growth factor receptor (EGFR (show EGFR Proteins)) and vimentin show a stronger prognostic value for and disease-free survival than any of the single biomarkers.
AHR (show AHR Proteins) protein-vimentin protein complex is formed in the cytoplasm resulting in proteasome degradation of vimentin.
TRIM56 (show TRIM56 Proteins) is the ubiquitin ligase that is degrading vimentin in ovarian cancer cells, regulation cell migration and neoplasm invasiveness.
TIS21 (show BTG2 Proteins) attenuated Doxorubicin-induced cancer cell senescence by inhibiting linear actin nucleation via Nox4 (show NOX4 Proteins)-ROS (show ROS1 Proteins)-ABI2-DRF (show MPO Proteins) signal cascade
this study indicates that OPN (show SPP1 Proteins) can induce epithelial-mesenchymal transition of hepatocellular carcinoma cells through increasing vimentin stability
The findings support a mechanism in which miR (show MLXIP Proteins)-375 suppresses RUNX1 (show RUNX1 Proteins) levels, resulting in reduced vimentin and L-plastin (show LCP1 Proteins) expression. Knockdown of RUNX1 (show RUNX1 Proteins), L-plastin (show LCP1 Proteins), and vimentin resulted in significant reductions in cell invasion in vitro, indicating the functional significance of miR (show MLXIP Proteins)-375 regulation of specific proteins involved in head and neck squamous cell carcinoma (HNSCC) invasion.
Results indicate that vimentin orchestrates the healing by controlling fibroblast proliferation, TGF-beta1 (show TGFB1 Proteins)-Slug signaling, and epithelial-mesenchymal transition (EMT (show ITK Proteins)) processing, and all of which in turn govern the required keratinocyte activation.
Protein phosphatase 1 (show PPP1CB Proteins) is a key protein serine/threonine phosphatase that controls vimentin Ser (show SIGLEC1 Proteins)-56 dephosphorylation in smooth muscle.
These findings identify vimentin as a positive regulator of stemness in the developing mouse mammary gland and in breast cancer cells.
This study is the first to show that vimentin has an important role in tumor metastasis in vivo in the setting of pre-diabetes and endogenous hyperinsulinemia.
These findings identify two specific sites on vimentin that are phosphorylated by Cadmium.
both arthritis-susceptible and -resistant mice can generate cellular and humoral immunity to Vim.
vimentin knockout neurons were insensitive to the axonotrophic effects of Clostridium botulinum C3 exoenzyme
These findings suggest that Plk1 regulates smooth muscle contraction by modulating vimentin phosphorylation at Ser (show SIGLEC1 Proteins)-56.
findings thus show that the inability to produce GFAP (show GFAP Proteins) and Vim affects normal retinal physiology and that the effect of IF deficiency on retinal cell survival differs, depending on the underlying pathologic condition
these findings identify a hereto-unappreciated role for serine-38 phosphorylated vimentin as an important determinant of myofibroblast sensitivity to Withaferin A.
Knockdown of filamin A (show FLNA Proteins) or vimentin in normal cells profoundly suppresses apical extrusion of the neighbouring transformed cells.
Immunocytochemistry for Vimentin detection in nuclei of IVF (show SCN5A Proteins) and NT bovine embryos
These results indicate that the inner mass differentiates dynamically in blastocysts, as reflected by the expression of vimentin; higher vimentin expression may reflect the higher developmental competence of embryos.
an intact vimentin intermediate filament network contributes to the maintenance of the chondrocyte phenotype
Vimentin- like transcript was expressed in both chordocytes and chordoblasts, whereas the elastin (show ELN Proteins)- like transcript was uniquely expressed in the chordoblasts lining the notochordal sheath.
This study evaluated the expression pattern of vimentin in testes of mature Arabian stallions and correlated its distribution with grade of seminiferous tubule impairment as indicated by a Johnsen score.
As the inner cell mass forms the epiblast, SSEA1 (show FUT4 Proteins) is lost and VIMENTIN is lost and re-expressed.
These observations indicate that vimentin serves as a putative receptor for Japanese encephalitis virus in porcine kidney cells.
Interaction of nucleocapsid protein of transmissible gastroenteritis virus with host vimentin is required for virus infection.
protein(s) that associated with RPTPbeta in response to IGF-I and IGFBP-2 in vascular smooth muscle cells
This study demonstrates that maternal VIM, as a genomic protector, is crucial for nuclear reprogramming in porcine cloned embryos.
Vim expression in corneal epithelium is found in a cell population composed of highly motile cells.
This gene encodes a member of the intermediate filament family. Intermediate filamentents, along with microtubules and actin microfilaments, make up the cytoskeleton. The protein encoded by this gene is responsible for maintaining cell shape, integrity of the cytoplasm, and stabilizing cytoskeletal interactions. It is also involved in the immune response, and controls the transport of low-density lipoprotein (LDL)-derived cholesterol from a lysosome to the site of esterification. It functions as an organizer of a number of critical proteins involved in attachment, migration, and cell signaling. Mutations in this gene causes a dominant, pulverulent cataract.
, vimentin 1
, class-III intermediate microfilament