The world's first wiki where authorship really matters (Nature Genetics, 2008). Due credit and reputation for authors. Imagine a global collaborative knowledge base for original thoughts. Search thousands of articles and collaborate with scientists around the globe.

wikigene or wiki gene protein drug chemical gene disease author authorship tracking collaborative publishing evolutionary knowledge reputation system wiki2.0 global collaboration genes proteins drugs chemicals diseases compound
Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)



Gene Review

VIM  -  vimentin

Bos taurus

Welcome! If you are familiar with the subject of this article, you can contribute to this open access knowledge base by deleting incorrect information, restructuring or completely rewriting any text. Read more.

Disease relevance of VIM


High impact information on VIM


Biological context of VIM


Anatomical context of VIM


Associations of VIM with chemical compounds

  • These data, taken together with the observation that the NH2-terminal end of vimentin is implicated in the polymerization process (Traub, P., and C. Vorgias, J. Cell Sci., 1983, 63:43-67), imply that intermediate filaments may contact the membrane in an end-on fashion, using the exposed head domains of their terminal subunits [13].
  • Once associated with the lipid bilayer, the vimentin polypeptide resists urea treatment, suggesting that it has become an integral constituent associated with part of the membrane [15].
  • In the absence of MgCl2 we found a net permanent dipole moment, approximately 45-nm-long dimers for vimentin, approximately 65-nm-long tetramers, hexamers, and possibly octamers for both proteins, and 100-nm aggregates for glial fibrillary acidic protein [16].
  • These results indicate that the organization of the intermediate-size filament protein vimentin is markedly affected by cholesterol oxides [17].
  • The Triton-insoluble pellet fraction contained several major polypeptides (30-, 43-, 58-, and 240,000 mol-wt), two of which were identified by immunoblotting as cytoplasmic actin (43,000 mol-st) and vimentin (58,000 mol-wt) [18].

Other interactions of VIM


Analytical, diagnostic and therapeutic context of VIM


  1. Expression of cytokeratins and vimentin in normal and neoplastic tissue from the bovine female reproductive tract. Pérez-Martínez, C., García-Fernández, R.A., Escudero, A., Ferreras, M.C., García-Iglesias, M.J. J. Comp. Pathol. (2001) [Pubmed]
  2. Point mutation of neu oncogene in animal peripheral nerve sheath tumors. Stoica, G., Tasca, S.I., Kim, H.T. Vet. Pathol. (2001) [Pubmed]
  3. Expression of vimentin in the tubular epithelium of bovine kidneys with interstitial nephritis. Scanziani, E., Grieco, V., Salvi, S. Vet. Pathol. (1993) [Pubmed]
  4. Quantification of somatic and spermatogenic cell proliferation in the testes of ruminants, using a proliferation marker and flow cytometry analysis. Blottner, S., Roelants, H. Theriogenology (1998) [Pubmed]
  5. Integration of different keratins into the same filament system after microinjection of mRNA for epidermal keratins into kidney epithelial cells. Franke, W.W., Schmid, E., Mittnacht, S., Grund, C., Jorcano, J.L. Cell (1984) [Pubmed]
  6. De novo synthesis and specific assembly of keratin filaments in nonepithelial cells after microinjection of mRNA for epidermal keratin. Kreis, T.E., Geiger, B., Schmid, E., Jorcano, J.L., Franke, W.W. Cell (1983) [Pubmed]
  7. Phosphorylation of intermediate filament proteins by cAMP-dependent protein kinases. O'Connor, C.M., Gard, D.L., Lazarides, E. Cell (1981) [Pubmed]
  8. Mitosis-specific phosphorylation of vimentin by protein kinase C coupled with reorganization of intracellular membranes. Takai, Y., Ogawara, M., Tomono, Y., Moritoh, C., Imajoh-Ohmi, S., Tsutsumi, O., Taketani, Y., Inagaki, M. J. Cell Biol. (1996) [Pubmed]
  9. Nucleotide sequence of the bovine vimentin-encoding cDNA. Hess, J.F., Casselman, J.T., FitzGerald, P.G. Gene (1994) [Pubmed]
  10. Two distinct attachment sites for vimentin along the plasma membrane and the nuclear envelope in avian erythrocytes: a basis for a vectorial assembly of intermediate filaments. Georgatos, S.D., Blobel, G. J. Cell Biol. (1987) [Pubmed]
  11. Complete sequence of a bovine type I cytokeratin gene: conserved and variable intron positions in genes of polypeptides of the same cytokeratin subfamily. Rieger, M., Jorcano, J.L., Franke, W.W. EMBO J. (1985) [Pubmed]
  12. Differential control of cytokeratins and vimentin synthesis by cell-cell contact and cell spreading in cultured epithelial cells. Ben-Ze'ev, A. J. Cell Biol. (1984) [Pubmed]
  13. Site specificity in vimentin-membrane interactions: intermediate filament subunits associate with the plasma membrane via their head domains. Georgatos, S.D., Weaver, D.C., Marchesi, V.T. J. Cell Biol. (1985) [Pubmed]
  14. The binding of vimentin to human erythrocyte membranes: a model system for the study of intermediate filament-membrane interactions. Georgatos, S.D., Marchesi, V.T. J. Cell Biol. (1985) [Pubmed]
  15. Lenticular intermediate-sized filaments: biosynthesis and interaction with plasma membrane. Ramaekers, F.C., Dunia, I., Dodemont, H.J., Benedetti, E.L., Bloemendal, H. Proc. Natl. Acad. Sci. U.S.A. (1982) [Pubmed]
  16. Transient electric birefringence study of intermediate filament formation from vimentin and glial fibrillary acidic protein. Kooijman, M., Bloemendal, M., Traub, P., van Grondelle, R., van Amerongen, H. J. Biol. Chem. (1997) [Pubmed]
  17. Modifications of vimentin filament architecture and vimentin-nuclear interactions by cholesterol oxides in 73/73 endothelial cells. Palladini, G., Finardi, G., Bellomo, G. Exp. Cell Res. (1996) [Pubmed]
  18. Isolation of bovine aortic endothelial cell plasma membranes: identification of membrane-associated cytoskeletal proteins. Ketis, N.V., Hoover, R.L., Karnovsky, M.J. J. Cell. Physiol. (1986) [Pubmed]
  19. Chaperone activity of alpha-crystallins modulates intermediate filament assembly. Nicholl, I.D., Quinlan, R.A. EMBO J. (1994) [Pubmed]
  20. Proteomic analysis of a detergent-resistant membrane skeleton from neutrophil plasma membranes. Nebl, T., Pestonjamasp, K.N., Leszyk, J.D., Crowley, J.L., Oh, S.W., Luna, E.J. J. Biol. Chem. (2002) [Pubmed]
  21. Cultured microvascular endothelial cells (MVEC) differ in cytoskeleton, expression of cadherins and fibronectin matrix. A study under the influence of interferon-gamma. Fenyves, A.M., Behrens, J., Spanel-Borowski, K. J. Cell. Sci. (1993) [Pubmed]
  22. An epithelial cell line with elongated myoid morphology derived from bovine mammary gland. Expression of cytokeratins and desmosomal plaque proteins in unusual arrays. Schmid, E., Franke, W.W., Grund, C., Schiller, D.L., Kolb, H., Paweletz, N. Exp. Cell Res. (1983) [Pubmed]
  23. Sustained orbital shear stress stimulates smooth muscle cell proliferation via the extracellular signal-regulated protein kinase 1/2 pathway. Asada, H., Paszkowiak, J., Teso, D., Alvi, K., Thorisson, A., Frattini, J.C., Kudo, F.A., Sumpio, B.E., Dardik, A. J. Vasc. Surg. (2005) [Pubmed]
  24. Paracrine stimulation of polarized secretion from monolayers of a neoplastic prostatic epithelial cell line by prostatic stromal cell proteins. Djakiew, D., Tarkington, M.A., Lynch, J.H. Cancer Res. (1990) [Pubmed]
  25. Interference in vimentin assembly in vitro by synthetic peptides derived from the vimentin head domain. Hofmann, I., Herrmann, H. J. Cell. Sci. (1992) [Pubmed]
WikiGenes - Universities