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MeSH Review

Microfibrils

 
 
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Disease relevance of Microfibrils

 

Psychiatry related information on Microfibrils

 

High impact information on Microfibrils

  • Microfibrils, either associated with or devoid of elastin, give rise to a variety of extracellular networks in elastic and non-elastic tissues [7].
  • We propose a model for the arrangement of fibrillin monomers in microfibrils that reconciles structural and antibody binding data, and we describe a set of disease-causing mutations that provide the first clues to the specificity of cbEFG interactions [8].
  • Although elastic fibres are known to be composed of microfibril proteins (for example, fibrillins and latent transforming growth factor (TGF)-beta-binding proteins) and polymerized elastin, the mechanism of their assembly and development is not well understood [9].
  • Amyloid P component is located on elastic fibre microfibrils in normal human tissue [10].
  • Calcofluor white ST Alters the in vivo assembly of cellulose microfibrils [2].
 

Chemical compound and disease context of Microfibrils

 

Biological context of Microfibrils

 

Anatomical context of Microfibrils

 

Associations of Microfibrils with chemical compounds

 

Gene context of Microfibrils

 

Analytical, diagnostic and therapeutic context of Microfibrils

References

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  2. Calcofluor white ST Alters the in vivo assembly of cellulose microfibrils. Haigler, C.H., Brown, R.M., Benziman, M. Science (1980) [Pubmed]
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  10. Amyloid P component is located on elastic fibre microfibrils in normal human tissue. Breathnach, S.M., Melrose, S.M., Bhogal, B., de Beer, F.C., Dyck, R.F., Tennent, G., Black, M.M., Pepys, M.B. Nature (1981) [Pubmed]
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  12. A Danish kindred with familial amyloid cardiomyopathy revisited: identification of a mutant transthyretin-methionine111 variant in serum from patients and carriers. Ranløv, I., Alves, I.L., Ranløv, P.J., Husby, G., Costa, P.P., Saraiva, M.J. Am. J. Med. (1992) [Pubmed]
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  14. Fibrillary glomerulonephritis. Hsu, B.G., Chang, C.H., Chiang, S.S., Yang, A.H. Zhonghua Yi Xue Za Zhi (Taipei) (2001) [Pubmed]
  15. Mutation or drug-dependent microtubule disruption causes radial swelling without altering parallel cellulose microfibril deposition in Arabidopsis root cells. Sugimoto, K., Himmelspach, R., Williamson, R.E., Wasteneys, G.O. Plant Cell (2003) [Pubmed]
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  17. Missense mutations impair intracellular processing of fibrillin and microfibril assembly in Marfan syndrome. Aoyama, T., Tynan, K., Dietz, H.C., Francke, U., Furthmayr, H. Hum. Mol. Genet. (1993) [Pubmed]
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  19. Mutation of the gene encoding fibrillin-2 results in syndactyly in mice. Chaudhry, S.S., Gazzard, J., Baldock, C., Dixon, J., Rock, M.J., Skinner, G.C., Steel, K.P., Kielty, C.M., Dixon, M.J. Hum. Mol. Genet. (2001) [Pubmed]
  20. Partial sequence of a candidate gene for the Marfan syndrome. Maslen, C.L., Corson, G.M., Maddox, B.K., Glanville, R.W., Sakai, L.Y. Nature (1991) [Pubmed]
  21. Marfan syndrome and mitral valve prolapse. Weyman, A.E., Scherrer-Crosbie, M. J. Clin. Invest. (2004) [Pubmed]
  22. Fibrillin, a new 350-kD glycoprotein, is a component of extracellular microfibrils. Sakai, L.Y., Keene, D.R., Engvall, E. J. Cell Biol. (1986) [Pubmed]
  23. Versican is expressed in the proliferating zone in the epidermis and in association with the elastic network of the dermis. Zimmermann, D.R., Dours-Zimmermann, M.T., Schubert, M., Bruckner-Tuderman, L. J. Cell Biol. (1994) [Pubmed]
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  27. The supramolecular organization of fibrillin-rich microfibrils. Baldock, C., Koster, A.J., Ziese, U., Rock, M.J., Sherratt, M.J., Kadler, K.E., Shuttleworth, C.A., Kielty, C.M. J. Cell Biol. (2001) [Pubmed]
  28. COBRA, an Arabidopsis extracellular glycosyl-phosphatidyl inositol-anchored protein, specifically controls highly anisotropic expansion through its involvement in cellulose microfibril orientation. Roudier, F., Fernandez, A.G., Fujita, M., Himmelspach, R., Borner, G.H., Schindelman, G., Song, S., Baskin, T.I., Dupree, P., Wasteneys, G.O., Benfey, P.N. Plant Cell (2005) [Pubmed]
  29. Disruption of the gene encoding the latent transforming growth factor-beta binding protein 4 (LTBP-4) causes abnormal lung development, cardiomyopathy, and colorectal cancer. Sterner-Kock, A., Thorey, I.S., Koli, K., Wempe, F., Otte, J., Bangsow, T., Kuhlmeier, K., Kirchner, T., Jin, S., Keski-Oja, J., von Melchner, H. Genes Dev. (2002) [Pubmed]
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  33. An Arabidopsis endo-1,4-beta-D-glucanase involved in cellulose synthesis undergoes regulated intracellular cycling. Robert, S., Bichet, A., Grandjean, O., Kierzkowski, D., Satiat-Jeunemaître, B., Pelletier, S., Hauser, M.T., Höfte, H., Vernhettes, S. Plant Cell (2005) [Pubmed]
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  35. Bovine latent transforming growth factor beta 1-binding protein 2: molecular cloning, identification of tissue isoforms, and immunolocalization to elastin-associated microfibrils. Gibson, M.A., Hatzinikolas, G., Davis, E.C., Baker, E., Sutherland, G.R., Mecham, R.P. Mol. Cell. Biol. (1995) [Pubmed]
  36. An elastin gene mutation producing abnormal tropoelastin and abnormal elastic fibres in a patient with autosomal dominant cutis laxa. Tassabehji, M., Metcalfe, K., Hurst, J., Ashcroft, G.S., Kielty, C., Wilmot, C., Donnai, D., Read, A.P., Jones, C.J. Hum. Mol. Genet. (1998) [Pubmed]
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