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Disease relevance of Biotinylation


High impact information on Biotinylation

  • Protease and biotinylation accessibility studies of right side-out and inside-out membrane vesicles derived from this strain revealed that SecA was exposed to the periplasmic surface of the inner membrane [6].
  • After cell-surface biotinylation, full-length biotinylated beta APP was recovered inside the cells [7].
  • Single-channel analysis and biotinylation assays indicate that MPS-1 reduces the macroscopic current by lowering the open probability of the channel [8].
  • Biotinylation of single cysteine mutants of the glutamate transporter GLT-1 from rat brain reveals its unusual topology [9].
  • Cell surface biotinylation experiments confirmed that AQP4 is internalized after 20 min of histamine exposure, which may account for the downregulation of water transport [10].

Chemical compound and disease context of Biotinylation


Biological context of Biotinylation


Anatomical context of Biotinylation


Associations of Biotinylation with chemical compounds


Gene context of Biotinylation


Analytical, diagnostic and therapeutic context of Biotinylation


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  3. Cytosolic stress reduces degradation of connexin43 internalized from the cell surface and enhances gap junction formation and function. VanSlyke, J.K., Musil, L.S. Mol. Biol. Cell (2005) [Pubmed]
  4. Genes for two subunits of acetyl coenzyme A carboxylase of Anabaena sp. strain PCC 7120: biotin carboxylase and biotin carboxyl carrier protein. Gornicki, P., Scappino, L.A., Haselkorn, R. J. Bacteriol. (1993) [Pubmed]
  5. Structural characterization of the E2 glycoprotein from Sindbis by lysine biotinylation and LC-MS/MS. Sharp, J.S., Nelson, S., Brown, D., Tomer, K.B. Virology (2006) [Pubmed]
  6. SecA protein is exposed to the periplasmic surface of the E. coli inner membrane in its active state. Kim, Y.J., Rajapandi, T., Oliver, D. Cell (1994) [Pubmed]
  7. Targeting of cell-surface beta-amyloid precursor protein to lysosomes: alternative processing into amyloid-bearing fragments. Haass, C., Koo, E.H., Mellon, A., Hung, A.Y., Selkoe, D.J. Nature (1992) [Pubmed]
  8. MPS-1 is a K+ channel beta-subunit and a serine/threonine kinase. Cai, S.Q., Hernandez, L., Wang, Y., Park, K.H., Sesti, F. Nat. Neurosci. (2005) [Pubmed]
  9. Biotinylation of single cysteine mutants of the glutamate transporter GLT-1 from rat brain reveals its unusual topology. Grunewald, M., Bendahan, A., Kanner, B.I. Neuron (1998) [Pubmed]
  10. Histamine treatment induces rearrangements of orthogonal arrays of particles (OAPs) in human AQP4-expressing gastric cells. Carmosino, M., Procino, G., Nicchia, G.P., Mannucci, R., Verbavatz, J.M., Gobin, R., Svelto, M., Valenti, G. J. Cell Biol. (2001) [Pubmed]
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  12. A plasmid expression system for quantitative in vivo biotinylation of thioredoxin fusion proteins in Escherichia coli. Smith, P.A., Tripp, B.C., DiBlasio-Smith, E.A., Lu, Z., LaVallie, E.R., McCoy, J.M. Nucleic Acids Res. (1998) [Pubmed]
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  15. Recombinant OspC from Borrelia burgdorferi sensu stricto, B. afzelii and B. garinii in the serodiagnosis of Lyme borreliosis. Panelius, J., Lahdenne, P., Heikkilä, T., Peltomaa, M., Oksi, J., Seppälä, I. J. Med. Microbiol. (2002) [Pubmed]
  16. Synaptic-like microvesicles of neuroendocrine cells originate from a novel compartment that is continuous with the plasma membrane and devoid of transferrin receptor. Schmidt, A., Hannah, M.J., Huttner, W.B. J. Cell Biol. (1997) [Pubmed]
  17. Isolation of a cDNA encoding human holocarboxylase synthetase by functional complementation of a biotin auxotroph of Escherichia coli. León-Del-Rio, A., Leclerc, D., Akerman, B., Wakamatsu, N., Gravel, R.A. Proc. Natl. Acad. Sci. U.S.A. (1995) [Pubmed]
  18. Native polycystin 2 functions as a plasma membrane Ca2+-permeable cation channel in renal epithelia. Luo, Y., Vassilev, P.M., Li, X., Kawanabe, Y., Zhou, J. Mol. Cell. Biol. (2003) [Pubmed]
  19. Membrane trafficking of the cystic fibrosis gene product, cystic fibrosis transmembrane conductance regulator, tagged with green fluorescent protein in madin-darby canine kidney cells. Moyer, B.D., Loffing, J., Schwiebert, E.M., Loffing-Cueni, D., Halpin, P.A., Karlson, K.H., Ismailov, I.I., Guggino, W.B., Langford, G.M., Stanton, B.A. J. Biol. Chem. (1998) [Pubmed]
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  21. Membrane type I-matrix metalloproteinase-mediated degradation of type I collagen by oral squamous cell carcinoma cells. Aznavoorian, S., Moore, B.A., Alexander-Lister, L.D., Hallit, S.L., Windsor, L.J., Engler, J.A. Cancer Res. (2001) [Pubmed]
  22. Calreticulin is expressed on the cell surface of activated human peripheral blood T lymphocytes in association with major histocompatibility complex class I molecules. Arosa, F.A., de Jesus, O., Porto, G., Carmo, A.M., de Sousa, M. J. Biol. Chem. (1999) [Pubmed]
  23. Metabolic biotinylation as a probe of supramolecular structure of the triad junction in skeletal muscle. Lorenzon, N.M., Haarmann, C.S., Norris, E.E., Papadopoulos, S., Beam, K.G. J. Biol. Chem. (2004) [Pubmed]
  24. Immunolocalization of acyl-coenzyme A:cholesterol O-acyltransferase in macrophages. Khelef, N., Buton, X., Beatini, N., Wang, H., Meiner, V., Chang, T.Y., Farese, R.V., Maxfield, F.R., Tabas, I. J. Biol. Chem. (1998) [Pubmed]
  25. Molecular cloning and characterization of the cDNA coding for the biotin-containing subunit of 3-methylcrotonoyl-CoA carboxylase: identification of the biotin carboxylase and biotin-carrier domains. Song, J., Wurtele, E.S., Nikolau, B.J. Proc. Natl. Acad. Sci. U.S.A. (1994) [Pubmed]
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  28. Holocarboxylase synthetase is an obligate participant in biotin-mediated regulation of its own expression and of biotin-dependent carboxylases mRNA levels in human cells. Solórzano-Vargas, R.S., Pacheco-Alvarez, D., León-Del-Río, A. Proc. Natl. Acad. Sci. U.S.A. (2002) [Pubmed]
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  33. Identification of the tRNA-binding protein Arc1p as a novel target of in vivo biotinylation in Saccharomyces cerevisiae. Kim, H.S., Hoja, U., Stolz, J., Sauer, G., Schweizer, E. J. Biol. Chem. (2004) [Pubmed]
  34. The glycosylphosphatidyl inositol-anchored adhesion molecule F3/contactin is required for surface transport of paranodin/contactin-associated protein (caspr). Faivre-Sarrailh, C., Gauthier, F., Denisenko-Nehrbass, N., Le Bivic, A., Rougon, G., Girault, J.A. J. Cell Biol. (2000) [Pubmed]
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