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Chemical Compound Review

kifunensine     (2R,3R,4S,5S,6S)-3,4,5- trihydroxy-2...

Synonyms: CHEMBL1233851, SureCN2856417, CHEBI:43662, CTK8F0856, ZINC03795857, ...
 
 
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High impact information on kifunensine

 

Biological context of kifunensine

 

Anatomical context of kifunensine

  • In addition, natural killer cell lysis of kifunensine-treated cells increases 34% over that of controls [9].
  • Studies with rat liver microsomes also indicated that kifunensine inhibited the Golgi mannosidase I, but probably does not inhibit the endoplasmic reticulum mannosidase [6].
  • Demonstration that a kifunensine-resistant alpha-mannosidase with a unique processing action on N-linked oligosaccharides occurs in rat liver endoplasmic reticulum and various cultured cells [10].
  • Kifunensine also decreased the binding of the labeled acetyl-LDL by the scavenger receptor of the endothelial cells, but the amount of this inhibition relative to controls was significantly less than that of the degradation, suggesting that kifunensine affects two different steps of acetyl-LDL metabolism in these cells [11].
  • Studies were undertaken to evaluate the relationship of the recently described (S. Weng and R. G. Spiro, 1993, J. Biol. chem. 268, 25656-25663) rat liver kifunensine (KIF)-resistant mannosidase (ER mannosidase II) to the mannose-trimming enzyme of cytosol [12].
 

Associations of kifunensine with other chemical compounds

 

Gene context of kifunensine

  • In this paper, the 1.80 A resolution crystal structure of kifunensine bound to Drosophila melanogaster Golgi alpha-mannosidase II (dGMII) is presented [15].
  • Monoclonal antibodies to the adhesion molecule LFA-1 and its ligand ICAM-1 reduce lysis of control targets but are less effective in blocking lysis of kifunensine-treated cells [9].
 

Analytical, diagnostic and therapeutic context of kifunensine

  • Kifunensine was tested in cell culture by examining its ability to inhibit processing of the influenza viral glycoproteins in Madin-Darby canine kidney cells [6].

References

  1. The C-terminal T peptide of acetylcholinesterase enhances degradation of unassembled active subunits through the ERAD pathway. Belbeoc'h, S., Massoulié, J., Bon, S. EMBO J. (2003) [Pubmed]
  2. Degradation of trafficking-defective long QT syndrome type II mutant channels by the ubiquitin-proteasome pathway. Gong, Q., Keeney, D.R., Molinari, M., Zhou, Z. J. Biol. Chem. (2005) [Pubmed]
  3. Sialylated complex-type N-glycans enhance the signaling activity of soluble intercellular adhesion molecule-1 in mouse astrocytes. Otto, V.I., Schürpf, T., Folkers, G., Cummings, R.D. J. Biol. Chem. (2004) [Pubmed]
  4. Endoplasmic reticulum (ER)-associated degradation of misfolded N-linked glycoproteins is suppressed upon inhibition of ER mannosidase I. Tokunaga, F., Brostrom, C., Koide, T., Arvan, P. J. Biol. Chem. (2000) [Pubmed]
  5. Oligosaccharide modification in the early secretory pathway directs the selection of a misfolded glycoprotein for degradation by the proteasome. Liu, Y., Choudhury, P., Cabral, C.M., Sifers, R.N. J. Biol. Chem. (1999) [Pubmed]
  6. Kifunensine, a potent inhibitor of the glycoprotein processing mannosidase I. Elbein, A.D., Tropea, J.E., Mitchell, M., Kaushal, G.P. J. Biol. Chem. (1990) [Pubmed]
  7. Comparison of biological activity among nonfucosylated therapeutic IgG1 antibodies with three different N-linked Fc oligosaccharides: the high-mannose, hybrid, and complex types. Kanda, Y., Yamada, T., Mori, K., Okazaki, A., Inoue, M., Kitajima-Miyama, K., Kuni-Kamochi, R., Nakano, R., Yano, K., Kakita, S., Shitara, K., Satoh, M. Glycobiology (2007) [Pubmed]
  8. The fate of beta-d-mannopyranose after its formation by endoplasmic reticulum alpha-(1-->2)-mannosidase I catalysis. Mulakala, C., Nerinckx, W., Reilly, P.J. Carbohydr. Res. (2007) [Pubmed]
  9. Role of target cell glycoproteins in sensitivity to natural killer cell lysis. Ahrens, P.B. J. Biol. Chem. (1993) [Pubmed]
  10. Demonstration that a kifunensine-resistant alpha-mannosidase with a unique processing action on N-linked oligosaccharides occurs in rat liver endoplasmic reticulum and various cultured cells. Weng, S., Spiro, R.G. J. Biol. Chem. (1993) [Pubmed]
  11. Kifunensine inhibits glycoprotein processing and the function of the modified LDL receptor in endothelial cells. Elbein, A.D., Kerbacher, J.K., Schwartz, C.J., Sprague, E.A. Arch. Biochem. Biophys. (1991) [Pubmed]
  12. Endoplasmic reticulum kifunensine-resistant alpha-mannosidase is enzymatically and immunologically related to the cytosolic alpha-mannosidase. Weng, S., Spiro, R.G. Arch. Biochem. Biophys. (1996) [Pubmed]
  13. Structural basis for catalysis and inhibition of N-glycan processing class I alpha 1,2-mannosidases. Vallee, F., Karaveg, K., Herscovics, A., Moremen, K.W., Howell, P.L. J. Biol. Chem. (2000) [Pubmed]
  14. N-linked oligosaccharide processing, but not association with calnexin/calreticulin is highly correlated with endoplasmic reticulum-associated degradation of antithrombin Glu313-deleted mutant. Tokunaga, F., Hara, K., Koide, T. Arch. Biochem. Biophys. (2003) [Pubmed]
  15. Comparison of kifunensine and 1-deoxymannojirimycin binding to class I and II alpha-mannosidases demonstrates different saccharide distortions in inverting and retaining catalytic mechanisms. Shah, N., Kuntz, D.A., Rose, D.R. Biochemistry (2003) [Pubmed]
 
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