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MeSH Review

Membrane Fusion

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Disease relevance of Membrane Fusion


High impact information on Membrane Fusion

  • Despite reports suggesting a potential role in membrane fusion, the V(0) subunit of the (+)H/ATPase has remained an unlikely candidate for the fusion pore [6].
  • Mutations in VPS33B, encoding a regulator of SNARE-dependent membrane fusion, cause arthrogryposis-renal dysfunction-cholestasis (ARC) syndrome [7].
  • VCP is associated with a variety of cellular activities, including cell cycle control, membrane fusion and the ubiquitin-proteasome degradation pathway [8].
  • VPS33B encodes a homolog of the class C yeast vacuolar protein sorting gene, Vps33, that contains a Sec1-like domain important in the regulation of vesicle-to-target SNARE complex formation and subsequent membrane fusion [7].
  • Oligomeric complexes link Rab5 effectors with NSF and drive membrane fusion via interactions between EEA1 and syntaxin 13 [9].

Chemical compound and disease context of Membrane Fusion


Biological context of Membrane Fusion


Anatomical context of Membrane Fusion


Associations of Membrane Fusion with chemical compounds


Gene context of Membrane Fusion


Analytical, diagnostic and therapeutic context of Membrane Fusion


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  2. Regions in beta-chemokine receptors CCR5 and CCR2b that determine HIV-1 cofactor specificity. Rucker, J., Samson, M., Doranz, B.J., Libert, F., Berson, J.F., Yi, Y., Smyth, R.J., Collman, R.G., Broder, C.C., Vassart, G., Doms, R.W., Parmentier, M. Cell (1996) [Pubmed]
  3. pH-independent HIV entry into CD4-positive T cells via virus envelope fusion to the plasma membrane. Stein, B.S., Gowda, S.D., Lifson, J.D., Penhallow, R.C., Bensch, K.G., Engleman, E.G. Cell (1987) [Pubmed]
  4. Retroviral entry mediated by receptor priming and low pH triggering of an envelope glycoprotein. Mothes, W., Boerger, A.L., Narayan, S., Cunningham, J.M., Young, J.A. Cell (2000) [Pubmed]
  5. A single point mutation controls the cholesterol dependence of Semliki Forest virus entry and exit. Vashishtha, M., Phalen, T., Marquardt, M.T., Ryu, J.S., Ng, A.C., Kielian, M. J. Cell Biol. (1998) [Pubmed]
  6. A new view of an old pore. Bajjalieh, S. Cell (2005) [Pubmed]
  7. Mutations in VPS33B, encoding a regulator of SNARE-dependent membrane fusion, cause arthrogryposis-renal dysfunction-cholestasis (ARC) syndrome. Gissen, P., Johnson, C.A., Morgan, N.V., Stapelbroek, J.M., Forshew, T., Cooper, W.N., McKiernan, P.J., Klomp, L.W., Morris, A.A., Wraith, J.E., McClean, P., Lynch, S.A., Thompson, R.J., Lo, B., Quarrell, O.W., Di Rocco, M., Trembath, R.C., Mandel, H., Wali, S., Karet, F.E., Knisely, A.S., Houwen, R.H., Kelly, D.A., Maher, E.R. Nat. Genet. (2004) [Pubmed]
  8. Inclusion body myopathy associated with Paget disease of bone and frontotemporal dementia is caused by mutant valosin-containing protein. Watts, G.D., Wymer, J., Kovach, M.J., Mehta, S.G., Mumm, S., Darvish, D., Pestronk, A., Whyte, M.P., Kimonis, V.E. Nat. Genet. (2004) [Pubmed]
  9. Oligomeric complexes link Rab5 effectors with NSF and drive membrane fusion via interactions between EEA1 and syntaxin 13. McBride, H.M., Rybin, V., Murphy, C., Giner, A., Teasdale, R., Zerial, M. Cell (1999) [Pubmed]
  10. AMD3100, a small molecule inhibitor of HIV-1 entry via the CXCR4 co-receptor. Donzella, G.A., Schols, D., Lin, S.W., Esté, J.A., Nagashima, K.A., Maddon, P.J., Allaway, G.P., Sakmar, T.P., Henson, G., De Clercq, E., Moore, J.P. Nat. Med. (1998) [Pubmed]
  11. Structural features of membrane fusion between influenza virus and liposome as revealed by quick-freezing electron microscopy. Kanaseki, T., Kawasaki, K., Murata, M., Ikeuchi, Y., Ohnishi, S. J. Cell Biol. (1997) [Pubmed]
  12. A duodenally absorbable CXC chemokine receptor 4 antagonist, KRH-1636, exhibits a potent and selective anti-HIV-1 activity. Ichiyama, K., Yokoyama-Kumakura, S., Tanaka, Y., Tanaka, R., Hirose, K., Bannai, K., Edamatsu, T., Yanaka, M., Niitani, Y., Miyano-Kurosaki, N., Takaku, H., Koyanagi, Y., Yamamoto, N. Proc. Natl. Acad. Sci. U.S.A. (2003) [Pubmed]
  13. Membrane fusion induced by vesicular stomatitis virus depends on histidine protonation. Carneiro, F.A., Stauffer, F., Lima, C.S., Juliano, M.A., Juliano, L., Da Poian, A.T. J. Biol. Chem. (2003) [Pubmed]
  14. Characterization of the infectious salmon anemia virus fusion protein. Aspehaug, V., Mikalsen, A.B., Snow, M., Biering, E., Villoing, S. J. Virol. (2005) [Pubmed]
  15. Relocation of the t-SNARE SNAP-23 from lamellipodia-like cell surface projections regulates compound exocytosis in mast cells. Guo, Z., Turner, C., Castle, D. Cell (1998) [Pubmed]
  16. A mutation in OTOF, encoding otoferlin, a FER-1-like protein, causes DFNB9, a nonsyndromic form of deafness. Yasunaga, S., Grati, M., Cohen-Salmon, M., El-Amraoui, A., Mustapha, M., Salem, N., El-Zir, E., Loiselet, J., Petit, C. Nat. Genet. (1999) [Pubmed]
  17. GTPase activity of Rab5 acts as a timer for endocytic membrane fusion. Rybin, V., Ullrich, O., Rubino, M., Alexandrov, K., Simon, I., Seabra, M.C., Goody, R., Zerial, M. Nature (1996) [Pubmed]
  18. High-affinity NGF binding requires coexpression of the trk proto-oncogene and the low-affinity NGF receptor. Hempstead, B.L., Martin-Zanca, D., Kaplan, D.R., Parada, L.F., Chao, M.V. Nature (1991) [Pubmed]
  19. Regulation of caveolar endocytosis by syntaxin 6-dependent delivery of membrane components to the cell surface. Choudhury, A., Marks, D.L., Proctor, K.M., Gould, G.W., Pagano, R.E. Nat. Cell Biol. (2006) [Pubmed]
  20. Organelle membrane fusion: a novel function for the syntaxin homolog Ufe1p in ER membrane fusion. Patel, S.K., Indig, F.E., Olivieri, N., Levine, N.D., Latterich, M. Cell (1998) [Pubmed]
  21. Calcium-dependent interaction of N-type calcium channels with the synaptic core complex. Sheng, Z.H., Rettig, J., Cook, T., Catterall, W.A. Nature (1996) [Pubmed]
  22. NSF--fusion and beyond. Haas, A. Trends Cell Biol. (1998) [Pubmed]
  23. Diacylglycerol metabolism in mast cells: a potential role in membrane fusion and arachidonic acid release. Kennerly, D.A., Sullivan, T.J., Sylwester, P., Parker, C.W. J. Exp. Med. (1979) [Pubmed]
  24. Three-dimensional structure of the complexin/SNARE complex. Chen, X., Tomchick, D.R., Kovrigin, E., Araç, D., Machius, M., Südhof, T.C., Rizo, J. Neuron (2002) [Pubmed]
  25. ATP-dependent fusion of liposomes with the Golgi apparatus of perforated cells. Kobayashi, T., Pagano, R.E. Cell (1988) [Pubmed]
  26. Membrane fusion takes excitatory turn: syntaxin, vesicle docking protein, or glutamate receptor? Brose, N. Cell (1993) [Pubmed]
  27. Atomic structure of the ectodomain from HIV-1 gp41. Weissenhorn, W., Dessen, A., Harrison, S.C., Skehel, J.J., Wiley, D.C. Nature (1997) [Pubmed]
  28. Exocytotic fusion is activated by Rab3a peptides. Oberhauser, A.F., Monck, J.R., Balch, W.E., Fernandez, J.M. Nature (1992) [Pubmed]
  29. Calcium-induced displacement of membrane-associated particles upon aggregation of chromaffin granules. Schober, R., Nitsch, C., Rinne, U., Morris, S.J. Science (1977) [Pubmed]
  30. Synaptobrevin binding to synaptophysin: a potential mechanism for controlling the exocytotic fusion machine. Edelmann, L., Hanson, P.I., Chapman, E.R., Jahn, R. EMBO J. (1995) [Pubmed]
  31. Sly1 protein bound to Golgi syntaxin Sed5p allows assembly and contributes to specificity of SNARE fusion complexes. Peng, R., Gallwitz, D. J. Cell Biol. (2002) [Pubmed]
  32. A soluble SNARE drives rapid docking, bypassing ATP and Sec17/18p for vacuole fusion. Thorngren, N., Collins, K.M., Fratti, R.A., Wickner, W., Merz, A.J. EMBO J. (2004) [Pubmed]
  33. nSec1 binds a closed conformation of syntaxin1A. Yang, B., Steegmaier, M., Gonzalez, L.C., Scheller, R.H. J. Cell Biol. (2000) [Pubmed]
  34. A role for the disintegrin domain of cyritestin, a sperm surface protein belonging to the ADAM family, in mouse sperm-egg plasma membrane adhesion and fusion. Yuan, R., Primakoff, P., Myles, D.G. J. Cell Biol. (1997) [Pubmed]
  35. Conformational changes in the AAA ATPase p97-p47 adaptor complex. Beuron, F., Dreveny, I., Yuan, X., Pye, V.E., McKeown, C., Briggs, L.C., Cliff, M.J., Kaneko, Y., Wallis, R., Isaacson, R.L., Ladbury, J.E., Matthews, S.J., Kondo, H., Zhang, X., Freemont, P.S. EMBO J. (2006) [Pubmed]
  36. Identification of a membrane fusion domain and an oligomerization domain in the baculovirus GP64 envelope fusion protein. Monsma, S.A., Blissard, G.W. J. Virol. (1995) [Pubmed]
  37. Inhibitory effects of small-molecule CCR5 antagonists on human immunodeficiency virus type 1 envelope-mediated membrane fusion and viral replication. Takashima, K., Miyake, H., Furuta, R.A., Fujisawa, J.I., Iizawa, Y., Kanzaki, N., Shiraishi, M., Okonogi, K., Baba, M. Antimicrob. Agents Chemother. (2001) [Pubmed]
  38. Differences between cell membrane fusion activities of two dengue type-1 isolates reflect modifications of viral structure. Desprès, P., Frenkiel, M.P., Deubel, V. Virology (1993) [Pubmed]
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