Literature DB >> 7922379

Membrane fusion. Anchors aweigh.

T Stegmann1.   

Abstract

A recent study using a version of the influenza virus hemagglutinin protein in which its membrane anchor was replaced by a lipid tail provides new insights into how proteins can mediate the fusion of membranes.

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Year:  1994        PMID： 7922379     DOI： 10.1016/s0960-9822(00)00123-8

Source DB:  PubMed          Journal:  Curr Biol        ISSN： 0960-9822            Impact factor:   10.834


  6 in total

1.  Polymorphism and interactions of a viral fusion peptide in a compressed lipid monolayer.

Authors:  G Schwarz; S E Taylor
Journal:  Biophys J       Date:  1999-06       Impact factor: 4.033

2.  A rhombohedral phase of lipid containing a membrane fusion intermediate structure.

Authors:  Lin Yang; Huey W Huang
Journal:  Biophys J       Date:  2003-03       Impact factor: 4.033

3.  The transmembrane domain of influenza hemagglutinin exhibits a stringent length requirement to support the hemifusion to fusion transition.

Authors:  R T Armstrong; A S Kushnir; J M White
Journal:  J Cell Biol       Date:  2000-10-16       Impact factor: 10.539

4.  Mechanisms of enveloped virus entry into animal cells.

Authors: 
Journal:  Adv Drug Deliv Rev       Date:  1998-10-05       Impact factor: 15.470

5.  Paramyxovirus F1 protein has two fusion peptides: implications for the mechanism of membrane fusion.

Authors:  S G Peisajovich; O Samuel; Y Shai
Journal:  J Mol Biol       Date:  2000-03-10       Impact factor: 5.469

6.  Influenza hemagglutinin assumes a tilted conformation during membrane fusion as determined by attenuated total reflection FTIR spectroscopy.

Authors:  S A Tatulian; P Hinterdorfer; G Baber; L K Tamm
Journal:  EMBO J       Date:  1995-11-15       Impact factor: 11.598
  6 in total

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