Literature DB >> 11426687

Membrane fusion.

R M Epand1.   

Abstract

The fusion of biological membranes results in two bilayer-based membranes merging into a single membrane. In this process the lipids have to undergo considerable rearrangement. The nature of the intermediates that are formed during this rearrangement has been investigated. Certain fusion proteins facilitate this process. In many cases short segments of these fusion proteins have a particularly important role in accelerating the fusion process. Studies of the interaction of model peptides with membranes have allowed for increased understanding at the molecular level of the mechanism of the promotion of membrane fusion by fusion proteins. There is an increased appreciation of the roles of several independent segments of fusion proteins in promoting the fusion process. Many of the studies of the fusion of biological membranes have been done with the fusion of enveloped viruses with other membranes. One reason for this is that the number of proteins involved in viral fusion is relatively simple, often requiring only a single protein. For many enveloped viruses, the structure of their fusion proteins has certain common elements, suggesting that they all promote fusion by an analogous mechanism. Some aspects of this mechanism also appears to be common to intracellular fusion, although several proteins are involved in that process which is more complex and regulated than is viral fusion.

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Year:  2000        PMID: 11426687     DOI: 10.1023/a:1010498618600

Source DB:  PubMed          Journal:  Biosci Rep        ISSN: 0144-8463            Impact factor:   3.840


  8 in total

1.  Mechanism of the lamellar/inverse hexagonal phase transition examined by high resolution x-ray diffraction.

Authors:  Michael Rappolt; Andrea Hickel; Frank Bringezu; Karl Lohner
Journal:  Biophys J       Date:  2003-05       Impact factor: 4.033

2.  Structure and energy of fusion stalks: the role of membrane edges.

Authors:  Sylvio May
Journal:  Biophys J       Date:  2002-12       Impact factor: 4.033

3.  The role of calcium in neutrophil granule-phagosome fusion.

Authors:  Pontus Nordenfelt; Hans Tapper
Journal:  Commun Integr Biol       Date:  2010-05

4.  HIV gp41 fusion peptide increases membrane ordering in a cholesterol-dependent fashion.

Authors:  Alex L Lai; Jack H Freed
Journal:  Biophys J       Date:  2014-01-07       Impact factor: 4.033

5.  Mechanism of pH-triggered collapse of phosphatidylethanolamine liposomes stabilized by an ortho ester polyethyleneglycol lipid.

Authors:  Xin Guo; J Andrew MacKay; Francis C Szoka
Journal:  Biophys J       Date:  2003-03       Impact factor: 4.033

Review 6.  Membrane Fusion Involved in Neurotransmission: Glimpse from Electron Microscope and Molecular Simulation.

Authors:  Zhiwei Yang; Lu Gou; Shuyu Chen; Na Li; Shengli Zhang; Lei Zhang
Journal:  Front Mol Neurosci       Date:  2017-06-07       Impact factor: 5.639

7.  Negatively charged residues in the membrane ordering activity of SARS-CoV-1 and -2 fusion peptides.

Authors:  Alex L Lai; Jack H Freed
Journal:  Biophys J       Date:  2021-12-18       Impact factor: 4.033

8.  Critical Negatively Charged Residues Are Important for the Activity of SARS-CoV-1 and SARS-CoV-2 Fusion Peptides.

Authors:  Alex L Lai; Jack H Freed
Journal:  bioRxiv       Date:  2021-12-06
  8 in total

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