Literature DB >> 8810049

Non-bilayer lipids and biological fusion intermediates.

L Chernomordik1.   

Abstract

Disparate biological fusion reactions and fusion of purely lipid bilayers are similarly influenced by 'non-bilayer' lipids (lipids which do not form lipid bilayers in water by themselves). Lipid composition of membranes affects biological fusion at a stage downstream of activation of fusion proteins and prior to fusion pore formation. These data suggest that actual merger of membrane lipid bilayers in different fusion reactions proceeds via the same pathway. The effects of non-bilayer lipids specifically correlate with their ability to bend lipid monolayers in different directions, and appear to be consistent with the specific hypothesis of membrane fusion suggesting that fusion proceeds through highly bent intermediates--stalks, local connections between contacting monolayers of fusing membranes.

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Year:  1996        PMID: 8810049     DOI: 10.1016/0009-3084(96)02583-2

Source DB:  PubMed          Journal:  Chem Phys Lipids        ISSN: 0009-3084            Impact factor:   3.329


  51 in total

1.  Voltage-induced nonconductive pre-pores and metastable single pores in unmodified planar lipid bilayer.

Authors:  K C Melikov; V A Frolov; A Shcherbakov; A V Samsonov; Y A Chizmadzhev; L V Chernomordik
Journal:  Biophys J       Date:  2001-04       Impact factor: 4.033

2.  Reversible merger of membranes at the early stage of influenza hemagglutinin-mediated fusion.

Authors:  E Leikina; L V Chernomordik
Journal:  Mol Biol Cell       Date:  2000-07       Impact factor: 4.138

3.  Membrane fusion: stalk model revisited.

Authors:  Vladislav S Markin; Joseph P Albanesi
Journal:  Biophys J       Date:  2002-02       Impact factor: 4.033

4.  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

5.  The influenza hemagglutinin fusion domain is an amphipathic helical hairpin that functions by inducing membrane curvature.

Authors:  Sean T Smrt; Adrian W Draney; Justin L Lorieau
Journal:  J Biol Chem       Date:  2014-11-14       Impact factor: 5.157

6.  Field theoretic study of bilayer membrane fusion. I. Hemifusion mechanism.

Authors:  K Katsov; M Müller; M Schick
Journal:  Biophys J       Date:  2004-08-23       Impact factor: 4.033

Review 7.  Chemical shift tensor - the heart of NMR: Insights into biological aspects of proteins.

Authors:  Hazime Saitô; Isao Ando; Ayyalusamy Ramamoorthy
Journal:  Prog Nucl Magn Reson Spectrosc       Date:  2010-05-07       Impact factor: 9.795

8.  Non-lamellar lipid assembly at interfaces: controlling layer structure by responsive nanogel particles.

Authors:  Aleksandra P Dabkowska; Maria Valldeperas; Christopher Hirst; Costanza Montis; Gunnar K Pálsson; Meina Wang; Sofi Nöjd; Luigi Gentile; Justas Barauskas; Nina-Juliane Steinke; Gerd E Schroeder-Turk; Sebastian George; Maximilian W A Skoda; Tommy Nylander
Journal:  Interface Focus       Date:  2017-06-16       Impact factor: 3.906

9.  A consistent model for thermal fluctuations and protein-induced deformations in lipid bilayers.

Authors:  Grace Brannigan; Frank L H Brown
Journal:  Biophys J       Date:  2005-12-02       Impact factor: 4.033

10.  Molecular dynamics simulation of the evolution of hydrophobic defects in one monolayer of a phosphatidylcholine bilayer: relevance for membrane fusion mechanisms.

Authors:  D Peter Tieleman; Joe Bentz
Journal:  Biophys J       Date:  2002-09       Impact factor: 4.033

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