Membrane pore formation at protein-lipid interfaces (Articolo in rivista)

Type
Label
  • Membrane pore formation at protein-lipid interfaces (Articolo in rivista) (literal)
Anno
  • 2014-01-01T00:00:00+01:00 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
  • 10.1016/j.tibs.2014.09.002 (literal)
Alternative label
  • Robert J.C. Gilbert1, Mauro Dalla Serra2, Christopher J. Froelich3, Mark I. Wallace4, and Gregor Anderluh (2014)
    Membrane pore formation at protein-lipid interfaces
    in Trends in biochemical sciences (Amst., Ref. ed.)
    (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
  • Robert J.C. Gilbert1, Mauro Dalla Serra2, Christopher J. Froelich3, Mark I. Wallace4, and Gregor Anderluh (literal)
Pagina inizio
  • 510 (literal)
Pagina fine
  • 516 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume
  • 39 (literal)
Rivista
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroFascicolo
  • 11 (literal)
Note
  • ISI Web of Science (WOS) (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
  • 1 Division of Structural Biology, Wellcome Trust Centre for Human Genetics, University of Oxford, Roosevelt Drive, Oxford OX3 7BN, UK 2 Consiglio Nazionale delle Ricerche, Istituto di Biofisica and Fondazione Bruno Kessler, Via alla Cascata 56/C, 38123, Trento, Italy 3 NorthShore University Health Systems Research Institute and University of Chicago, Evanston, IL 60201, USA 4 Department of Chemistry, University of Oxford, 12 Mansfield Road, Oxford, OX1 3TA, UK 5 Department of Biology, Biotechnical Faculty, University of Ljubljana, Jamnikarjeva 101, 1000 Ljubljana, Slovenia 6 National Institute of Chemistry, Hajdrihova 19, 1000 Ljubljana, Slovenia (literal)
Titolo
  • Membrane pore formation at protein-lipid interfaces (literal)
Abstract
  • Pore-forming proteins (PFPs) interact with lipid bilayers to compromise membrane integrity. Many PFPs function by inserting a ring of oligomerized subunits into the bilayer to form a protein-lined hydrophilic channel. However, mounting evidence suggests that PFPs can also generate 'proteolipidic' pores by contributing to the fusion of inner and outer bilayer leaflets to form a toroidal structure. We discuss here toroidal pore formation by peptides including melittin, protegrin, and Alzheimer's A beta 1-41, as well as by PFPs from several evolutionarily unrelated families: the colicin/Bcl-2 grouping including the pro-apoptotic protein Bax, actinoporins derived from sea anemones, and the membrane attack complex-perforin/cholesterol dependent cytolysin (MACPF/CDC) set of proteins. We also explore how the structure and biological role of toroidal pores might be investigated further. (literal)
Prodotto di
Autore CNR

Incoming links:


Prodotto
Autore CNR di
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#rivistaDi
data.CNR.it