| Literature DB >> 8970739 |
L D Hernandez1, L R Hoffman, T G Wolfsberg, J M White.
Abstract
Significant progress has been made in elucidating the mechanisms of viral membrane fusion proteins; both those that function at low, as well as those that function at neutral, pH. For many viral fusion proteins evidence now suggests that a triggered conformational change that exposes a previously cryptic fusion peptide, along with a rearrangement of the fusion protein oligomer, allows the fusion peptide to gain access to the target bilayer and thus initiate the fusion reaction. Although the topologically equivalent process of cell-cell fusion is less well understood, several cell surface proteins, including members of the newly described ADAM gene family, have emerged as candidate adhesion/fusion proteins.Mesh:
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Year: 1996 PMID: 8970739 DOI: 10.1146/annurev.cellbio.12.1.627
Source DB: PubMed Journal: Annu Rev Cell Dev Biol ISSN: 1081-0706 Impact factor: 13.827