Reovirus FAST proteins: virus-encoded cellular fusogens
M Ciechonska, R Duncan - Trends in microbiology, 2014 - cell.com
Reovirus fusion-associated small transmembrane (FAST) proteins are the only known
nonenveloped virus fusogens and are dedicated to inducing cell-to-cell, not virus–cell …
nonenveloped virus fusogens and are dedicated to inducing cell-to-cell, not virus–cell …
Thermodynamically reversible paths of the first fusion intermediate reveal an important role for membrane anchors of fusion proteins
YG Smirnova, HJ Risselada… - Proceedings of the …, 2019 - National Acad Sciences
Biological membrane fusion proceeds via an essential topological transition of the two
membranes involved. Known players such as certain lipid species and fusion proteins are …
membranes involved. Known players such as certain lipid species and fusion proteins are …
Life at the border: Adaptation of proteins to anisotropic membrane environment
This review discusses main features of transmembrane (TM) proteins which distinguish them
from water‐soluble proteins and allow their adaptation to the anisotropic membrane …
from water‐soluble proteins and allow their adaptation to the anisotropic membrane …
pHLIP®-mediated delivery of PEGylated liposomes to cancer cells
L Yao, J Daniels, D Wijesinghe, OA Andreev… - Journal of Controlled …, 2013 - Elsevier
We develop a method for pH-dependent fusion between liposomes and cellular membranes
using pHLIP®(pH Low Insertion Peptide), which inserts into lipid bilayer of membrane only …
using pHLIP®(pH Low Insertion Peptide), which inserts into lipid bilayer of membrane only …
Viral fusion protein transmembrane domain adopts β-strand structure to facilitate membrane topological changes for virus–cell fusion
The C-terminal transmembrane domain (TMD) of viral fusion proteins such as HIV gp41 and
influenza hemagglutinin (HA) is traditionally viewed as a passive α-helical anchor of the …
influenza hemagglutinin (HA) is traditionally viewed as a passive α-helical anchor of the …
Oligomeric structure and three-dimensional fold of the HIV gp41 membrane-proximal external region and transmembrane domain in phospholipid bilayers
The HIV-1 glycoprotein, gp41, mediates fusion of the virus lipid envelope with the target cell
membrane during virus entry into cells. Despite extensive studies of this protein, inconsistent …
membrane during virus entry into cells. Despite extensive studies of this protein, inconsistent …
Effect of lipid composition and amino acid sequence upon transmembrane peptide-accelerated lipid transleaflet diffusion (flip-flop)
J LeBarron, E London - Biochimica et Biophysica Acta (BBA) …, 2016 - Elsevier
We examined how hydrophobic peptide-accelerated transleaflet lipid movement (flip-flop)
was affected by peptide sequence and vesicle composition and properties. A peptide with a …
was affected by peptide sequence and vesicle composition and properties. A peptide with a …
Residue-specific side-chain packing determines the backbone dynamics of transmembrane model helices
S Quint, S Widmaier, D Minde, D Hornburg… - Biophysical journal, 2010 - cell.com
The transmembrane domains (TMDs) of membrane-fusogenic proteins contain an
overabundance of β-branched residues. In a previous effort to systematically study the …
overabundance of β-branched residues. In a previous effort to systematically study the …
Conformation and trimer association of the transmembrane domain of the parainfluenza virus fusion protein in lipid bilayers from solid-state NMR: insights into the …
Enveloped viruses enter cells by using their fusion proteins to merge the virus lipid envelope
and the cell membrane. While crystal structures of the water-soluble ectodomains of many …
and the cell membrane. While crystal structures of the water-soluble ectodomains of many …
Beyond anchoring: the expanding role of the hendra virus fusion protein transmembrane domain in protein folding, stability, and function
While work with viral fusion proteins has demonstrated that the transmembrane domain
(TMD) can affect protein folding, stability, and membrane fusion promotion, the mechanism …
(TMD) can affect protein folding, stability, and membrane fusion promotion, the mechanism …