Results 71 to 80 of about 319,921 (262)

Chaperone fusion proteins aid entropy-driven maturation of class II viral fusion proteins [PDF]

Trends in Microbiology, 2014
Class II viral fusion proteins are present on the envelope of flaviviruses and togaviruses, viruses that often cause tropical and subtropical diseases. These proteins use a second membrane protein as a molecular chaperone to assist their folding and to ensure proper function during viral assembly, maturation, and infection.
Peng Ge, Peng Ge, Z. Hong Zhou, Z. Hong Zhou   +3 more
openaire   +5 more sources

The membrane fusion step of vaccinia virus entry is cooperatively mediated by multiple viral proteins and host cell components. [PDF]

PLoS Pathogens, 2011
For many viruses, one or two proteins allow cell attachment and entry, which occurs through the plasma membrane or following endocytosis at low pH. In contrast, vaccinia virus (VACV) enters cells by both neutral and low pH routes; four proteins mediate ...
Jason P Laliberte, Andrea S Weisberg, Bernard Moss   +2 more
doaj   +1 more source

Virtual screening of Microalgal compounds as potential inhibitors of Type 2 Human Transmembrane serine protease (TMPRSS2) [PDF]

arXiv, 2021
More than 198 million cases of severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) has been reported that result in no fewer than 4.2 million deaths globally. The rapid spread of the disease coupled with the lack of specific registered drugs for its treatment pose a great challenge that necessitate the development of therapeutic agents from a ...
arxiv  

Fusion pore conductance to determine the effects of mutating the structure of influenza virus hemagglutinin [PDF]

, 2016
Enveloped viruses, such as influenza, infect cells by fusing their viral envelope with the cell membrane. The fusion pore is a macromolecular structure that links two membranes that are fusing.
Wachter, Rebecca
core   +1 more source

Amino acid substitutions within the heptad repeat domain 1 of murine coronavirus spike protein restrict viral antigen spread in the central nervous system. [PDF]

, 2003
Targeted recombination was carried out to select mouse hepatitis viruses (MHVs) in a defined genetic background, containing an MHV-JHM spike gene encoding either three heptad repeat 1 (HR1) substitutions (Q1067H, Q1094H, and L1114R) or L1114R alone.
de Groot, Linda, Iacono, Kathryn T, Lavi, Ehud, Phillips, Joanna J, Pinon, Josefina D, Seo, Su-hun, Tsai, Jean C, Weiss, Susan R   +7 more
core   +1 more source

IFITM Proteins Incorporated into HIV-1 Virions Impair Viral Fusion and Spread [PDF]

Cell Host & Microbe, 2014
The interferon-induced transmembrane (IFITM) proteins protect cells from diverse virus infections by inhibiting virus-cell fusion. IFITM proteins also inhibit HIV-1 replication through mechanisms only partially understood. We show that when expressed in uninfected lymphocytes, IFITM proteins exert protective effects during cell-free virus infection ...
Nicoletta Casartelli, Nicoletta Casartelli, Chen Liang, Martin Sachse, Adeline Mallet, Marine Euvrard, Olivier Schwartz, Olivier Schwartz, Timothée Bruel, Timothée Bruel, Alex A. Compton, Alex A. Compton, Françoise Porrot, Françoise Porrot   +13 more
openaire   +4 more sources

Fusoselect: cell-cell fusion activity engineered by directed evolution of a retroviral glycoprotein [PDF]

, 2017
Membrane fusion plays a key role in many biological processes including vesicle trafficking, synaptic transmission, fertilization or cell entry of enveloped viruses. As a common feature the fusion process is mediated by distinct membrane proteins.
Braun, Gundula, Buchholz, Christian J., Cichutek, Klaus, Medvedovska, Julia, Merten, Christoph A., Stitz, Jörn   +5 more
core  

Herpes simplex virus ICP27 protein directly interacts with the nuclear pore complex through NUP62, inhibiting host nucleocytoplasmic transport pathways [PDF]

, 2012
The herpes simplex virus ICP27 protein is important for the expression and nuclear export of viral mRNAs. Although several binding sites have been mapped along the ICP27 sequence for various RNA and protein partners including the transport receptor TAP ...
Arnold, Aubert, Bachi, Bonifaci, Braun, Bryant, Chen, Chen, Copeland, Cullen, Darshan, Ellison, Ellison, Escudero-Paunetto, Faria, Fischer, Flach, Fontaine-Rodriguez, Fontoura, Fornerod, Fridell, Gerace, Gruffat, Grüter, Gustin, Gustin, Gustin, Han, Hardwicke, Hernandez, Hiriart, Hofemeister, Hutten, Johnson, Kambach, Koffa, Larralde, Lengyel, Lengyel, Li, Lilley, Long, Macaulay, Malik, Malik, McCarthy, Mears, Mears, Mears, Meyer, Michael, Nelson, Park, Pasdeloup, Pasquinelli, Pearson, Pellet, Petersen, Phelan, Piñol-Roma, Pollard, Pritchard, Rice, Rice, Rice, Rice, Rojas, Saavedra, Sandri-Goldin, Satterly, Schmitt, Sekulovich, Siomi, Smith, Soliman, Soliman, Souki, Strambio-De-Castillia, Strässer, Tsuji, Wagstaff, Wente, Zhi, Zhi   +83 more
core   +3 more sources

A general computational design strategy for stabilizing viral class I fusion proteins

Nature Communications, 2023
AbstractMany pathogenic viruses rely on class I fusion proteins to fuse their viral membrane with the host cell membrane. To drive the fusion process, class I fusion proteins undergo an irreversible conformational change from a metastable prefusion state to an energetically more stable postfusion state.
Karen J. Gonzalez, Jiachen Huang, Miria F. Criado, Avik Banerjee, Stephen M. Tompkins, Jarrod J. Mousa, Eva-Maria Strauch   +6 more
openaire   +5 more sources

Analysis of the subunit stoichiometries in viral entry. [PDF]

PLoS ONE, 2012
Virions of the Human Immunodeficiency Virus (HIV) infect cells by first attaching with their surface spikes to the CD4 receptor on target cells. This leads to conformational changes in the viral spikes, enabling the virus to engage a coreceptor, commonly
Carsten Magnus, Roland R Regoes
doaj   +1 more source