Results 51 to 60 of about 319,921 (262)

A Bimolecular Multicellular Complementation System for the Detection of Syncytium Formation: A New Methodology for the Identification of Nipah Virus Entry Inhibitors

open access: yesViruses, 2019
Fusion of viral and cellular membranes is a key step during the viral life cycle. Enveloped viruses trigger this process by means of specialized viral proteins expressed on their surface, the so-called viral fusion proteins.
María J. García-Murria   +4 more
doaj   +1 more source

Influence of N-glycosylation on Expression and Function of Pseudorabies Virus Glycoprotein gB

open access: yesPathogens, 2021
Envelope glycoprotein (g)B is conserved throughout the Herpesviridae and mediates fusion of the viral envelope with cellular membranes for infectious entry and spread.
Melina Vallbracht   +2 more
doaj   +1 more source

Expression of Human ACE2 N-terminal Domain, Part of the Receptor for SARS-CoV-2, in Fusion With Maltose-Binding Protein, E. coli Ribonuclease I and Human RNase A

open access: yesFrontiers in Microbiology, 2021
The SARS-CoV-2 viral genome contains a positive-strand single-stranded RNA of ∼30 kb. Human ACE2 protein is the receptor for SARS-CoV-2 virus attachment and infection.
Shuang-yong Xu   +3 more
doaj   +1 more source

Interferon-induced transmembrane protein 3 (IFITM3) and its antiviral activity [PDF]

open access: yesarXiv, 2022
Enveloped viral infections require fusion with cellular membranes for viral genome entry, occurring only following interaction of viral and cellular membranes allowing fusion pore formation, by which the virus accesses the cytoplasm. Here, we focus on interferon-induced transmembrane protein 3 (IFITM3) and its antiviral activity. IFITM3 is predicted to
arxiv  

Conformational reorganization of the SARS coronavirus spike following receptor binding: implications for membrane fusion. [PDF]

open access: yesPLoS ONE, 2007
The SARS coronavirus (SARS-CoV) spike is the largest known viral spike molecule, and shares a similar function with all class 1 viral fusion proteins.
Daniel R Beniac   +4 more
doaj   +1 more source

A compact, multifunctional fusion module directs cholesterol-dependent homomultimerization and syncytiogenic efficiency of reovirus p10 FAST proteins. [PDF]

open access: yesPLoS Pathogens, 2014
The homologous p10 fusion-associated small transmembrane (FAST) proteins of the avian (ARV) and Nelson Bay (NBV) reoviruses are the smallest known viral membrane fusion proteins, and are virulence determinants of the fusogenic reoviruses.
Tim Key, Roy Duncan
doaj   +1 more source

Human papillomavirus 16 L2 inhibits the transcriptional activation function, but not the DNA replication function, of HPV-16 E2 [PDF]

open access: yes, 2005
In this study we analysed the outcome of the interaction between HPV-16 L2 and E2 on the transactivation and DNA replication functions of E2. When E2 was expressed on its own, it transactivated a number of E2-responsive promoters but co-expression of L2 ...
A. Okoye   +32 more
core   +1 more source

Structure and Neutralization of Viral Fusion Proteins

open access: yes, 2023
Emerging infectious diseases remain persistent threats that are challenging to predict. Humanity has faced many terrible pandemics and will face more, but to pinpoint the specific time and place of an outbreak, the type of pathogen, and the consequences is effectively impossible.
openaire   +2 more sources

Classification of capped tubular viral particles in the family of Papovaviridae [PDF]

open access: yesJ.Phys.:Condens.Matter 18 (2006) S375-S387, 2005
A vital constituent of a virus is its protein shell, called the viral capsid, that encapsulates and hence provides protection for the viral genome. Viral capsids are usually spherical, and for a significant number of viruses exhibit overall icosahedral symmetry.
arxiv   +1 more source

Functional domains of the influenza A virus PB2 protein:identification of NP- and PB1-binding sites [PDF]

open access: yes, 2004
Influenza virus genomic RNA segments are packaged into ribonucleoprotein (RNP) structures by the PB1, PB2, and PA subunits of an RNA polymerase and a single-strand RNA-binding nucleoprotein (NP).
Digard, Paul   +3 more
core   +1 more source

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