Results 31 to 40 of about 166,210 (263)

Protein Kinase C subtype δ interacts with Venezuelan equine encephalitis virus capsid protein and regulates viral RNA binding through modulation of capsid phosphorylation.

open access: yesPLoS Pathogens, 2020
Protein phosphorylation plays an important role during the life cycle of many viruses. Venezuelan equine encephalitis virus (VEEV) capsid protein has recently been shown to be phosphorylated at four residues.
Brian D Carey   +9 more
doaj   +1 more source

The GTPase Domain of MX2 Interacts with the HIV-1 Capsid, Enabling Its Short Isoform to Moderate Antiviral Restriction

open access: yesCell Reports, 2019
Summary: Myxovirus resistance 2 (MX2/MXB) is an interferon (IFN)-induced HIV-1 restriction factor that inhibits viral nuclear DNA accumulation. The amino-terminal domain of MX2 binds the viral capsid and is essential for inhibition.
Gilberto Betancor   +5 more
doaj   +1 more source

The capsid protein of human immunodeficiency virus: designing inhibitors of capsid assembly [PDF]

open access: yesThe FEBS Journal, 2009
The mature capsid of human immunodeficiency virus, HIV‐1, is formed by the assembly of copies of a capsid protein (CA). The C‐terminal domain of CA, CTD, is able to homodimerize and most of the dimerization interface is formed by a single α‐helix from each monomer.
openaire   +2 more sources

Diagnostic Potential of Parechovirus Capsid Proteins [PDF]

open access: yesJournal of Clinical Microbiology, 2003
ABSTRACT To study humoral and cellular immunity against human parechovirus type 1 (HPEV1), the viral capsid proteins VP0, VP1, and VP3 were expressed and purified as glutathione S -transferase (GST)-tagged recombinant proteins. The fusion proteins were used to raise antisera in rabbits.
Annu, Alho   +3 more
openaire   +2 more sources

Rab14 regulates the transport of human papillomavirus to the trans‐Golgi network for infectious cell entry

open access: yesFEBS Letters, EarlyView.
This study reveals that the small GTPase Rab14 is necessary for human papillomavirus (HPV) infection and plays an essential role in the transport of virions to the trans‐Golgi network (TGN). HPV in the early endosome (EE), which harbors GTP‐bound Rab14, is transported to the TGN through the switch of Rab14 from its GTP‐bound to GDP‐bound form.
Yoshiyuki Ishii, Iwao Kukimoto
wiley   +1 more source

Phosphoinositides and inositol phosphates as molecular glues

open access: yesFEBS Letters, EarlyView.
Inositol phosphates (IPs) and phosphoinositides (PIPs) regulate diverse eukaryotic processes. Beyond recruiting signaling proteins or acting as structural cofactors, recent studies suggest they mediate protein–protein interactions as natural molecular glues.
Aleshia Seaton‐Terry   +9 more
wiley   +1 more source

Structures of Three Actinobacteriophage Capsids: Roles of Symmetry and Accessory Proteins

open access: yesViruses, 2020
Here, we describe the structure of three actinobacteriophage capsids that infect Mycobacterium smegmatis. The capsid structures were resolved to approximately six angstroms, which allowed confirmation that each bacteriophage uses the HK97-fold to form ...
Jennifer Podgorski   +6 more
doaj   +1 more source

Simultaneous membrane and RNA binding by tick-borne encephalitis virus capsid protein.

open access: yesPLoS Pathogens, 2023
Tick-borne encephalitis virus is an enveloped, pathogenic, RNA virus in the family Flaviviridae, genus Flavivirus. Viral particles are formed when the nucleocapsid, consisting of an RNA genome and multiple copies of the capsid protein, buds through the ...
Lauri Ilmari Aurelius Pulkkinen   +8 more
doaj   +1 more source

Trypsin is associated with the rotavirus capsid and is activated by solubilization of outer capsid proteins

open access: yesJournal of General Virology, 2005
The rotavirus capsid is made up of three concentric protein layers. The outer layer, consisting of VP7 and VP4, is lost during virus entry into the host cell. Rotavirus field isolates can be adapted to high-titre growth in tissue culture by treatment with trypsin and by supplementing the culture medium with trypsin, which cleaves VP4 into two fragments,
Benureau, Yann   +4 more
openaire   +4 more sources

Importin 7 mediates the nuclear import of HIV‐1 integrase via a specific interacting interface

open access: yesFEBS Open Bio, EarlyView.
HIV‐1 integrase enables viral DNA integration into the host genome. By binding to the core domain of the host protein Importin 7 via its C‐terminal domain, the integrase is transported across the nuclear membrane into the nucleus, where integration of the viral genome into host DNA takes place. This translocation is a critical step for subsequent viral
Juana Bana   +5 more
wiley   +1 more source

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