Results 51 to 60 of about 263,074 (309)

Cryotomography of budding influenza a virus reveals filaments with diverse morphologies that mostly do not bear a genome at their distal end [PDF]

open access: yes, 2013
Influenza viruses exhibit striking variations in particle morphology between strains. Clinical isolates of influenza A virus have been shown to produce long filamentous particles while laboratory-adapted strains are predominantly spherical.
Swetha Vijayakrishnan   +29 more
core   +1 more source

ASFV pE146L-induced ER remodeling is essential for viral replication

open access: yesJournal of Virology
African swine fever virus (ASFV) causes a severe hemorrhagic disease, posing a significant threat to the global pig industry. Although the ASFV encodes nearly 200 proteins, the functions of many remain unknown.
Yilin Guo   +12 more
doaj   +1 more source

Zika Virus NS2A-Mediated Virion Assembly

open access: yesmBio, 2019
The flavivirus virion consists of an envelope outer layer, formed by envelope (E) and membrane (M) proteins on a lipid bilayer, and an internal core, formed by capsid (C) protein and genomic RNA. The molecular mechanism of flavivirus assembly is not well
Xianwen Zhang   +7 more
doaj   +1 more source

Phosphatidylinositol 4‐kinase as a target of pathogens—friend or foe?

open access: yesFEBS Letters, EarlyView.
This graphical summary illustrates the roles of phosphatidylinositol 4‐kinases (PI4Ks). PI4Ks regulate key cellular processes and can be hijacked by pathogens, such as viruses, bacteria and parasites, to support their intracellular replication. Their dual role as essential host enzymes and pathogen cofactors makes them promising drug targets.
Ana C. Mendes   +3 more
wiley   +1 more source

A highly conserved basic motif in the wing domain of portal protein is necessary for oligomerization and incorporation in phage P22

open access: yesJournal of Virology
The dodecameric portal ring complex plays a critical role in the assembly of most double-stranded DNA (dsDNA) viruses and bacteriophages. The fidelity of ring oligomerization and incorporation of a single 12-mer portal ring is driven by interactions with
Makayla N. Leroux   +3 more
doaj   +1 more source

An Alphavirus E2 Membrane-Proximal Domain Promotes Envelope Protein Lateral Interactions and Virus Budding

open access: yesmBio, 2017
Alphaviruses are members of a group of small enveloped RNA viruses that includes important human pathogens such as Chikungunya virus and the equine encephalitis viruses.
Emily A. Byrd, Margaret Kielian
doaj   +1 more source

Y-Box Binding Protein 1 Interacts with Dengue Virus Nucleocapsid and Mediates Viral Assembly

open access: yesmBio, 2022
Infection with dengue virus (DENV) induces vast rearrangements of the endoplasmic reticulum, which allows the compartmentalization of viral RNA replication and particle assembly. Both processes occur in concert with viral and cellular proteins.
Mayra Diosa-Toro   +5 more
doaj   +1 more source

Protein pyrophosphorylation by inositol pyrophosphates — detection, function, and regulation

open access: yesFEBS Letters, EarlyView.
Protein pyrophosphorylation is an unusual signaling mechanism that was discovered two decades ago. It can be driven by inositol pyrophosphate messengers and influences various cellular processes. Herein, we summarize the research progress and challenges of this field, covering pathways found to be regulated by this posttranslational modification as ...
Sarah Lampe   +3 more
wiley   +1 more source

Virus imprinted particles [PDF]

open access: yes, 2013
Living organisms are capable of identifying and neutralizing exogenous threats. Such a distinguishing feature, developed over millions of years of evolution, is achieved thanks to the immune system, and in particular through the molecular recognition ...
Cumbo, Alessandro
core   +1 more source

Assembly and Cellular Exit of Coronaviruses: Hijacking an Unconventional Secretory Pathway from the Pre-Golgi Intermediate Compartment via the Golgi Ribbon to the Extracellular Space

open access: yesCells, 2021
Coronaviruses (CoVs) assemble by budding into the lumen of the intermediate compartment (IC) at the endoplasmic reticulum (ER)-Golgi interface. However, why CoVs have chosen the IC as their intracellular site of assembly and how progeny viruses are ...
Jaakko Saraste, Kristian Prydz
doaj   +1 more source

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