The human polyoma JC virus agnoprotein acts as a viroporin - Test2 - elhamkhani - TriplyDB

The human polyoma JC virus agnoprotein acts as a viroporin

The human polyoma JC virus agnoprotein acts as a viroporin

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Infection by agnoprotein-negative mutants of polyomavirus JC and SV40 results in the release of virions that are mostly deficient in DNA content Human polyomavirus reactivation: disease pathogenesis and treatment approaches Molecular biology, epidemiology, and pathogenesis of progressive multifocal leukoencephalopathy, the JC virus-induced demyelinating disease of the human brain Emerging Roles of Viroporins Encoded by DNA Viruses: Novel Targets for Antivirals?Structural and Functional Properties of the Hepatitis C Virus p7 Viroporin New insights on human polyomavirus JC and pathogenesis of progressive multifocal leukoencephalopathy JC polyomavirus (JCV) and monoclonal antibodies: friends or potential foes?Human polyomaviruses in skin diseases.Use of genetically-encoded calcium indicators for live cell calcium imaging and localization in virus-infected cells The human metapneumovirus small hydrophobic protein has properties consistent with those of a viroporin and can modulate viral fusogenic activity.The SV40 late protein VP4 is a viroporin that forms pores to disrupt membranes for viral release.BKV agnoprotein interacts with α-soluble N-ethylmaleimide-sensitive fusion attachment protein, and negatively influences transport of VSVG-EGFP.JC virus encephalopathy is associated with a novel agnoprotein-deletion JCV variant.The viroporin activity of the minor structural proteins VP2 and VP3 is required for SV40 propagation.Essential roles of Leu/Ile/Phe-rich domain of JC virus agnoprotein in dimer/oligomer formation, protein stability and splicing of viral transcripts Rotavirus disrupts calcium homeostasis by NSP4 viroporin activity Nuclear magnetic resonance structure revealed that the human polyomavirus JC virus agnoprotein contains an α-helix encompassing the Leu/Ile/Phe-rich domain.The agnoprotein of polyomavirus JC is released by infected cells: evidence for its cellular uptake by uninfected neighboring cells.Emerging From the Unknown: Structural and Functional Features of Agnoprotein of Polyomaviruses.Cysteine residues in the major capsid protein, Vp1, of the JC virus are important for protein stability and oligomer formation.Agnogene deletion in a novel pathogenic JC virus isolate impairs VP1 expression and virion production Agnoprotein of polyomavirus BK interacts with proliferating cell nuclear antigen and inhibits DNA replication.JC virus nucleotides 376-396 are critical for VP1 capsid protein expression.Viral miniproteins The Simian virus 40 late viral protein VP4 disrupts the nuclear envelope for viral release.NLRP3 Inflammasome Activation by Viroporins of Animal Viruses Recombinant Dengue virus protein NS2B alters membrane permeability in different membrane models Viroporins customize host cells for efficient viral propagation.Viroporin activity of the JC polyomavirus is regulated by interactions with the adaptor protein complex 3.Bovine ephemeral fever rhabdovirus α1 protein has viroporin-like properties and binds importin β1 and importin 7.Differences in T cell cytotoxicity and cell death mechanisms between progressive multifocal leukoencephalopathy, herpes simplex virus encephalitis and cytomegalovirus encephalitis.Hepatitis C virus p7-a viroporin crucial for virus assembly and an emerging target for antiviral therapy.Structure-based release analysis of the JC virus agnoprotein regions: A role for the hydrophilic surface of the major alpha helix domain in release.The Presumed Polyomavirus Viroporin VP4 of Simian Virus 40 or Human BK Polyomavirus Is Not Required for Viral Progeny Release.Hepatitis E virus ORF3 is a functional ion channel required for release of infectious particles Entry, infection, replication, and egress of human polyomaviruses: an update.Comparing effects of BK virus agnoprotein and herpes simplex-1 ICP47 on MHC-I and MHC-II expression.JC virus agnoprotein enhances large T antigen binding to the origin of viral DNA replication: evidence for its involvement in viral DNA replication.Role of JC virus agnoprotein in virion formation.Human polyomavirus JC small regulatory agnoprotein forms highly stable dimers and oligomers: implications for their roles in agnoprotein function

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The human polyoma JC virus agnoprotein acts as a viroporin

http://www.wikidata.org/entity/Q27315541

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2010 nî lūn-bûn

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2010 թուականի Մարտին հրատարակուած գիտական յօդուած

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2010 թվականի մարտին հրատարակված գիտական հոդված

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2010年の論文

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2010年論文

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2010年論文

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2010年論文

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2010年论文

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The human polyoma JC virus agnoprotein acts as a viroporin

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The human polyoma JC virus agnoprotein acts as a viroporin

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The human polyoma JC virus agnoprotein acts as a viroporin

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The human polyoma JC virus agnoprotein acts as a viroporin

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The human polyoma JC virus agnoprotein acts as a viroporin

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The human polyoma JC virus agnoprotein acts as a viroporin

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The human polyoma JC virus agnoprotein acts as a viroporin

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Hirofumi Sawa

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Kazuo Nagashima

http://www.w3.org/2001/XMLSchema#string

Shinya Tanaka

http://www.w3.org/2001/XMLSchema#string

Tadaki Suzuki

http://www.w3.org/2001/XMLSchema#string

Takashi Kimura

http://www.w3.org/2001/XMLSchema#string

William W Hall

http://www.w3.org/2001/XMLSchema#string

Yasuko Orba

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Yuji Sunden

http://www.w3.org/2001/XMLSchema#string

Yuki Okada

http://www.w3.org/2001/XMLSchema#string

P2860

A very late viral protein triggers the lytic release of SV40

Naked2 acts as a cargo recognition and targeting protein to ensure proper delivery and fusion of TGF-alpha containing exocytic vesicles at the lower lateral membrane of polarized MDCK cells.

Mechanism of the spatio-temporal regulation of Ras and Rap1.

Diacylglycerol kinase delta suppresses ER-to-Golgi traffic via its SAM and PH domains

A simple method for displaying the hydropathic character of a protein

Phase separation of integral membrane proteins in Triton X-114 solution

Expanded dynamic range of fluorescent indicators for Ca(2+) by circularly permuted yellow fluorescent proteins.

Influenza virus M2 protein has ion channel activity.

Predicting the orientation of eukaryotic membrane-spanning proteins.

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