Efficient inhibition of hepatitis B virus infection by acylated peptides derived from the large viral surface protein. - Test2 - elhamkhani - TriplyDB

Efficient inhibition of hepatitis B virus infection by acylated peptides derived from the large viral surface protein.

Efficient inhibition of hepatitis B virus infection by acylated peptides derived from the large viral surface protein.

http://www.wikidata.org/entity/Q33717942

about

Sodium taurocholate cotransporting polypeptide is a functional receptor for human hepatitis B and D virus Hepatitis B virus morphogenesis Viral and cellular determinants involved in hepadnaviral entry Fine mapping of pre-S sequence requirements for hepatitis B virus large envelope protein-mediated receptor interaction Properties of subviral particles of hepatitis B virus Advances and Challenges in Studying Hepatitis B Virus In Vitro NTCP and beyond: opening the door to unveil hepatitis B virus entry Applications of human hepatitis B virus preS domain in bio- and nanotechnology.Molecular biology of hepatitis B virus infection Bats carry pathogenic hepadnaviruses antigenically related to hepatitis B virus and capable of infecting human hepatocytes Hepatitis B virus molecular biology and pathogenesis Asian-Pacific clinical practice guidelines on the management of hepatitis B: a 2015 update.Neutralization epitope responsible for the hepatitis B virus subtype-specific protection in chimpanzees.Purinergic receptor functionality is necessary for infection of human hepatocytes by hepatitis delta virus and hepatitis B virus.Emerging antivirals for the treatment of hepatitis B.Mapping of the hepatitis B virus pre-S1 domain involved in receptor recognition Interferon impedes an early step of hepatitis delta virus infection.Strategies to eliminate HBV infection.Sodium-dependent bile salt transporters of the SLC10A transporter family: more than solute transporters.Proteoglycans act as cellular hepatitis delta virus attachment receptors.Cyclosporin A and its analogs inhibit hepatitis B virus entry into cultured hepatocytes through targeting a membrane transporter, sodium taurocholate cotransporting polypeptide (NTCP).Dysregulation of retinoic acid receptor diminishes hepatocyte permissiveness to hepatitis B virus infection through modulation of sodium taurocholate cotransporting polypeptide (NTCP) expression Selection of HBV preS1-binding penta-peptides by phage display.HBV life cycle: entry and morphogenesis.Interaction of human tumor viruses with host cell surface receptors and cell entry A Novel Tricyclic Polyketide, Vanitaracin A, Specifically Inhibits the Entry of Hepatitis B and D Viruses by Targeting Sodium Taurocholate Cotransporting Polypeptide.Inhibition of preS1-hepatocyte interaction by an array of recombinant human antibodies from naturally recovered individuals.Efficient Inhibition of Hepatitis B Virus Infection by a preS1-binding Peptide.Mucroporin-M1 inhibits hepatitis B virus replication by activating the mitogen-activated protein kinase (MAPK) pathway and down-regulating HNF4α in vitro and in vivo Molecular virology of hepatitis B virus for clinicians.Hepatitis B virus efficiently infects non-adherent hepatoma cells via human sodium taurocholate cotransporting polypeptide Sodium taurocholate cotransporting polypeptide mediates woolly monkey hepatitis B virus infection of Tupaia hepatocytes.A Scorpion Defensin BmKDfsin4 Inhibits Hepatitis B Virus Replication in Vitro.PreS1 epitope recognition in newborns after vaccination with the third-generation Sci-B-Vac vaccine and their relation to the antibody response to hepatitis B surface antigen.Hepatitis B Virus Polymerase Localizes to the Mitochondria, and Its Terminal Protein Domain Contains the Mitochondrial Targeting Signal.Immunotherapy With the PreS-based Grass Pollen Allergy Vaccine BM32 Induces Antibody Responses Protecting Against Hepatitis B Infection The first transmembrane domain of the hepatitis B virus large envelope protein is crucial for infectivity The pre-S1 and antigenic loop infectivity determinants of the hepatitis B virus envelope proteins are functionally independent.Human induced-pluripotent stem cell-derived hepatocyte-like cells as an in vitro model of human hepatitis B virus infection.Hepatitis B virus resistance to antiviral drugs: where are we going?

P2860

Q21128797-80FD578F-181E-4050-A5F4-3F4051330B3E Q24563883-677BABC0-B0CD-4DC2-B736-43A545191CD9 Q24563902-9191C9CB-EDA0-4E5B-A476-D3BDD946CAB6 Q24656570-4439A1D5-9105-485F-9B3F-9118F60A7115 Q24658234-94E4A027-C5FA-4A0B-86ED-A4210027C55D Q26771134-FCC352BD-C155-4C08-823F-0310E1B5D133 Q26999712-99DB0B41-1CC8-4D31-8303-A67F3A9F9196 Q27693188-23A02916-7996-40B0-9475-CAB83D96C17A Q28083478-1B4F8765-43F6-4853-A6B5-9F86AA02E951 Q28676360-4A4BCF7D-D5E7-4B5A-A730-177C26C491AF Q28818406-016A17CE-906A-4C89-9C0D-AEBE6BA21318 Q30391932-98DE4EC2-B7CA-495C-8DFA-21B0181B87F6 Q33245946-F3B49BF3-3885-4ACB-B204-C0A7AE3BC269 Q33781062-B4E5DC08-7549-4315-8D56-C5915CD78984 Q33801328-FD7EF8CA-86CE-46EA-AE0F-BAE7199523F0 Q33908723-4C6111B2-4F6F-4F6A-A97C-8709700C5DD7 Q33979916-4BD052A6-1AC9-4159-A031-4EA9F310AB6B Q34308129-35CB6BE8-A7F4-4C13-A849-9B130107D080 Q34382931-CC0EDC75-FEE6-45A7-A039-69A580660652 Q34625734-3CCF2DA8-AF58-4D6D-8FD0-652D2650E729 Q34693445-2AF7A3C9-34BD-429A-884B-EFACCCF43380 Q35126674-A0AA685D-5B64-4C53-BAD6-CE3BBC28BBC0 Q35195132-C8FDA90D-7230-4E6E-8C5D-7F5D46228543 Q35259698-B3C5D5C5-45CD-477B-92C8-717C5EF42387 Q35676027-62C99789-CFFE-4572-94F2-8A7926C16594 Q35778059-ADAF6160-2D6A-4716-BC60-33631E91F917 Q35926878-EFFF9185-5631-4420-BA2A-524F747739BA Q36069081-B243A3E5-1C24-42A1-A932-2B0DEE4133B1 Q36216315-A2D8973C-3E06-4A1D-88C3-8BB4ED0AA4A9 Q36282234-D69A2044-3124-4A04-96CE-788FCAC60465 Q36305699-E88E20B9-F87E-4BBC-915D-1F7813D8B5B8 Q36911797-F65C6C15-9C89-454B-85F2-787BCDE59A70 Q36946907-34B5AEAD-1DBC-499A-BA6A-951F7BCD1E66 Q37082600-001AAD4A-2DC1-4B7E-8836-9C3003FCFD43 Q37253020-A9CABCAB-C34C-45C6-872F-C91C75550ED8 Q37309327-99380575-E217-45DF-A36C-00FBA0CEC7FF Q37410736-86284C18-B0D4-4AC6-A992-0D4DCCE207BE Q37451938-5AC57D0A-56D9-4EB0-A258-9B04AE609DF7 Q37736696-6FC12EE6-6C1A-408C-81B9-38E03B62B36C Q37825963-DC6923F2-050D-4187-B060-4F699682D668

P2860

Efficient inhibition of hepatitis B virus infection by acylated peptides derived from the large viral surface protein.

http://www.wikidata.org/entity/Q33717942

description

2005 nî lūn-bûn

@nan

2005 թուականի Փետրուարին հրատարակուած գիտական յօդուած

@hyw

2005 թվականի փետրվարին հրատարակված գիտական հոդված

@hy

2005年の論文

@ja

2005年論文

@yue

2005年論文

@zh-hant

2005年論文

@zh-hk

2005年論文

@zh-mo

2005年論文

@zh-tw

2005年论文

@wuu

name

Efficient inhibition of hepati ...... e large viral surface protein.

@ast

Efficient inhibition of hepati ...... e large viral surface protein.

@en

type

label

Efficient inhibition of hepati ...... e large viral surface protein.

@ast

Efficient inhibition of hepati ...... e large viral surface protein.

@en

prefLabel

Efficient inhibition of hepati ...... e large viral surface protein.

@ast

Efficient inhibition of hepati ...... e large viral surface protein.

@en

P1433

Q33717942-119163D6-8CAF-4992-B541-E01F235C7334

P1476

Q33717942-4CB6DEDF-1DBE-45B4-9948-70C0BC17800E

P2093

Q33717942-3558963E-0513-4A6F-9FC1-B10129317FDA

Q33717942-4423DED2-3622-4A02-B906-DCB6EC29F9ED

Q33717942-6E49B617-0E27-4018-B7CA-D5DD113F0E70

P2860

Q33717942-07A4C837-1F84-4784-AA08-C0C0304238CA

Q33717942-0EA43509-718C-43AF-BC04-C4186243FDB3

Q33717942-1115100F-DB22-456B-A6F6-A75CD000A114

Q33717942-18229075-72AA-4FF6-9829-F7408B7656CF

Q33717942-1FE87C40-2550-4D5B-93B7-4E61A5E12101

Q33717942-2EE6BC85-31E3-4D53-BA4B-5B67DB378421

Q33717942-335B3369-05CD-4BD6-822E-B37A5C814FB5

Q33717942-33E4DD57-4414-42B8-9889-67F3CDB63231

Q33717942-4000D879-D4E1-425B-9533-2B720D33C941

Q33717942-48940DB6-1E6B-4551-91E9-8FCFB5BBFAD1

P304

Q33717942-50C6B72F-0482-4A4D-8F4B-4E9531D9A31E

P31

Q33717942-02EB53E1-A10F-4317-8542-275521267829

P356

Q33717942-28EAE1C1-6E23-4D03-A429-2DC18A1D8DD4

P433

Q33717942-04CB0F5F-A549-485A-886E-B63DF8CC8A9B

P478

Q33717942-5D7D9A35-0977-4EFC-8799-4EB0102DA233

P577

Q33717942-84AAF6A4-E06B-4E56-8E1C-B0C3B0AE365B

P698

Q33717942-A12B1358-CCC7-43F9-8855-2F6E42189DDF

P932

Q33717942-E4F6A69F-BA20-4444-852A-8571551E2DB9

P356

JVI.79.3.1613-1622.2005

P1433

Journal of Virology

P1476

Efficient inhibition of hepati ...... e large viral surface protein.

@en

P2093

Isabelle Cannie

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

Philippe Gripon

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

Stephan Urban

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

P2860

Structural and functional characterization of a monoclonal antibody specific for the preS1 region of hepatitis B virus

Crystal structure of a myristoylated CAP-23/NAP-22 N-terminal domain complexed with Ca2+/calmodulin

Receptor binding and membrane fusion in virus entry: the influenza hemagglutinin

Membrane fusion machines of paramyxoviruses: capture of intermediates of fusion

Infection process of the hepatitis B virus depends on the presence of a defined sequence in the pre-S1 domain

Role of the pre-S2 domain of the large envelope protein in hepatitis B virus assembly and infectivity

A short N-proximal region in the large envelope protein harbors a determinant that contributes to the species specificity of human hepatitis B virus.

Hepatitis B virus biology.

Production of hepatitis B virus in vitro by transient expression of cloned HBV DNA in a hepatoma cell line.

Virus of Pekin ducks with structural and biological relatedness to human hepatitis B virus

P304

1613-1622

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

P31

scholarly article

P356

10.1128/JVI.79.3.1613-1622.2005

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

P433

3

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

P478

79

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

P577

2005-02-01T00:00:00Z

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

P698

15650187

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

P932

544121

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