DEB025 (Alisporivir) inhibits hepatitis C virus replication by preventing a cyclophilin A induced cis-trans isomerisation in domain II of NS5A - Wikidata - wikimedia - TriplyDB

DEB025 (Alisporivir) inhibits hepatitis C virus replication by preventing a cyclophilin A induced cis-trans isomerisation in domain II of NS5A

DEB025 (Alisporivir) inhibits hepatitis C virus replication by preventing a cyclophilin A induced cis-trans isomerisation in domain II of NS5A

http://www.wikidata.org/entity/Q28748683

about

sameAs

Hepatitis C virus NS5B and host cyclophilin A share a common binding site on NS5A Ca2+ toxicity and mitochondrial damage in acute pancreatitis: translational overview Chaperones in hepatitis C virus infection Host-Targeting Agents to Prevent and Cure Hepatitis C Virus Infection Suppression of coronavirus replication by cyclophilin inhibitors Oral antiviral therapies for chronic hepatitis C infection Future classes of hepatitis C virus therapeutic agents Direct acting antivirals for the treatment of chronic viral hepatitis Cyclophilin Inhibitors Remodel the Endoplasmic Reticulum of HCV-Infected Cells in a Unique Pattern Rendering Cells Impervious to a Reinfection Inhibitor-Based Therapeutics for Treatment of Viral Hepatitis Elucidating novel hepatitis C virus-host interactions using combined mass spectrometry and functional genomics approaches Infection Counter: Automated Quantification of in Vitro Virus Replication by Fluorescence Microscopy Cyclosporin A inhibits the influenza virus replication through cyclophilin A-dependent and -independent pathways An analogue of the antibiotic teicoplanin prevents flavivirus entry in vitro Genetic characterization of hepatitis C virus in long-term RNA replication using Li23 cell culture systems Characterization of the Anti-HCV Activities of the New Cyclophilin Inhibitor STG-175 Selective Inhibitor of Nuclear Export (SINE) Compounds Alter New World Alphavirus Capsid Localization and Reduce Viral Replication in Mammalian Cells Randomised clinical trial: alisporivir combined with peginterferon and ribavirin in treatment-naïve patients with chronic HCV genotype 1 infection (ESSENTIAL II).Both Cyclophilin Inhibitors and Direct-Acting Antivirals Prevent PKR Activation in HCV-Infected Cells.The combination of alisporivir plus an NS5A inhibitor provides additive to synergistic anti-hepatitis C virus activity without detectable cross-resistance.The TPR domain in the host Cyp40-like cyclophilin binds to the viral replication protein and inhibits the assembly of the tombusviral replicase Novel indole-2-carboxamide compounds are potent broad-spectrum antivirals active against western equine encephalitis virus in vivo.Profile of alisporivir and its potential in the treatment of hepatitis C.Hepatitis C NS5A protein: two drug targets within the same protein with different mechanisms of resistance.A cell culture adapted HCV JFH1 variant that increases viral titers and permits the production of high titer infectious chimeric reporter viruses.Resistance patterns associated with HCV NS5A inhibitors provide limited insight into drug binding.Antiviral drugs against hepatitis C virus.Cyclophilin and NS5A inhibitors, but not other anti-hepatitis C virus (HCV) agents, preclude HCV-mediated formation of double-membrane-vesicle viral factories Inhibitors of peptidyl proline isomerases as antivirals in hepatitis C and other viruses.New developments in small molecular compounds for anti-hepatitis C virus (HCV) therapy.Discovery of Novel Small Molecule Anti-HCV Agents via the CypA Inhibitory Mechanism Using O-Acylation-Directed Lead Optimization.Analysis of hepatitis C virus intrahost diversity across the coding region by ultradeep pyrosequencing Cyclosporin A inhibits the replication of diverse coronaviruses Treating hepatitis C infection by targeting the host.Targeting the cyclophilin domain of Ran-binding protein 2 (Ranbp2) with novel small molecules to control the proteostasis of STAT3, hnRNPA2B1 and M-opsin.Coxsackievirus mutants that can bypass host factor PI4KIIIβ and the need for high levels of PI4P lipids for replication.Hepatitis C viral kinetics: the past, present, and future.Hepatitis C virus: virology and life cycle Correlation of naturally occurring HIV-1 resistance to DEB025 with capsid amino acid polymorphisms The C terminus of NS5A domain II is a key determinant of hepatitis C virus genome replication, but is not required for virion assembly and release.

P2860

Q24303838-0E090962-9592-4641-8FCC-5C7B6BDB6190 Q26744695-F7D4DAEF-5ECA-449A-ACFF-E46BDCF3F72E Q26771251-F3C88CF1-B368-4053-B4F8-CA713CC4B90E Q26779128-C84CD44E-70F1-4CAA-BA7E-E7B6D3D0D1AC Q26825245-3084124E-21CC-4195-8B1C-F1A55CAE9ABE Q26830426-C6C0BDCD-EDAF-4F43-847F-3E1A759D0832 Q27009321-EC955D6B-050C-462B-8D07-5CF9F2CC9008 Q27022216-B2FA0751-ACE9-414F-BA8B-92680AE6ABE7 Q27468931-B2DAECB9-E121-4AD2-8DCF-4B1FF2BD2DCE Q28073697-54C25F8A-E87C-4855-9575-56B8C6C4ED08 Q28115639-7115C1F0-3E4D-4E4D-B726-70D882F0D512 Q28364857-42C471F8-8D0A-4B80-98B7-692EE1CEA91F Q28483731-33BDF15C-2AD4-4D80-B3E1-C56E7F2DFBA2 Q28483817-02FA9A68-7ED2-4B0A-8DA7-D552A6984912 Q28540849-8A3A602C-D9BF-4E9A-9504-C1ADA52DFDB0 Q28551538-A2158B52-1E57-43D8-BFBA-F0E35CCD5357 Q28554595-330621F1-BDE9-41F2-99FD-8E01E59BAC2F Q33424900-FF9A8BA4-3FCE-4099-975B-3D2FAE824729 Q33565080-B0DC2FD7-8C14-4690-98B1-DBC85D554AAD Q33797891-9DC9B54F-0818-4F3B-9600-73F7E1E46E7E Q34162254-407DA53E-742B-4F9D-A4FB-E61AA6DFC0AE Q34261735-7AC2583F-9AF2-4217-8780-9EB2462335EF Q34329744-FEEE2A89-863A-4372-A435-5CA04ED2D1CC Q34332546-459B4A57-C345-4599-A521-B53FF0FB4E12 Q34427768-1EA30CA5-26FE-43D7-A1C2-1852D05B82F6 Q34580799-3949350C-3151-4D98-8C0C-D47BEC679B4E Q35105567-531ACFD2-9B39-4102-8C71-A73085EEE69C Q35385005-041910BF-41D2-4BD0-964F-0710A0CF55DB Q35400246-E28B2A6E-4B6A-4719-BA0E-C64C59AC2F23 Q35653358-1F045781-F5F4-46D9-A839-7B50739275DF Q35656614-BA82139C-6AA7-44FA-84D5-9E5A9EE9C9E3 Q35826862-E193846E-9031-4666-8DCC-0818444492C9 Q35960586-5C9F301C-536F-4241-BE89-1581A56447F3 Q35992555-8CC8092E-8C4A-4DDB-8594-9CDC4C5E83BA Q36016095-63973260-7553-479C-AFF8-E7C4560D1414 Q36387676-06E17DD7-4A14-4F03-B950-CBE83678C0C6 Q36645517-FCA6A24A-D9AA-461B-AB95-B8B6AD028093 Q36756358-2CABB33F-7BBE-4621-8392-DAA57241648A Q36993953-78F3CB44-6A24-4087-A7DB-10990C3AE97B Q37006634-6A7C3BB6-FF04-48A2-8684-1E9C1559A775

P2860

DEB025 (Alisporivir) inhibits hepatitis C virus replication by preventing a cyclophilin A induced cis-trans isomerisation in domain II of NS5A

http://www.wikidata.org/entity/Q28748683

description

2010 nî lūn-bûn

@nan

2010 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած

@hyw

2010 թվականի հոտեմբերին հրատարակված գիտական հոդված

@hy

2010年の論文

@ja

2010年論文

@yue

2010年論文

@zh-hant

2010年論文

@zh-hk

2010年論文

@zh-mo

2010年論文

@zh-tw

2010年论文

@wuu

name

DEB025 (Alisporivir) inhibits ...... erisation in domain II of NS5A

@ast

DEB025 (Alisporivir) inhibits ...... erisation in domain II of NS5A

@en

DEB025 (Alisporivir) inhibits ...... erisation in domain II of NS5A

@nl

type

label

DEB025 (Alisporivir) inhibits ...... erisation in domain II of NS5A

@ast

DEB025 (Alisporivir) inhibits ...... erisation in domain II of NS5A

@en

DEB025 (Alisporivir) inhibits ...... erisation in domain II of NS5A

@nl

prefLabel

DEB025 (Alisporivir) inhibits ...... erisation in domain II of NS5A

@ast

DEB025 (Alisporivir) inhibits ...... erisation in domain II of NS5A

@en

DEB025 (Alisporivir) inhibits ...... erisation in domain II of NS5A

@nl

P1433

Q28748683-5B034FDE-00B5-4A37-A23B-32817CFF7F13

P1476

Q28748683-8942605A-C7BA-4D51-8FA6-F9985D3D0C76

P2093

Q28748683-359EE762-EE86-4DCE-AEAA-088EB6E4BE6C

Q28748683-369B6A3C-05C7-470E-96B5-910ED8D7D142

Q28748683-45DC1246-9F76-4747-AA57-7E7451A8A3F4

Q28748683-6617A875-E3CA-447F-843F-84716913B4CE

Q28748683-85B76A84-9EDC-4674-AC7B-926FF058D3D6

Q28748683-E526B827-3334-4589-BA13-19A7974602B0

Q28748683-EC28B7C7-92F8-4DC0-B8CA-CDA23A7FEFAA

P2860

Q28748683-015B8B67-36E5-4975-AA22-6568F51627EA

Q28748683-0245BCE6-ABCB-4E8B-B496-81B1BAC69419

Q28748683-062B5B85-DBE4-4A6E-93D4-07C6F3D8B87B

Q28748683-0983DB4B-3DB4-4F39-B525-E93B3352E195

Q28748683-0C50884F-EBD7-4B46-8868-EFBB35552771

Q28748683-1260E282-E6BB-42CD-B9F7-A1500D53C074

Q28748683-1408D7B1-EC8C-4721-883B-A8A5E7E5B39F

Q28748683-1673DEAD-BE75-4F9D-BECC-CB800541475A

Q28748683-16C781B4-C5C1-4832-8F8F-5C87EF49587D

Q28748683-1705E997-A107-487D-B1A2-954B573E5DD8

P304

Q28748683-CB51C3A4-4997-4642-B1F0-3E2439FFEE9B

P31

Q28748683-83346444-33CB-4A0F-8CF5-B7828DE7BC8B

P3181

Q28748683-440522A7-EE81-4FF2-ACC1-748BEC907704

P356

Q28748683-180425D5-C532-4012-889E-7284A66BEE9A

P407

Q28748683-E3CDC0B5-DE89-467A-966E-FEBDEBBA4549

P433

Q28748683-2A532728-87C3-45E7-AE40-22A7361E4091

P478

Q28748683-3F6D79FC-20ED-4079-ABBD-2407FBE513F2

P50

Q28748683-00D8F2EE-5D11-4426-BA1B-EEBCFB086F9B

Q28748683-056E69EC-D8C3-4898-82FF-872DF3084406

Q28748683-062B593B-4DFB-4038-8B6F-27426B0B8975

Q28748683-0F969721-AE0B-4413-9FED-B8577727B8D8

Q28748683-28DB4347-71FC-49DF-869D-C8BD73AEAF7D

Q28748683-56352432-E5CF-400E-BC85-F1394382CB89

Q28748683-A3E0D4AA-FEBA-4F77-A409-8820491E26B4

Q28748683-C9A6B478-AA45-4787-833B-97D7B276F33C

P577

Q28748683-C7BF7F0D-6EFB-4B8A-8E3B-BB0AAB83ADCF

P5875

Q28748683-868E618F-16CD-4881-880D-D42212A24FC3

P698

Q28748683-17FA4609-B269-434E-8DA8-9718A3D4A46F

P932

Q28748683-618FA3AB-EA74-480B-88D9-4F028A53FF4D

P3181

P356

JOURNAL.PONE.0013687

P1433

P1476

DEB025 (Alisporivir) inhibits ...... erisation in domain II of NS5A

@en

P2093

Carola Berger

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

Grégoire Vuagniaux

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

Joke Snoeck

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

Michael Bobardt

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

Philippe Gallay

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

Precious Lim

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

Udayan Chatterji

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

P2860

Cyclophilin B is a functional regulator of hepatitis C virus RNA polymerase

Phosphorylation of hepatitis C virus nonstructural protein 5A modulates its protein interactions and viral RNA replication

Debio 025, a cyclophilin binding molecule, is highly efficient in clearing hepatitis C virus (HCV) replicon-containing cells when used alone or in combination with specifically targeted antiviral therapy for HCV (STAT-C) inhibitors

Inhibition of human immunodeficiency virus type 1 replication in human cells by Debio-025, a novel cyclophilin binding agent

Mutations in Hepatitis C Virus RNAs Conferring Cell Culture Adaptation

Structure of the zinc-binding domain of an essential component of the hepatitis C virus replicase

Characterization of the Early Steps of Hepatitis C Virus Infection by Using Luciferase Reporter Viruses

NIM811, a Cyclophilin Inhibitor, Exhibits Potent In Vitro Activity against Hepatitis C Virus Alone or in Combination with Alpha Interferon

euHCVdb: the European hepatitis C virus database

Characterization of Hepatitis C Virus Subgenomic Replicon Resistance to Cyclosporine In Vitro

P304

e13687

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

P31

scholarly article

P3181

2143482

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

P356

10.1371/JOURNAL.PONE.0013687

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

P407

P433

10

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

P478

5

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

P50

Ralf Bartenschlager

Anne-Mieke Vandamme

Xavier Hanoulle

P577

2010-10-27T00:00:00Z

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

P5875

47718801

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

P698

21060866

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

P932

2965138

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