The Isomerase Active Site of Cyclophilin A Is Critical for Hepatitis C Virus Replication - Test2 - elhamkhani - TriplyDB

The Isomerase Active Site of Cyclophilin A Is Critical for Hepatitis C Virus Replication

The Isomerase Active Site of Cyclophilin A Is Critical for Hepatitis C Virus Replication

http://www.wikidata.org/entity/Q27489053

about

Cyclosporin A associated helicase-like protein facilitates the association of hepatitis C virus RNA polymerase with its cellular cyclophilin B Current management and perspectives for HCV recurrence after liver transplantation Structure and functionality in flavivirus NS-proteins: perspectives for drug design Hepatitis C virus NS5B and host cyclophilin A share a common binding site on NS5A Inhibition of cyclophilins alters lipid trafficking and blocks hepatitis C virus secretion A host YB-1 ribonucleoprotein complex is hijacked by hepatitis C virus for the control of NS3-dependent particle production Chaperones in hepatitis C virus infection Curing a viral infection by targeting the host: the example of cyclophilin inhibitors Cyclophilin Inhibitors Remodel the Endoplasmic Reticulum of HCV-Infected Cells in a Unique Pattern Rendering Cells Impervious to a Reinfection Essential Role of Cyclophilin A for Hepatitis C Virus Replication and Virus Production and Possible Link to Polyprotein Cleavage Kinetics SCY-635, a Novel Nonimmunosuppressive Analog of Cyclosporine That Exhibits Potent Inhibition of Hepatitis C Virus RNA Replication In Vitro Acetylation regulates Cyclophilin A catalysis, immunosuppression and HIV isomerization Structure and evolution of the spliceosomal peptidyl-prolyl cis-trans isomerase Cwc27 Structural and biochemical characterization of the human cyclophilin family of peptidyl-prolyl isomerases Characterization of the Anti-HCV Activities of the New Cyclophilin Inhibitor STG-175 DEB025 (Alisporivir) inhibits hepatitis C virus replication by preventing a cyclophilin A induced cis-trans isomerisation in domain II of NS5A Both Cyclophilin Inhibitors and Direct-Acting Antivirals Prevent PKR Activation in HCV-Infected Cells.A major determinant of cyclophilin dependence and cyclosporine susceptibility of hepatitis C virus identified by a genetic approach Cyclophilin A-regulated ubiquitination is critical for RIG-I-mediated antiviral immune responses.Regulation of de novo-initiated RNA synthesis in hepatitis C virus RNA-dependent RNA polymerase by intermolecular interactions.Systematic identification of novel, essential host genes affecting bromovirus RNA replication.Cyclophilin A associates with enterovirus-71 virus capsid and plays an essential role in viral infection as an uncoating regulator 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 cryptic sensor for HIV-1 activates antiviral innate immunity in dendritic cells.Domain 3 of NS5A protein from the hepatitis C virus has intrinsic alpha-helical propensity and is a substrate of cyclophilin A.Bioengineering and semisynthesis of an optimized cyclophilin inhibitor for treatment of chronic viral infection.The requirement for nucleoporin NUP153 during human immunodeficiency virus type 1 infection is determined by the viral capsid.Cyclophilin and NS5A inhibitors, but not other anti-hepatitis C virus (HCV) agents, preclude HCV-mediated formation of double-membrane-vesicle viral factories Discovery of Novel Small Molecule Anti-HCV Agents via the CypA Inhibitory Mechanism Using O-Acylation-Directed Lead Optimization.The Novel Cyclophilin Inhibitor CPI-431-32 Concurrently Blocks HCV and HIV-1 Infections via a Similar Mechanism of Action.Treatment of chronic hepatitis C in liver transplant candidates and recipients: Where do we stand?A Proline-Tryptophan Turn in the Intrinsically Disordered Domain 2 of NS5A Protein Is Essential for Hepatitis C Virus RNA Replication Cyclosporin A inhibits the replication of diverse coronaviruses Hepatitis C virus-host interactions, replication, and viral assembly Development of a flow cytometry live cell assay for the screening of inhibitors of hepatitis C virus (HCV) replication.Conformational plasticity of an enzyme during catalysis: intricate coupling between cyclophilin A dynamics and substrate turnover.Insights into the roles of cyclophilin A during influenza virus infection.Two-Year Follow-Up Analysis of Telaprevir-Based Antiviral Triple Therapy for HCV Recurrence in Genotype 1 Infected Liver Graft Recipients as a First Step towards Modern HCV Therapy.Correlation of naturally occurring HIV-1 resistance to DEB025 with capsid amino acid polymorphisms

P2860

Q21135500-3BA64B74-41FE-46FE-A8FF-678F5A0ED0DB Q22299427-D96FFAF3-7C8E-46A2-8E3B-83DC460EDEDC Q23011530-0C68FA05-ED15-44E1-8496-D64E8070C1FB Q24303838-B29DCDB9-8562-429A-814C-CA87EE636D6A Q24308039-E5FA6C25-F915-4503-8C77-0D09B1A2437B Q24320237-0496E955-F2B6-4116-80DD-668E2E0E4D42 Q26771251-D26EA1D0-1676-4240-BF45-ABB3558630A0 Q26828727-059828FB-6BCE-4571-876F-BA9D5D3561E3 Q27468931-EB5D7E67-B810-4F55-8CE8-28AAFE437650 Q27489037-09B694F9-492A-4EE2-9C11-E351AF21D882 Q27490844-0E86A587-732A-440C-990D-5058F2F8D580 Q27660416-618CE5E9-A303-485B-9BA1-34628BF8F274 Q27696314-2927BB64-177C-4ECA-9AF9-F4100FD08AA7 Q28289498-FECC669B-027E-4B1D-BDD4-25F780C84D9D Q28551538-4E314109-6C88-4A7B-A81B-F1DFF2910865 Q28748683-0983DB4B-3DB4-4F39-B525-E93B3352E195 Q33565080-E385B85B-BA7A-478F-91F1-313DCFD18637 Q33707739-34270668-CC81-44BB-A8D9-00286366672B Q33835048-6ED6A5E3-BBA2-4E02-B37F-217D49C1E954 Q33877412-1A0418F2-D192-45A8-8328-0E29B9DE8C11 Q34018821-9DC08363-9C35-47CF-A55B-5AB0A73EF542 Q34282430-FE6ED94B-C7F7-405F-8B49-952897411606 Q34329744-1EECA250-AF55-49B7-AC16-AEB2966DFA80 Q34332546-24E231CA-0A7F-48F7-A481-58A2A3EDE20C Q34635742-859B3966-C75E-4F8D-ACD1-63359F89C334 Q35063336-8C9CEC0F-4206-4EF3-A206-7063CA3D6C64 Q35108069-F08DAC36-20A1-44E7-AC7B-7680EFB30F1C Q35140243-B878780A-9334-45C7-AF0C-6FC9D879D68A Q35385005-FCE81BA7-97E8-434B-8289-1F034B27F8CF Q35656614-2762BD3B-9FFC-4DD6-BA75-4E96F84559CE Q35742761-B9ED65BE-BEBB-4B9D-938B-2F6DCE666932 Q35790393-6FDC1F41-7582-42A7-8C43-30E588A28174 Q35905354-EC9FF0C8-3803-4DDF-9106-C28F10A6E6AF Q35960586-66CBE98A-AA9A-414F-BCA0-4D13546A0077 Q36427976-CE77B970-2188-40B7-8648-61A3EA3B0073 Q36446336-C7C36C6F-F4E2-4A7D-AD76-D7871E5BF113 Q36518422-CC57268E-A274-470F-A20D-1923A336429A Q36586871-9529AA47-60AB-4A66-B443-5D7DCFDD3FFC Q36855565-D0CDCD1F-B4A2-4EBA-BBC8-00C26D0198AB Q36993953-EC767411-1ACD-4311-A4AA-51377DBCCCC6

P2860

The Isomerase Active Site of Cyclophilin A Is Critical for Hepatitis C Virus Replication

http://www.wikidata.org/entity/Q27489053

description

2009 nî lūn-bûn

@nan

2009 թուականի Յունիսին հրատարակուած գիտական յօդուած

@hyw

2009 թվականի հունիսին հրատարակված գիտական հոդված

@hy

2009年の論文

@ja

2009年論文

@yue

2009年論文

@zh-hant

2009年論文

@zh-hk

2009年論文

@zh-mo

2009年論文

@zh-tw

2009年论文

@wuu

name

The Isomerase Active Site of Cyclophilin A Is Critical for Hepatitis C Virus Replication

@ast

The Isomerase Active Site of Cyclophilin A Is Critical for Hepatitis C Virus Replication

@en

The Isomerase Active Site of Cyclophilin A Is Critical for Hepatitis C Virus Replication

@nl

type

label

The Isomerase Active Site of Cyclophilin A Is Critical for Hepatitis C Virus Replication

@ast

The Isomerase Active Site of Cyclophilin A Is Critical for Hepatitis C Virus Replication

@en

The Isomerase Active Site of Cyclophilin A Is Critical for Hepatitis C Virus Replication

@nl

prefLabel

The Isomerase Active Site of Cyclophilin A Is Critical for Hepatitis C Virus Replication

@ast

The Isomerase Active Site of Cyclophilin A Is Critical for Hepatitis C Virus Replication

@en

The Isomerase Active Site of Cyclophilin A Is Critical for Hepatitis C Virus Replication

@nl

P1433

Q27489053-F49A420C-0680-40CF-988F-B8DD675EFD2C

P1476

Q27489053-BAB52E33-1F72-4E8F-94EB-BBA3C55D6CD0

P2093

Q27489053-48E0C9F8-F89D-4B7C-87B4-D514322CA725

Q27489053-4ADA35CC-58DC-43D2-9EB8-F4E71D3DACB1

Q27489053-4AE3E8E0-C6F2-4F3E-AB0B-B8EDA92FF365

Q27489053-86DEC829-7814-4C14-BECC-516D9DC908BD

Q27489053-87EC310A-3B8C-478A-A8E1-C678C30BEFC2

Q27489053-B7732CC2-725A-40A9-B4D7-8877F25AA2CB

Q27489053-B827C9C3-FF80-45A2-AE53-D557A1C8AC21

Q27489053-D8FA887C-4F3A-4626-B571-41F69890F1D5

P2860

Q27489053-0C8DDAFC-F918-4D44-8CED-9DB77152EF99

Q27489053-0D28CA9E-0CAD-4160-8C7D-E35055C91DB3

Q27489053-15BD5B0F-1DA5-4270-8181-93A27D9E1D26

Q27489053-295F9DB3-6EE5-4F17-95C4-D21A7642E948

Q27489053-2D7EAD3C-AA02-4DE4-A1F2-3D7A98EE19EC

Q27489053-2FA0C969-370D-4522-BF4A-A16B1446BAE8

Q27489053-31A069EE-AC5E-4CB9-87E3-63FB0598217C

Q27489053-34954A13-3405-4563-97AF-7FDFF70F68BC

Q27489053-38142058-06B5-460F-BF1C-B9D5EDD5EFE3

Q27489053-3CF1A413-A6CE-4841-BFC4-62F89A88D4AC

P304

Q27489053-3FC2DAAE-8391-4D0A-8918-5E7C97B9458A

P31

Q27489053-1FF5FDB1-16AD-48BD-99B6-5304759A260A

P3181

Q27489053-F3257B46-B6B5-4E16-BA4C-62B160576EAF

P356

Q27489053-3FFB4F47-EB8A-44F0-A607-CC356C7275F4

P407

Q27489053-6A23DA7E-087F-440F-9228-0A92902DB92E

P433

Q27489053-FDE22740-0EF5-4EE3-ACDF-492359ABBF3C

P478

Q27489053-C69CC18A-E430-4536-9CD8-FCE443844CCD

P50

Q27489053-534581D1-E6B7-40AD-97DD-83AAD5EB5AC7

P577

Q27489053-48840D45-868B-482D-A7EB-F3F4B90C401D

P698

Q27489053-63EBE099-0CF4-48D6-B04E-19592CF99F90

P921

Q27489053-D350A8F3-A284-41A9-92FC-BE3DB8EF8F32

P932

Q27489053-92A73B81-DB94-462D-AE31-ED038C633F2E

P3181

P356

JBC.M109.007625

P1433

Journal of Biological Chemistry

P1476

The Isomerase Active Site of Cyclophilin A Is Critical for Hepatitis C Virus Replication

@en

P2093

Feng Yang

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

Gregoire Vuagniaux

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

Michael Bobardt

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

Noayo Sakamoto

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

Philippe Gallay

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

Suganya Selvarajah

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

Tanya Parkinson

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

Udayan Chatterji

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

P2860

Cyclophilin A regulates HIV-1 infectivity, as demonstrated by gene targeting in human T cells

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

Inhibition of HIV-1 multiplication by antisense U7 snRNAs and siRNAs targeting cyclophilin A

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

The hydrophobic pocket of cyclophilin is the binding site for the human immunodeficiency virus type 1 Gag polyprotein

The cyclophilins

Diverse Effects of Cyclosporine on Hepatitis C Virus Strain Replication

Interference of hepatitis C virus RNA replication by short interfering RNAs

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

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

P304

16998-7005

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

P31

scholarly article

P3181

2143469

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

P356

10.1074/JBC.M109.007625

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

P407

P433

25

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

P478

284

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

P50

P577

2009-06-19T00:00:00Z

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

P698

19380579

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

P921

P932

2719337

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