Domain 2 of nonstructural protein 5A (NS5A) of hepatitis C virus is natively unfolded.
about
Intrinsically unstructured domain 3 of hepatitis C Virus NS5A forms a "fuzzy complex" with VAPB-MSP domain which carries ALS-causing mutationsHepatitis C virus NS5B and host cyclophilin A share a common binding site on NS5AStructures of hepatitis C virus nonstructural proteins required for replicase assembly and functionCrystal Structure of a Novel Dimeric Form of NS5A Domain I Protein from Hepatitis C VirusHepatitis C Virus NS5A Protein Is a Substrate for the Peptidyl-prolyl cis/trans Isomerase Activity of Cyclophilins A and BThe crystal structure of NS5A domain 1 from genotype 1a reveals new clues to the mechanism of action for dimeric HCV inhibitorsSeed Sequence-Matched Controls Reveal Limitations of Small Interfering RNA Knockdown in Functional and Structural Studies of Hepatitis C Virus NS5A-MOBKL1B InteractionMetabolism of phosphatidylinositol 4-kinase IIIα-dependent PI4P Is subverted by HCV and is targeted by a 4-anilino quinazoline with antiviral activityCoordination of Hepatitis C Virus Assembly by Distinct Regulatory Regions in Nonstructural Protein 5ADEB025 (Alisporivir) inhibits hepatitis C virus replication by preventing a cyclophilin A induced cis-trans isomerisation in domain II of NS5ARNA Viruses: ROS-Mediated Cell Death.Simultaneous reduction and digestion of proteins with disulfide bonds for hydrogen/deuterium exchange monitored by mass spectrometry.A major determinant of cyclophilin dependence and cyclosporine susceptibility of hepatitis C virus identified by a genetic approachSmall molecules targeting hepatitis C virus-encoded NS5A cause subcellular redistribution of their target: insights into compound modes of action.Resistance analysis of the hepatitis C virus NS5A inhibitor BMS-790052 in an in vitro replicon system.All three domains of the hepatitis C virus nonstructural NS5A protein contribute to RNA binding.Distinct functions of NS5A in hepatitis C virus RNA replication uncovered by studies with the NS5A inhibitor BMS-790052Hepatitis C NS5A protein: two drug targets within the same protein with different mechanisms of resistance.Insights into the complexity and functionality of hepatitis C virus NS5A phosphorylation.Potent hepatitis C inhibitors bind directly to NS5A and reduce its affinity for RNA.Structural and molecular basis of interaction of HCV non-structural protein 5A with human casein kinase 1α and PKR.Domain 3 of NS5A protein from the hepatitis C virus has intrinsic alpha-helical propensity and is a substrate of cyclophilin A.Serine phosphorylation of the hepatitis C virus NS5A protein controls the establishment of replication complexes.Nonstructural protein 5A (NS5A) and human replication protein A increase the processivity of hepatitis C virus NS5B polymerase activity in vitro.A Proline-Tryptophan Turn in the Intrinsically Disordered Domain 2 of NS5A Protein Is Essential for Hepatitis C Virus RNA ReplicationdsRNA-dependent protein kinase PKR and its role in stress, signaling and HCV infection.Hepatitis C Virus NS5A Protein Triggers Oxidative Stress by Inducing NADPH Oxidases 1 and 4 and Cytochrome P450 2E1Coevolution analysis of Hepatitis C virus genome to identify the structural and functional dependency network of viral proteins.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.Preclinical Profile and Clinical Efficacy of a Novel Hepatitis C Virus NS5A Inhibitor, EDP-239.Approaches to hepatitis C treatment and cure using NS5A inhibitorsCyclophilins as modulators of viral replication.Oxidative stress and hepatitis C virus.Ombitasvir (ABT-267), a novel NS5A inhibitor for the treatment of hepatitis C.Intragenic complementation of hepatitis C virus NS5A RNA replication-defective alleles.Analysis of the Domains of Hepatitis C Virus Core and NS5A Proteins that Activate the Nrf2/ARE Cascade.A conserved tandem cyclophilin-binding site in hepatitis C virus nonstructural protein 5A regulates Alisporivir susceptibility.NMR reveals the intrinsically disordered domain 2 of NS5A protein as an allosteric regulator of the hepatitis C virus RNA polymerase NS5B.The Casein Kinase 2-Dependent Phosphorylation of NS5A Domain 3 from Hepatitis C Virus Followed by Time-Resolved NMR Spectroscopy.New insights regarding HCV-NS5A structure/function and indication of genotypic differences.
P2860
Q21560973-BB5C72A1-A13B-487D-9A01-129C7D237D7AQ24303838-55C9E80C-8F34-4EDD-B8B2-68447707EB16Q26991855-D209B7A1-B6F6-4F2E-BC5F-5763E0F3FA0DQ27488306-BD39AF97-5082-4AD4-8824-4CB32E1E89CBQ27488369-FF43FD91-4958-413E-9C06-90A904869BE5Q27682272-966EBDDE-4662-4061-B894-3839E20D015DQ27684710-BB77D166-0B3B-4966-8ED8-0875EE1E337CQ28481438-24E26A75-BA46-4A2E-AF99-8454BCBC5E6DQ28551959-FDC027C2-F873-41E8-8EAF-E22CB39AF067Q28748683-B7C9CD11-4316-4183-B3A1-920F8CF4DA54Q33668416-128E967C-E3CC-49AF-A729-DA7BDB376E27Q33673223-94AC2159-4892-4298-98EB-F73F73FCC596Q33707739-3CD07F85-F6DF-45D5-8A1F-8C448D39D2FBQ33878202-B23D2ECA-DBFB-40FA-A8E7-0F2CA82A3F6BQ34022926-4D8D8E05-4491-4E75-89F7-B0B06A73978AQ34120165-5CC5DDA9-73C8-4CD5-BE2F-8AB777620942Q34185949-577E5219-D344-463A-8828-E3AEE6874243Q34332546-67BAEF7D-1D70-49EA-A948-66AC141AC3C7Q34386515-9D0158E3-29B8-4541-94EA-EBC97CCBBB49Q34416582-8C1E685B-A2C6-4344-8422-83D812C2E701Q34475801-17E28B5B-DE75-4748-BD19-35BEC7E9CA5AQ35063336-3FA41549-0A60-45E9-8DCC-93247EF5A430Q35110962-1277B7C4-325A-4657-9552-0EF272DE3431Q35336114-77B0BB2B-B4AD-4611-827E-184220A7A67AQ35905354-F362D52C-4966-4947-88C6-4905CD398C1FQ36432681-16846CDC-E020-4DA2-B9F0-3CD3B53E8383Q36864157-5BD7916C-4583-4CF3-83A2-1F7919E90913Q36919211-8B1CED10-D1E9-4218-846B-90940C0FF085Q37006634-276DB59C-0BA8-4BBA-A5A0-663FDCDF7D26Q37287839-490FC227-A88D-4DB5-9800-ECBF4C1FB19BQ37630422-1AAE6068-CB15-427D-AAB6-D7FC8BDF3780Q38121470-AFA8B999-1C34-45CD-90DB-945D80C8A24CQ38127242-6D2391DA-D578-498E-9444-CC4539697494Q38262922-57F5B97D-DECD-48D9-AB64-C6FC7B6A8009Q39227082-590C2121-0278-4E79-B2C5-1481427347A4Q39234727-B9E23107-62EE-4D1C-A67E-ABE0B92155E3Q39394432-19186DEB-8BBF-43CA-871C-A4C479005C3CQ40040199-F7E7B510-14DA-4A5C-B1EF-A4D29C035C70Q40193153-C86A7E6F-7F4C-4963-8876-6CDEB82013DBQ40839503-1D40A188-85E2-4F62-9445-FDAFDD382D3A
P2860
Domain 2 of nonstructural protein 5A (NS5A) of hepatitis C virus is natively unfolded.
description
2007 nî lūn-bûn
@nan
2007年の論文
@ja
2007年学术文章
@wuu
2007年学术文章
@zh
2007年学术文章
@zh-cn
2007年学术文章
@zh-hans
2007年学术文章
@zh-my
2007年学术文章
@zh-sg
2007年學術文章
@yue
2007年學術文章
@zh-hant
name
Domain 2 of nonstructural protein 5A (NS5A) of hepatitis C virus is natively unfolded.
@en
Domain 2 of nonstructural protein 5A
@nl
type
label
Domain 2 of nonstructural protein 5A (NS5A) of hepatitis C virus is natively unfolded.
@en
Domain 2 of nonstructural protein 5A
@nl
prefLabel
Domain 2 of nonstructural protein 5A (NS5A) of hepatitis C virus is natively unfolded.
@en
Domain 2 of nonstructural protein 5A
@nl
P356
P1433
P1476
Domain 2 of nonstructural protein 5A (NS5A) of hepatitis C virus is natively unfolded
@en
P2093
P304
11550-11558
P356
10.1021/BI700776E
P407
P577
2007-09-19T00:00:00Z