XAP2, a novel hepatitis B virus X-associated protein that inhibits X transactivation
about
Binding of aryl hydrocarbon receptor (AhR) to AhR-interacting protein - The role of hsp90Hepatitis B virus pX interacts with HBXAP, a PHD finger protein to coactivate transcriptionPhosphodiesterase 2A forms a complex with the co-chaperone XAP2 and regulates nuclear translocation of the aryl hydrocarbon receptorQuantitative mass spectrometry catalogues Salmonella pathogenicity island-2 effectors and identifies their cognate host binding partnersEpstein-Barr virus encoded nuclear protein EBNA-3 binds a novel human uridine kinase/uracil phosphoribosyltransferaseThe inherited blindness associated protein AIPL1 interacts with the cell cycle regulator protein NUB1XAP2 inhibits glucocorticoid receptor activity in mammalian cellsHepatitis B virus X-associated protein 2 is a subunit of the unliganded aryl hydrocarbon receptor core complex and exhibits transcriptional enhancer activityThe hsp90 chaperone complex regulates intracellular localization of the dioxin receptorHepatitis B virus X protein interacts with beta5 subunit of heterotrimeric guanine nucleotide binding protein.Structure of the TPR Domain of AIP: Lack of Client Protein Interaction with the C-Terminal α-7 Helix of the TPR Domain of AIP Is Sufficient for Pituitary Adenoma PredispositionThe immunophilin-like protein XAP2 regulates ubiquitination and subcellular localization of the dioxin receptorThe hsp90 Co-chaperone XAP2 alters importin beta recognition of the bipartite nuclear localization signal of the Ah receptor and represses transcriptional activityTwo distinct regions of the immunophilin-like protein XAP2 regulate dioxin receptor function and interaction with hsp90Evidence that peroxisome proliferator-activated receptor alpha is complexed with the 90-kDa heat shock protein and the hepatitis virus B X-associated protein 2The aryl hydrocarbon receptor complex and the control of gene expressionAttenuation of the activity of the cAMP-specific phosphodiesterase PDE4A5 by interaction with the immunophilin XAP2NMR assignments of the FKBP-type PPIase domain of the human aryl-hydrocarbon receptor-interacting protein (AIP).The immunophilin-like protein XAP2 is a negative regulator of estrogen signaling through interaction with estrogen receptor αSeek protein which can interact with hepatitis B virus X protein from human liver cDNA library by yeast two-hybrid system.Epstein-Barr virus encoded nuclear protein EBNA-3 binds XAP-2, a protein associated with Hepatitis B virus X antigen.Hepatitis B virus X protein interferes with cellular DNA repair.The aryl hydrocarbon receptor-interacting protein (AIP) is required for dioxin-induced hepatotoxicity but not for the induction of the Cyp1a1 and Cyp1a2 genesAryl Hydrocarbon Receptor Interacting Protein Targets IRF7 to Suppress Antiviral Signaling and the Induction of Type I Interferon.Functional specificity of co-chaperone interactions with Hsp90 client proteins.Familial isolated pituitary adenomas (FIPA) and the pituitary adenoma predisposition due to mutations in the aryl hydrocarbon receptor interacting protein (AIP) gene.Molecular chaperones and photoreceptor function.Toxicology mechanism of the persistent organic pollutants (POPs) in fish through AhR pathway.Familial isolated pituitary adenomas: an emerging clinical entity.An update on viral association of human cancers.Molecular cochaperones: tumor growth and cancer treatment.The E3 ligase CHIP: insights into its structure and regulation.The Leber congenital amaurosis protein AIPL1 functions as part of a chaperone heterocomplex.Redefining the role of the endogenous XAP2 and C-terminal hsp70-interacting protein on the endogenous Ah receptors expressed in mouse and rat cell lines.Aryl hydrocarbon (Ah) receptor levels are selectively modulated by hsp90-associated immunophilin homolog XAP2.ARA9 modifies agonist signaling through an increase in cytosolic aryl hydrocarbon receptor.Interaction of U-box-type ubiquitin-protein ligases (E3s) with molecular chaperones.The aryl hydrocarbon (Ah) receptor transcriptional regulator hepatitis B virus X-associated protein 2 antagonizes p23 binding to Ah receptor-Hsp90 complexes and is dispensable for receptor function.The hepatitis B virus X-associated protein, XAP3, is a protein kinase C-binding protein.Sequence diversification of the FK506-binding proteins in several different genomes.
P2860
Q23911835-17738814-C0AB-4CA9-8DF9-73A7D47055A6Q24292159-7A8AC0EE-5854-453B-9A47-328262E4210BQ24298550-704A47CD-FD63-4A8A-9074-C0F3F5534D70Q24302123-BBCF6162-EC91-4D6B-9165-75E6EFB3B651Q24305370-4409C343-6AA5-4234-AAFD-34EFAC706642Q24310496-5E23E9E2-0F73-4E23-B39D-7DA50F244783Q24317168-A7F1576C-F27F-4E37-9AB5-DAE95319023AQ24324699-83BE2D9C-1AE3-4773-B9F4-C12AC84427A0Q24550978-608995F1-531E-4CB4-9E0D-E2407853883DQ24815081-8EC1E7AE-F314-4010-B3B4-5CEC395D3EB9Q27675839-FA635F55-7E92-4F6A-9D7E-D7B5FD943520Q28140027-DCD688D2-EB5F-4655-B774-77B7B78D87DEQ28214778-8CC9A0E7-D5AD-4D41-BAED-F7B2599667EAQ28216266-53B6D66A-BBBE-4A90-9164-38DBE2CD58CAQ28217612-B799ED17-CB3D-4211-A8B7-A6C4E73BC287Q28386260-5F7A1F90-0B15-4918-963A-FB4767F91D66Q28573529-34348B87-5904-4146-9FB8-FD096C69CDD2Q30318200-A858B836-8ADD-4A74-B89C-43489A512740Q30473787-162A3EA9-B7F4-45F1-8D02-370B00486CF8Q30724254-086516A0-8A2A-401B-8E58-339AB57C427DQ30860599-474CB917-6399-4C8E-9F71-818D748C3C23Q33781959-16BF0418-E2D0-4978-8111-069554A1B8F6Q34285173-3D29FC5B-1B3E-430F-A786-98769D331E63Q35860858-1C701815-E108-40DC-9A53-CF16E0761932Q36069359-B527DAAA-7B22-4BB4-9F36-AFAA36FC54D9Q36724063-6B527D84-9C53-43EF-B3D6-17E06953EA55Q37167901-71727369-FCEE-46FB-8543-019396A703ECQ37761179-3929C232-C2DC-42F2-A83D-76F6520709C4Q38073256-34523483-AC09-4695-84FB-D63FB424A623Q38082388-EB1C8F71-92AA-4A77-8FE9-6C7B6B72426AQ38166376-6A00B866-7A7D-448C-84FC-07C4EB02153FQ38215523-D65BA365-4AFE-4457-A526-20396C3FC632Q39992486-D703AA3B-36B7-4D34-BE13-9A91FCF22A6AQ40387490-320BAB9D-D355-4729-8EEB-49AC5BBCF9FAQ40424897-617E446F-137A-443F-945C-0E7EF3287BE7Q40897851-9EF6C9C4-8A9D-40C5-8333-FD2E946DF6AAQ44930825-EF8734D5-B2A2-4776-888A-B968BA4411C4Q45025050-82C6F1F2-BA11-4F5A-AD9C-7264AEB9414AQ45762365-CC85FDFB-5C24-4C27-9D04-729415CE01EEQ47069148-CB8893A5-DD61-4C3E-92DA-5A84CE9F8AC5
P2860
XAP2, a novel hepatitis B virus X-associated protein that inhibits X transactivation
description
1996 nî lūn-bûn
@nan
1996 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած
@hyw
1996 թվականի դեկտեմբերին հրատարակված գիտական հոդված
@hy
1996年の論文
@ja
1996年論文
@yue
1996年論文
@zh-hant
1996年論文
@zh-hk
1996年論文
@zh-mo
1996年論文
@zh-tw
1996年论文
@wuu
name
XAP2, a novel hepatitis B virus X-associated protein that inhibits X transactivation
@ast
XAP2, a novel hepatitis B virus X-associated protein that inhibits X transactivation
@en
XAP2, a novel hepatitis B virus X-associated protein that inhibits X transactivation
@nl
type
label
XAP2, a novel hepatitis B virus X-associated protein that inhibits X transactivation
@ast
XAP2, a novel hepatitis B virus X-associated protein that inhibits X transactivation
@en
XAP2, a novel hepatitis B virus X-associated protein that inhibits X transactivation
@nl
prefLabel
XAP2, a novel hepatitis B virus X-associated protein that inhibits X transactivation
@ast
XAP2, a novel hepatitis B virus X-associated protein that inhibits X transactivation
@en
XAP2, a novel hepatitis B virus X-associated protein that inhibits X transactivation
@nl
P2093
P2860
P356
P1476
XAP2, a novel hepatitis B virus X-associated protein that inhibits X transactivation
@en
P2093
P2860
P304
P356
10.1093/NAR/24.23.4741
P407
P577
1996-12-01T00:00:00Z