Adenovirus E1B 19 kDa and Bcl-2 proteins interact with a common set of cellular proteins
about
Identification of a cell protein (FIP-3) as a modulator of NF-kappaB activity and as a target of an adenovirus inhibitor of tumor necrosis factor alpha-induced apoptosisBtf, a novel death-promoting transcriptional repressor that interacts with Bcl-2-related proteins.Evidence for a novel Cdc42GAP domain at the carboxyl terminus of BNIP-2BNIP3 and genetic control of necrosis-like cell death through the mitochondrial permeability transition poreGuidelines for the use and interpretation of assays for monitoring autophagy (3rd edition)The BNIP-2 and Cdc42GAP homology/Sec14p-like domain of BNIP-Salpha is a novel apoptosis-inducing sequenceThe apoptosis-associated protein BNIPL interacts with two cell proliferation-related proteins, MIF and GFERInvolvement of BNIP1 in apoptosis and endoplasmic reticulum membrane fusionBNIP3 and NIX mediate Mieap-induced accumulation of lysosomal proteins within mitochondriaThe E1B 19K/Bcl-2-binding protein Nip3 is a dimeric mitochondrial protein that activates apoptosisInteraction of an adenovirus 14.7-kilodalton protein inhibitor of tumor necrosis factor alpha cytolysis with a new member of the GTPase superfamily of signal transducersp28 Bap31, a Bcl-2/Bcl-XL- and procaspase-8-associated protein in the endoplasmic reticulumThe p53-binding protein 53BP2 also interacts with Bc12 and impedes cell cycle progression at G2/Mharakiri, a novel regulator of cell death, encodes a protein that activates apoptosis and interacts selectively with survival-promoting proteins Bcl-2 and Bcl-X(L)Coding sequences of functioning human genes derived entirely from mobile element sequencesA conserved domain in Bak, distinct from BH1 and BH2, mediates cell death and protein binding functionsLegionella pneumophila inhibits macrophage apoptosis by targeting pro-death members of the Bcl2 protein familyRegulation of apoptosis by viral gene productsAutophagy as a regulatory component of erythropoiesisMitophagy: mechanisms, pathophysiological roles, and analysisStructure of the Human Sulfhydryl Oxidase Augmenter of Liver Regeneration and Characterization of a Human Mutation Causing an Autosomal Recessive Myopathy,Transglutaminase 2 has opposing roles in the regulation of cellular functions as well as cell growth and deathHypoxia-induced autophagy is mediated through hypoxia-inducible factor induction of BNIP3 and BNIP3L via their BH3 domainsThe BNIP-2 and Cdc42GAP homology domain of BNIP-2 mediates its homophilic association and heterophilic interaction with Cdc42GAPTyrosine phosphorylation of the Bcl-2-associated protein BNIP-2 by fibroblast growth factor receptor-1 prevents its binding to Cdc42GAP and Cdc42Apoptosis in the pathogenesis and treatment of diseaseThe proapoptotic protein BNIP3 interacts with VDAC to induce mitochondrial release of endonuclease GDifferential gene expression in human hepatocellular carcinoma Hep3B cells induced by apoptosis-related gene BNIPL-2Increased expression of proapoptotic BMCC1, a novel gene with the BNIP2 and Cdc42GAP homology (BCH) domain, is associated with favorable prognosis in human neuroblastomasActivation of Ras up-regulates pro-apoptotic BNIP3 in nitric oxide-induced cell deathNix and Nip3 form a subfamily of pro-apoptotic mitochondrial proteinsIdentification of drm, a novel gene whose expression is suppressed in transformed cells and which can inhibit growth of normal but not transformed cells in cultureAntagonism of E2F-1 regulated Bnip3 transcription by NF-kappaB is essential for basal cell survivalAdenovirus E1A inhibits cardiac myocyte-specific gene expression through its amino terminusProapoptotic Nix activates the JNK pathway by interacting with POSH and mediates death in a Parkinson disease modelApoptosis: molecular regulation of cell deathThe histone H3K9 demethylase KDM3A promotes anoikis by transcriptionally activating pro-apoptotic genes BNIP3 and BNIP3LNIX is required for programmed mitochondrial clearance during reticulocyte maturationInteraction of Epstein-Barr virus nuclear antigen leader protein (EBNA-LP) with HS1-associated protein X-1: implication of cytoplasmic function of EBNA-LP.Analysis of synthesis, stability, phosphorylation, and interacting polypeptides of the 34-kilodalton product of open reading frame 6 of the early region 4 protein of human adenovirus type 5
P2860
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
P248
Q22008750-0D631A01-BEEA-45AA-881F-9567A6E90118Q22010049-5B489DF5-1265-490B-9DA6-739FE95097DBQ22254035-3009E923-3D1B-42DF-9D39-10090BC396ABQ22254597-A4A69413-5628-430E-B6F1-81669ABB7E00Q22676705-8D77471D-48A1-4F93-8476-ACDBFA2676EAQ24292005-64A166A1-E536-41AD-9CB4-72B86821502FQ24299508-4E09DC0F-58B0-4374-B90D-FD9CF5FBC3B5Q24299994-D6A9798D-6422-486E-A937-556384F74D7EQ24304086-FEE98587-EA3B-4788-B4FD-1450EDA5565DQ24312877-C2CC79A3-6196-4B89-B7A9-D20429371DC5Q24313249-E2A2805F-C3AF-4BCD-A96A-68B0309FF068Q24318875-554B2EAF-4E83-4AC9-A3E8-C70F726D052DQ24323137-4E131A4F-B334-4885-971B-C10B978D85C8Q24532147-C89C1849-0568-430A-893B-84D24DBDCD3CQ24559112-4741889E-E951-4AE9-8FAD-5C26DB3325F4Q24597482-38C8B2CB-8D12-4F56-A316-BE3D8313F36CQ24677004-3730162C-38F3-46A2-A90E-78E34C184421Q24678703-4DDB1A6E-D60D-4A34-BB10-0D51C9AD1F2CQ26851454-D92B4DDD-E6F6-4FB4-BCA7-B42AA0B047CCQ26865743-6E407373-4134-4D35-BDC4-60B33F57DA50Q27662931-6496B798-77F9-426E-BB2A-1CE5B1C0A516Q28069852-91E03B31-17C0-435A-A54D-60C5DB4C1401Q28114920-A4435325-A868-44DF-8B71-0636E8D7B77BQ28144356-A7E0D234-3BE2-4780-BF0A-CD288E1D30F4Q28146238-8B685D35-C87E-4D92-A36A-3C9685A7BFECQ28235731-EC32823C-5310-4AF5-A878-0FCEFEF8D3C9Q28252454-0C36F1B2-4B83-4095-B8F3-226725324BF2Q28258914-95EA9481-AAD6-478E-8C30-875BC935124AQ28281864-91A19F4D-97ED-4507-AE1D-E495C800135AQ28505436-FBA51A39-36A7-46BB-B34B-59797FEB1B6FQ28511235-FABA4E8A-513D-404D-B124-EE0DDCEC6753Q28576024-19C2B3AC-3B2E-4BC8-A1D4-BCE94B6AE23DQ28580647-E62F5779-8373-4742-9ADD-D0137C2607F2Q28583270-1C771C9B-182B-47CC-84A4-0B76FE16FE4FQ28592509-3BE6DA1E-F4F9-4FB5-8662-20B9E86D47CDQ28611445-1073FEB1-DEA6-4A54-BF52-7AD61A7CD803Q28829578-BCDB4554-30BE-429E-800A-FF7F7E75C8C4Q29614484-188C8E43-ECE6-46D0-926B-70D222445E34Q30939262-BB12ABF6-F903-48C3-8040-EB6C2FF4BD48Q33641023-F153F640-592B-40F8-AD1C-8A96D737AB2B
P2860
Adenovirus E1B 19 kDa and Bcl-2 proteins interact with a common set of cellular proteins
description
1994 nî lūn-bûn
@nan
1994 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած
@hyw
1994 թվականի հոտեմբերին հրատարակված գիտական հոդված
@hy
1994年の論文
@ja
1994年論文
@yue
1994年論文
@zh-hant
1994年論文
@zh-hk
1994年論文
@zh-mo
1994年論文
@zh-tw
1994年论文
@wuu
name
Adenovirus E1B 19 kDa and Bcl-2 proteins interact with a common set of cellular proteins
@ast
Adenovirus E1B 19 kDa and Bcl-2 proteins interact with a common set of cellular proteins
@en
Adenovirus E1B 19 kDa and Bcl-2 proteins interact with a common set of cellular proteins
@en-gb
Adenovirus E1B 19 kDa and Bcl-2 proteins interact with a common set of cellular proteins
@nl
type
label
Adenovirus E1B 19 kDa and Bcl-2 proteins interact with a common set of cellular proteins
@ast
Adenovirus E1B 19 kDa and Bcl-2 proteins interact with a common set of cellular proteins
@en
Adenovirus E1B 19 kDa and Bcl-2 proteins interact with a common set of cellular proteins
@en-gb
Adenovirus E1B 19 kDa and Bcl-2 proteins interact with a common set of cellular proteins
@nl
prefLabel
Adenovirus E1B 19 kDa and Bcl-2 proteins interact with a common set of cellular proteins
@ast
Adenovirus E1B 19 kDa and Bcl-2 proteins interact with a common set of cellular proteins
@en
Adenovirus E1B 19 kDa and Bcl-2 proteins interact with a common set of cellular proteins
@en-gb
Adenovirus E1B 19 kDa and Bcl-2 proteins interact with a common set of cellular proteins
@nl
P2093
P921
P3181
P1433
P1476
Adenovirus E1B 19 kDa and Bcl-2 proteins interact with a common set of cellular proteins
@en
P2093
B Elangovan
C D'Sa-Eipper
G Chinnadurai
L K Venkatesh
S Malstrom
T Subramanian
U Schaeper
P304
P3181
P356
10.1016/0092-8674(94)90202-X
P407
P577
1994-10-21T00:00:00Z