Mad: a heterodimeric partner for Max that antagonizes Myc transcriptional activity
about
Ski is a component of the histone deacetylase complex required for transcriptional repression by Mad and thyroid hormone receptorNmi protein interacts with regions that differ between MycN and Myc and is localized in the cytoplasm of neuroblastoma cells in contrast to nuclear MycNMlx, a new Max-like bHLHZip family member: the center stage of a novel transcription factors regulatory pathway?A novel 16-kilodalton cellular protein physically interacts with and antagonizes the functional activity of c-myc promoter-binding protein 1The bovine herpesvirus 1 immediate-early protein (bICP0) associates with histone deacetylase 1 to activate transcription.Repression of promoter activity by CNOT2, a subunit of the transcription regulatory Ccr4-not complexHuman protein NEFA, a novel DNA binding/EF-hand/leucine zipper protein. Molecular cloning and sequence analysis of the cDNA, isolation and characterization of the proteinStructure of a dominant-negative helix-loop-helix transcriptional regulator suggests mechanisms of autoinhibitionRox, a novel bHLHZip protein expressed in quiescent cells that heterodimerizes with Max, binds a non-canonical E box and acts as a transcriptional repressor.Mad3 and Mad4: novel Max-interacting transcriptional repressors that suppress c-myc dependent transformation and are expressed during neural and epidermal differentiationMyc-Max heterodimers activate a DEAD box gene and interact with multiple E box-related sites in vivoA novel genetic system to isolate a dominant negative effector on DNA-binding activity of Oct-2Immunochemical characterization and transacting properties of upstream stimulatory factor isoformsRole of Mxi1 in ageing organ systems and the regulation of normal and neoplastic growthAdenovirus E1B 55K represses p53 activation in vitro.Mad4 is regulated by a transcriptional repressor complex that contains Miz-1 and c-MycJLP: A scaffolding protein that tethers JNK/p38MAPK signaling modules and transcription factors.The c-myc coding region determinant-binding protein: a member of a family of KH domain RNA-binding proteinsMondoA, a novel basic helix-loop-helix-leucine zipper transcriptional activator that constitutes a positive branch of a max-like networkThe essential cofactor TRRAP recruits the histone acetyltransferase hGCN5 to c-MycHelix-loop-helix proteins: regulators of transcription in eucaryotic organismsMDMX: a novel p53-binding protein with some functional properties of MDM2Myc and Max: molecular evolution of a family of proto-oncogene products and their dimerization partnerMxi2, a mitogen-activated protein kinase that recognizes and phosphorylates Max proteinInteraction of c-Myc with the pRb-related protein p107 results in inhibition of c-Myc-mediated transactivationTranscriptional activation by Myc is under negative control by the transcription factor AP-2Structure and function of the b/HLH/Z domain of USFThe cytoplasmic Purkinje onconeural antigen cdr2 down-regulates c-Myc function: implications for neuronal and tumor cell survivalIdentification of a novel mechanism of regulation of Ah (dioxin) receptor functionIKKalpha, a critical regulator of epidermal differentiation and a suppressor of skin cancerMxi1 inhibits the proliferation of U87 glioma cells through down-regulation of cyclin B1 gene expressionTranscription enhancer factor 1 interacts with a basic helix-loop-helix zipper protein, Max, for positive regulation of cardiac alpha-myosin heavy-chain gene expressionIsolation of an AP-1 repressor by a novel method for detecting protein-protein interactionsTwo new members of the murine Sim gene family are transcriptional repressors and show different expression patterns during mouse embryogenesismSin3A/histone deacetylase 2- and PRMT5-containing Brg1 complex is involved in transcriptional repression of the Myc target gene cadCell Proliferation in NeuroblastomaSGF29 and Sry pathway in hepatocarcinogenesisFunctional interactions among members of the MAX and MLX transcriptional network during oncogenesisHDAC activity is required during Xenopus tail regenerationRtg3p, a basic helix-loop-helix/leucine zipper protein that functions in mitochondrial-induced changes in gene expression, contains independent activation domains.
P2860
Q22008813-5CD3BADD-B568-42DD-95EF-65DA90DAA5D4Q22010928-21A416E3-CA57-4A93-9322-544215DAFE92Q22254702-31CA76B6-C3D0-4D7D-B6AC-AC751C32D965Q24290678-FACFE81B-E08B-4034-A857-22D652D9FF0BQ24291697-9ECDC6BD-3CC0-4E81-8FE1-CF7E7CA3F912Q24304106-0F213316-E5E9-4744-AFF4-28FEA13E3B9EQ24308489-77BE4198-CD63-44D9-AA41-3C623EF88742Q24310008-66365BA4-D2C1-42D3-A008-AE127CEAD3B4Q24310015-D981B881-FF98-48F8-9AE5-3FA0210D09A0Q24310266-9134BF8B-BC96-4634-B2F9-143F70F2DD91Q24313545-BFA40C97-5680-4C51-B473-C92F8EA17472Q24315271-EC9D6FEE-4F39-4A02-A5D2-662441BF8965Q24318718-0DF1CE85-0BE9-46F9-98DE-11DC7BA14922Q24324261-B7D5676F-1201-4E0F-98C1-7633C38C8B06Q24523301-62774AA2-26FE-4BE6-BE35-45F5DB7595B5Q24535514-F9A80F32-3AA0-4708-AE90-E24BE78F3A9FQ24540351-5D4BAF61-6E10-40EA-ADA5-092A4DE01729Q24548296-59ACE907-35D0-4BDB-ACF3-ED4B1C667042Q24551066-3028BA14-8269-44ED-BFCB-49587697821FQ24554343-8EE2C592-936F-4CC4-B852-7D0B2B9EF7A1Q24554353-F94F9C9B-6BA2-49B0-8C3F-712B3F3D545CQ24561971-7E327562-7061-4F7F-AD17-3795685149B1Q24563644-E9FE0B0A-DEA9-450A-AED2-F423E3D8C8C3Q24564025-5B70022F-05AF-4EA8-A95B-9680CED2C09FQ24568291-B5074698-EE43-4B68-954F-4FBAB7C73A1CQ24568331-5D2AF9F5-12E8-4EAC-802D-A1FBE73614D9Q24596919-5EC29408-BE6E-4428-A5C3-0C23E9FB5559Q24600187-DA64D3B6-861C-4CD1-ABDB-A81C6C8CAEA4Q24609846-DDF3E12E-F4E9-4128-B53D-5088B8B6B3E9Q24642963-B8758607-FD7A-43EF-B6DD-90152E34D222Q24643042-3D323102-8301-4FF9-AEBA-42DD19E3D16DQ24645990-B74A06C9-BB69-4B18-903A-C3B152A2697AQ24646252-5A5F35F1-E971-4798-8A24-FD7AF19E3415Q24648064-DB3A5EDF-2ED5-412D-B555-004901F08BC7Q24679145-743B7526-BFFE-4513-A6EA-8015BE31D08FQ26771708-9707E1BB-B4FF-4F8A-B49F-B36ADD42CE3AQ26795760-AECB796B-2866-4E48-BD1D-6BBF076B3091Q26853567-99E19E58-28C8-4B44-A818-03C7B49C59F2Q27316244-5BBD46E6-B690-439B-B55A-A47BB4ACB10EQ27929957-79869BD0-BB71-4207-ABF5-69C77F8BC55E
P2860
Mad: a heterodimeric partner for Max that antagonizes Myc transcriptional activity
description
1993 nî lūn-bûn
@nan
1993 թուականի Յունուարին հրատարակուած գիտական յօդուած
@hyw
1993 թվականի հունվարին հրատարակված գիտական հոդված
@hy
1993年の論文
@ja
1993年論文
@yue
1993年論文
@zh-hant
1993年論文
@zh-hk
1993年論文
@zh-mo
1993年論文
@zh-tw
1993年论文
@wuu
name
Mad: a heterodimeric partner for Max that antagonizes Myc transcriptional activity
@ast
Mad: a heterodimeric partner for Max that antagonizes Myc transcriptional activity
@en
Mad: a heterodimeric partner for Max that antagonizes Myc transcriptional activity
@en-gb
Mad: a heterodimeric partner for Max that antagonizes Myc transcriptional activity
@nl
type
label
Mad: a heterodimeric partner for Max that antagonizes Myc transcriptional activity
@ast
Mad: a heterodimeric partner for Max that antagonizes Myc transcriptional activity
@en
Mad: a heterodimeric partner for Max that antagonizes Myc transcriptional activity
@en-gb
Mad: a heterodimeric partner for Max that antagonizes Myc transcriptional activity
@nl
prefLabel
Mad: a heterodimeric partner for Max that antagonizes Myc transcriptional activity
@ast
Mad: a heterodimeric partner for Max that antagonizes Myc transcriptional activity
@en
Mad: a heterodimeric partner for Max that antagonizes Myc transcriptional activity
@en-gb
Mad: a heterodimeric partner for Max that antagonizes Myc transcriptional activity
@nl
P2093
P3181
P1433
P1476
Mad: a heterodimeric partner for Max that antagonizes Myc transcriptional activity
@en
P2093
L Kretzner
R N Eisenman
P304
P3181
P356
10.1016/0092-8674(93)90661-9
P407
P577
1993-01-29T00:00:00Z