Solution structure of the ets domain of Fli-1 when bound to DNA
about
Solution structure of the DNA-binding domain of interleukin enhancer binding factor 1 (FOXK1a)Solution structure of the ETS domain from murine Ets-1: a winged helix-turn-helix DNA binding motifProtein complexes studied by NMR spectroscopyCrystal structure of the human Pax6 paired domain-DNA complex reveals specific roles for the linker region and carboxy-terminal subdomain in DNA bindingCrystal Structure of Mouse Elf3 C-terminal DNA-binding Domain in Complex with Type II TGF-β Receptor Promoter DNAAutoinhibition of ETV6 (TEL) DNA Binding: Appended Helices Sterically Block the ETS DomainStructural and dynamic studies of the transcription factor ERG reveal DNA binding is allosterically autoinhibitedIdentification of amino acid residues in the ETS transcription factor Erg that mediate Erg-Jun/Fos-DNA ternary complex formationOverexpression of Fli-1 in astrocytoma is associated with poor prognosis.Structures of the Ets Protein DNA-binding Domains of Transcription Factors Etv1, Etv4, Etv5, and Fev: DETERMINANTS OF DNA BINDING AND REDOX REGULATION BY DISULFIDE BOND FORMATION.Identification of soluble protein fragments by gene fragmentation and genetic selection.Identification of nuclear import and export signals within Fli-1: roles of the nuclear import signals in Fli-1-dependent activation of megakaryocyte-specific promoters.A domain of TEL conserved in a subset of ETS proteins defines a specific oligomerization interface essential to the mitogenic properties of the TEL-PDGFR beta oncoprotein.The role of Fli-1 in normal cell function and malignant transformation.Regulation of Ets function by protein - protein interactions.Classification of multi-helical DNA-binding domains and application to predict the DBD structures of sigma factor, LysR, OmpR/PhoB, CENP-B, Rapl, and Xy1S/Ada/AraC.Structural modeling and DNA binding autoinhibition analysis of Ergp55, a critical transcription factor in prostate cancer.Protein-protein interaction between Fli-1 and GATA-1 mediates synergistic expression of megakaryocyte-specific genes through cooperative DNA binding.Structural coupling of the inhibitory regions flanking the ETS domain of murine Ets-1.Characterization of the cooperative function of inhibitory sequences in Ets-1.Determinants of DNA-binding specificity of ETS-domain transcription factorsThe SRC family tyrosine kinase HCK and the ETS family transcription factors SPIB and EHF regulate transcytosis across a human follicle-associated epithelium model.Molecular characterisation of murine acute myeloid leukaemia induced by 56Fe ion and 137Cs gamma ray irradiation.Ets-1 regulates radial glia formation during vertebrate embryogenesis.Genomic and biochemical insights into the specificity of ETS transcription factors.Co-crystallization of an ETS domain (PU.1) in complex with DNA. Engineering the length of both protein and oligonucleotide.Transactivation of the Moloney murine leukemia virus and T-cell receptor beta-chain enhancers by cbf and ets requires intact binding sites for both proteins.Different domains of the transcription factor ELF3 are required in a promoter-specific manner and multiple domains control its binding to DNA.Purification, crystallization and preliminary X-ray crystallographic analysis of the ETS domain of human Ergp55 in complex with the cfos promoter DNA sequence.New insights on DNA recognition by ets proteins from the crystal structure of the PU.1 ETS domain-DNA complex.The oncogene ERG: a key factor in prostate cancer.Progress in the molecular biology of ewing tumors.The expression of a novel, epithelium-specific ets transcription factor is restricted to the most differentiated layers in the epidermisDNA binding domain-independent pathways are involved in EWS/FLI1-mediated oncogenesis.Expression pattern of the Ets-related transcription factor Elf-1Dimer formation by ternary complex factor ELK-1.Amino acid residues in the beta3 strand and subsequent loop of the conserved ETS domain that mediate basic leucine zipper (bZIP) recruitment and potentially distinguish functional attributes of Ets proteins.Erythroblast transformation by FLI-1 depends upon its specific DNA binding and transcriptional activation properties.Identification of two types of GGAA-microsatellites and their roles in EWS/FLI binding and gene regulation in Ewing sarcoma.Proteasomal Degradation of the EWS-FLI1 Fusion Protein Is Regulated by a Single Lysine Residue.
P2860
Q24313587-2B812488-7913-429D-98B2-924303B613BBQ24563315-77819940-FC44-4B6A-A8DB-92E6455116E9Q24600374-EC3F4C4D-C5D5-47DF-AB09-710FF83EACADQ27618361-4F525EE8-962D-4CCE-8C86-854968B57D7EQ27658979-7AF5EE8B-7480-4FFB-AEF6-45586BFEB862Q27679088-5BB9B6FF-3BD1-4CF8-BA72-46791BCE969CQ27679276-B1FA70CB-2A69-4EA1-9419-E1056D3A1662Q28208097-1526E4F6-4930-4566-A264-2F8B739B73A4Q30252603-CB68931C-43B8-4D3A-8830-836DA9328B99Q30373611-5708C22A-BAED-4EBC-8978-69FE8C598CF6Q33329036-4F4DCC73-3AB0-48B7-BF2A-B28068D55AD1Q33724367-FD10C85C-97AF-4226-96EF-B54E3C44F8CCQ33885920-8543387C-F823-4CEA-85F6-074AB99CF6E8Q33933215-DEB87045-9CB5-4C16-8272-A009809F1DDBQ33933221-E13ACD0B-2A4A-4EB4-9C06-1CABE6D82D6AQ34057931-F17B5C51-AB70-4F0E-BB52-F03ACCD432F8Q34326572-B43D8B97-56EF-409D-B703-8CB9C993CA2CQ34533281-9D28D1B9-026C-4D04-AD73-02F71934D169Q36279666-7A4A7E1C-E7DB-463C-B32A-CE19DDB06D34Q36559022-29835CE3-91C2-4734-A533-CE312763D522Q36560535-3AC9ABAE-E8A5-47A8-A764-E5C28ECEEFDCQ36760307-2670FE6D-9BAA-432A-A407-9BF0A4A29940Q37026983-EE3745A8-E054-4957-BF42-4BDC8BABEC63Q37080098-7943385B-39F2-4E75-B24E-7B6005FE8EECQ37872764-6362CB3D-D592-4EC4-BF5D-1FF4CD3DB587Q38290364-A173D8C9-7EC4-4ADE-A843-6493A35756DEQ38293060-F66755F9-4CB7-4EC1-A6B1-CBF226FE78CEQ38306980-495EFCC5-7A91-4544-B35C-0C99F33FE8D8Q38320097-8ECEE845-4924-4901-BFDA-7CD95BC021B8Q38352942-BCDED024-AACB-4163-A0A6-8F4BDF4B7870Q38444138-419C4A22-E9DB-416E-B33D-C7B54D970D97Q38612055-B42EACF5-5D4D-4694-B2CB-B22CC52CA7F5Q39721575-83BF5349-9F6E-43D7-B25B-0FC293E14924Q40781045-DFB1B4A4-B511-4593-BF32-EB2BEC594744Q40884031-AB795AE1-8815-49F4-A27C-35E4F5644E6EQ40906065-68FEFC9E-741E-4050-BB48-A72368CE056EQ43045210-62C2980B-9D52-47AA-8921-C6CCAEF75E6EQ44626778-33882FD5-07B8-421D-8181-5B05B6FCCDECQ46131586-5995C309-F39A-466D-826B-977A8070146AQ51310744-01718D92-9198-4BF7-9E81-ADB3AF081640
P2860
Solution structure of the ets domain of Fli-1 when bound to DNA
description
1994 nî lūn-bûn
@nan
1994 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած
@hyw
1994 թվականի դեկտեմբերին 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
Solution structure of the ets domain of Fli-1 when bound to DNA
@ast
Solution structure of the ets domain of Fli-1 when bound to DNA
@en
Solution structure of the ets domain of Fli-1 when bound to DNA
@nl
type
label
Solution structure of the ets domain of Fli-1 when bound to DNA
@ast
Solution structure of the ets domain of Fli-1 when bound to DNA
@en
Solution structure of the ets domain of Fli-1 when bound to DNA
@nl
prefLabel
Solution structure of the ets domain of Fli-1 when bound to DNA
@ast
Solution structure of the ets domain of Fli-1 when bound to DNA
@en
Solution structure of the ets domain of Fli-1 when bound to DNA
@nl
P2093
P2860
P356
P1476
Solution structure of the ets domain of Fli-1 when bound to DNA
@en
P2093
Meadows RP
Nettesheim DG
Olejniczak ET
Thompson CB
P2860
P304
P356
10.1038/NSB1294-871
P50
P577
1994-12-01T00:00:00Z