Physical interaction between the mitogen-responsive serum response factor and myogenic basic-helix-loop-helix proteins
about
SMYD1, the myogenic activator, is a direct target of serum response factor and myogeninThe B-box dominates SAP-1-SRF interactions in the structure of the ternary complexCardiac tissue enriched factors serum response factor and GATA-4 are mutual coregulatorsDominant negative murine serum response factor: alternative splicing within the activation domain inhibits transactivation of serum response factor binding targetsMyogenic basic helix-loop-helix proteins and Sp1 interact as components of a multiprotein transcriptional complex required for activity of the human cardiac alpha-actin promoterNet (ERP/SAP2) one of the Ras-inducible TCFs, has a novel inhibitory domain with resemblance to the helix-loop-helix motifThe three members of the pocket proteins family share the ability to repress E2F activity through recruitment of a histone deacetylaseThe basic domain of myogenic basic helix-loop-helix (bHLH) proteins is the novel target for direct inhibition by another bHLH protein, TwistMos activates myogenic differentiation by promoting heterodimerization of MyoD and E12 proteinsInteractions of the Mcm1 MADS box protein with cofactors that regulate mating in yeast.Cooperative transcriptional activation by serum response factor and the high mobility group protein SSRP1Differential binding of an SRF/NK-2/MEF2 transcription factor complex in normal versus neoplastic smooth muscle tissuesDermo-1, a multifunctional basic helix-loop-helix protein, represses MyoD transactivation via the HLH domain, MEF2 interaction, and chromatin deacetylationSerum response factor is essential for mesoderm formation during mouse embryogenesisIdentification of a novel serum response factor cofactor in cardiac gene regulationPIAS1 activates the expression of smooth muscle cell differentiation marker genes by interacting with serum response factor and class I basic helix-loop-helix proteins.The homeodomain protein Barx2 promotes myogenic differentiation and is regulated by myogenic regulatory factorsAn initial blueprint for myogenic differentiationThe smooth muscle gamma-actin gene promoter is a molecular target for the mouse bagpipe homologue, mNkx3-1, and serum response factorSmooth muscle differentiation marker gene expression is regulated by RhoA-mediated actin polymerization.The orf13 T-DNA gene of Agrobacterium rhizogenes confers meristematic competence to differentiated cells.Myogenic enhancers regulate expression of the facioscapulohumeral muscular dystrophy-associated DUX4 gene.Basic fibroblast growth factor activates serum response factor gene expression by multiple distinct signaling mechanismsInhibition of MuSK expression by CREB interacting with a CRE-like element and MyoD.KLF3 regulates muscle-specific gene expression and synergizes with serum response factor on KLF binding sitesOverexpression of p49/STRAP alters cellular cytoskeletal structure and gross anatomy in mice.New role for serum response factor in postnatal skeletal muscle growth and regeneration via the interleukin 4 and insulin-like growth factor 1 pathwaysExpression of the myosin heavy chain IIB gene in porcine skeletal muscle: the role of the CArG-Box promoter response elementIdentifying pattern-defined regulatory islands in mammalian genomes.The myocardin-related transcription factor, MASTR, cooperates with MyoD to activate skeletal muscle gene expression.Growth and differentiation of C2 myogenic cells are dependent on serum response factor.RhoA GTPase and serum response factor control selectively the expression of MyoD without affecting Myf5 in mouse myoblastsFunctional studies of the Ciona intestinalis myogenic regulatory factor reveal conserved features of chordate myogenesisBarx2 controls myoblast fusion and promotes MyoD-mediated activation of the smooth muscle alpha-actin gene.Measuring spatial preferences at fine-scale resolution identifies known and novel cis-regulatory element candidates and functional motif-pair relationshipsMyoD Regulates Skeletal Muscle Oxidative Metabolism Cooperatively with Alternative NF-κBIncreased actin polymerization reduces the inhibition of serum response factor activity by Yin Yang 1.The dystrophin promoter is negatively regulated by YY1 in undifferentiated muscle cells.The Rho family G proteins play a critical role in muscle differentiationMyopathy-causing actin mutations promote defects in serum-response factor signalling.
P2860
Q24318909-605F5194-ACC0-4FBD-B14D-B41C73C23F61Q24550909-1EBB770D-E53A-44F5-BD6E-86788D92B77EQ24551186-DA450A4C-2C84-4CA2-865A-F6373AE788E9Q24554488-A5FB4241-333C-4904-B5FA-5EABF879DD1DQ24554518-E205B7B1-6B39-48D2-871A-4BB600FD0ACBQ24561871-B7B33311-8B8C-4D68-B00F-DA30CDF93AB7Q24642494-C0EA551F-9464-4B91-83ED-015B49067303Q24644315-B255AD59-EC42-4376-AEBC-22639F10185BQ24647342-9AF37B0C-1089-407E-81B1-6ADFBA4CDA7BQ27940149-4842122C-3360-4D45-8C7A-520F47E3AFD5Q28144390-3F560CD2-BDF8-446F-8504-5BE242DF4988Q28206982-3C619575-1FB9-4D7D-B110-0F81569BE40FQ28216516-4E58E4FF-BEB6-4B4F-BF0D-8B9421BACEBAQ28505560-EFE4E789-171C-47A3-9E9C-4B39B216FB2EQ28510988-5717E898-15FB-4DB6-B6A3-7CF097F567A6Q28569320-05D03643-FD67-4FA4-B580-D58928436E5EQ28583372-DD4B7275-59DE-4E85-B682-D95A11A0988DQ28588060-2B23EDEE-1E4D-4718-9B01-2A1C7C1CE4FCQ28591502-278C5967-B5CD-4D2E-991D-A7269EBB0D61Q30306237-135B5A44-5C27-462F-AE02-B4FBD771FD7DQ33340210-AFA4FA5F-07F9-421E-ABF5-E21BC738833DQ33602618-1297C232-71BA-41EE-B386-C85E598645B6Q33651582-F2D7F055-DFA0-4459-8C8B-4E31BBBA658CQ33863044-798BAF89-30AF-4A59-8928-4E5865D33CA6Q33963844-64B8880C-3536-49FB-9284-E79076501781Q34162543-03EE6F8D-A4A1-49D0-A699-2D45A8668533Q35071138-78E1C8CA-4BF0-470A-BA4C-E7D93BEBD3C1Q35484398-09B431A0-2C94-4CDB-90A3-20F2F576035BQ35840563-242C769E-46F0-4F9A-AC53-3023ED54ECEBQ36446376-3077E853-2C4A-4682-8AD3-38A90792CD23Q36563379-DAE6F47F-16FA-4F37-8F2C-672F2BCA85CBQ36891609-0529E8F7-3D36-451D-BFC9-D7413DDB8F8FQ36904587-826AEEE3-E23E-4AB6-BC17-3BEC9B604D50Q37200852-EC102DE5-58E1-4CB8-85DC-7C3AF8DDCE0CQ37273674-2386F1F7-2B8D-44FB-B8B1-C5433480DD4DQ37329000-45595512-1AD4-4F3B-B34E-0EFC6E5AA448Q38289021-023393A2-53BC-40EC-8079-CB3BCE7EB8F1Q38330791-A612D00E-4F6F-45BA-AF23-43CA03EF2521Q39574637-E4114D55-7C9D-48E2-AE78-95150FD6CD78Q39750008-616CDA13-60F6-4595-A3B4-47E0A6F3084A
P2860
Physical interaction between the mitogen-responsive serum response factor and myogenic basic-helix-loop-helix proteins
description
1996 nî lūn-bûn
@nan
1996 թուականի Մարտին հրատարակուած գիտական յօդուած
@hyw
1996 թվականի մարտին 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
Physical interaction between t ...... asic-helix-loop-helix proteins
@ast
Physical interaction between t ...... asic-helix-loop-helix proteins
@en
Physical interaction between t ...... asic-helix-loop-helix proteins
@nl
type
label
Physical interaction between t ...... asic-helix-loop-helix proteins
@ast
Physical interaction between t ...... asic-helix-loop-helix proteins
@en
Physical interaction between t ...... asic-helix-loop-helix proteins
@nl
prefLabel
Physical interaction between t ...... asic-helix-loop-helix proteins
@ast
Physical interaction between t ...... asic-helix-loop-helix proteins
@en
Physical interaction between t ...... asic-helix-loop-helix proteins
@nl
P2093
P50
P356
P1476
Physical interaction between t ...... asic-helix-loop-helix proteins
@en
P2093
H Masutani
M P Leibovitch
P304
P356
10.1074/JBC.271.9.5258
P407
P577
1996-03-01T00:00:00Z