Structure/function analysis of mouse Purbeta, a single-stranded DNA-binding repressor of vascular smooth muscle alpha-actin gene transcription.
about
Induction of vascular smooth muscle alpha-actin gene transcription in transforming growth factor beta1-activated myofibroblasts mediated by dynamic interplay between the Pur repressor proteins and Sp1/Smad coactivatorsDetection of protein-DNA interaction with a DNA probe: distinction between single-strand and double-strand DNA-protein interaction.Hydrodynamic studies on the quaternary structure of recombinant mouse Purbeta.YB-1 coordinates vascular smooth muscle alpha-actin gene activation by transforming growth factor beta1 and thrombin during differentiation of human pulmonary myofibroblastsThe Purα/Purβ single-strand DNA-binding proteins attenuate smooth-muscle actin gene transactivation in myofibroblasts.Puralpha and Purbeta collaborate with Sp3 to negatively regulate beta-myosin heavy chain gene expression during skeletal muscle inactivity.Smooth muscle alpha-actin expression and myofibroblast differentiation by TGFbeta are dependent upon MK2.Transforming growth factor beta1-mediated activation of the smooth muscle alpha-actin gene in human pulmonary myofibroblasts is inhibited by tumor necrosis factor-alpha via mitogen-activated protein kinase kinase 1-dependent induction of the Egr-1 tMechanism of strand-specific smooth muscle alpha-actin enhancer interaction by purine-rich element binding protein B (Purbeta).Sequence specificity of single-stranded DNA-binding proteins: a novel DNA microarray approachDynamic Interplay of Smooth Muscle α-Actin Gene-Regulatory Proteins Reflects the Biological Complexity of Myofibroblast Differentiation.Structure-function analysis of mouse Pur beta II. Conformation altering mutations disrupt single-stranded DNA and protein interactions crucial to smooth muscle alpha-actin gene repression.Cell cycle-mediated regulation of smooth muscle alpha-actin gene transcription in fibroblasts and vascular smooth muscle cells involves multiple adenovirus E1A-interacting cofactors.Structural basis of multisite single-stranded DNA recognition and ACTA2 repression by purine-rich element binding protein B (Purβ).Isolation and characterization of the core single-stranded DNA-binding domain of purine-rich element binding protein B (Purβ).Expression and network analysis of YBX1 interactors for identification of new drug targets in lung adenocarcinoma.
P2860
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P2860
Structure/function analysis of mouse Purbeta, a single-stranded DNA-binding repressor of vascular smooth muscle alpha-actin gene transcription.
description
2003 nî lūn-bûn
@nan
2003年の論文
@ja
2003年学术文章
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2003年学术文章
@zh-cn
2003年学术文章
@zh-hans
2003年学术文章
@zh-my
2003年学术文章
@zh-sg
2003年學術文章
@yue
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@zh-hant
name
Structure/function analysis of ...... lpha-actin gene transcription.
@en
type
label
Structure/function analysis of ...... lpha-actin gene transcription.
@en
prefLabel
Structure/function analysis of ...... lpha-actin gene transcription.
@en
P2093
P2860
P356
P1476
Structure/function analysis of ...... lpha-actin gene transcription.
@en
P2093
Arthur R Strauch
John A Polikandriotis
Robert J Kelm
Shu-Xia Wang
P2860
P304
38749-38757
P356
10.1074/JBC.M306163200
P407
P577
2003-07-21T00:00:00Z