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LDB2 wa (显示 LDLR ELISA试剂盒)s the most co (显示 APOB ELISA试剂盒)nnected gene in a transcription factor regulatory network inferred from transendothelial migration of leukocyte and atherosclerosis module genes in coronary and carotid artery disease macrophages.
The transcription co-factor LIM domain binding 2 (LDB2) was identified as a potential high-hierarchy regulator of the atherosclerosis-module.
Results show that CLP36 is accumulated in Atg7 (显示 ATG7 ELISA试剂盒)-deficient cardiomyocytes, and suggest that autophagy may protect cardiomyocytes from the ischemia-reperfusion injury through the clearance of CLP36.
An intricate regulatory network exists that is mediated by Ldb1 (显示 LDB1 ELISA试剂盒) and Ldb2, and promotes retinal progenitor cells proliferation and multipotency; it also controls specification of mammalian retina cells.
CLIM interacts with estrogen receptor alpha (显示 ESR1 ELISA试剂盒) at the H19 (显示 NCKAP1 ELISA试剂盒) locus, potentially explaining the higher expression of H19 (显示 NCKAP1 ELISA试剂盒) in female than male corneas.
In Ldlr (显示 LDLR ELISA试剂盒)(-/-)Apob(100 (显示 APOB ELISA试剂盒)/100) mice, loss of Ldb2 increased atherosclerotic lesion size approximately 2-fold and decreased plaque stability.
Isl1 (显示 ISL1 ELISA试剂盒) and the Ldb co-regulators of transcription are essential early determinants of mouse limb development
Data show an inhibitory function of CLP-36 in GPVI (显示 GP6 ELISA试剂盒) immunoreceptor tyrosine-based activation motif signaling and as a key regulator of arterial thrombosis.
Data suggest that Ldb1 (显示 LDB1 ELISA试剂盒)/2 function to maintain SLK (显示 SLK ELISA试剂盒) in an inactive state before its activation.
results indicate that alpha-actinin, CLP36 and palladin form a protein complex and contribute to regulation of the actin cytoskeleton
splice isoforms lacking the LIm (显示 PDLIM5 ELISA试剂盒)-interaction domain are present in the Ldb1 (显示 LDB1 ELISA试剂盒) genes of mammals, chick, and Xenopus.
The fine tuning of TGF-beta (显示 TGFB1 ELISA试剂盒) signaling derives from positive and negative control by Ldb2a.
Genes encoding LIM domain-binding factors were initially isolated in a screen for proteins that physically interact with the LIM domains of nuclear proteins (summarized by Semina et al., 1998
LIM domain binding 2
, LIM domain-binding protein 2-like
, LIM domain binding protein CLIM-1
, LIM domain-binding factor CLIM1
, LIM domain-binding protein 2
, carboxyl-terminal LIM domain-binding protein 1
, LIM binding domain 2
, LIM domain-binding factor-2
, LIM-domain-binding protein 2a
, LIM-domain-binding protein 2b
, LIM-domain binding factor 2