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Human SMAD2 Protein expressed in HEK-293 Cells - ABIN2732219
Atanelishvili, Shirai, Akter, Buckner, Noguchi, Silver, Bogatkevich: M10, a caspase cleavage product of the hepatocyte growth factor receptor, interacts with Smad2 and demonstrates antifibrotic properties in vitro and in vivo. in Translational research : the journal of laboratory and clinical medicine 2016
The non-Smad (show SMAD1 Proteins) JNK (show MAPK8 Proteins) signaling pathway, which is downstream of Nodal signaling, regulates nuclear movement independently of the Smad (show SMAD1 Proteins) pathway, and this nuclear movement is associated with Smad (show SMAD1 Proteins) signal transduction toward the nucleus.
The results of this study found that Bptf and TGF-beta (show TGFB1 Proteins)/Smad2 mediate nucleosome remodeling to regulate wnt8a (show WNT8A Proteins) expression and hence neural posteriorization.
Smad2 and Eomesodermin (show EOMES Proteins) a (Eomesa (show EOMES Proteins)) bind common genomic regions proximal to genes involved in mesoderm and endoderm formation, suggesting Eomesa (show EOMES Proteins) forms a general component of the Smad2 signalling complex in zebrafish.
These results reveal that kinesin-mediated transport of Smad2 along microtubules to the receptors is an essential step in ligand-induced Smad2 activation.
study systemically uncovers a large number of Smad2 targets in early gastrulas and suggests cooperative roles of Smad2 and other transcription factors in controlling target gene transcription
Nodal signaling and mesendoderm induction depend on Smad2/3 and suggest that transforming growth factor-beta signals other than Nodal also contribute to Smad2/3 signaling and embryonic patterning.
Smad2/3 activities play important roles not only in mesendodermal development but also in neural development during early vertebrate embryogenesis
Smad2 (and myostatin (show MSTN Proteins)) were significantly up-regulated in the failing heart of female patients, but not male patients.
Nodal signaling through the Smad2/3 pathway up-regulated Slug, Snail (show SNAI1 Proteins) and c-Myc (show MYC Proteins) to induce EMT (show ITK Proteins), thereby promotingVasculogenic mimicry (VM) formation.
this study shows that EGF (show EGF Proteins) induces epithelial-mesenchymal transition through phospho-Smad2/3-Snail (show SNAI1 Proteins) signaling pathway in breast cancer cells
Multiple myeloma cells adapted to long-term exposure to hypoxia exhibit stem cell characteristics with TGF-beta (show TGFB1 Proteins)/Smad (show SMAD1 Proteins) pathway activation.
a novel heterozygous missense mutation (c.833C>T, p.A278V) in the SMAD2 gene in a family with early onset aortic aneurysms
Data suggest that oncogenic Y-box binding protein 1 (YB-1 (show YBX1 Proteins)) indirectly enhances transforming growth factor beta (TGFbeta (show TGFB1 Proteins)) signaling cascades via Sma (show SMN1 Proteins)/Mad related protein 2 (Smad2)phospho-activation and may represent a promising factor for future diagnosis and therapy of breast cancer.
Asiaticoside hindered the invasive growth of KFs (show GDF6 Proteins) by inhibiting the GDF-9 (show GDF9 Proteins)/MAPK (show MAPK1 Proteins)/Smad (show SMAD1 Proteins) pathway.
High Smad2 expression is associated with invasion and metastasis in pancreatic ductal adenocarcinoma.
Data indicate that miR (show MLXIP Proteins)-206 inhibits neuropilin-1 (NRP1 (show NRP1 Proteins)) and SMAD2 gene expression by directly binding to their 3'-UTRs.
Results show that members of the Activin branch of the TGFbeta (show TGFB1 Proteins) signaling pathway, namely Put and Smad2, are autonomously required for cell and tissue growth in the Drosophila larval salivary gland.
Grg4 occupancy at the Xnr1 (show NODAL Proteins) enhancer significantly decreases with Smad2 overexpression.Nodal-activated Smad2 physically displaces Grg4 from FoxH1 (show FOXH1 Proteins) at the Xnr1 (show NODAL Proteins) enhancer, an essential feature of the transcriptional switch mechanism.
E2a (show TCF3 Proteins) is necessary to drive transcription of Smad2/3 target genes, including critical regulators of dorsal cell fate and morphogenesis
GDF11 (show GDF11 Proteins) has a central role in the activation of Smad2 phosphorylation in tailbud stage Xenopus embryos.
XPIASy functions as an essential negative regulator of the XSmad2 pathway to ensure proper mesoderm induction at the appropriate time and in the appropriate region.
Activin A (show INHBA Proteins) and overexpression of SMAD2/3 significantly promoted expressions of porcine NANOG (show NANOG Proteins) and OCT4 (show POU5F1 Proteins),maintaining induced pluripotent stem cell self-renewal through up-regulation of Nanog (show NANOG Proteins)/OCT4 (show POU5F1 Proteins) expression.
the present work provides evidence supporting a functional role of SMAD2/3 in bovine early embryogenesis
Mechanical compression not only with physiological but also with excessive stress can activate Smad2/3P signaling, which is known to be protective for articular cartilage and to block chondrocyte terminal differentiation.
a detailed computational model for TGF-beta (show TGFB1 Proteins) signalling that incorporates elements of previous models together with crosstalking between Smad1 (show SMAD1 Proteins)/5/8 and Smad2/3 channels through a negative feedback loop dependent on Smad7 (show SMAD7 Proteins).
Results suggest that Smad2/3 linker threonine phosphorylation is expressed during acinar-ductal metaplasia.
NODAL/Activin signaling induces dramatic chromatin landscape changes, and a dynamic transcriptional network regulated by SMAD2, acting via multiple mechanisms.
Blocking Smad2/3 signaling in pluripotent stem cells results in epigenetic changes that enhance the capacity for endoderm differentiation.
cells expressing mutant huntingtin (show HTT Proteins) have a dysregulated transcriptional response to epidermal growth factor (show EGF Proteins) stimulation
Smad2- and Smad3 (show SMAD3 Proteins)-deficient bone marrow (BM) cells display reduced sensitivity to transforming growth factor-beta (TGFbeta (show TGFB1 Proteins)) inhibition.
Data (including data from studies using knockout mice) suggest Garp/Lrrc32 (show LRRC32 Proteins) is involved in up-regulation of Tgfb3 (show TGFB3 Proteins) and is essential for embryogenesis of palate; Garp (show LRRC32 Proteins) knockout causes postnatal lethality, cleft palate, and decreased apoptosis and Smad2 phosphorylation in medial edge epithelial cells of palatal shelf of embryos. (Garp (show LRRC32 Proteins) = glycoprotein A repetitions predominant (show LRRC32 Proteins) protein; Tgfb3 (show TGFB3 Proteins) = transforming growth factor beta 3 (show TGFB3 Proteins))
This study tested the hypothesis that inhibins act in an autocrine manner on Leydig cells using a pre-pubertal Leydig cell line, TM3 (show TPM1 Proteins), as a model of immature Leydig cells.
Lnc-LFAR1 binds directly to Smad2/3 and promotes transcription of TGFbeta (show TGFB1 Proteins), Smad2, Smad3 (show SMAD3 Proteins), Notch2 (show NOTCH2 Proteins) and Notch3 (show NOTCH3 Proteins) which, in turn, results in TGFbeta (show TGFB1 Proteins) and Notch (show NOTCH1 Proteins) pathway activation.
P311 (show C5orf13 Proteins) is a novel TGFbeta1 (show TGFB1 Proteins)/Smad (show SMAD1 Proteins) signaling-mediated regulator of transdifferentiation in epidermal stem cells during cutaneous wound healing.
the levels of Smad2/3, P-Smad2/3 expressions were decreased, while the level of Smad7 (show SMAD7 Proteins) expression was increased after treatment with osthole.
The protein encoded by this gene belongs to the SMAD, a family of proteins similar to the gene products of the Drosophila gene 'mothers against decapentaplegic' (Mad) and the C. elegans gene Sma. SMAD proteins are signal transducers and transcriptional modulators that mediate multiple signaling pathways. This protein mediates the signal of the transforming growth factor (TGF)-beta, and thus regulates multiple cellular processes, such as cell proliferation, apoptosis, and differentiation. This protein is recruited to the TGF-beta receptors through its interaction with the SMAD anchor for receptor activation (SARA) protein. In response to TGF-beta signal, this protein is phosphorylated by the TGF-beta receptors. The phosphorylation induces the dissociation of this protein with SARA and the association with the family member SMAD4. The association with SMAD4 is important for the translocation of this protein into the nucleus, where it binds to target promoters and forms a transcription repressor complex with other cofactors. This protein can also be phosphorylated by activin type 1 receptor kinase, and mediates the signal from the activin. Alternatively spliced transcript variants have been observed for this gene.
SMAD, mothers against DPP homolog 2
, MAD (mothers against decapentaplegic, Drosophila) homolog 2
, SMA- and MAD-related protein 2
, SMAD 2
, SMAD family member 2
, mothers against DPP homolog 2
, mothers against decapentaplegic homolog 2
, MAD homolog 2
, Sma- and Mad-related protein 2
, mother against DPP homolog 2
, mothers against decapentaplegic-like 2
, Smad 2
, mad-related protein 2