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Data suggest that up-regulation of SHC threonine phosphorylation is responsible for elevated Akt (show AKT1 Proteins)-signaling and Erk (show EPHB2 Proteins)-signaling in triple-negative breast cancer cell lines.
Characterization of bioenergetic parameters and reactive oxygen species production showed that the cellular model of Leigh syndrome is described by increased intracellular oxidative stress and oxidative damage to DNA and proteins, which correlate with increased p66Shc phosphorylation at Ser36.
A positive relationship between the p66Shc expression and oxidative stress was found. p66Shc and oxidative stress were significant predictors of the degree of tubular damage.
Adeno (show ADORA2A Proteins)-X Adenoviral System 3 can be used to efficiently construct recombinant adenovirus containing p66Shc gene, and the Adeno (show ADORA2A Proteins)-X can inhibit the proliferation of MCF-7 cells by inducing cell cycle arrest at the G2/M phase
STAT4 (show STAT4 Proteins) is a novel transcriptional regulator of p66Shc in normal and chronic lymphocytic leukemia B cells
Isoform b of DDR1 is responsible for collagen I-induced up-regulation of N-cadherin (show CDH2 Proteins) and tyrosine 513 of DDR1b is necessary.
NIC (show NCSTN Proteins) exacerbated AZA-dependent injury via augmenting p66shc transcription. While RES suppressed NIC (show NCSTN Proteins)+AZA-mediated injury, -surprisingly-it further enhanced activity of the p66shc promoter. RES protected cells via the cytoplasmic p66shc/Nrf2 (show GABPA Proteins)/heme oxygenase-1 (HO-1 (show HMOX1 Proteins)) axis
The results show that the interaction between STS-1 (show STS1 Proteins) and ShcA is regulated in response to EGF receptor (show EGFR Proteins) activation.
Nox4 (show NOX4 Proteins)-derived H2O2 in part activates Nox2 (show CYBB Proteins) to increase mitochondrial ROS (show ROS1 Proteins) via pSer36-p66Shc, thereby enhancing VEGFR2 (show KDR Proteins) signaling and angiogenesis in endothelial cells.
Taken together, these data argue for a complex mechanism of PKC-beta-dependent regulation of SH (show POLD3 Proteins)CA (p66) activation invol (show SIGLEC1 Proteins)ving Ser(139) and a motif surroun (show SIGLEC1 Proteins)ding Ser(213).
Data show that adaptor protein Shc is required for angiogenesis in zebrafish (accession number LOC563639), mice, and human vascular endothelial cell-culture models.
ShcA is required for Wnt-5a (show WNT5A Proteins)/Ror2 (show ROR2 Proteins) mediated upregulation of xPAPC (show PCDH8 Proteins), which demonstrates the functional relevance of this interaction.
Studied p66Shc levels, redox state, and developmental potential in early bovine embryos. p66Shc content was increased by either high (20%) O(2) culture or H(2)O(2) treatment, and significantly dec'd by antioxidant polyethylene glycol-conjugated catalase (show CAT Proteins).
p66shc, but not p53 (show TP53 Proteins), is significantly more abundant in an embryo population that exhibits higher frequencies of embryo arrest.
p66Shc is involved in the regulation of embryo development specifically in mediating early cleavage arrest and facilitating development to the blastocyst stage for in vitro produced bovine embryos
These results support a model in which Shc orchestrates signals from cell-cell and cell-matrix adhesions to elicit flow-induced inflammatory signaling.
Sirt3 (show SIRT3 Proteins) modulates age-associated mitochondrial biology and function via lysine deacetylation of target proteins, and authors show that its regulation depends on its nitration status and is benefited by the improved NAD(+)/NADH ratio in aged p66(Shc(-/-)) brain mitochondria.
miR (show MLXIP Proteins)-200c might be responsible for muscle wasting and myotube loss, most probably via a p66Shc-dependent mechanism in a pathological disease such as Duchenne muscular dystrophy (show DMD Proteins).
Data show that 66-kDa Src (show SRC Proteins) homology 2 domain-containing protein (p66Shc) is acetylated under high glucose conditions and is deacetylated by Sirtuin1 (show SIRT1 Proteins) lysine deacetylase (Sirt1 (show SIRT1 Proteins)) on lysine 81.
P66Shc, a key regulator of metabolism and mitochondrial ROS (show ROS1 Proteins) production, is dysregulated by mouse embryo culture
The results indicate that Shc proteins should be considered as potential targets for developing interventions to mitigate weight gain on high-fat diet by stimulating energy expenditure.
Hyperglycemia and elevated free fatty acids in the diabetic milieu recruit p66Shc to upregulate endothelial miR (show MLXIP Proteins)-34a via an oxidant-sensitive mechanism, which leads to endothelial dysfunction by targeting Sirt1 (show SIRT1 Proteins).
p66SHC-mediated oxidative stress and telomere shortening synergize in some tissues (including testes) to accelerate aging.
Taken together, these data argue for a complex mechanism of PKCbeta-dependent regulation of p66 (show POLD3 Proteins) activation involving Ser (show SIGLEC1 Proteins)(139) and a motif surrounding Ser (show SIGLEC1 Proteins)(213).
JNK1 (show MAPK8 Proteins)/2-dependent regulation of p66ShcS36 phosphorylation, is reported.
Data show that the major mitochondrial partner of Shc adaptor protein p46Shc is the lipid oxidation enzyme 3-ketoacylCoA thiolase (show HADHB Proteins) ACAA2 (show ACAA2 Proteins), to which p46Shc binds directly and with a strong affinity.
This gene encodes three main isoforms that differ in activities and subcellular location. While all three are adapter proteins in signal transduction pathways, the longest (p66Shc) may be involved in regulating life span and the effects of reactive oxygen species. The other two isoforms, p52Shc and p46Shc, link activated receptor tyrosine kinases to the Ras pathway by recruitment of the GRB2/SOS complex. p66Shc is not involved in Ras activation. Unlike the other two isoforms, p46Shc is targeted to the mitochondrial matrix. Several transcript variants encoding different isoforms have been found for this gene.
SHC (Src homology 2 domain containing) transforming protein 1
, Sporulation-specific activator of Chs3p (chitin synthase III), required for the synthesis of the chitosan layer of ascospores; has similarity to Skt5p, which activates Chs3p during vegetative growth; transcriptionally induced at alkaline pH
, squalene--hopene cyclase
, SH2 domain protein C1
, SHC-transforming protein 1
, src homology 2 domain-containing-transforming protein C1
, SHC-transforming protein 1-like
, SHC (Src homology 2 domain-containing) transforming protein 1
, SHC-transforming protein 3
, SHC-transforming protein A
, src homology 2 domain-containing transforming protein C1
, src homology collagen
, adaptor protein SHC