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proteins. Page last changed on 19 Dec 2016.
Thioredoxin
Thioredoxin, SASP
The protein encoded by this gene acts as a homodimer and is involved in many redox reactions. The encoded protein is active in the reversible S-nitrosylation of cysteines in certain proteins, which is part of the response to intracellular nitric oxide. This protein is found in the cytoplasm. Two transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Oct 2011] (from
NCBI)
We demonstrate that the loss of salivary function was closely accompanied by cellular senescence, as evidenced by a persistent DNA damage response (γH2AX, 53BP1) and the expression of senescence-associated markers (SA-βgal, p19ARF, DcR2) and secretory phenotype (SASP) factors (PAI-1, IL-6).
da Silva Neto et al., São Paulo, Brazil. In Free Radic Res, Feb 2016
Thioredoxin (Trx) proteins were the first enzymes described to accelerate thiol-disulfide exchange reactions and their high reactivity is related to the high nucleophilicity of the attacking thiol.
Bonafè et al., Ancona, Italy. In Oncotarget, Dec 2015
DDR activation in senescent cells promotes acquisition of a proinflammatory secretory phenotype (SASP), which in turn elicits DDR and SASP activation in neighboring cells, thereby creating a proinflammatory environment extending at the local and eventually the systemic level.
Yoon et al., Suwŏn, South Korea. In Bmb Rep, Oct 2015
The most significant environmental effector resulting from senescent cells is the senescence-associated secretory phenotype (SASP), which is constituted by a strikingly increased expression and secretion of diverse pro-inflammatory cytokines.
Elledge et al., Boston, United States. In Science, Oct 2015
A striking feature of senescence is the senescence-associated secretory phenotype (SASP), a pro-inflammatory response linked to tumor promotion and aging.
Campisi et al., Novato, United States. In Nat Cell Biol, Aug 2015
However, as senescent cells accumulate with age, the senescence-associated secretory phenotype (SASP) can disrupt tissues and contribute to age-related pathologies, including cancer.
Sheer et al., Memphis, United States. In Acta Neuropathol Commun, 2014
Furthermore, IGFBP7 and CEBPB, which are transcriptional inducers of the senescence-associated secretory phenotype (SASP), were also up-regulated together with the markers of senescence and inflammation, CDKN1A (p21), CDKN2A (p16) and IL1B.
Santos et al., Buenos Aires, Argentina. In Protein Pept Lett, 2014
Thioredoxin (TRX) catalyzes redox reactions via the reversible oxidation of the conserved active center CGPC and it is involved in multiple biological processes, some of them linked to redox activity while others not.
Mishra et al., Mumbai, India. In Indian J Med Res, 2014
Besides persistent double strand (ds) DNA breaks and increased β-galactosidase activity, biological significance of telomeric attrition in conjunction with senescence associated secretory phenotype (SASP) has been highlighted in SIPS.
Embryonic senescent cells are nonproliferative and share features with oncogene-induced senescence (OIS), including expression of p21, p15, and mediators of the senescence-associated secretory phenotype (SASP).
We demonstrate that this is linked to massive proteotoxic stress, which is a consequence of the senescence-associated secretory phenotype (SASP) described previously.
Mazo et al., Philadelphia, United States. In Cell, 2012
Data imply that Trx, Pc, and E(z) remain bound or rapidly rebind to nascent DNA in the absence of trimethylated histones during DNA replication in Drosophila embryos.
Rouis et al., Paris, France. In Arterioscler Thromb Vasc Biol, 2012
The ability of Trx-1 to promote differentiation of macrophages into an alternative, anti-inflammatory phenotype may explain its protective effects in cardiovascular diseases.
Pham et al., Houston, United States. In Oncotarget, 2012
Trx-1 plays a key role in cell growth and survival, as well as chemoresistance, and is a potential target to overcome drug resistance in relapsed/refractory Diffuse large B-cell lymphoma.
Dikiy et al., Trondheim, Norway. In J Biomed Biotechnol, 2011
MsrB1/Trx complex was studied in attempt to understand MsrB1 reduction mechanism. Using NMR data, molecular mechanics, protein docking & molecular dynamics simulations, found that intermediate MsrB1/Trx complex is stabilized by interprotein beta-layer.