gopubmed logo
find other proteinsAll proteins
GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 19 Dec 2016.

Dual specificity phosphatase 26

DUSP26, ldp4, MKP-8, dsp4, MAP kinase phosphatase-8, mitogen-activated protein kinase phosphatase-8
Top mentioned proteins: MAPK, p38, p53, Phospho, ACID
Papers on DUSP26
Common variants associated with changes in levels of circulating free fatty acids after administration of glucose-insulin-potassium (GIK) therapy in the IMMEDIATE trial.
Peter et al., New York City, United States. In Pharmacogenomics J, Jan 2016
Nearest to DUSP26, rs7464104 was associated with a decrease in unsaturated FFAs (P2df=5.51 × 10(-7)).
VHR/DUSP3 phosphatase: structure, function and regulation.
Köhn et al., Heidelberg, Germany. In Febs J, May 2015
We give a detailed overview of VHR/DUSP3 phosphatase and compare it with its most closely related phosphatases DUSP13B, DUSP26 and DUSP27.
NSC-87877 inhibits DUSP26 function in neuroblastoma resulting in p53-mediated apoptosis.
Yang et al., Houston, United States. In Cell Death Dis, 2014
Dual specificity protein phosphatase 26 (DUSP26) is overexpressed in high-risk neuroblastoma (NB) and contributes to chemoresistance by inhibiting p53 function.
Targeting DUSPs in glioblastomas - wielding a double-edged sword?
Velpula et al., Lakeland, United States. In Cell Biol Int, 2014
This review identifies and summarize the specific roles of DUSP1, DUSP4, DUSP6 and DUSP26 that have been implicated in GBM.
The DUSP26 phosphatase activator adenylate kinase 2 regulates FADD phosphorylation and cell growth.
Jung et al., Seoul, South Korea. In Nat Commun, 2013
AK2 forms a complex with dual-specificity phosphatase 26 (DUSP26) phosphatase and stimulates DUSP26 activity independently of its AK activity.
Combining affinity proteomics and network context to identify new phosphatase substrates and adapters in growth pathways.
Cesareni et al., Roma, Italy. In Front Genet, 2013
By this approach we rediscover several previously described phosphatase substrate interactions and characterize two new protein scaffolds that promote the dephosphorylation of PTPN11 and ERK by DUSP18 and DUSP26, respectively.
High-resolution crystal structure of the catalytic domain of human dual-specificity phosphatase 26.
Chi et al., Taejŏn, South Korea. In Acta Crystallogr D Biol Crystallogr, 2013
Human DUSP26 inhibits the apoptosis of cancer cells by dephosphorylating substrates such as p38 and p53.
Atomic structure of dual-specificity phosphatase 26, a novel p53 phosphatase.
Cingolani et al., Philadelphia, United States. In Biochemistry, 2013
Dual-specificity phosphatase 26 (DUSP26) is a brain phosphatase highly overexpressed in neuroblastoma, which has been implicated in dephosphorylating phospho-Ser20 and phospho-Ser37 in the p53 transactivation domain.
Distinct adrenergic system changes and neuroinflammation in response to induced locus ceruleus degeneration in APP/PS1 transgenic mice.
Heneka et al., Berlin, Germany. In Neuroscience, 2011
In order to study the effects of NE depletion on cortical and hippocampal adrenergic system changes, LC degeneration was induced in 3-month-old APP/PS1 mice by the neurotoxin N-(2-chloroethyl)-N-ethyl-bromo-benzylamine (dsp4).
Induced LC degeneration in APP/PS1 transgenic mice accelerates early cerebral amyloidosis and cognitive deficits.
Heneka et al., Berlin, Germany. In Neurochem Int, 2010
In order to model the pathology of the human disease and to study the effects of norepinephrine-depletion on amyloid precursor protein processing, behaviour, and neuroinflammation, locus ceruleus degeneration was induced in mice coexpressing the swedish mutant of the amyloid precursor protein and the presenilin 1 DeltaExon 9 mutant (APP/PS1) using the neurotoxin N-(2-chloroethyl)-N-ethyl-bromo-benzylamine (dsp4) starting treatment at 3 months of age.
Dual-specificity phosphatase 26 is a novel p53 phosphatase and inhibits p53 tumor suppressor functions in human neuroblastoma.
Yang et al., Houston, United States. In Oncogene, 2010
DUSP26 functions as a p53 phosphatase
DUSP26 negatively affects the proliferation of epithelial cells, an effect not mediated by dephosphorylation of MAPKs.
O'Brien et al., Australia. In Biochim Biophys Acta, 2010
DUSP26 may function as a tumour suppressor in particular cancers.
NSC-87877, inhibitor of SHP-1/2 PTPs, inhibits dual-specificity phosphatase 26 (DUSP26).
Cho et al., Seoul, South Korea. In Biochem Biophys Res Commun, 2009
Phosphatase activity of dual-specificity protein phosphatase 26 (DUSP26) was decreased by the inhibitor in a dose-dependent manner.
Protein phosphatase Dusp26 associates with KIF3 motor and promotes N-cadherin-mediated cell-cell adhesion.
Shima et al., Japan. In Oncogene, 2009
Downregulation of Dusp26 may contribute to malignant phenotypes of glioma.
A novel amplification target, DUSP26, promotes anaplastic thyroid cancer cell growth by inhibiting p38 MAPK activity.
Inazawa et al., Tokyo, Japan. In Oncogene, 2007
DUSP26 effectively dephosphorylates p38 and has a little effect on extracellular signal-regulated kinase in anaplastic thyroid cancer.
share on facebooktweetadd +1mail to friends