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Dual specificity phosphatase 18

Dual-specificity phosphatases (DUSPs) constitute a large heterogeneous subgroup of the type I cysteine-based protein-tyrosine phosphatase superfamily. DUSPs are characterized by their ability to dephosphorylate both tyrosine and serine/threonine residues. They have been implicated as major modulators of critical signaling pathways. DUSP18 contains the consensus DUSP C-terminal catalytic domain but lacks the N-terminal CH2 domain found in the MKP (mitogen-activated protein kinase phosphatase) class of DUSPs (see MIM 600714) (summary by Patterson et al., 2009 [PubMed 19228121]).[supplied by OMIM, Dec 2009] (from NCBI)
Top mentioned proteins: DSP, DUSP26, iMpact, p38, des-1
Papers on DSP18
Comparative analysis of molecular mechanism of spinal cord injury with time based on bioinformatics data.
Sun et al., Beijing, China. In Spinal Cord, Nov 2015
Moreover, the TFs ZBTB7A and ELK1 and their target gene (dual specificity phosphatase 18 (DUSP18)) might be therapeutic targets for the treatment of SCI.Spinal Cord advance online publication, 27 October 2015; doi:10.1038/sc.2015.171.
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.
Distinguishing mitochondrial inner membrane orientation of dual specific phosphatase 18 and 21.
Dixon et al., San Diego, United States. In Methods Enzymol, 2008
DSP18 and DSP21 are targeted to mitochondria by internal localization signals.
Dual specificity phosphatases 18 and 21 target to opposing sides of the mitochondrial inner membrane.
Dixon et al., San Diego, United States. In J Biol Chem, 2008
Here, we identify two members of the atypical dual specificity phosphatases (DSP), DSP18 and DSP21, that are localized in mitochondria.
Structure of human DSP18, a member of the dual-specificity protein tyrosine phosphatase family.
Kim et al., Taej┼Ćn, South Korea. In Acta Crystallogr D Biol Crystallogr, 2006
The crystal structure of human DSP18 (official symbol DUSP18) has been determined at 2.0 A resolution.
Dual specificity phosphotase 18, interacting with SAPK, dephosphorylates SAPK and inhibits SAPK/JNK signal pathway in vivo.
Mao et al., Shanghai, China. In Front Biosci, 2005
DUSP18 appears to serve an important role by regulation of SAPK/JNK pathway
Molecular cloning and characterization of a novel dual-specificity phosphatase18 gene from human fetal brain.
Mao et al., Shanghai, China. In Biochim Biophys Acta, 2003
molecular cloning, base sequence and amino acid sequence
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