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Dual specificity protein phosphatase (EC 3 1 3 16) (EC 3 1 3 48)

 J9P4Q2_CANLF            Unreviewed;       369 AA.
J9P4Q2;
31-OCT-2012, integrated into UniProtKB/TrEMBL.
31-OCT-2012, sequence version 1.
13-FEB-2019, entry version 44.
RecName: Full=Dual specificity protein phosphatase {ECO:0000256|PIRNR:PIRNR000939};
EC=3.1.3.16 {ECO:0000256|PIRNR:PIRNR000939};
EC=3.1.3.48 {ECO:0000256|PIRNR:PIRNR000939};
Name=DUSP1 {ECO:0000313|VGNC:VGNC:51892};
Canis lupus familiaris (Dog) (Canis familiaris).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae;
Canis.
NCBI_TaxID=9615 {ECO:0000313|Ensembl:ENSCAFP00000040531, ECO:0000313|Proteomes:UP000002254};
[1] {ECO:0000313|Ensembl:ENSCAFP00000040531, ECO:0000313|Proteomes:UP000002254}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Boxer {ECO:0000313|Ensembl:ENSCAFP00000040531,
ECO:0000313|Proteomes:UP000002254};
PubMed=16341006; DOI=10.1038/nature04338;
Broad Sequencing Platform;
Lindblad-Toh K., Wade C.M., Mikkelsen T.S., Karlsson E.K., Jaffe D.B.,
Kamal M., Clamp M., Chang J.L., Kulbokas E.J. III, Zody M.C.,
Mauceli E., Xie X., Breen M., Wayne R.K., Ostrander E.A.,
Ponting C.P., Galibert F., Smith D.R., deJong P.J., Kirkness E.F.,
Alvarez P., Biagi T., Brockman W., Butler J., Chin C.-W., Cook A.,
Cuff J., Daly M.J., DeCaprio D., Gnerre S., Grabherr M., Kellis M.,
Kleber M., Bardeleben C., Goodstadt L., Heger A., Hitte C., Kim L.,
Koepfli K.-P., Parker H.G., Pollinger J.P., Searle S.M.J.,
Sutter N.B., Thomas R., Webber C., Baldwin J., Abebe A.,
Abouelleil A., Aftuck L., Ait-Zahra M., Aldredge T., Allen N., An P.,
Anderson S., Antoine C., Arachchi H., Aslam A., Ayotte L.,
Bachantsang P., Barry A., Bayul T., Benamara M., Berlin A.,
Bessette D., Blitshteyn B., Bloom T., Blye J., Boguslavskiy L.,
Bonnet C., Boukhgalter B., Brown A., Cahill P., Calixte N.,
Camarata J., Cheshatsang Y., Chu J., Citroen M., Collymore A.,
Cooke P., Dawoe T., Daza R., Decktor K., DeGray S., Dhargay N.,
Dooley K., Dooley K., Dorje P., Dorjee K., Dorris L., Duffey N.,
Dupes A., Egbiremolen O., Elong R., Falk J., Farina A., Faro S.,
Ferguson D., Ferreira P., Fisher S., FitzGerald M., Foley K.,
Foley C., Franke A., Friedrich D., Gage D., Garber M., Gearin G.,
Giannoukos G., Goode T., Goyette A., Graham J., Grandbois E.,
Gyaltsen K., Hafez N., Hagopian D., Hagos B., Hall J., Healy C.,
Hegarty R., Honan T., Horn A., Houde N., Hughes L., Hunnicutt L.,
Husby M., Jester B., Jones C., Kamat A., Kanga B., Kells C.,
Khazanovich D., Kieu A.C., Kisner P., Kumar M., Lance K., Landers T.,
Lara M., Lee W., Leger J.-P., Lennon N., Leuper L., LeVine S., Liu J.,
Liu X., Lokyitsang Y., Lokyitsang T., Lui A., Macdonald J., Major J.,
Marabella R., Maru K., Matthews C., McDonough S., Mehta T.,
Meldrim J., Melnikov A., Meneus L., Mihalev A., Mihova T., Miller K.,
Mittelman R., Mlenga V., Mulrain L., Munson G., Navidi A., Naylor J.,
Nguyen T., Nguyen N., Nguyen C., Nguyen T., Nicol R., Norbu N.,
Norbu C., Novod N., Nyima T., Olandt P., O'Neill B., O'Neill K.,
Osman S., Oyono L., Patti C., Perrin D., Phunkhang P., Pierre F.,
Priest M., Rachupka A., Raghuraman S., Rameau R., Ray V., Raymond C.,
Rege F., Rise C., Rogers J., Rogov P., Sahalie J., Settipalli S.,
Sharpe T., Shea T., Sheehan M., Sherpa N., Shi J., Shih D., Sloan J.,
Smith C., Sparrow T., Stalker J., Stange-Thomann N., Stavropoulos S.,
Stone C., Stone S., Sykes S., Tchuinga P., Tenzing P., Tesfaye S.,
Thoulutsang D., Thoulutsang Y., Topham K., Topping I., Tsamla T.,
Vassiliev H., Venkataraman V., Vo A., Wangchuk T., Wangdi T.,
Weiand M., Wilkinson J., Wilson A., Yadav S., Yang S., Yang X.,
Young G., Yu Q., Zainoun J., Zembek L., Zimmer A., Lander E.S.;
"Genome sequence, comparative analysis and haplotype structure of the
domestic dog.";
Nature 438:803-819(2005).
[2] {ECO:0000313|Ensembl:ENSCAFP00000040531}
IDENTIFICATION.
STRAIN=Boxer {ECO:0000313|Ensembl:ENSCAFP00000040531};
Ensembl;
Submitted (SEP-2012) to UniProtKB.
-!- CATALYTIC ACTIVITY:
Reaction=H2O + O-phospho-L-threonyl-[protein] = L-threonyl-
[protein] + phosphate; Xref=Rhea:RHEA:47004, Rhea:RHEA-
COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15377,
ChEBI:CHEBI:30013, ChEBI:CHEBI:43474, ChEBI:CHEBI:61977;
EC=3.1.3.16; Evidence={ECO:0000256|PIRNR:PIRNR000939};
-!- CATALYTIC ACTIVITY:
Reaction=H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein]
+ phosphate; Xref=Rhea:RHEA:10684, Rhea:RHEA-COMP:10136,
Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474,
ChEBI:CHEBI:46858, ChEBI:CHEBI:82620; EC=3.1.3.48;
Evidence={ECO:0000256|PIRNR:PIRNR000939};
-!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family.
Non-receptor class dual specificity subfamily.
{ECO:0000256|PIRNR:PIRNR000939, ECO:0000256|SAAS:SAAS00724126}.
-----------------------------------------------------------------------
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EMBL; AAEX03003007; -; NOT_ANNOTATED_CDS; Genomic_DNA.
SMR; J9P4Q2; -.
STRING; 9615.ENSCAFP00000040531; -.
PaxDb; J9P4Q2; -.
Ensembl; ENSCAFT00000047739; ENSCAFP00000040531; ENSCAFG00000029826.
VGNC; VGNC:51892; DUSP1.
eggNOG; KOG1716; Eukaryota.
eggNOG; COG2453; LUCA.
GeneTree; ENSGT00940000159044; -.
InParanoid; J9P4Q2; -.
OMA; MVIMEVP; -.
TreeFam; TF105122; -.
Reactome; R-CFA-112409; RAF-independent MAPK1/3 activation.
Reactome; R-CFA-5675221; Negative regulation of MAPK pathway.
Proteomes; UP000002254; Chromosome 4.
Bgee; ENSCAFG00000029826; Expressed in 3 organ(s), highest expression level in liver.
GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
GO; GO:0005634; C:nucleus; IBA:GO_Central.
GO; GO:0017017; F:MAP kinase tyrosine/serine/threonine phosphatase activity; IBA:GO_Central.
GO; GO:0051019; F:mitogen-activated protein kinase binding; IEA:Ensembl.
GO; GO:0004722; F:protein serine/threonine phosphatase activity; IEA:Ensembl.
GO; GO:0004725; F:protein tyrosine phosphatase activity; IEA:UniProtKB-EC.
GO; GO:0008138; F:protein tyrosine/serine/threonine phosphatase activity; IBA:GO_Central.
GO; GO:1990869; P:cellular response to chemokine; IEA:Ensembl.
GO; GO:0000188; P:inactivation of MAPK activity; IBA:GO_Central.
GO; GO:0007162; P:negative regulation of cell adhesion; IEA:Ensembl.
GO; GO:0008285; P:negative regulation of cell population proliferation; IEA:Ensembl.
GO; GO:0090027; P:negative regulation of monocyte chemotaxis; IEA:Ensembl.
GO; GO:1903753; P:negative regulation of p38MAPK cascade; IEA:Ensembl.
GO; GO:0070262; P:peptidyl-serine dephosphorylation; IEA:Ensembl.
GO; GO:0035970; P:peptidyl-threonine dephosphorylation; IEA:Ensembl.
CDD; cd00127; DSPc; 1.
Gene3D; 3.90.190.10; -; 1.
InterPro; IPR020417; Atypical_DUSP.
InterPro; IPR000340; Dual-sp_phosphatase_cat-dom.
InterPro; IPR024950; DUSP.
InterPro; IPR008343; MKP.
InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
InterPro; IPR016130; Tyr_Pase_AS.
InterPro; IPR003595; Tyr_Pase_cat.
InterPro; IPR000387; TYR_PHOSPHATASE_dom.
InterPro; IPR020422; TYR_PHOSPHATASE_DUAL_dom.
PANTHER; PTHR10159; PTHR10159; 1.
Pfam; PF00782; DSPc; 1.
PIRSF; PIRSF000939; MAPK_Ptase; 1.
PRINTS; PR01908; ADSPHPHTASE.
PRINTS; PR01764; MAPKPHPHTASE.
SMART; SM00195; DSPc; 1.
SMART; SM00404; PTPc_motif; 1.
SUPFAM; SSF52799; SSF52799; 1.
PROSITE; PS00383; TYR_PHOSPHATASE_1; 1.
PROSITE; PS50056; TYR_PHOSPHATASE_2; 1.
PROSITE; PS50054; TYR_PHOSPHATASE_DUAL; 1.
3: Inferred from homology;
Complete proteome {ECO:0000313|Proteomes:UP000002254};
Hydrolase {ECO:0000256|PIRNR:PIRNR000939};
Protein phosphatase {ECO:0000256|PIRNR:PIRNR000939};
Reference proteome {ECO:0000313|Proteomes:UP000002254}.
DOMAIN 175 315 Tyrosine-protein phosphatase.
{ECO:0000259|PROSITE:PS50054}.
DOMAIN 240 294 TYR_PHOSPHATASE_2.
{ECO:0000259|PROSITE:PS50056}.
ACT_SITE 260 260 Phosphocysteine intermediate.
{ECO:0000256|PIRSR:PIRSR000939-1}.
SEQUENCE 369 AA; 39573 MW; 23FA04D0A99D96EE CRC64;
IVVDVGAVHA GVLRTLLRER AAQCLLLDCR FFLAANAGHS AGSGHVRFRT MVQRRDRGAT
GPEPVGPLAR RRGRLRAGAH PARVLLLKRT PPGGARAPRP APRAPRPAPA GPQPPRAAPP
GLPEEGYEAF SASCPELCSK QSTPMGLSLP LSTSVPDSTE SGCSSCSTPL YDQGGPVEIL
PFLYLGSAYH ASRKDMLDAL GITALINVSA NCPNHFEGHY QYKSIPVEDN HKADISSWFN
EAIDFIDSIK NAGGRVFVHC QAGISRSATI CLAYLMRTNR VKLDEAFEFV KQRRSIISPN
FSFMGQLLQF ESQVLAPHCS AEAGSPAMAV LDRSTSTTTV FNFPVSIPVH STNSALSYLQ
SPITTSPSC


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Pathways :
WP1654: gamma-Hexachlorocyclohexane degradation
WP1049: G Protein Signaling Pathways
WP1165: G Protein Signaling Pathways
WP1371: G Protein Signaling Pathways
WP1438: Influenza A virus infection
WP1493: Carbon assimilation C4 pathway
WP1502: Mitochondrial biogenesis
WP1531: Vitamin D synthesis
WP1566: Citrate cycle (TCA cycle)
WP1613: 1,4-Dichlorobenzene degradation
WP1616: ABC transporters
WP1624: Bacterial secretion system
WP1625: Base excision repair
WP1644: DNA replication
WP1650: Fluorobenzoate degradation
WP1652: Fructose and mannose metabolism
WP1657: Glycerolipid metabolism
WP1659: Glycine, serine and threonine metabolism
WP1661: Glyoxylate and dicarboxylate metabolism
WP1663: Homologous recombination
WP1665: Limonene and pinene degradation
WP1672: Mismatch repair
WP1673: Naphthalene and anthracene degradation
WP1675: Nitrogen metabolism
WP1676: Non-homologous end-joining

Related Genes :
[pteN ptenA DDB_G0286557] Phosphatidylinositol 3,4,5-trisphosphate 3-phosphatase and dual-specificity protein phosphatase PTEN (EC 3.1.3.16) (EC 3.1.3.48) (EC 3.1.3.67) (Pten 3-phosphoinositide phosphatase alpha)
[DUSP6 MKP3 PYST1] Dual specificity protein phosphatase 6 (EC 3.1.3.16) (EC 3.1.3.48) (Dual specificity protein phosphatase PYST1) (Mitogen-activated protein kinase phosphatase 3) (MAP kinase phosphatase 3) (MKP-3)
[PTEN MMAC1 TEP1] Phosphatidylinositol 3,4,5-trisphosphate 3-phosphatase and dual-specificity protein phosphatase PTEN (EC 3.1.3.16) (EC 3.1.3.48) (EC 3.1.3.67) (Mutated in multiple advanced cancers 1) (Phosphatase and tensin homolog)
[DUSP7 PYST2] Dual specificity protein phosphatase 7 (EC 3.1.3.16) (EC 3.1.3.48) (Dual specificity protein phosphatase PYST2)
[DUSP4 MKP2 VH2] Dual specificity protein phosphatase 4 (EC 3.1.3.16) (EC 3.1.3.48) (Dual specificity protein phosphatase hVH2) (Mitogen-activated protein kinase phosphatase 2) (MAP kinase phosphatase 2) (MKP-2)
[Pten Mmac1] Phosphatidylinositol 3,4,5-trisphosphate 3-phosphatase and dual-specificity protein phosphatase PTEN (EC 3.1.3.16) (EC 3.1.3.48) (EC 3.1.3.67) (Mutated in multiple advanced cancers 1) (Phosphatase and tensin homolog)
[DUSP12] Dual specificity protein phosphatase 12 (EC 3.1.3.16) (EC 3.1.3.48) (Dual specificity tyrosine phosphatase YVH1)
[PTEN MMAC1] Phosphatidylinositol 3,4,5-trisphosphate 3-phosphatase and dual-specificity protein phosphatase PTEN (EC 3.1.3.16) (EC 3.1.3.48) (EC 3.1.3.67) (Mutated in multiple advanced cancers 1) (Phosphatase and tensin homolog)
[daf-18 T07A9.6] Phosphatidylinositol 3,4,5-trisphosphate 3-phosphatase and dual-specificity protein phosphatase daf-18 (EC 3.1.3.16) (EC 3.1.3.48) (EC 3.1.3.67) (Abnormal dauer formation protein 18)
[Mkp3 CG14080] Dual specificity protein phosphatase Mpk3 (EC 3.1.3.16) (EC 3.1.3.48) (Drosophila MKP3) (DMKP3) (Mitogen-activated protein kinase phosphatase 3) (MAP kinase phosphatase 3) (MKP-3)
[] Genome polyprotein [Cleaved into: P3; Protein 3AB; P1; Capsid protein VP0 (VP4-VP2); Capsid protein VP4 (P1A) (Virion protein 4); Capsid protein VP2 (P1B) (Virion protein 2); Capsid protein VP3 (P1C) (Virion protein 3); Capsid protein VP1 (P1D) (Virion protein 1); P2; Protease 2A (P2A) (EC 3.4.22.29) (Picornain 2A) (Protein 2A); Protein 2B (P2B); Protein 2C (P2C) (EC 3.6.1.15); Protein 3A (P3A); Viral protein genome-linked (VPg) (Protein 3B) (P3B); Protein 3CD (EC 3.4.22.28); Protease 3C (P3C) (EC 3.4.22.28); RNA-directed RNA polymerase (RdRp) (EC 2.7.7.48) (3D polymerase) (3Dpol) (Protein 3D) (3D)]
[Dusp6 Mkp3] Dual specificity protein phosphatase 6 (EC 3.1.3.16) (EC 3.1.3.48) (Mitogen-activated protein kinase phosphatase 3) (MAP kinase phosphatase 3) (MKP-3)
[lip-1 C05B10.1] Dual specificity protein phosphatase lip-1 (EC 3.1.3.16) (EC 3.1.3.48) (Lateral signaling-induced phosphatase 1) (Mitogen-activated protein kinase phosphatase lip-1) (MAP kinase phosphatase lip-1)
[Dusp12 Gkap] Dual specificity protein phosphatase 12 (EC 3.1.3.16) (EC 3.1.3.48) (Glucokinase-associated dual specificity phosphatase) (GKAP)
[DSPTP1B MKP2 At3g06110 F28L1.5] Dual specificity protein phosphatase 1B (AtDsPTP1B) (EC 3.1.3.16) (EC 3.1.3.48) (MAPK phosphatase 2) (AtMKP2)
[hchA A8C65_13880 A9R57_25255 AKG99_20940 AMK83_16550 B7C53_22525 B9M99_11580 B9T59_01945 BJJ90_15205 BMT49_12710 BMT53_00170 BUE81_10670 BW690_17225 BZL69_29425 C2U48_24800 C5715_19445 C5N07_21380 C6669_19295 C7B06_02290 C7B07_03930 CDL37_00765 CG691_19145 CG705_13560 CG706_14580 CIJ94_05515 COD46_23180 CRD98_26150 D3I61_11545 DL800_09215 DNQ41_14245 DQE83_22775 DTL43_21780 DTL84_23375 DTM25_06080 EC95NR1_00961 ERS085379_01273 ERS085386_05041 HMPREF3040_01583 HW43_13705 NCTC10082_04431 NCTC10418_03071 NCTC10767_03558 NCTC11022_01867 NCTC11126_04427 NCTC11181_05650 NCTC12950_02263 NCTC13462_05714 NCTC8985_00529 NCTC9111_05933 NCTC9703_00277 PU06_24500 SAMEA3472055_03589 SAMEA3472056_01268 SAMEA3472070_00654 SAMEA3472080_04213 SAMEA3472090_03376 SAMEA3472110_00060 SAMEA3472112_00448 SAMEA3752372_00752 SAMEA3753106_00003 SAMEA3753391_00513 UN91_23615 WQ89_10695] Protein/nucleic acid deglycase HchA (EC 3.1.2.-) (EC 3.5.1.-) (EC 3.5.1.124) (Maillard deglycase)
[] Genome polyprotein [Cleaved into: P3; Protein 3AB; P2; P1; Capsid protein VP0 (VP4-VP2); Capsid protein VP4 (P1A) (Virion protein 4); Capsid protein VP2 (P1B) (Virion protein 2); Capsid protein VP3 (P1C) (Virion protein 3); Capsid protein VP1 (P1D) (Virion protein 1); Protease 2A (P2A) (EC 3.4.22.29) (Picornain 2A) (Protein 2A); Protein 2B (P2B); Protein 2C (P2C) (EC 3.6.1.15); Protein 3A (P3A); Viral protein genome-linked (VPg) (Protein 3B) (P3B); Protein 3CD (EC 3.4.22.28); Protease 3C (P3C) (EC 3.4.22.28); RNA-directed RNA polymerase (RdRp) (EC 2.7.7.48) (3D polymerase) (3Dpol) (Protein 3D) (3D)]
[dusp1-a] Dual specificity protein phosphatase 1-A (EC 3.1.3.16) (EC 3.1.3.48) (XCL100) (XCL100-alfa)
[PTEN] Phosphatidylinositol 3,4,5-trisphosphate 3-phosphatase and dual-specificity protein phosphatase PTEN (EC 3.1.3.16) (EC 3.1.3.48) (EC 3.1.3.67) (Phosphatase and tensin homolog)
[CDKN3 CDI1 CIP2 KAP] Cyclin-dependent kinase inhibitor 3 (EC 3.1.3.16) (EC 3.1.3.48) (CDK2-associated dual-specificity phosphatase) (Cyclin-dependent kinase interactor 1) (Cyclin-dependent kinase-interacting protein 2) (Kinase-associated phosphatase)
[] Genome polyprotein [Cleaved into: Capsid protein C (Core protein); Protein prM; Peptide pr; Small envelope protein M (Matrix protein); Envelope protein E; Non-structural protein 1 (NS1); Non-structural protein 2A (NS2A); Serine protease subunit NS2B (Flavivirin protease NS2B regulatory subunit) (Non-structural protein 2B); Serine protease NS3 (EC 3.4.21.91) (EC 3.6.1.15) (EC 3.6.4.13) (Flavivirin protease NS3 catalytic subunit) (Non-structural protein 3); Non-structural protein 4A (NS4A); Peptide 2k; Non-structural protein 4B (NS4B); RNA-directed RNA polymerase NS5 (EC 2.1.1.56) (EC 2.1.1.57) (EC 2.7.7.48) (Non-structural protein 5)]
[CDC14A] Dual specificity protein phosphatase CDC14A (EC 3.1.3.16) (EC 3.1.3.48) (CDC14 cell division cycle 14 homolog A)
[AHK4 CRE1 RAW1 WOL At2g01830 T23K3.2] Histidine kinase 4 (EC 2.7.13.3) (Arabidopsis histidine kinase 4) (AtHK4) (Cytokinin receptor CYTOKININ RESPONSE 1) (AtCRE1) (Cytokinin receptor CRE1) (Phosphoprotein phosphatase AHK4) (EC 3.1.3.16) (Protein AUTHENTIC HIS-KINASE 4) (Protein ROOT AS IN WOL 1) (Protein WOODEN LEG)
[MKP-4 CG14211] Dual specificity protein phosphatase MPK-4 (EC 3.1.3.16) (EC 3.1.3.48)
[PTEN] Phosphatidylinositol 3,4,5-trisphosphate 3-phosphatase and dual-specificity protein phosphatase PTEN (EC 3.1.3.16) (EC 3.1.3.48) (EC 3.1.3.67) (Phosphatase and tensin homolog)
[PTEN] Phosphatidylinositol 3,4,5-trisphosphate 3-phosphatase and dual-specificity protein phosphatase PTEN (EC 3.1.3.16) (EC 3.1.3.48) (EC 3.1.3.67) (Phosphatase and tensin homolog)
[PTEN] Phosphatidylinositol 3,4,5-trisphosphate 3-phosphatase and dual-specificity protein phosphatase PTEN (EC 3.1.3.16) (EC 3.1.3.48) (EC 3.1.3.67) (Phosphatase and tensin homolog)
[PTEN] Phosphatidylinositol 3,4,5-trisphosphate 3-phosphatase and dual-specificity protein phosphatase PTEN (EC 3.1.3.16) (EC 3.1.3.48) (EC 3.1.3.67) (Phosphatase and tensin homolog)
[PTEN] Phosphatidylinositol 3,4,5-trisphosphate 3-phosphatase and dual-specificity protein phosphatase PTEN (EC 3.1.3.16) (EC 3.1.3.48) (EC 3.1.3.67) (Phosphatase and tensin homolog)
[PTEN] Phosphatidylinositol 3,4,5-trisphosphate 3-phosphatase and dual-specificity protein phosphatase PTEN (EC 3.1.3.16) (EC 3.1.3.48) (EC 3.1.3.67) (Phosphatase and tensin homolog)

Bibliography :
[30816666] p38-MAP Kinase Negatively Regulates the Slow Force Response to Stretch in Rat Myocardium through the Up-Regulation of Dual Specificity Phosphatase 6 (DUSP6).
[30636257] Antidepressive Effects of Taraxacum Officinale in a Mouse Model of Depression Are Due to Inhibition of Corticosterone Levels and Modulation of Mitogen-Activated Protein Kinase Phosphatase-1 (Mkp-1) and Brain-Derived Neurotrophic Factor (Bdnf) Expression.
[30584966] Differential regulation of the durum wheat MAPK phosphatase 1 by calmodulin, bivalent cations and possibly mitogen activated protein kinase 3.
[30504726] Hyperglycaemia Stress-Induced Renal Injury is Caused by Extensive Mitochondrial Fragmentation, Attenuated MKP1 Signalling, and Activated JNK-CaMKII-Fis1 Biological Axis.
[30451863] RIG-I like receptor sensing of host RNAs facilitates the cell-intrinsic immune response to KSHV infection.
[30387548] P68 RNA helicase promotes invasion of glioma cells through negatively regulating DUSP5.
[30381640] [Elucidation of a New Mechanism of Onset of Insulin Resistance: Effects of Statins and Tumor Necrosis Factor-α on Insulin Signal Transduction].
[30348505] Mycosis fungoides in Taiwan shows a relatively high frequency of large cell transformation and CD56 expression.
[30315197] DUSP10 constrains innate IL-33-mediated cytokine production in ST2 memory-type pathogenic Th2 cells.
[30260967] GPx3-mediated redox signaling arrests the cell cycle and acts as a tumor suppressor in lung cancer cell lines.