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http://purl.uniprot.org/citations/9618306http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/9618306http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/9618306http://www.w3.org/2000/01/rdf-schema#comment"To identify transcriptionally regulated genes potentially involved in the effect of shear stress on endothelial gene expression, we performed a differential display analysis of mRNAs from human umbilical vein endothelial cell (HUVEC) exposed to laminar shear stress (12 dynes/cm2) in comparison to HUVEC maintained in static condition. We identified a cDNA fragment overexpressed by laminar shear stress. The full-length, SSK1, was 3653 long and encoded for a novel protein of 1050 amino acids. Northern blot demonstrates that SSK1 mRNA is expressed at high levels also in placenta, a weak transcript was present in heart, skeletal muscle, kidney and pancreas. Homology searches of the protein databases showed that SSK1 is related to numerous serine-threonine kinases. The highest homology was found with a very recently described gene, BUBR1, an analogue of BUB1, which is a kinase involved in the regulation of cell cycle. The most conserved residues in catalytic domains II, III, VIb, VII, VIII and IX of serine-threonine protein kinases were found in the C terminal region of SSK1 which further supports the kinase nature of the new protein. The putative serine-threonine kinase SSK1 may represent a tool by which mechanical forces regulates phosphorylation events within endothelial cells."xsd:string
http://purl.uniprot.org/citations/9618306http://purl.org/dc/terms/identifier"doi:10.1006/bbrc.1998.8713"xsd:string
http://purl.uniprot.org/citations/9618306http://purl.org/dc/terms/identifier"doi:10.1006/bbrc.1998.8713"xsd:string
http://purl.uniprot.org/citations/9618306http://purl.uniprot.org/core/author"Benatti L."xsd:string
http://purl.uniprot.org/citations/9618306http://purl.uniprot.org/core/author"Benatti L."xsd:string
http://purl.uniprot.org/citations/9618306http://purl.uniprot.org/core/author"Donadelli R."xsd:string
http://purl.uniprot.org/citations/9618306http://purl.uniprot.org/core/author"Donadelli R."xsd:string
http://purl.uniprot.org/citations/9618306http://purl.uniprot.org/core/author"Noris M."xsd:string
http://purl.uniprot.org/citations/9618306http://purl.uniprot.org/core/author"Noris M."xsd:string
http://purl.uniprot.org/citations/9618306http://purl.uniprot.org/core/author"Remuzzi G."xsd:string
http://purl.uniprot.org/citations/9618306http://purl.uniprot.org/core/author"Remuzzi G."xsd:string
http://purl.uniprot.org/citations/9618306http://purl.uniprot.org/core/author"Benigni A."xsd:string
http://purl.uniprot.org/citations/9618306http://purl.uniprot.org/core/author"Benigni A."xsd:string
http://purl.uniprot.org/citations/9618306http://purl.uniprot.org/core/author"Gullans S.R."xsd:string
http://purl.uniprot.org/citations/9618306http://purl.uniprot.org/core/author"Gullans S.R."xsd:string
http://purl.uniprot.org/citations/9618306http://purl.uniprot.org/core/author"Morigi M."xsd:string
http://purl.uniprot.org/citations/9618306http://purl.uniprot.org/core/author"Morigi M."xsd:string
http://purl.uniprot.org/citations/9618306http://purl.uniprot.org/core/author"Remuzzi A."xsd:string
http://purl.uniprot.org/citations/9618306http://purl.uniprot.org/core/author"Remuzzi A."xsd:string
http://purl.uniprot.org/citations/9618306http://purl.uniprot.org/core/date"1998"xsd:gYear
http://purl.uniprot.org/citations/9618306http://purl.uniprot.org/core/date"1998"xsd:gYear
http://purl.uniprot.org/citations/9618306http://purl.uniprot.org/core/name"Biochem. Biophys. Res. Commun."xsd:string
http://purl.uniprot.org/citations/9618306http://purl.uniprot.org/core/name"Biochem. Biophys. Res. Commun."xsd:string