SPARQL | HTML5 RDFa and Microdata document
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http://www.w3.org/1999/02/22-rdf-syntax-ns#type
http://www.w3.org/2004/02/skos/core#Collection
http://vocabularies.wikipathways.org/wp#Pathway
http://vocabularies.wikipathways.org/wp#diseaseOntologyTag
http://purl.obolibrary.org/obo/DOID_162
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http://vocabularies.wikipathways.org/wp#Curation:AnalysisCollection
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http://purl.obolibrary.org/obo/PW_0000297
http://purl.obolibrary.org/obo/DOID_162
http://vocabularies.wikipathways.org/wp#organism
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PDGF belongs to the PDGF/VEGF (vascular endothelial growth factor) family, which is characterized by eight strictly conserved cysteine residues with similar spacing in between (Joukov et al., 1997; Heldin and Westermark, 1999). The A-, B-, C-, and D-chain genes of PDGF are localized to the chromosomes 7p22, 22q13, 4q31, and 11q22, respectively, and their expression is independently regulated. Two forms of the PDGF A-chain, containing 196 and 211 amino acid residues resulting from differential splicing of the transcript, are synthesized, dimerized, proteolytically processed in the Nterminus, and secreted from the cell as a ~30 kDa dimer. The PDGF B chain encoding 241 amino acid residues is dimerized, processed by additional proteolysis, and secreted as a 24 kDa dimer. The homodimers PDGF AA, BB, and the heterodimer AB contain three intrachain disulfide bonds made between the 1st
http://purl.org/dc/terms/identifier http://purl.org/spar/cito/cites
https://identifiers.org/pubmed/2546599
https://identifiers.org/pubmed/2557116
https://identifiers.org/pubmed/2841963
https://identifiers.org/pubmed/1755382
https://identifiers.org/pubmed/1661577
https://identifiers.org/pubmed/21769672
https://identifiers.org/pubmed/22512244
https://identifiers.org/pubmed/2545232
https://identifiers.org/pubmed/18483217
https://identifiers.org/pubmed/20657170