| http://purl.uniprot.org/citations/28962834 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/28962834 | http://www.w3.org/2000/01/rdf-schema#comment | "The exposure and release of TF is regulated by post-translational modifications of its cytoplasmic domain. Here, the potential of Pin1 to interact with the cytoplasmic domain of TF, and the outcome on TF function was examined. MDA-MB-231 and transfected-primary endothelial cells were incubated with either Pin1 deactivator Juglone, or its control Plumbagin, as well as transfected with Pin1-specific or control siRNA. TF release into microvesicles following activation, and also phosphorylation and ubiquitination states of cellular-TF were then assessed. Furthermore, the ability of Pin1 to bind wild-type and mutant forms of overexpressed TF-tGFP was investigated by co-immunoprecipitation. Additionally, the ability of recombinant or cellular Pin1 to bind to peptides of the C-terminus of TF, synthesised in different phosphorylation states was examined by binding assays and spectroscopically. Finally, the influence of recombinant Pin1 on the ubiquitination and dephosphorylation of the TF-peptides was examined. Pre-incubation of Pin1 with Juglone but not Plumbagin, reduced TF release as microvesicles and was also achievable following transfection with Pin1-siRNA. This was concurrent with early ubiquitination and dephosphorylation of cellular TF at Ser253. Pin1 co-immunoprecipitated with overexpressed wild-type TF-tGFP but not Ser258→Ala or Pro259→Ala substituted mutants. Pin1 did interact with Ser258-phosphorylated and double-phosphorylated TF-peptides, with the former having higher affinity. Finally, recombinant Pin1 was capable of interfering with the ubiquitination and dephosphorylation of TF-derived peptides. In conclusion, Pin1 is a fast-acting enzyme which may be utilised by cells to protect the phosphorylation state of TF in activated cells prolonging TF activity and release, and therefore ensuring adequate haemostasis."xsd:string |
| http://purl.uniprot.org/citations/28962834 | http://purl.org/dc/terms/identifier | "doi:10.1016/j.bbamcr.2017.09.016"xsd:string |
| http://purl.uniprot.org/citations/28962834 | http://purl.uniprot.org/core/author | "Greenman J."xsd:string |
| http://purl.uniprot.org/citations/28962834 | http://purl.uniprot.org/core/author | "Ettelaie C."xsd:string |
| http://purl.uniprot.org/citations/28962834 | http://purl.uniprot.org/core/author | "Maraveyas A."xsd:string |
| http://purl.uniprot.org/citations/28962834 | http://purl.uniprot.org/core/author | "Featherby S."xsd:string |
| http://purl.uniprot.org/citations/28962834 | http://purl.uniprot.org/core/author | "Collier M.E.W."xsd:string |
| http://purl.uniprot.org/citations/28962834 | http://purl.uniprot.org/core/date | "2018"xsd:gYear |
| http://purl.uniprot.org/citations/28962834 | http://purl.uniprot.org/core/name | "Biochim Biophys Acta Mol Cell Res"xsd:string |
| http://purl.uniprot.org/citations/28962834 | http://purl.uniprot.org/core/pages | "12-24"xsd:string |
| http://purl.uniprot.org/citations/28962834 | http://purl.uniprot.org/core/title | "Peptidyl-prolyl isomerase 1 (Pin1) preserves the phosphorylation state of tissue factor and prolongs its release within microvesicles."xsd:string |
| http://purl.uniprot.org/citations/28962834 | http://purl.uniprot.org/core/volume | "1865"xsd:string |
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