| http://purl.uniprot.org/citations/8033213 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/8033213 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/8033213 | http://www.w3.org/2000/01/rdf-schema#comment | "Using a yeast interaction screen to search for proteins that interact with cyclin D1-Cdk4, we identified a 27 kDa mouse protein related to the p21 cyclin-Cdk inhibitor. p27 interacts strongly with D-type cyclins and Cdk4 in vitro and more weakly with cyclin E and Cdk2. In mouse fibroblasts, p27 is associated predominantly with cyclin D1-Cdk4. Recombinant p27 is a potent inhibitor of cyclin D1-Cdk4 and cyclin A-Cdk2 protein kinase activity and a weaker inhibitor of cyclin B1-Cdc2. Overexpression of p27 in Saos-2 cells causes G1 arrest. p27 protein levels do not change as serum-stimulated quiescent mouse fibroblasts progress through the cell cycle. p27 is identical to p27Kip1, a cyclin-Cdk inhibitor present in TGF beta-treated cells. p27 has the hallmarks of a negative regulator of G1 progression and may mediate TGF beta-induced G1 arrest."xsd:string |
| http://purl.uniprot.org/citations/8033213 | http://purl.org/dc/terms/identifier | "doi:10.1016/0092-8674(94)90573-8"xsd:string |
| http://purl.uniprot.org/citations/8033213 | http://purl.org/dc/terms/identifier | "doi:10.1016/0092-8674(94)90573-8"xsd:string |
| http://purl.uniprot.org/citations/8033213 | http://purl.uniprot.org/core/author | "Hunter T."xsd:string |
| http://purl.uniprot.org/citations/8033213 | http://purl.uniprot.org/core/author | "Hunter T."xsd:string |
| http://purl.uniprot.org/citations/8033213 | http://purl.uniprot.org/core/author | "Toyoshima H."xsd:string |
| http://purl.uniprot.org/citations/8033213 | http://purl.uniprot.org/core/author | "Toyoshima H."xsd:string |
| http://purl.uniprot.org/citations/8033213 | http://purl.uniprot.org/core/date | "1994"xsd:gYear |
| http://purl.uniprot.org/citations/8033213 | http://purl.uniprot.org/core/date | "1994"xsd:gYear |
| http://purl.uniprot.org/citations/8033213 | http://purl.uniprot.org/core/name | "Cell"xsd:string |
| http://purl.uniprot.org/citations/8033213 | http://purl.uniprot.org/core/name | "Cell"xsd:string |
| http://purl.uniprot.org/citations/8033213 | http://purl.uniprot.org/core/pages | "67-74"xsd:string |
| http://purl.uniprot.org/citations/8033213 | http://purl.uniprot.org/core/pages | "67-74"xsd:string |
| http://purl.uniprot.org/citations/8033213 | http://purl.uniprot.org/core/title | "p27, a novel inhibitor of G1 cyclin-Cdk protein kinase activity, is related to p21."xsd:string |
| http://purl.uniprot.org/citations/8033213 | http://purl.uniprot.org/core/title | "p27, a novel inhibitor of G1 cyclin-Cdk protein kinase activity, is related to p21."xsd:string |
| http://purl.uniprot.org/citations/8033213 | http://purl.uniprot.org/core/volume | "78"xsd:string |
| http://purl.uniprot.org/citations/8033213 | http://purl.uniprot.org/core/volume | "78"xsd:string |
| http://purl.uniprot.org/citations/8033213 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/8033213 |
| http://purl.uniprot.org/citations/8033213 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/8033213 |
| http://purl.uniprot.org/citations/8033213 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/8033213 |
| http://purl.uniprot.org/citations/8033213 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/8033213 |
| http://purl.uniprot.org/embl-cds/AAA21149.1 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/8033213 |
| http://purl.uniprot.org/uniprot/P46414 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/8033213 |