PubMed:8242751 JSONTXT

{"project":"AIMed","denotations":[{"id":"T1","span":{"begin":4,"end":7},"obj":"protein"},{"id":"T2","span":{"begin":32,"end":36},"obj":"protein"},{"id":"T3","span":{"begin":119,"end":123},"obj":"protein"},{"id":"T4","span":{"begin":140,"end":149},"obj":"protein"},{"id":"T5","span":{"begin":265,"end":269},"obj":"protein"},{"id":"T6","span":{"begin":394,"end":398},"obj":"protein"},{"id":"T7","span":{"begin":446,"end":454},"obj":"protein"},{"id":"T8","span":{"begin":456,"end":465},"obj":"protein"},{"id":"T9","span":{"begin":467,"end":475},"obj":"protein"},{"id":"T10","span":{"begin":481,"end":485},"obj":"protein"},{"id":"T11","span":{"begin":506,"end":513},"obj":"protein"},{"id":"T12","span":{"begin":598,"end":600},"obj":"protein"},{"id":"T13","span":{"begin":604,"end":612},"obj":"protein"},{"id":"T14","span":{"begin":613,"end":617},"obj":"protein"},{"id":"T15","span":{"begin":619,"end":627},"obj":"protein"},{"id":"T16","span":{"begin":628,"end":632},"obj":"protein"},{"id":"T17","span":{"begin":634,"end":643},"obj":"protein"},{"id":"T18","span":{"begin":644,"end":648},"obj":"protein"},{"id":"T19","span":{"begin":654,"end":663},"obj":"protein"},{"id":"T20","span":{"begin":664,"end":668},"obj":"protein"},{"id":"T21","span":{"begin":721,"end":725},"obj":"protein"},{"id":"T22","span":{"begin":730,"end":744},"obj":"protein"}],"text":"The p21 Cdk-interacting protein Cip1 is a potent inhibitor of G1 cyclin-dependent kinases.\nThe cyclin-dependent kinase Cdk2 associates with cyclins A, D, and E and has been implicated in the control of the G1 to S phase transition in mammals. To identify potential Cdk2 regulators, we have employed an improved two-hybrid system to isolate human genes encoding Cdk-interacting proteins (Cips). CIP1 encodes a novel 21 kd protein that is found in cyclin A, cyclin D1, cyclin E, and Cdk2 immunoprecipitates. p21CIP1 is a potent, tight-binding inhibitor of Cdks and can inhibit the phosphorylation of Rb by cyclin A-Cdk2, cyclin E-Cdk2, cyclin D1-Cdk4, and cyclin D2-Cdk4 complexes. Cotransfection experiments indicate that CIP1 and SV40 T antigen function in a mutually antagonistic manner to control cell cycle progression."}

{"project":"GlyCosmos15-Glycan","denotations":[{"id":"T1","span":{"begin":735,"end":744},"obj":"Glycan"}],"attributes":[{"id":"A1","pred":"glycosmos_id","subj":"T1","obj":"https://glycosmos.org/glycans/show/G00031MO"},{"id":"A2","pred":"image","subj":"T1","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G00031MO"}],"text":"The p21 Cdk-interacting protein Cip1 is a potent inhibitor of G1 cyclin-dependent kinases.\nThe cyclin-dependent kinase Cdk2 associates with cyclins A, D, and E and has been implicated in the control of the G1 to S phase transition in mammals. To identify potential Cdk2 regulators, we have employed an improved two-hybrid system to isolate human genes encoding Cdk-interacting proteins (Cips). CIP1 encodes a novel 21 kd protein that is found in cyclin A, cyclin D1, cyclin E, and Cdk2 immunoprecipitates. p21CIP1 is a potent, tight-binding inhibitor of Cdks and can inhibit the phosphorylation of Rb by cyclin A-Cdk2, cyclin E-Cdk2, cyclin D1-Cdk4, and cyclin D2-Cdk4 complexes. Cotransfection experiments indicate that CIP1 and SV40 T antigen function in a mutually antagonistic manner to control cell cycle progression."}

{"project":"Glycan-GlyCosmos","denotations":[{"id":"T1","span":{"begin":735,"end":744},"obj":"Glycan"}],"attributes":[{"id":"A1","pred":"glycosmos_id","subj":"T1","obj":"https://glycosmos.org/glycans/show/G00031MO"},{"id":"A2","pred":"image","subj":"T1","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G00031MO"}],"text":"The p21 Cdk-interacting protein Cip1 is a potent inhibitor of G1 cyclin-dependent kinases.\nThe cyclin-dependent kinase Cdk2 associates with cyclins A, D, and E and has been implicated in the control of the G1 to S phase transition in mammals. To identify potential Cdk2 regulators, we have employed an improved two-hybrid system to isolate human genes encoding Cdk-interacting proteins (Cips). CIP1 encodes a novel 21 kd protein that is found in cyclin A, cyclin D1, cyclin E, and Cdk2 immunoprecipitates. p21CIP1 is a potent, tight-binding inhibitor of Cdks and can inhibit the phosphorylation of Rb by cyclin A-Cdk2, cyclin E-Cdk2, cyclin D1-Cdk4, and cyclin D2-Cdk4 complexes. Cotransfection experiments indicate that CIP1 and SV40 T antigen function in a mutually antagonistic manner to control cell cycle progression."}

{"project":"GlyCosmos-GlycoEpitope","denotations":[{"id":"T1","span":{"begin":735,"end":744},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"}],"attributes":[{"id":"A1","pred":"glycoepitope_id","subj":"T1","obj":"http://www.glycoepitope.jp/epitopes/EP0020"}],"text":"The p21 Cdk-interacting protein Cip1 is a potent inhibitor of G1 cyclin-dependent kinases.\nThe cyclin-dependent kinase Cdk2 associates with cyclins A, D, and E and has been implicated in the control of the G1 to S phase transition in mammals. To identify potential Cdk2 regulators, we have employed an improved two-hybrid system to isolate human genes encoding Cdk-interacting proteins (Cips). CIP1 encodes a novel 21 kd protein that is found in cyclin A, cyclin D1, cyclin E, and Cdk2 immunoprecipitates. p21CIP1 is a potent, tight-binding inhibitor of Cdks and can inhibit the phosphorylation of Rb by cyclin A-Cdk2, cyclin E-Cdk2, cyclin D1-Cdk4, and cyclin D2-Cdk4 complexes. Cotransfection experiments indicate that CIP1 and SV40 T antigen function in a mutually antagonistic manner to control cell cycle progression."}

{"project":"GlyCosmos15-UBERON","denotations":[{"id":"T1","span":{"begin":799,"end":809},"obj":"Body_part"}],"attributes":[{"id":"A1","pred":"uberon_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/UBERON_2000098"}],"text":"The p21 Cdk-interacting protein Cip1 is a potent inhibitor of G1 cyclin-dependent kinases.\nThe cyclin-dependent kinase Cdk2 associates with cyclins A, D, and E and has been implicated in the control of the G1 to S phase transition in mammals. To identify potential Cdk2 regulators, we have employed an improved two-hybrid system to isolate human genes encoding Cdk-interacting proteins (Cips). CIP1 encodes a novel 21 kd protein that is found in cyclin A, cyclin D1, cyclin E, and Cdk2 immunoprecipitates. p21CIP1 is a potent, tight-binding inhibitor of Cdks and can inhibit the phosphorylation of Rb by cyclin A-Cdk2, cyclin E-Cdk2, cyclin D1-Cdk4, and cyclin D2-Cdk4 complexes. Cotransfection experiments indicate that CIP1 and SV40 T antigen function in a mutually antagonistic manner to control cell cycle progression."}

{"project":"GlyCosmos15-Taxon","denotations":[{"id":"T1","span":{"begin":340,"end":345},"obj":"Organism"},{"id":"T2","span":{"begin":446,"end":454},"obj":"Organism"},{"id":"T3","span":{"begin":604,"end":612},"obj":"Organism"}],"attributes":[{"id":"A1","pred":"db_id","subj":"T1","obj":"9606"},{"id":"A2","pred":"db_id","subj":"T2","obj":"120565"},{"id":"A3","pred":"db_id","subj":"T3","obj":"120565"}],"text":"The p21 Cdk-interacting protein Cip1 is a potent inhibitor of G1 cyclin-dependent kinases.\nThe cyclin-dependent kinase Cdk2 associates with cyclins A, D, and E and has been implicated in the control of the G1 to S phase transition in mammals. To identify potential Cdk2 regulators, we have employed an improved two-hybrid system to isolate human genes encoding Cdk-interacting proteins (Cips). CIP1 encodes a novel 21 kd protein that is found in cyclin A, cyclin D1, cyclin E, and Cdk2 immunoprecipitates. p21CIP1 is a potent, tight-binding inhibitor of Cdks and can inhibit the phosphorylation of Rb by cyclin A-Cdk2, cyclin E-Cdk2, cyclin D1-Cdk4, and cyclin D2-Cdk4 complexes. Cotransfection experiments indicate that CIP1 and SV40 T antigen function in a mutually antagonistic manner to control cell cycle progression."}

{"project":"GlyCosmos15-Sentences","blocks":[{"id":"T1","span":{"begin":0,"end":90},"obj":"Sentence"},{"id":"T2","span":{"begin":91,"end":242},"obj":"Sentence"},{"id":"T3","span":{"begin":243,"end":393},"obj":"Sentence"},{"id":"T4","span":{"begin":394,"end":679},"obj":"Sentence"},{"id":"T5","span":{"begin":680,"end":822},"obj":"Sentence"}],"text":"The p21 Cdk-interacting protein Cip1 is a potent inhibitor of G1 cyclin-dependent kinases.\nThe cyclin-dependent kinase Cdk2 associates with cyclins A, D, and E and has been implicated in the control of the G1 to S phase transition in mammals. To identify potential Cdk2 regulators, we have employed an improved two-hybrid system to isolate human genes encoding Cdk-interacting proteins (Cips). CIP1 encodes a novel 21 kd protein that is found in cyclin A, cyclin D1, cyclin E, and Cdk2 immunoprecipitates. p21CIP1 is a potent, tight-binding inhibitor of Cdks and can inhibit the phosphorylation of Rb by cyclin A-Cdk2, cyclin E-Cdk2, cyclin D1-Cdk4, and cyclin D2-Cdk4 complexes. Cotransfection experiments indicate that CIP1 and SV40 T antigen function in a mutually antagonistic manner to control cell cycle progression."}

{"project":"GlyCosmos15-GlycoEpitope","denotations":[{"id":"T1","span":{"begin":735,"end":744},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"}],"attributes":[{"id":"A1","pred":"glycoepitope_id","subj":"T1","obj":"http://www.glycoepitope.jp/epitopes/EP0020"}],"text":"The p21 Cdk-interacting protein Cip1 is a potent inhibitor of G1 cyclin-dependent kinases.\nThe cyclin-dependent kinase Cdk2 associates with cyclins A, D, and E and has been implicated in the control of the G1 to S phase transition in mammals. To identify potential Cdk2 regulators, we have employed an improved two-hybrid system to isolate human genes encoding Cdk-interacting proteins (Cips). CIP1 encodes a novel 21 kd protein that is found in cyclin A, cyclin D1, cyclin E, and Cdk2 immunoprecipitates. p21CIP1 is a potent, tight-binding inhibitor of Cdks and can inhibit the phosphorylation of Rb by cyclin A-Cdk2, cyclin E-Cdk2, cyclin D1-Cdk4, and cyclin D2-Cdk4 complexes. Cotransfection experiments indicate that CIP1 and SV40 T antigen function in a mutually antagonistic manner to control cell cycle progression."}

{"project":"NCBITAXON","denotations":[{"id":"T1","span":{"begin":340,"end":345},"obj":"OrganismTaxon"},{"id":"T2","span":{"begin":446,"end":454},"obj":"OrganismTaxon"},{"id":"T3","span":{"begin":604,"end":612},"obj":"OrganismTaxon"}],"attributes":[{"id":"A1","pred":"db_id","subj":"T1","obj":"9606"},{"id":"A2","pred":"db_id","subj":"T2","obj":"120565"},{"id":"A3","pred":"db_id","subj":"T3","obj":"120565"}],"text":"The p21 Cdk-interacting protein Cip1 is a potent inhibitor of G1 cyclin-dependent kinases.\nThe cyclin-dependent kinase Cdk2 associates with cyclins A, D, and E and has been implicated in the control of the G1 to S phase transition in mammals. To identify potential Cdk2 regulators, we have employed an improved two-hybrid system to isolate human genes encoding Cdk-interacting proteins (Cips). CIP1 encodes a novel 21 kd protein that is found in cyclin A, cyclin D1, cyclin E, and Cdk2 immunoprecipitates. p21CIP1 is a potent, tight-binding inhibitor of Cdks and can inhibit the phosphorylation of Rb by cyclin A-Cdk2, cyclin E-Cdk2, cyclin D1-Cdk4, and cyclin D2-Cdk4 complexes. Cotransfection experiments indicate that CIP1 and SV40 T antigen function in a mutually antagonistic manner to control cell cycle progression."}

{"project":"Anatomy-UBERON","denotations":[{"id":"T1","span":{"begin":799,"end":809},"obj":"Body_part"}],"attributes":[{"id":"A1","pred":"uberon_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/UBERON_2000098"}],"text":"The p21 Cdk-interacting protein Cip1 is a potent inhibitor of G1 cyclin-dependent kinases.\nThe cyclin-dependent kinase Cdk2 associates with cyclins A, D, and E and has been implicated in the control of the G1 to S phase transition in mammals. To identify potential Cdk2 regulators, we have employed an improved two-hybrid system to isolate human genes encoding Cdk-interacting proteins (Cips). CIP1 encodes a novel 21 kd protein that is found in cyclin A, cyclin D1, cyclin E, and Cdk2 immunoprecipitates. p21CIP1 is a potent, tight-binding inhibitor of Cdks and can inhibit the phosphorylation of Rb by cyclin A-Cdk2, cyclin E-Cdk2, cyclin D1-Cdk4, and cyclin D2-Cdk4 complexes. Cotransfection experiments indicate that CIP1 and SV40 T antigen function in a mutually antagonistic manner to control cell cycle progression."}