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http://purl.uniprot.org/citations/11732181http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/11732181http://www.w3.org/2000/01/rdf-schema#comment"DNA replication and mitosis are dependent on the activity of cyclin-dependent protein kinase (CDK) enzymes, which are heterodimers of a catalytic subunit with a cyclin subunit. Cyclin binding to specific individual proteins is thought to provide potential substrates to Cdk. Protein binding by cyclins is assessed in terms of its mechanisms and biological significance, using evidence from diverse organisms including substrate specificity in animal Cdk enzymes containing D-, A-, and B-type cyclins and extensive cyclin gene manipulations in yeasts. Assembly of protein complexes with cyclin/Cdk is noted and the capacity of the cyclin-dependent kinase subunit Cks, in such complex, to extend the range of Cdk substrates is documented and discussed in terms of cell cycle regulation. Cell cycle progression involves changing abundance of individual cyclins, due to changing rates of their transcription or proteolysis, with consequent changes in the substrates of CDK through the cell cycle. Some overlap of the functions of individual cyclins in vivo has been identified by cyclin deletions and is suggested to follow a pattern in which cyclins can commonly complete functions initiated by the preceding cyclins well enough to preserve viability as groups of cyclins are removed by proteolysis. Cyclin accumulation is particularly important in terminating the G1 phase, when it raises CDK activity and starts events leading to DNA replication. It is suggested that plants share this mechanism. The distribution of cyclins and Cdk in maize root tip cells during mitosis and cytokinesis indicates the presence of Cdk1 (Cdc2a) and cyclin CycB1zm;2 at the mature and disassembling preprophase band and the presence of CycB1zm;2 at condensing and condensed chromosomes. Both observations correlate with the earlier-reported capacity of injected metaphase cyclin/CDK to accelerate preprophase band disassembly and chromosome condensation and with observations of the location of Cdk and cyclins in other laboratories. Additionally CycB1zm;2 is seen at the nuclear envelope during its breakdown, which correlates with an acceleration of the process by injected metaphase cyclin B/CDK. A phenomenon possibly unique to the plant kingdom is the persistence of mitotic cyclins after anaphase. Participation of cyclins in cytokinesis is indicated by the concentration of the mitotic cyclin CycA1;zm;1 at the phragmoplast. It is suggested that cyclins have a general function of spatially focusing Cdk activity and that in the plant cell the concentrations of cyclins are important mediators of CDK activity at the cytoskeleton, chromosomes, spindle, nuclear envelope, and phragmoplast."xsd:string
http://purl.uniprot.org/citations/11732181http://purl.org/dc/terms/identifier"doi:10.1007/bf02673865"xsd:string
http://purl.uniprot.org/citations/11732181http://purl.uniprot.org/core/author"Moore R."xsd:string
http://purl.uniprot.org/citations/11732181http://purl.uniprot.org/core/author"John P.C."xsd:string
http://purl.uniprot.org/citations/11732181http://purl.uniprot.org/core/author"Mews M."xsd:string
http://purl.uniprot.org/citations/11732181http://purl.uniprot.org/core/date"2001"xsd:gYear
http://purl.uniprot.org/citations/11732181http://purl.uniprot.org/core/name"Protoplasma"xsd:string
http://purl.uniprot.org/citations/11732181http://purl.uniprot.org/core/pages"119-142"xsd:string
http://purl.uniprot.org/citations/11732181http://purl.uniprot.org/core/title"Cyclin/Cdk complexes: their involvement in cell cycle progression and mitotic division."xsd:string
http://purl.uniprot.org/citations/11732181http://purl.uniprot.org/core/volume"216"xsd:string
http://purl.uniprot.org/citations/11732181http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/11732181
http://purl.uniprot.org/citations/11732181http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/11732181
http://purl.uniprot.org/uniprot/#_P00546-mappedCitation-11732181http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/11732181
http://purl.uniprot.org/uniprot/#_P13365-mappedCitation-11732181http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/11732181
http://purl.uniprot.org/uniprot/#_P30283-mappedCitation-11732181http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/11732181
http://purl.uniprot.org/uniprot/#_P20437-mappedCitation-11732181http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/11732181
http://purl.uniprot.org/uniprot/#_P20438-mappedCitation-11732181http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/11732181
http://purl.uniprot.org/uniprot/#_P24868-mappedCitation-11732181http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/11732181
http://purl.uniprot.org/uniprot/#_P24869-mappedCitation-11732181http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/11732181
http://purl.uniprot.org/uniprot/#_P24870-mappedCitation-11732181http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/11732181
http://purl.uniprot.org/uniprot/#_P24871-mappedCitation-11732181http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/11732181
http://purl.uniprot.org/uniprot/#_P32943-mappedCitation-11732181http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/11732181
http://purl.uniprot.org/uniprot/P24870http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/11732181
http://purl.uniprot.org/uniprot/P24871http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/11732181