Polo-like kinases: structural variations lead to multiple functions.
about
Maintaining Genome Stability in Defiance of Mitotic DNA DamageRegulation of Microtubule Dynamics in Axon Regeneration: Insights from C. elegansThe Ran Pathway in Drosophila melanogaster MitosisPutting a bit into the polo-box domain of polo-like kinase 1Molecular dynamics of PLK1 during mitosisPhysical Association of Saccharomyces cerevisiae Polo-like Kinase Cdc5 with Chromosomal Cohesin Facilitates DNA Damage Response.Polo kinase Cdc5 associates with centromeres to facilitate the removal of centromeric cohesin during mitosisThe PLK4-STIL-SAS-6 module at the core of centriole duplicationA mechanism for the elimination of the female gamete centrosome in Drosophila melanogasterPhosphoproteomic Profiling Reveals Epstein-Barr Virus Protein Kinase Integration of DNA Damage Response and Mitotic SignalingStructure-Bioactivity Relationship for Benzimidazole Thiophene Inhibitors of Polo-Like Kinase 1 (PLK1), a Potential Drug Target in Schistosoma mansoniIdentification of Polo-like kinase 1 interaction inhibitors using a novel cell-based assayInterdomain allosteric regulation of Polo kinase by Aurora B and Map205 is required for cytokinesis.Spatiotemporal dynamics of Aurora B-PLK1-MCAK signaling axis orchestrates kinetochore bi-orientation and faithful chromosome segregation.53BP1 and USP28 mediate p53 activation and G1 arrest after centrosome loss or extended mitotic duration.DNA replication licensing factor Cdc6 and Plk4 kinase antagonistically regulate centrosome duplication via Sas-6.Synergistic interactions between PLK1 and HDAC inhibitors in non-Hodgkin's lymphoma cells occur in vitro and in vivo and proceed through multiple mechanismsTowards Prognostic Profiling of Non-Small Cell Lung Cancer: New Perspectives on the Relevance of Polo-Like Kinase 1 Expression, the TP53 Mutation Status and HypoxiaPolo-like kinase 4 inhibition: a strategy for cancer therapy?Cell biology. Reversible centriole depletion with an inhibitor of Polo-like kinase 4.Five factors can reconstitute all three phases of microtubule polymerization dynamics.Mio depletion links mTOR regulation to Aurora A and Plk1 activation at mitotic centrosomesPLK1 is a critical determinant of tumor cell sensitivity to CPT11 and its inhibition enhances the drug antitumor efficacy in squamous cell carcinoma models sensitive and resistant to camptothecins.Increased Expression of Phosphorylated Polo-Like Kinase 1 and Histone in Bypass Vein Graft and Coronary Arteries following Angioplasty.Phosphorylation of SAF-A/hnRNP-U Serine 59 by Polo-Like Kinase 1 Is Required for Mitosis.STIL binding to Polo-box 3 of PLK4 regulates centriole duplicationProteomic identification of novel cytoskeletal proteins associated with TbPLK, an essential regulator of cell morphogenesis in Trypanosoma bruceiDynamic Bcl-xL (S49) and (S62) Phosphorylation/Dephosphorylation during Mitosis Prevents Chromosome Instability and Aneuploidy in Normal Human Diploid FibroblastsA Synthetic Dosage Lethal Genetic Interaction Between CKS1B and PLK1 Is Conserved in Yeast and Human Cancer Cells.Interactions of Prototype Foamy Virus Capsids with Host Cell Polo-Like Kinases Are Important for Efficient Viral DNA Integration.Cdk1 plays matchmaker for the Polo-like kinase and its activator SPAT-1/Bora.Efficacy of the polo-like kinase inhibitor rigosertib, alone or in combination with Abelson tyrosine kinase inhibitors, against break point cluster region-c-Abelson-positive leukemia cells.Polo-like kinase 2 acting as a promoter in human tumor cells with an abundance of TAp73.Recent Advances and New Strategies in Targeting Plk1 for Anticancer TherapyChromophobe renal cell carcinoma with and without sarcomatoid change: a clinicopathological, comparative genomic hybridization, and whole-exome sequencing study.PLK2 phosphorylates and inhibits enriched TAp73 in human osteosarcoma cellsCDK1 Prevents Unscheduled PLK4-STIL Complex Assembly in Centriole BiogenesisThe chromatin remodeller RSF1 is essential for PLK1 deposition and function at mitotic kinetochores.Antibody h-R3-dendrimer mediated siRNA has excellent endosomal escape and tumor targeted delivery ability, and represents efficient siPLK1 silencing and inhibition of cell proliferation, migration and invasion.Myt1 inhibition of Cyclin A/Cdk1 is essential for fusome integrity and premeiotic centriole engagement in Drosophila spermatocytes.
P2860
Q26738970-BAE27195-0236-44B2-9B73-15D34C7C6ACFQ26746785-9A4BC675-3D80-4A4E-8A8F-A1B314988236Q26774420-AD2830BB-AB08-4131-9FA7-6E5E9C201BD3Q26779135-C88E3495-7A6E-4AF1-84EA-1DCE9A17DD95Q27025174-586719C9-F4E9-47E9-B1C8-8A4DF8163CECQ27932118-94C87639-5AD1-419D-B9B8-8375A81AFA00Q27937317-CB4682D8-D9FA-4C1F-887D-411E08A918BCQ28071761-AF97EC25-D2D3-44D0-9A1D-C9D5731D7CD1Q28275930-CF1BE41A-52A9-4942-85A4-C43F214845F2Q28551996-C62531D6-DB59-4FB3-B9F8-27037187A0FDQ28552326-B1438A3E-DE1C-4681-9242-A45A5CB42306Q28820936-491E4C8A-B564-4ACB-95F3-9A4E8839FD3CQ30596297-9B42A541-46DC-4868-B324-267D21DEC865Q30658815-566A2700-D9DD-4FEA-B8FB-FB5AAC2707E7Q30786652-E662C350-CC90-422D-BAA3-290E30F899C1Q30847570-32B57D5A-5CD0-4BF2-96CF-25EA8B052908Q33761796-D010C7BF-1055-48AF-B5C8-502BA03594A0Q33820876-8F0B295F-E64B-4FB6-8B0B-3736FDB1685DQ34103564-1494E208-7687-47E8-8FE5-201DD34BDE7BQ34474551-975924C1-D539-4E98-84A5-511070CF4AE5Q34543786-049E4BB0-0766-4BA4-A359-B9912D0DECDBQ35826056-4FCA9A5F-2B38-472D-BE14-A3749D8E5636Q35832219-EE3B3351-5AE8-44BF-A823-DD45208577DEQ35907201-8569F3AC-F758-4FD0-B6D3-BCBB82C53FB7Q35914029-FE6595C5-10D5-4DD2-B37B-9042F29E782EQ35933358-10D14DFF-7588-4DBA-96D0-6B13C826AC03Q36000726-A9DD2C80-8E19-4921-92A8-1CE53D9F0B8CQ36072488-E9793783-5374-409D-AE0D-E0B3EAFE6CBBQ36112179-A5A1C7C0-4EA7-442C-9634-7A3D82DDA7FBQ36118484-8198A39D-36CE-4C94-8269-71578FBCFB89Q36188452-7E9D659C-2B1F-45D6-8DB1-B28164B4A2D9Q36299646-CA8959A7-2901-442D-AC24-CB62E28317BCQ36326031-8D0E89FA-8622-4231-B3B4-6E24D540F1FBQ36386336-72061E8D-88C6-4820-AA99-D7E333FB8D2DQ36420306-EDB5DD91-A95F-4C29-97A2-32BB25BD3675Q36451518-BD27194D-037D-47F4-B7D0-A729A3D31E22Q36901878-EFBED020-FEC7-4CC0-A1B8-5EB6CE01CDE5Q37031833-E2FA3738-3E7F-4C03-87DA-F4D5C23404F9Q37046458-388441EB-BE7F-41A6-99C0-0AE061603FB3Q37052736-70A6F470-14EE-4F91-B889-68F54AF400CA
P2860
Polo-like kinases: structural variations lead to multiple functions.
description
2014 nî lūn-bûn
@nan
2014年の論文
@ja
2014年学术文章
@wuu
2014年学术文章
@zh-cn
2014年学术文章
@zh-hans
2014年学术文章
@zh-my
2014年学术文章
@zh-sg
2014年學術文章
@yue
2014年學術文章
@zh
2014年學術文章
@zh-hant
name
Polo-like kinases: structural variations lead to multiple functions.
@en
type
label
Polo-like kinases: structural variations lead to multiple functions.
@en
prefLabel
Polo-like kinases: structural variations lead to multiple functions.
@en
P2860
P50
P356
P1476
Polo-like kinases: structural variations lead to multiple functions.
@en
P2860
P2888
P304
P356
10.1038/NRM3819
P577
2014-07-01T00:00:00Z
P5875
P6179
1042225971