Results 11 to 20 of about 9,921 (221)
PLK1, A Potential Target for Cancer Therapy [PDF]
Translational Oncology, 2017 Polo-like kinase 1 (PLK1) plays an important role in the initiation, maintenance, and completion of mitosis. Dysfunction of PLK1 may promote cancerous transformation and drive its progression.
Zhixian Liu +2 more
doaj +4 more sources
Spatial separation of Plk1 phosphorylation and activity [PDF]
Frontiers in Oncology, 2015 Polo-like kinase 1 (Plk1) is one of the major kinases controlling mitosis and cell division. Plk1 is first recruited to the centrosome in S phase, then appears on the kinetochores in late G2 and at the end of mitosis it translocates to the central ...
Wytse eBruinsma +10 more
doaj +7 more sources
Self-regulated mechanism of Plk1 localization to kinetochores: lessons from the Plk1-PBIP1 interaction [PDF]
Cell Division, 2008 Mammalian polo-like kinase 1 (Plk1) has been studied extensively as a critical element in regulating various mitotic events during M-phase progression. Plk1 function is spatially regulated through the targeting activity of the conserved polo-box domain ...
Kang Young H +3 more
doaj +5 more sources
Computational Design of Targeted Inhibitors of Polo-Like Kinase 1 (Plk1)
Bioinformatics and Biology Insights, 2012 Computational design of small molecule putative inhibitors of Polo-like kinase 1 (Plk1) is presented. Plk1, which regulates the cell cycle, is often over expressed in cancers. Down regulation of Plk1 has been shown to inhibit tumor progression.
Krupa S. Jani, D.S. Dalafave
doaj +2 more sources
Self-Regulated Plk1 Recruitment to Kinetochores by the Plk1-PBIP1 Interaction Is Critical for Proper Chromosome Segregation [PDF]
Molecular Cell, 2006 The polo-box domain (PBD) of mammalian polo-like kinase 1 (Plk1) is essential in targeting its catalytic activity to specific subcellular structures critical for mitosis. The mechanism underlying Plk1 recruitment to the kinetochores and the role of Plk1 at this site remain elusive.
Kang, Young H. +10 more
openaire +3 more sources
Ubiquitylation-dependent localization of PLK1 in mitosis
Nature Cell Biology, 2013 Polo-like kinase 1 (PLK1) critically regulates mitosis through its dynamic localization to kinetochores, centrosomes and the midzone. The polo-box domain (PBD) and activity of PLK1 mediate its recruitment to mitotic structures, but the mechanisms regulating PLK1 dynamics remain poorly understood. Here, we identify PLK1 as a target of the cullin 3 (CUL3)
Beck, Jochen +11 more
openaire +6 more sources
A Role for Plk1 Phosphorylation of NudC in Cytokinesis [PDF]
Developmental Cell, 2003 Polo-like kinase 1 (Plk1) plays essential roles at multiple events during cell division, yet little is known about its physiological substrates. In a cDNA phage display screen using Plk1 C-terminal affinity columns, we identified NudC (nuclear distribution gene C) as a Plk1 binding protein.
Zhou, Tianhua +4 more
openaire +4 more sources
The Plk1-dependent Phosphoproteome of the Early Mitotic Spindle [PDF]
Molecular & Cellular Proteomics, 2011 Polo-like kinases regulate many aspects of mitotic and meiotic progression from yeast to man. In early mitosis, mammalian Polo-like kinase 1 (Plk1) controls centrosome maturation, spindle assembly, and microtubule attachment to kinetochores. However, despite the essential and diverse functions of Plk1, the full range of Plk1 substrates remains to be ...
Santamaria, A. +9 more
openaire +7 more sources
Polo-like kinase 1 (PLK1) signaling in cancer and beyond.
Biochemical Pharmacology, 2021 PLK1 is an evolutionary conserved Ser/Thr kinase that is best known for its role in cell cycle regulation and is expressed predominantly during the G2/S and M phase of the cell cycle.
Styliani Iliaki +2 more
semanticscholar +2 more sources
Cell, 2003 New work by Elia et al. in this issue of Cell reveals the molecular basis of phosphopeptide recognition by the polo domain and the domain's dual function to promote substrate recognition by targeting the kinase to subcellular structures and to autoregulate the adjacent protein kinase catalytic domain.
Leung, Genie C., Sicheri, Frank
openaire +2 more sources