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Mps1 as a link between centrosomes and genomic instability
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What this work says
Outgoing claims: the papers this work cites, builds on, or argues with.
inferredcites →https://doi.org/10.1007/978-1-4612-0411-4_18openalex-snapshot
Tumor Progression in Breast Cancer
inferredcites →https://doi.org/10.1007/978-1-59745-198-7openalex-snapshot
The Protein Protocols Handbook
inferredcites →https://doi.org/10.1007/s10549-004-1424-7openalex-snapshot
Genomic patterns of allelic imbalance in disease free tissue adjacent to primary breast carcinomas
inferredcites →https://doi.org/10.1016/j.ceb.2005.12.008openalex-snapshot
Controlling centrosome number: licenses and blocks
inferredcites →https://doi.org/10.1016/j.devcel.2007.07.002openalex-snapshot
Plk4-Induced Centriole Biogenesis in Human Cells
inferredcites →https://doi.org/10.1016/j.tcb.2007.03.003openalex-snapshot
Centrosome duplication: of rules and licenses
inferredcites →https://doi.org/10.1016/s0002-9440(10)65513-7openalex-snapshot
Altered Centrosome Structure Is Associated with Abnormal Mitoses in Human Breast Tumors
inferredcites →https://doi.org/10.1016/s0070-2153(99)49015-5openalex-snapshot
The role of the centrosome in the development of malignant tumors
inferredcites →https://doi.org/10.1016/s0092-8674(01)00410-xopenalex-snapshot
Mps1 Is a Kinetochore-Associated Kinase Essential for the Vertebrate Mitotic Checkpoint
inferredcites →https://doi.org/10.1016/s0092-8674(01)00411-1openalex-snapshot
The Mouse Mps1p-like Kinase Regulates Centrosome Duplication
inferredcites →https://doi.org/10.1016/s0955-0674(02)00385-xopenalex-snapshot
Centrosomes and tumour suppressors
inferredcites →https://doi.org/10.1016/s0960-9822(01)00094-xopenalex-snapshot
Kinetics and regulation of de novo centriole assembly
inferredcites →https://doi.org/10.1016/s1097-2765(02)00654-8openalex-snapshot
Duplicating Dangerously
inferredcites →https://doi.org/10.1016/s1470-2045(04)01653-5openalex-snapshot
Genomic instability in histologically normal breast tissues: implications for carcinogenesis
inferredcites →https://doi.org/10.1038/nrc2249openalex-snapshot
Oncogenes and tumour suppressors take on centrosomes
inferredcites →https://doi.org/10.1038/nrc924openalex-snapshot
Centrosome aberrations: cause or consequence of cancer progression?
inferredcites →https://doi.org/10.1038/sj.onc.1210456openalex-snapshot
Centriole overduplication through the concurrent formation of multiple daughter centrioles at single maternal templates
inferredcites →https://doi.org/10.1038/sj.onc.1210815openalex-snapshot
Ovarian hyperstimulation induces centrosome amplification and aneuploid mammary tumors independently of alterations in p53 in a transgenic mouse model of breast cancer
inferredcites →https://doi.org/10.1073/pnas.032479999openalex-snapshot
Centrosome amplification drives chromosomal instability in breast tumor development
inferredcites →https://doi.org/10.1073/pnas.0401139101openalex-snapshot
The Six1 homeoprotein stimulates tumorigenesis by reactivation of cyclin A1
inferredcites →https://doi.org/10.1073/pnas.2434156100openalex-snapshot
Human Mps1 protein kinase is required for centrosome duplication and normal mitotic progression
inferredcites →https://doi.org/10.1073/pnas.95.6.2950openalex-snapshot
Centrosome hypertrophy in human breast tumors: Implications for genomic stability and cell polarity
inferredcites →https://doi.org/10.1074/jbc.m002446200openalex-snapshot
Cell Cycle-regulated Phosphorylation of the Human SIX1 Homeodomain Protein
inferredcites →https://doi.org/10.1083/jcb.114.4.745openalex-snapshot
MPS1 and MPS2: novel yeast genes defining distinct steps of spindle pole body duplication.
inferredcites →https://doi.org/10.1083/jcb.132.1.111openalex-snapshot
The Saccharomyces cerevisiae spindle pole body duplication gene MPS1 is part of a mitotic checkpoint.
inferredcites →https://doi.org/10.1083/jcb.149.2.317openalex-snapshot
The Respective Contributions of the Mother and Daughter Centrioles to Centrosome Activity and Behavior in Vertebrate Cells
inferredcites →https://doi.org/10.1083/jcb.200411126openalex-snapshot
The de novo centriole assembly pathway in HeLa cells
inferredcites →https://doi.org/10.1091/mbc.02-05-0074openalex-snapshot
Human MPS1 Kinase Is Required for Mitotic Arrest Induced by the Loss of CENP-E from Kinetochores
inferredcites →https://doi.org/10.1091/mbc.9.4.759openalex-snapshot
New Alleles of the YeastMPS1Gene Reveal Multiple Requirements in Spindle Pole Body Duplication
inferredcites →https://doi.org/10.1091/mbc.e04-10-0939openalex-snapshot
The Forkhead-associated Domain Protein Cep170 Interacts with Polo-like Kinase 1 and Serves as a Marker for Mature Centrioles
inferredcites →https://doi.org/10.1091/mbc.e07-03-0283openalex-snapshot
Preventing the Degradation of Mps1 at Centrosomes Is Sufficient to Cause Centrosome Reduplication in Human Cells
inferredcites →https://doi.org/10.1093/emboj/21.7.1723openalex-snapshot
Human Mps1 kinase is required for the spindle assembly checkpoint but not for centrosome duplication
inferredcites →https://doi.org/10.1097/01.coc.0000198740.33617.2fopenalex-snapshot
Biology of Ductal Carcinoma in Situ Classification Based on Biologic Potential
inferredcites →https://doi.org/10.1111/j.1365-2443.2007.01091.xopenalex-snapshot
Physical and functional interaction between mortalin and Mps1 kinase
inferredcites →https://doi.org/10.1126/science.273.5277.953openalex-snapshot
Activation of the Budding Yeast Spindle Assembly Checkpoint Without Mitotic Spindle Disruption
inferredcites →https://doi.org/10.1158/0008-5472.can-03-0110openalex-snapshot
The Cyclin-dependent Kinase Inhibitor CYC202 (R-Roscovitine) Inhibits Retinoblastoma Protein Phosphorylation, Causes Loss of Cyclin D1, and Activates the Mitogen-activated Protein Kinase Pathway
inferredcites →https://doi.org/10.1158/1078-0432.ccr-05-0903openalex-snapshot
Increased Expression of Mitotic Checkpoint Genes in Breast Cancer Cells with Chromosomal Instability
inferredcites →https://doi.org/10.1242/jcs.005231openalex-snapshot
Structure and duplication of the centrosome
inferredcites →https://doi.org/10.1242/jcs.115.9.1825openalex-snapshot
CEP110 and ninein are located in a specific domain of the centrosome associated with centrosome maturation
What points at this work
Incoming claims: where this work appears in other papers’ reference lists and arguments.
inferred← citeshttps://doi.org/10.1002/cm.22032openalex-snapshot
Inactivation of the Catalytic Activity of Mps1 Kinase Prevents Its Own Degradation at Centrosomes
inferred← citeshttps://doi.org/10.1007/978-1-4419-0461-4_576openalex-snapshot
Monopolar Spindle 1 (Mps1)
inferred← citeshttps://doi.org/10.1007/978-1-62703-035-9_8openalex-snapshot
Many Pathways to Destruction: The Role of the Centrosome in, and Its Control by Regulated Proteolysis
inferred← citeshttps://doi.org/10.1007/978-3-030-23173-6_17openalex-snapshot
Breaking Bad: Uncoupling of Modularity in Centriole Biogenesis and the Generation of Excess Centrioles in Cancer
inferred← citeshttps://doi.org/10.1007/978-3-319-67199-4_576openalex-snapshot
Monopolar Spindle 1 (Mps1)
inferred← citeshttps://doi.org/10.1016/j.bmc.2017.02.030openalex-snapshot
Novel pyrrolopyrimidines as Mps1/TTK kinase inhibitors for breast cancer
inferred← citeshttps://doi.org/10.1016/j.canlet.2013.05.029openalex-snapshot
Oncogenic B-RafV600E abrogates the AKT/B-Raf/Mps1 interaction in melanoma cells
inferred← citeshttps://doi.org/10.1016/j.ejmech.2019.04.047openalex-snapshot
Molecular design and anticancer activities of small-molecule monopolar spindle 1 inhibitors: A Medicinal chemistry perspective
inferred← citeshttps://doi.org/10.1016/j.ejmech.2020.113023openalex-snapshot
Pyrido[2, 3-d]pyrimidin-7(8H)-ones as new selective orally bioavailable Threonine Tyrosine Kinase (TTK) inhibitors
inferred← citeshttps://doi.org/10.1016/j.ejmech.2022.114887openalex-snapshot
Design, Synthesis and Biological Evaluation of a New Class of 7H-Pyrrolo[2,3-D]Pyrimidine Derivatives as Mps1 Inhibitors for the Treatment of Breast Cancer
inferred← citeshttps://doi.org/10.1016/j.ejmech.2024.116504openalex-snapshot
Hijacking monopolar spindle 1 (MPS1) for various cancer types by small molecular inhibitors: Deep insights from a decade of research and patents
inferred← citeshttps://doi.org/10.1021/acs.jmedchem.3c00963openalex-snapshot
Development of MPS1 Inhibitors: Recent Advances and Perspectives
inferred← citeshttps://doi.org/10.1038/onc.2012.94openalex-snapshot
Phosphorylation of Mps1 by BRAFV600E prevents Mps1 degradation and contributes to chromosome instability in melanoma
inferred← citeshttps://doi.org/10.1073/pnas.1607421113openalex-snapshot
Modular elements of the TPR domain in the Mps1 N terminus differentially target Mps1 to the centrosome and kinetochore
inferred← citeshttps://doi.org/10.1074/jbc.m110.140905openalex-snapshot
Degradation of the Human Mitotic Checkpoint Kinase Mps1 Is Cell Cycle-regulated by APC-cCdc20 and APC-cCdh1 Ubiquitin Ligases*
inferred← citeshttps://doi.org/10.1091/mbc.e10-04-0281openalex-snapshot
Antizyme Restrains Centrosome Amplification by Regulating the Accumulation of Mps1 at Centrosomes
inferred← citeshttps://doi.org/10.1091/mbc.e10-04-0298openalex-snapshot
Mps1 Phosphorylation Sites Regulate the Function of Centrin 2 in Centriole Assembly
inferred← citeshttps://doi.org/10.1091/mbc.e14-07-1248openalex-snapshot
Centrin 3 is an inhibitor of centrosomal Mps1 and antagonizes centrin 2 function
inferred← citeshttps://doi.org/10.1158/1541-7786.mcr-14-0462-topenalex-snapshot
Targeting MPS1 Enhances Radiosensitization of Human Glioblastoma by Modulating DNA Repair Proteins
inferred← citeshttps://doi.org/10.1186/1747-1028-6-9openalex-snapshot
Centriole assembly and the role of Mps1: defensible or dispensable?
inferred← citeshttps://doi.org/10.1186/1747-1028-9-3openalex-snapshot
Differential expression of centrosome regulators in Her2+ breast cancer cells versus non-tumorigenic MCF10A cells
inferred← citeshttps://doi.org/10.1371/journal.pone.0067822openalex-snapshot
CDC25B Overexpression Stabilises Centrin 2 and Promotes the Formation of Excess Centriolar Foci
inferred← citeshttps://doi.org/10.18632/oncotarget.6432openalex-snapshot
Whole-genome duplication increases tumor cell sensitivity to MPS1 inhibition
inferred← citeshttps://doi.org/10.18632/oncotarget.6552openalex-snapshot
Mps1 is SUMO-modified during the cell cycle
inferred← citeshttps://doi.org/10.24275/uami.2r36tx79mopenalex-snapshot
Análisis de la participación de MPS1 en la inducción de amplificación de centrosomas por mutantes de P53 en líneas celulares de cáncer
inferred← citeshttps://doi.org/10.3389/fonc.2013.00277openalex-snapshot
Centrosome Dysfunction Contributes to Chromosome Instability, Chromoanagenesis, and Genome Reprograming in Cancer
inferred← citeshttps://doi.org/10.3892/ijmm.2014.1961openalex-snapshot
Effects of ornithine decarboxylase antizyme 1 on the proliferation and differentiation of human oral cancer cells
inferred← citeshttps://doi.org/10.3892/ol.2019.9924openalex-snapshot
Mps1 is associated with the BRAFV600E mutation and predicts poor outcome in patients with colorectal cancer
inferred← citeshttps://doi.org/10.4137/cin.s6631openalex-snapshot
In silico Analysis of Combinatorial microRNA Activity Reveals Target Genes and Pathways Associated with Breast Cancer Metastasis
inferred← citeshttps://doi.org/10.4161/cc.10.5.14955openalex-snapshot
Mip1 associates with both the Mps1 kinase and actin, and is required for cell cortex stability and anaphase spindle positioning
inferred← citeshttps://doi.org/10.4161/cc.21927openalex-snapshot
VDAC3 regulates centriole assembly by targeting Mps1 to centrosomes
inferred← citeshttps://doi.org/10.4161/cc.23824openalex-snapshot
VDAC3 and Mps1 negatively regulate ciliogenesis
inferred← citeshttps://doi.org/10.5772/intechopen.87547openalex-snapshot
Ubiquitin - Proteasome Pathway
inferred← citeshttps://doi.org/10.5772/intechopen.92623openalex-snapshot
Ubiquitin-Independent Proteasomal Degradation Mediated by Antizyme
inferred← citeshttps://doi.org/10.70675/2ae3e010zff79z4dd2zadfez7f3daabd476bopenalex-snapshot
Phosphoregulation of Mps1 kinase activity
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