Phosphorylation by Cdk1 induces Plk1-mediated vimentin phosphorylation during mitosis. - Wikidata - wikimedia - TriplyDB

Phosphorylation by Cdk1 induces Plk1-mediated vimentin phosphorylation during mitosis.

Phosphorylation by Cdk1 induces Plk1-mediated vimentin phosphorylation during mitosis.

http://www.wikidata.org/entity/Q40356177

about

Cep164, a novel centriole appendage protein required for primary cilium formation Choice of Plk1 docking partners during mitosis and cytokinesis is controlled by the activation state of Cdk1 Phosphorylation by polo-like kinase 1 induces the tumor-suppressing activity of FADD Role of phosphorylation on the structural dynamics and function of types III and IV intermediate filaments The Serine/threonine kinase Stk33 exhibits autophosphorylation and phosphorylates the intermediate filament protein Vimentin Proteomic identification of Hsp70 as a new Plk1 substrate in arsenic trioxide-induced mitotically arrested cells Intermediate Filaments Play a Pivotal Role in Regulating Cell Architecture and Function Suppression of Vimentin Phosphorylation by the Avian Reovirus p17 through Inhibition of CDK1 and Plk1 Impacting the G2/M Phase of the Cell Cycle DNA-PK target identification reveals novel links between DNA repair signaling and cytoskeletal regulation The serine/threonine kinase 33 is present and expressed in palaeognath birds but has become a unitary pseudogene in neognaths about 100 million years ago Use of the novel Plk1 inhibitor ZK-thiazolidinone to elucidate functions of Plk1 in early and late stages of mitosis.Polo kinase interacts with RacGAP50C and is required to localize the cytokinesis initiation complex.PI 3-kinase-dependent phosphorylation of Plk1-Ser99 promotes association with 14-3-3γ and is required for metaphase-anaphase transition.Enterovirus 71 VP1 activates calmodulin-dependent protein kinase II and results in the rearrangement of vimentin in human astrocyte cells.Activation of cyclin B1-Cdk1 synchronizes events in the nucleus and the cytoplasm at mitosis Polo-box domain: a versatile mediator of polo-like kinase function.Regulatory functional territory of PLK-1 and their substrates beyond mitosis.Vimentin as an integral regulator of cell adhesion and endothelial sprouting.Dissociation of Crk-associated substrate from the vimentin network is regulated by p21-activated kinase on ACh activation of airway smooth muscle.Proteomic screen defines the Polo-box domain interactome and identifies Rock2 as a Plk1 substrate.Cytokinetic Failure-induced Tetraploidy Develops into Aneuploidy, Triggering Skin Aging in Phosphovimentin-deficient Mice.Quantitative proteomics reveals the basis for the biochemical specificity of the cell-cycle machinery Wee1 is required to sustain ATR/Chk1 signaling upon replicative stress.A stringent requirement for Plk1 T210 phosphorylation during K-fiber assembly and chromosome congression Intermediate filaments in smooth muscle.A mitotic GlcNAcylation/phosphorylation signaling complex alters the posttranslational state of the cytoskeletal protein vimentin Polo-like kinase 1 is involved in invasion through extracellular matrix.Providing cellular signposts--post-translational modifications of intermediate filaments.Cdc42GAP, reactive oxygen species, and the vimentin network Identification of CDK2 substrates in human cell lysates.Tumour-specific delivery of siRNA-coupled superparamagnetic iron oxide nanoparticles, targeted against PLK1, stops progression of pancreatic cancer.Role of p47(phox) in regulating Cdc42GAP, vimentin, and contraction in smooth muscle cells Phosphorylation of myosin II-interacting guanine nucleotide exchange factor (MyoGEF) at threonine 544 by aurora B kinase promotes the binding of polo-like kinase 1 to MyoGEF.Liprin-α1 is a regulator of vimentin intermediate filament network in the cancer cell adhesion machinery.Lessons from Animal Models of Cytoplasmic Intermediate Filament Proteins.Sequential Cdk1 and Plk1 phosphorylation of protein tyrosine phosphatase 1B promotes mitotic cell death.Inhibition of endocytic vesicle fusion by Plk1-mediated phosphorylation of vimentin during mitosis.Defect of mitotic vimentin phosphorylation causes microophthalmia and cataract via aneuploidy and senescence in lens epithelial cells.An anti vimentin antibody promotes tube formation.Dronc caspase exerts a non-apoptotic function to restrain phospho-Numb-induced ectopic neuroblast formation in Drosophila.

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P2860

Phosphorylation by Cdk1 induces Plk1-mediated vimentin phosphorylation during mitosis.

http://www.wikidata.org/entity/Q40356177

description

2005 nî lūn-bûn

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2005年の論文

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2005年論文

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2005年論文

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2005年论文

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2005年论文

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name

Phosphorylation by Cdk1 induces Plk1-mediated vimentin phosphorylation during mitosis.

@en

type

label

Phosphorylation by Cdk1 induces Plk1-mediated vimentin phosphorylation during mitosis.

@en

prefLabel

Phosphorylation by Cdk1 induces Plk1-mediated vimentin phosphorylation during mitosis.

@en

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Journal of Cell Biology

P1476

Phosphorylation by Cdk1 induces Plk1-mediated vimentin phosphorylation during mitosis.

@en

P2093

Andreas Uldschmid

http://www.w3.org/2001/XMLSchema#string

Anja Hanisch

http://www.w3.org/2001/XMLSchema#string

Herman Silljé

http://www.w3.org/2001/XMLSchema#string

Masaki Inagaki

http://www.w3.org/2001/XMLSchema#string

Takashi Oguri

http://www.w3.org/2001/XMLSchema#string

Tomoya Yamaguchi

http://www.w3.org/2001/XMLSchema#string

Tomoya Yokoyama

http://www.w3.org/2001/XMLSchema#string

Yasushi Takai

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P2860

The molecular basis for phosphodependent substrate targeting and regulation of Plks by the Polo-box domain

Mitotic kinases as regulators of cell division and its checkpoints

Aurora-B regulates the cleavage furrow-specific vimentin phosphorylation in the cytokinetic process

Intermediate filaments: structure, dynamics, function, and disease

Polo-like kinases and the orchestration of cell division

Proteomic screen finds pSer/pThr-binding domain localizing Plk1 to mitotic substrates

The cellular geography of aurora kinases

Activation of Cdc2/cyclin B and inhibition of centrosome amplification in cells depleted of Plk1 by siRNA.

Identification of a consensus motif for Plk (Polo-like kinase) phosphorylation reveals Myt1 as a Plk1 substrate.

Intermediate filaments mediate cytoskeletal crosstalk.

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10.1083/JCB.200504091

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3

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171

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2005-10-31T00:00:00Z

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7505669

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16260496

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phosphorylation

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2171270

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