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Deacetylation of catalytic lysine in CDK1 is essential for Cyclin-B binding and cell cycle

https://doi.org/10.1101/420000

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What this work says

Outgoing claims: the papers this work cites, builds on, or argues with.

inferredcites →https://doi.org/10.1002/j.1460-2075.1986.tb04179.xopenalex-snapshot

A lysine in the ATP‐binding site of P130gag‐fps is essential for protein‐tyrosine kinase activity.

inferredcites →https://doi.org/10.1002/j.1460-2075.1991.tb04894.xopenalex-snapshot

Phosphorylation at Thr167 is required for Schizosaccharomyces pombe p34cdc2 function.

inferredcites →https://doi.org/10.1002/j.1460-2075.1991.tb04895.xopenalex-snapshot

cdc2 phosphorylation is required for its interaction with cyclin.

inferredcites →https://doi.org/10.1002/j.1460-2075.1991.tb04896.xopenalex-snapshot

Regulatory phosphorylation of the p34cdc2 protein kinase in vertebrates.

inferredcites →https://doi.org/10.1002/j.1460-2075.1991.tb04897.xopenalex-snapshot

Mutations of p34cdc2 phosphorylation sites induce premature mitotic events in HeLa cells: evidence for a double block to p34cdc2 kinase activation in vertebrates.

inferredcites →https://doi.org/10.1002/jcc.20289openalex-snapshot

Scalable molecular dynamics with NAMD

inferredcites →https://doi.org/10.1002/jcc.23422openalex-snapshot

Rapid parameterization of small molecules using the force field toolkit

inferredcites →https://doi.org/10.1006/jmbi.1993.1626openalex-snapshot

Comparative Protein Modelling by Satisfaction of Spatial Restraints

inferredcites →https://doi.org/10.1007/bf00268085openalex-snapshot

Genetic control of the cell division cycle in the fission yeast Schizosaccharomyces pombe

inferredcites →https://doi.org/10.1016/0003-2697(90)90133-topenalex-snapshot

Immunochemical detection of adenine nucleotide-binding proteins with antibodies to 5′-p-fluorosulfonylbenzoyladenosine

inferredcites →https://doi.org/10.1016/0014-5793(95)01514-0openalex-snapshot

Characterisation of human cdc2 lysine 33 mutations expressed in the fission yeast Schizosaccharomyces pombe

inferredcites →https://doi.org/10.1016/0168-9525(85)90023-xopenalex-snapshot

Cell cycle control genes in yeast

inferredcites →https://doi.org/10.1016/0263-7855(96)00018-5openalex-snapshot

VMD: Visual molecular dynamics

inferredcites →https://doi.org/10.1016/j.bbamcr.2010.04.004openalex-snapshot

A cancer-derived mutation in the PSTAIRE helix of cyclin-dependent kinase 2 alters the stability of cyclin binding

inferredcites →https://doi.org/10.1016/j.bbamcr.2014.02.001openalex-snapshot

Phosphorylation of p300 increases its protein degradation to enhance the lung cancer progression

inferredcites →https://doi.org/10.1016/j.bbapap.2009.10.017openalex-snapshot

Defining the conserved internal architecture of a protein kinase

inferredcites →https://doi.org/10.1016/j.bbrc.2014.03.118openalex-snapshot

Acetylation of cyclin-dependent kinase 5 is mediated by GCN5

inferredcites →https://doi.org/10.1016/j.tibs.2010.09.006openalex-snapshot

Protein kinases: evolution of dynamic regulatory proteins

inferredcites →https://doi.org/10.1021/acs.chemrev.7b00181openalex-snapshot

Lysine Acetylation Goes Global: From Epigenetics to Metabolism and Therapeutics

inferredcites →https://doi.org/10.1021/jp973084fopenalex-snapshot

All-Atom Empirical Potential for Molecular Modeling and Dynamics Studies of Proteins

inferredcites →https://doi.org/10.1038/292558a0openalex-snapshot

Gene required in G1 for commitment to cell cycle and in G2 for control of mitosis in fission yeast

inferredcites →https://doi.org/10.1038/302153a0openalex-snapshot

Control of timing of cell cycle events in fission yeast by the wee 1+ gene

inferredcites →https://doi.org/10.1038/327031a0openalex-snapshot

Complementation used to clone a human homologue of the fission yeast cell cycle control gene cdc2

inferredcites →https://doi.org/10.1038/342039a0openalex-snapshot

Tyrosine phosphorylation of the fission yeast cdc2+ protein kinase regulates entry into mitosis

inferredcites →https://doi.org/10.1038/363595a0openalex-snapshot

Crystal structure of cyclin-dependent kinase 2

inferredcites →https://doi.org/10.1038/376313a0openalex-snapshot

Mechanism of CDK activation revealed by the structure of a cyclinA-CDK2 complex

inferredcites →https://doi.org/10.1038/nature06046openalex-snapshot

Cdk1 is sufficient to drive the mammalian cell cycle

inferredcites →https://doi.org/10.1038/nature09543openalex-snapshot

Driving the cell cycle with a minimal CDK control network

inferredcites →https://doi.org/10.1038/ncomms7769openalex-snapshot

CDK1 structures reveal conserved and unique features of the essential cell cycle CDK

inferredcites →https://doi.org/10.1038/nrd4504openalex-snapshot

The history and future of targeting cyclin-dependent kinases in cancer therapy

inferredcites →https://doi.org/10.1038/nrm3841openalex-snapshot

The growing landscape of lysine acetylation links metabolism and cell signalling

inferredcites →https://doi.org/10.1038/nrm3931openalex-snapshot

50 years of protein acetylation: from gene regulation to epigenetics, metabolism and beyond

inferredcites →https://doi.org/10.1038/nsb0896-696openalex-snapshot

Structural basis of cyclin-dependent kinase activation by phosphorylation

inferredcites →https://doi.org/10.1038/s41418-018-0069-8openalex-snapshot

SIRT2 regulates oxidative stress-induced cell death through deacetylation of c-Jun NH2-terminal kinase

inferredcites →https://doi.org/10.1073/pnas.1301463110openalex-snapshot

SIRT2 directs the replication stress response through CDK9 deacetylation

inferredcites →https://doi.org/10.1073/pnas.82.23.7894openalex-snapshot

Lysine residue 121 in the proposed ATP-binding site of the v-mos protein is required for transformation.

inferredcites →https://doi.org/10.1073/pnas.84.3.704openalex-snapshot

Replacement of lysine residue 1030 in the putative ATP-binding region of the insulin receptor abolishes insulin- and antibody-stimulated glucose uptake and receptor kinase activity.

inferredcites →https://doi.org/10.1074/jbc.m107890200openalex-snapshot

Kinetic Mechanism of Activation of the Cdk2/Cyclin A Complex

inferredcites →https://doi.org/10.1074/jbc.m114.581843openalex-snapshot

Stoichiometry of Site-specific Lysine Acetylation in an Entire Proteome

inferredcites →https://doi.org/10.1074/jbc.m117.784546openalex-snapshot

Lysine acetylation stoichiometry and proteomics analyses reveal pathways regulated by sirtuin 1 in human cells

inferredcites →https://doi.org/10.1074/jbc.m407586200openalex-snapshot

Consequences of Lysine 72 Mutation on the Phosphorylation and Activation State of cAMP-dependent Kinase

inferredcites →https://doi.org/10.1074/mcp.t500029-mcp200openalex-snapshot

Absolute Quantification of Multisite Phosphorylation by Selective Reaction Monitoring Mass Spectrometry

inferredcites →https://doi.org/10.1091/mbc.6.4.371openalex-snapshot

The Wee1 protein kinase regulates T14 phosphorylation of fission yeast Cdc2.

inferredcites →https://doi.org/10.1091/mbc.e11-02-0136openalex-snapshot

Coupling of T161 and T14 phosphorylations protects cyclin B–CDK1 from premature activation

inferredcites →https://doi.org/10.1093/genetics/136.3.849openalex-snapshot

Efficient targeted integration at leu1-32 and ura4-294 in Schizosaccharomyces pombe.

inferredcites →https://doi.org/10.1093/nar/gkp777openalex-snapshot

The transcriptional co-activator PCAF regulates cdk2 activity

inferredcites →https://doi.org/10.1098/rsob.120136openalex-snapshot

On the molecular mechanisms of mitotic kinase activation

inferredcites →https://doi.org/10.1126/science.1175371openalex-snapshot

Lysine Acetylation Targets Protein Complexes and Co-Regulates Major Cellular Functions

inferredcites →https://doi.org/10.1126/science.8266103openalex-snapshot

Distinct Roles for Cyclin-Dependent Kinases in Cell Cycle Control

inferredcites →https://doi.org/10.1128/mcb.01205-10openalex-snapshot

Acetylation of a Conserved Lysine Residue in the ATP Binding Pocket of p38 Augments Its Kinase Activity during Hypertrophy of Cardiomyocytes

inferredcites →https://doi.org/10.1128/mcb.01557-07openalex-snapshot

Acetylation of Conserved Lysines in the Catalytic Core of Cyclin-Dependent Kinase 9 Inhibits Kinase Activity and Regulates Transcription

inferredcites →https://doi.org/10.1128/mcb.13.3.1675openalex-snapshot

Mechanisms of p34cdc2 regulation.

inferredcites →https://doi.org/10.1128/mcb.19.2.1605openalex-snapshot

Human TFIIIC Relieves Chromatin-Mediated Repression of RNA Polymerase III Transcription and Contains an Intrinsic Histone Acetyltransferase Activity

inferredcites →https://doi.org/10.1128/mcb.6.3.751openalex-snapshot

Neither arginine nor histidine can carry out the function of lysine-295 in the ATP-binding site of p60src.

inferredcites →https://doi.org/10.1146/annurev-biochem-052410-090317openalex-snapshot

The Structural Basis for Control of Eukaryotic Protein Kinases

inferredcites →https://doi.org/10.1146/annurev.bi.61.070192.002301openalex-snapshot

ANIMAL CELL CYCLES AND THEIR CONTROL

inferredcites →https://doi.org/10.1146/annurev.cellbio.13.1.261openalex-snapshot

CYCLIN-DEPENDENT KINASES: Engines, Clocks, and Microprocessors

inferredcites →https://doi.org/10.1158/0008-5472.can-06-1758openalex-snapshot

Combined Depletion of Cell Cycle and Transcriptional Cyclin-Dependent Kinase Activities Induces Apoptosis in Cancer Cells

inferredcites →https://doi.org/10.1186/gb4184openalex-snapshot

Cyclin-dependent kinases

inferredcites →https://doi.org/10.1371/journal.pbio.2000127openalex-snapshot

Decoding the Interactions Regulating the Active State Mechanics of Eukaryotic Protein Kinases

inferredcites →https://doi.org/10.1371/journal.pone.0004020openalex-snapshot

Phosphorylation Regulates SIRT1 Function

inferredcites →https://doi.org/10.4161/cc.5.9.2721openalex-snapshot

Unmasking the Redundancy Between Cdk1 and Cdk2 at G2 Phase in Human Cancer Cell Lines

inferredcites →https://doi.org/10.7554/elife.32952openalex-snapshot

SIRT2 deacetylase regulates the activity of GSK3 isoforms independent of inhibitory phosphorylation

What points at this work

Incoming claims: where this work appears in other papers’ reference lists and arguments.

inferred← citeshttps://doi.org/10.1016/j.bioorg.2020.104374openalex-snapshot

Synthesis of some novel methyl β-orsellinate based 3, 5-disubstituted isoxazoles and their anti-proliferative activity: Identification of potent leads active against MCF-7 breast cancer cell

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