Insights into Aurora-A Kinase Activation Using Unnatural Amino Acids Incorporated by Chemical Modification - Wikidata - wikimedia - TriplyDB

Insights into Aurora-A Kinase Activation Using Unnatural Amino Acids Incorporated by Chemical Modification

Insights into Aurora-A Kinase Activation Using Unnatural Amino Acids Incorporated by Chemical Modification

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Aurora-A-Dependent Control of TACC3 Influences the Rate of Mitotic Spindle Assembly Diverse functionalization of Aurora-A kinase at specified surface and buried sites by native chemical modification Chemoselective synthesis and analysis of naturally occurring phosphorylated cysteine peptides Issues in interpreting the in vivo activity of Aurora-A Linker-free incorporation of carbohydrates into in vitro displayed macrocyclic peptides.Developments and recent advancements in the field of endogenous amino acid selective bond forming reactions for bioconjugation.Synthetic approaches to protein phosphorylation.Chemical Protein Modification through Cysteine.7-(Pyrazol-4-yl)-3H-imidazo[4,5-b]pyridine-based derivatives for kinase inhibition: Co-crystallisation studies with Aurora-A reveal distinct differences in the orientation of the pyrazole N1-substituent Chemical Approaches to Studying Labile Amino Acid Phosphorylation.Switching Aurora-A kinase on and off at an allosteric site.Allosteric inhibition of Aurora-A kinase by a synthetic vNAR domain.Synthetic phosphorylation of p38α recapitulates protein kinase activity The structure of C290A:C393A Aurora A provides structural insights into kinase regulation.Dynamic Equilibrium of the Aurora A Kinase Activation Loop Revealed by Single-Molecule Spectroscopy.Incorporation of Phosphorylated Tyrosine into Proteins: In Vitro Translation and Study of Phosphorylated IκB-α and Its Interaction with NF-κB.A dynamic mechanism for allosteric activation of Aurora kinase A by activation loop phosphorylation.Mapping interactions between p27 and RhoA that stimulate cell migration.Production of Protein Kinases in E. coli.Mitotic spindle association of TACC3 requires Aurora-A-dependent stabilization of a cryptic α-helix.Mitotic phosphorylation regulates Hsp72 spindle localization by uncoupling ATP binding from substrate release

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Insights into Aurora-A Kinase Activation Using Unnatural Amino Acids Incorporated by Chemical Modification

http://www.wikidata.org/entity/Q27679437

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2013年の論文

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2013年論文

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ACS Chemical Biology

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Insights into Aurora-A Kinase ...... rated by Chemical Modification

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Fiona C Rowan

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Julian Blagg

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Meirion Richards

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Rachel A Bibby

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P2860

Structural basis of Aurora-A activation by TPX2 at the mitotic spindle

The chemical biology of protein phosphorylation

Effect of mutating the regulatory phosphoserine and conserved threonine on the activity of the expressed catalytic domain of Acanthamoeba myosin I heavy chain kinase

The 1.9 A resolution crystal structure of phosphono-CheY, an analogue of the active form of the response regulator, CheY

Crystal structure of an Aurora-A mutant that mimics Aurora-B bound to MLN8054: insights into selectivity and drug design

Development of o -Chlorophenyl Substituted Pyrimidines as Exceptionally Potent Aurora Kinase Inhibitors

The mitotic serine/threonine kinase Aurora2/AIK is regulated by phosphorylation and degradation

A homologue of Drosophila aurora kinase is oncogenic and amplified in human colorectal cancers

Mechanism of PhosphoThreonine/Serine Recognition and Specificity for Modular Domains from All-atom Molecular Dynamics

An essential role of the aPKC-Aurora A-NDEL1 pathway in neurite elongation by modulation of microtubule dynamics

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2184-91

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scholarly article

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3704917

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10.1021/CB400425T

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10

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8

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Richard Bayliss

Andrew Thompson

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2013-10-18T00:00:00Z

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255705644

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23924325

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3805324

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