Crystal structures of the myristylated catalytic subunit of cAMP-dependent protein kinase reveal open and closed conformations. - Wikidata - wikimedia - TriplyDB

Crystal structures of the myristylated catalytic subunit of cAMP-dependent protein kinase reveal open and closed conformations.

Crystal structures of the myristylated catalytic subunit of cAMP-dependent protein kinase reveal open and closed conformations.

http://www.wikidata.org/entity/Q36277661

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Molecular basis for activation of G protein-coupled receptor kinases SRPK2: a differentially expressed SR protein-specific kinase involved in mediating the interaction and localization of pre-mRNA splicing factors in mammalian cells Gaussian-weighted RMSD superposition of proteins: a structural comparison for flexible proteins and predicted protein structures.A PDK1 homolog is necessary and sufficient to transduce AGE-1 PI3 kinase signals that regulate diapause in Caenorhabditis elegans Effect of mutating the regulatory phosphoserine and conserved threonine on the activity of the expressed catalytic domain of Acanthamoeba myosin I heavy chain kinase Predicting N-terminal myristoylation sites in plant proteins Crystal structure of a conformation-selective casein kinase-1 inhibitor The structure of a binary complex between a mammalian mevalonate kinase and ATP: insights into the reaction mechanism and human inherited disease High resolution crystal structure of the human PDK1 catalytic domain defines the regulatory phosphopeptide docking site.Crystal structure of a myristoylated CAP-23/NAP-22 N-terminal domain complexed with Ca2+/calmodulin Comparative surface geometry of the protein kinase family Novel Isoform-Specific Interfaces Revealed by PKA RIIβ Holoenzyme Structures Structure of the Antibiotic Resistance Factor Spectinomycin Phosphotransferase from Legionella pneumophila Intersubunit capture of regulatory segments is a component of cooperative CaMKII activation Crystal structure of the ALK (anaplastic lymphoma kinase) catalytic domain Structure and Allostery of the PKA RII Tetrameric Holoenzyme Role of N-Terminal Myristylation in the Structure and Regulation of cAMP-Dependent Protein Kinase Characterization and Solution Structure of Mouse Myristoylated Methionine Sulfoxide Reductase A Molecular Features of Product Release for the PKA Catalytic Cycle Crystal structures of the trimeric human immunodeficiency virus type 1 matrix protein: implications for membrane association and assembly Identification of novel splice variants of the human catalytic subunit Cbeta of cAMP-dependent protein kinase N-Myristoylation is essential for protein phosphatases PPM1A and PPM1B to dephosphorylate their physiological substrates in cells Residue Geometry Networks: A Rigidity-Based Approach to the Amino Acid Network and Evolutionary Rate Analysis Analysis of PB2 protein from H9N2 and H5N1 avian flu virus Ligand-induced global transitions in the catalytic domain of protein kinase A.A transition path ensemble study reveals a linchpin role for Mg(2+) during rate-limiting ADP release from protein kinase A.A novel human gene similar to the protein kinase (PK) coding domain of the large subunit of herpes simplex virus type 2 ribonucleotide reductase (ICP10) codes for a serine-threonine PK and is expressed in melanoma cells.Structural characterization of protein kinase A as a function of nucleotide binding. Hydrogen-deuterium exchange studies using matrix-assisted laser desorption ionization-time of flight mass spectrometry detection.How much NMR data is required to determine a protein-ligand complex structure?Auto-inhibition of Ca(2+)/calmodulin-dependent protein kinase II by its ATP-binding domain.Chemical deacylation reduces the adhesive properties of proteolipid protein and leads to decompaction of the myelin sheath.The catalytic subunit of the cAMP-dependent protein kinase of ovine sperm flagella has a unique amino-terminal sequence.FlexOracle: predicting flexible hinges by identification of stable domains.Correlated mutation analysis on the catalytic domains of serine/threonine protein kinases.Single vector system for efficient N-myristoylation of recombinant proteins in E. coli.Protein myristoylation in health and disease.Protein kinase A type I activates a CRE-element more efficiently than protein kinase A type II regardless of C subunit isoform.Liberated PKA Catalytic Subunits Associate with the Membrane via Myristoylation to Preferentially Phosphorylate Membrane Substrates The protein kinase C inhibitor bisindolyl maleimide 2 binds with reversed orientations to different conformations of protein kinase A.β-Subunit myristoylation is the gatekeeper for initiating metabolic stress sensing by AMP-activated protein kinase (AMPK).

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P2860

Crystal structures of the myristylated catalytic subunit of cAMP-dependent protein kinase reveal open and closed conformations.

http://www.wikidata.org/entity/Q36277661

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1993 nî lūn-bûn

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1993年の論文

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1993年学术文章

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1993年学术文章

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1993年学术文章

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1993年学术文章

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1993年学术文章

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1993年學術文章

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1993年學術文章

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1993年學術文章

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Crystal structures of the myri ...... open and closed conformations.

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Crystal structures of the myri ...... open and closed conformations.

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type

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Crystal structures of the myri ...... open and closed conformations.

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Crystal structures of the myri ...... open and closed conformations.

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prefLabel

Crystal structures of the myri ...... open and closed conformations.

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Crystal structures of the myri ...... open and closed conformations.

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Protein Science

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Crystal structures of the myri ...... open and closed conformations.

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D R Knighton

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J M Sowadski

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J Zheng

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L F Ten Eyck

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N H Xuong

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S S Taylor

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P2860

Multiple, distinct forms of bovine and human protein kinase C suggest diversity in cellular signaling pathways

Crystal structure of the catalytic subunit of cyclic adenosine monophosphate-dependent protein kinase

The protein kinase family: conserved features and deduced phylogeny of the catalytic domains

Protein N-myristoylation in Escherichia coli: reconstitution of a eukaryotic protein modification in bacteria.

Structure of a peptide inhibitor bound to the catalytic subunit of cyclic adenosine monophosphate-dependent protein kinase

Slow-cooling protocols for crystallographic refinement by simulated annealing

Ordered phosphorylation of p42mapk by MAP kinase kinase.

Systematic mutational analysis of cAMP-dependent protein kinase identifies unregulated catalytic subunits and defines regions important for the recognition of the regulatory subunit.

Tyrosine kinase catalyzed phosphorylation and inactivation of the inhibitor protein of the cAMP-dependent protein kinase.

Phosphorylation independent activation of human cyclin-dependent kinase 2 by cyclin A in vitro.

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8251932

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protein structure

crystal structure

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2142252

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