Structures of parasitic CDPK domains point to a common mechanism of activation - Wikidata - thesis-toulmin - TriplyDB

Structures of parasitic CDPK domains point to a common mechanism of activation

Structures of parasitic CDPK domains point to a common mechanism of activation

http://www.wikidata.org/entity/Q27666632

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Calcium-dependent protein kinases: hubs in plant stress signaling and development Calcium and reactive oxygen species rule the waves of signaling The Cryptosporidium parvum Kinome Development of potent and selective Plasmodium falciparum calcium-dependent protein kinase 4 (PfCDPK4) inhibitors that block the transmission of malaria to mosquitoes Structure of the STRA6 receptor for retinol uptake A forward genetic screen reveals that calcium-dependent protein kinase 3 regulates egress in Toxoplasma Fast and accurate resonance assignment of small-to-large proteins by combining automated and manual approaches.Impact of Ca(2+) on structure of soybean CDPKβ and accessibility of the Tyr-24 autophosphorylation site The Toxoplasma gondii calcium-dependent protein kinase 7 is involved in early steps of parasite division and is crucial for parasite survival.Structural and evolutionary divergence of eukaryotic protein kinases in Apicomplexa.Optimizing small molecule inhibitors of calcium-dependent protein kinase 1 to prevent infection by Toxoplasma gondii Calcium-dependent protein kinases from Arabidopsis show substrate specificity differences in an analysis of 103 substrates Novel insights into the regulation of malarial calcium-dependent protein kinase 1 Toxoplasma and Plasmodium protein kinases: roles in invasion and host cell remodelling.Calmodulin-like proteins localized to the conoid regulate motility and cell invasion by Toxoplasma gondii Analysis of Noncanonical Calcium-Dependent Protein Kinases in Toxoplasma gondii by Targeted Gene Deletion Using CRISPR/Cas9.Autophosphorylation-based Calcium (Ca2+) Sensitivity Priming and Ca2+/Calmodulin Inhibition of Arabidopsis thaliana Ca2+-dependent Protein Kinase 28 (CPK28).Plasmodium kinases as targets for new-generation antimalarials.From crystal to compound: structure-based antimalarial drug discovery.Inhibition of Calcium-Dependent Protein Kinase 1 (CDPK1) In Vitro by Pyrazolopyrimidine Derivatives Does Not Correlate with Sensitivity of Cryptosporidium parvum Growth in Cell Culture.Functions of Calcium-Dependent Protein Kinases in Plant Innate Immunity.CDPKs of Cryptosporidium parvum--stage-specific expression in vitro.Genome-wide identification, classification, and expression analysis of CDPK and its closely related gene families in poplar (Populus trichocarpa).Biophysical characterization of the calmodulin-like domain of Plasmodium falciparum calcium dependent protein kinase 3.Phosphorylation-independent binding of 14-3-3 to NtCDPK1 by a new mode.Calcium/Calmodulin-dependent protein kinase is negatively and positively regulated by calcium, providing a mechanism for decoding calcium responses during symbiosis signaling.Calcium-dependent protein kinases in plants: evolution, expression and function.Revisiting paradigms of Ca2+ signaling protein kinase regulation in plants.An Overview of Signaling Regulons During Cold Stress Tolerance in Plants.Advances and current challenges in calcium signaling.Autophosphorylation Affects Substrate-Binding Affinity of Tobacco Ca2+-Dependent Protein Kinase1.Scaffold Function of Ca2+-Dependent Protein Kinase: Tobacco Ca2+-DEPENDENT PROTEIN KINASE1 Transfers 14-3-3 to the Substrate REPRESSION OF SHOOT GROWTH after Phosphorylation.Toxoplasma calcium-dependent protein kinase 1 inhibitors: probing activity and resistance using cellular thermal shift assays.Autophosphorylation of Ser-6 via an intermolecular mechanism is important for the rapid reduction of NtCDPK1 kinase activity for substrate RSG.ZmCPK1, a calcium-independent kinase member of the Zea mays CDPK gene family, functions as a negative regulator in cold stress signalling.Plasmodial Kinase Inhibitors: License to Cure?

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P2860

Structures of parasitic CDPK domains point to a common mechanism of activation

http://www.wikidata.org/entity/Q27666632

description

2011 nî lūn-bûn

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2011 թուականի Մարտին հրատարակուած գիտական յօդուած

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2011 թվականի մարտին հրատարակված գիտական հոդված

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2011年の論文

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2011年論文

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2011年論文

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2011年論文

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2011年論文

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2011年論文

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2011年论文

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name

Structures of parasitic CDPK domains point to a common mechanism of activation

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Structures of parasitic CDPK domains point to a common mechanism of activation

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Structures of parasitic CDPK domains point to a common mechanism of activation

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Structures of parasitic CDPK domains point to a common mechanism of activation

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Structures of parasitic CDPK domains point to a common mechanism of activation

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Structures of parasitic CDPK domains point to a common mechanism of activation

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Structures of parasitic CDPK domains point to a common mechanism of activation

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Structures of parasitic CDPK domains point to a common mechanism of activation

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Structures of parasitic CDPK domains point to a common mechanism of activation

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Amy K Wernimont

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

Ashley Hutchinson

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

Jennifer D Artz

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

Jocelyn Lew

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

Juan C Pizarro

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

Merhnaz Amani

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

Raymond Hui

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

Wei Qiu

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Yu-Hui Lin

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

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803-20

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scholarly article

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10.1002/PROT.22919

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3

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79

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2011-03-01T00:00:00Z

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21287613

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