Domain stabilities in protein kinase R (PKR): evidence for weak interdomain interactions - Wikidata - wikimedia - TriplyDB

Domain stabilities in protein kinase R (PKR): evidence for weak interdomain interactions

Domain stabilities in protein kinase R (PKR): evidence for weak interdomain interactions

http://www.wikidata.org/entity/Q37312236

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Allosteric Activation Mechanism of the Mycobacterium tuberculosis Receptor Ser/Thr Protein Kinase, PknB Improved control of tuberculosis and activation of macrophages in mice lacking protein kinase R Heparin activates PKR by inducing dimerization.Monitoring activation of the antiviral pattern recognition receptors RIG-I and PKR by limited protease digestion and native PAGE.The Regulatory and Kinase Domains but Not the Interdomain Linker Determine Human Double-stranded RNA-activated Kinase (PKR) Sensitivity to Inhibition by Viral Non-coding RNAs Mechanism of PKR Activation by dsRNA.Analysis of PKR structure by small-angle scattering.Domain interactions in adenovirus VAI RNA mediate high-affinity PKR binding.Methods for analyzing and quantifying protein-protein interaction.Regulation of PKR by RNA: formation of active and inactive dimers.Role of the Interdomain Linker in RNA-Activated Protein Kinase Activation Analysis of monomeric and dimeric phosphorylated forms of protein kinase R.Interaction of PKR with single-stranded RNA Involvement of double-stranded RNA-dependent protein kinase and antisense viral RNA in the constitutive NFκB activation in adult T-cell leukemia/lymphoma cells.

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Domain stabilities in protein kinase R (PKR): evidence for weak interdomain interactions

http://www.wikidata.org/entity/Q37312236

description

article científic

@ca

article scientifique

@fr

articolo scientifico

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artigo científico

@pt

bilimsel makale

@tr

scientific article published on 08 April 2008

@en

vedecký článok

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vetenskaplig artikel

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videnskabelig artikel

@da

vědecký článek

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name

Domain stabilities in protein kinase R (PKR): evidence for weak interdomain interactions

@en

Domain stabilities in protein kinase R

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type

label

Domain stabilities in protein kinase R (PKR): evidence for weak interdomain interactions

@en

Domain stabilities in protein kinase R

@nl

prefLabel

Domain stabilities in protein kinase R (PKR): evidence for weak interdomain interactions

@en

Domain stabilities in protein kinase R

@nl

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Domain stabilities in protein kinase R (PKR): evidence for weak interdomain interactions

@en

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Eric Anderson

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

James L Cole

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

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Size-Distribution Analysis of Macromolecules by Sedimentation Velocity Ultracentrifugation and Lamm Equation Modeling

The conformational plasticity of protein kinases

Translation inhibition in apoptosis: caspase-dependent PKR activation and eIF2-alpha phosphorylation

The dsRNA protein kinase PKR: virus and cell control

Gene-specific regulation by general translation factors

On the analysis of protein self-association by sedimentation velocity analytical ultracentrifugation

Denaturant m values and heat capacity changes: relation to changes in accessible surface areas of protein unfolding

Regulation of protein kinases; controlling activity through activation segment conformation

The progressive development of structure and stability during the equilibrium folding of the alpha subunit of tryptophan synthase from Escherichia coli.

Folding mechanism of the alpha-subunit of tryptophan synthase, an alpha/beta barrel protein: global analysis highlights the interconversion of multiple native, intermediate, and unfolded forms through parallel channels.

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4887-4897

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scholarly article

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10.1021/BI702211J

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17

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47

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2008-04-08T00:00:00Z

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5458252

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18393532

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2729556

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