Intrinsically disordered PEP-19 confers unique dynamic properties to apo and calcium calmodulin. - Wikidata - wikimedia - TriplyDB

Intrinsically disordered PEP-19 confers unique dynamic properties to apo and calcium calmodulin.

Intrinsically disordered PEP-19 confers unique dynamic properties to apo and calcium calmodulin.

http://www.wikidata.org/entity/Q41141015

about

Crystal Structure of Calmodulin Binding Domain of Orai1 in Complex with Ca2+*Calmodulin Displays a Unique Binding Mode Neurogranin alters the structure and calcium binding properties of calmodulin.The calmodulin regulator protein, PEP-19, sensitizes ATP-induced Ca2+ release Relative Cosolute Size Influences the Kinetics of Protein-Protein Interactions.PEP-19 modulates calcium binding to calmodulin by electrostatic steering.Designing proteins to combat disease: Cardiac troponin C as an example.Network representation of protein interactions-Experimental results.Network representation of protein interactions: Theory of graph description and analysis.Specific 12CβD(2)12CγD(2)S13CεHD(2) isotopomer labeling of methionine to characterize protein dynamics by 1H and 13C NMR relaxation dispersion.Interaction of calmodulin with L-selectin at the membrane interface: implication on the regulation of L-selectin shedding.Tat peptide-calmodulin binding studies and bioinformatics of HIV-1 protein-calmodulin interactions.

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P2860

Intrinsically disordered PEP-19 confers unique dynamic properties to apo and calcium calmodulin.

http://www.wikidata.org/entity/Q41141015

description

2010 nî lūn-bûn

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2010年の論文

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2010年論文

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2010年論文

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2010年論文

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2010年論文

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2010年論文

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2010年论文

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2010年论文

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2010年论文

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name

Intrinsically disordered PEP-1 ...... to apo and calcium calmodulin.

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type

label

Intrinsically disordered PEP-1 ...... to apo and calcium calmodulin.

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prefLabel

Intrinsically disordered PEP-1 ...... to apo and calcium calmodulin.

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Intrinsically disordered PEP-1 ...... to apo and calcium calmodulin

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John A Putkey

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

Liang-wen Xiong

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Quinn K Kleerekoper

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P2860

The EF-hand domain: a globally cooperative structural unit

PEP-19, an intrinsically disordered regulator of calmodulin signaling

Structure, dynamics, and thermodynamics of the structural domain of troponin C in complex with the regulatory peptide 1-40 of troponin I

Calcium-induced conformational transition revealed by the solution structure of apo calmodulin

Backbone dynamics of a free and phosphopeptide-complexed Src homology 2 domain studied by 15N NMR relaxation

1H, 13C and 15N chemical shift referencing in biomolecular NMR

Systematic variation in gene expression patterns in human cancer cell lines

A new role for IQ motif proteins in regulating calmodulin function

Purification and characterization of a brain-specific protein kinase C substrate, neurogranin (p17). Identification of a consensus amino acid sequence between neurogranin and neuromodulin (GAP43) that corresponds to the protein kinase C phosphorylat

Crystal structures of the helix-loop-helix calcium-binding proteins

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10287-10297

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scholarly article

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10.1021/BI100500M

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48

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20973509

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