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Detailed structural characterization of unbound protein phosphatase 1 inhibitors.

Detailed structural characterization of unbound protein phosphatase 1 inhibitors.

http://www.wikidata.org/entity/Q37105049

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Spinophilin directs protein phosphatase 1 specificity by blocking substrate binding sites Structure and function of the two tandem WW domains of the pre-mRNA splicing factor FBP21 (formin-binding protein 21)The Molecular Basis for Substrate Specificity of the Nuclear NIPP1:PP1 Holoenzyme Understanding the antagonism of retinoblastoma protein dephosphorylation by PNUTS provides insights into the PP1 regulatory code Plasmodium falciparum inhibitor-3 homolog increases protein phosphatase type 1 activity and is essential for parasitic survival Dendritic geometry shapes neuronal cAMP signalling to the nucleus NMR studies of the C-terminus of alpha4 reveal possible mechanism of its interaction with MID1 and protein phosphatase 2A Ensemble modeling of protein disordered states: experimental restraint contributions and validation.Identification of a Plasmodium falciparum inhibitor-2 motif involved in the binding and regulation activity of protein phosphatase type 1 Molecular basis for an ancient partnership between prolyl isomerase Pin1 and phosphatase inhibitor-2 Structural diversity in free and bound states of intrinsically disordered protein phosphatase 1 regulators.Flexibility in the PP1:spinophilin holoenzyme Molecular investigations of the structure and function of the protein phosphatase 1-spinophilin-inhibitor 2 heterotrimeric complex Anchoring intrinsically disordered proteins to multiple targets: lessons from N-terminus of the p53 protein.The extended PP1 toolkit: designed to create specificity.Beyond the dopamine receptor: regulation and roles of serine/threonine protein phosphatases.DARPP-32, Jack of All Trades… Master of Which?Structural basis for protein phosphatase 1 regulation and specificity Folding of Intrinsically Disordered Protein Phosphatase 1 Regulatory Proteins.DARPP-32 interaction with adducin may mediate rapid environmental effects on striatal neurons Regulation of protein phosphatase 1 by intrinsically disordered proteins Biophysical characterization of intrinsically disordered proteins.Strategies to optimize protein expression in E. coli.Novel strategies for drug discovery based on Intrinsically Disordered Proteins (IDPs)Reciprocal regulation of ARPP-16 by PKA and MAST3 kinases provides a cAMP-regulated switch in protein phosphatase 2A inhibition.The evolutionary strata of DARPP-32 tail implicates hierarchical functional expansion in higher vertebrates.Strategies to make protein serine/threonine (PP1, calcineurin) and tyrosine phosphatases (PTP1B) druggable: achieving specificity by targeting substrate and regulatory protein interaction sites.t-Darpp is an elongated monomer that binds calcium and is phosphorylated by cyclin-dependent kinases 1 and 5.Structural signature of the MYPT1-PP1 interaction.Structured States of Disordered Proteins from Genomic Sequences Development of phosphatase inhibitor-1 peptides acting as indirect activators of phosphatase 1.Development of a colorimetric and a fluorescence phosphatase-inhibitor assay suitable for drug discovery approaches.

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Detailed structural characterization of unbound protein phosphatase 1 inhibitors.

http://www.wikidata.org/entity/Q37105049

description

2008 nî lūn-bûn

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2008年の論文

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2008年学术文章

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2008年学术文章

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2008年学术文章

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2008年学术文章

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2008年学术文章

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2008年學術文章

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2008年學術文章

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2008年學術文章

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name

Detailed structural characterization of unbound protein phosphatase 1 inhibitors.

@en

Detailed structural characterization of unbound protein phosphatase 1 inhibitors.

@nl

type

label

Detailed structural characterization of unbound protein phosphatase 1 inhibitors.

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Detailed structural characterization of unbound protein phosphatase 1 inhibitors.

@nl

prefLabel

Detailed structural characterization of unbound protein phosphatase 1 inhibitors.

@en

Detailed structural characterization of unbound protein phosphatase 1 inhibitors.

@nl

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Detailed structural characterization of unbound protein phosphatase 1 inhibitors.

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Barbara Dancheck

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

Wolfgang Peti

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P2860

Intrinsically unstructured proteins and their functions

Interaction of inhibitor-2 with the catalytic subunit of type 1 protein phosphatase. Identification of a sequence analogous to the consensus type 1 protein phosphatase-binding motif

Regulation of type 1 protein phosphatase/inhibitor-2 complex by glycogen synthase kinase-3beta in intact cells

Structural basis for the recognition of regulatory subunits by the catalytic subunit of protein phosphatase 1

Phosphorylation-induced conformational switching of CPI-17 produces a potent myosin phosphatase inhibitor

Probability-based protein secondary structure identification using combined NMR chemical-shift data

Characterization of the interaction between DARPP-32 and protein phosphatase 1 (PP-1): DARPP-32 peptides antagonize the interaction of PP-1 with binding proteins

Crystal structure of the tumor-promoter okadaic acid bound to protein phosphatase-1

Solution NMR structure of the myosin phosphatase inhibitor protein CPI-17 shows phosphorylation-induced conformational changes responsible for activation

Crystal structure of the complex between calyculin A and the catalytic subunit of protein phosphatase 1

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scholarly article

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10.1021/BI801308Y

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