Site-directed mutagenesis of amino acid residues of protein phosphatase 1 involved in catalysis and inhibitor binding.
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Phosphorylation of protein phosphatase inhibitor-1 by Cdk5Characterization of the interaction between DARPP-32 and protein phosphatase 1 (PP-1): DARPP-32 peptides antagonize the interaction of PP-1 with binding proteinsAn ultrasensitive Ca2+/calmodulin-dependent protein kinase II-protein phosphatase 1 switch facilitates specificity in postsynaptic calcium signalingCrystal structure of the tumor-promoter okadaic acid bound to protein phosphatase-1The nuclease activity of Mre11 is required for meiosis but not for mating type switching, end joining, or telomere maintenance.Amplification of dopaminergic signaling by a positive feedback loopVps29 has a phosphoesterase fold that acts as a protein interaction scaffold for retromer assemblyActive-site mutations impairing the catalytic function of the catalytic subunit of human protein phosphatase 2A permit baculovirus-mediated overexpression in insect cellsHypersensitive to red and blue 1 and its modification by protein phosphatase 7 are implicated in the control of Arabidopsis stomatal aperturePR65, the HEAT-repeat scaffold of phosphatase PP2A, is an elastic connector that links force and catalysisKNL1/Spc105 recruits PP1 to silence the spindle assembly checkpointCatalytically inactive protein phosphatase 2A can bind to polyomavirus middle tumor antigen and support complex formation with pp60(c-src).Role of protein phosphatases in the regulation of human mast cell and basophil function.Protein phosphatase 1 regulation by inhibitors and targeting subunitsThe rate of hydrolysis of phosphomonoester dianions and the exceptional catalytic proficiencies of protein and inositol phosphatasesBeyond the dopamine receptor: regulation and roles of serine/threonine protein phosphatases.Mechanistic study of protein phosphatase-1 (PP1), a catalytically promiscuous enzymeThe phosphoprotein phosphatase family of Ser/Thr phosphatases as principal targets of naturally occurring toxins.Structure-based thermodynamic analysis of the dissociation of protein phosphatase-1 catalytic subunit and microcystin-LR docked complexes.Effects of modification of the hydrophobic C-1-C-16 segment of tautomycin on its affinity to type-1 and type-2A protein phosphatases.Important role for phylogenetically invariant PP2Acalpha active site and C-terminal residues revealed by mutational analysis in Saccharomyces cerevisiaeCharacterization of the interactions between inhibitor-1 and recombinant PP1 by NMR spectroscopy.Decoding the selectivity of eIF2α holophosphatases and PPP1R15A inhibitors.Purple acid phosphatases of Arabidopsis thaliana. Comparative analysis and differential regulation by phosphate deprivation.Fostriecin, an antitumor antibiotic with inhibitory activity against serine/threonine protein phosphatases types 1 (PP1) and 2A (PP2A), is highly selective for PP2A.Characterization of the inhibition of protein phosphatase-1 by DARPP-32 and inhibitor-2.Inhibitor-1 interaction domain that mediates the inhibition of protein phosphatase-1.Measuring NDC80 binding reveals the molecular basis of tension-dependent kinetochore-microtubule attachments
P2860
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P2860
Site-directed mutagenesis of amino acid residues of protein phosphatase 1 involved in catalysis and inhibitor binding.
description
1997 nî lūn-bûn
@nan
1997年の論文
@ja
1997年論文
@yue
1997年論文
@zh-hant
1997年論文
@zh-hk
1997年論文
@zh-mo
1997年論文
@zh-tw
1997年论文
@wuu
1997年论文
@zh
1997年论文
@zh-cn
name
Site-directed mutagenesis of a ...... talysis and inhibitor binding.
@ast
Site-directed mutagenesis of a ...... talysis and inhibitor binding.
@en
type
label
Site-directed mutagenesis of a ...... talysis and inhibitor binding.
@ast
Site-directed mutagenesis of a ...... talysis and inhibitor binding.
@en
prefLabel
Site-directed mutagenesis of a ...... talysis and inhibitor binding.
@ast
Site-directed mutagenesis of a ...... talysis and inhibitor binding.
@en
P2093
P2860
P356
P1476
Site-directed mutagenesis of a ...... talysis and inhibitor binding.
@en
P2093
P2860
P304
P356
10.1073/PNAS.94.8.3530
P407
P577
1997-04-01T00:00:00Z