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Solution Structure of the MAPK Phosphatase PAC-1 Catalytic Domain
article published in 2003
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scholarly article
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title
Solution Structure of the MAPK Phosphatase PAC-1 Catalytic Domain
(English)
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main subject
solution structure
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author name string
Amjad Farooq
series ordinal
1
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Olga Plotnikova
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2
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Gaurav Chaturvedi
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3
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Sherry Yan
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4
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Lei Zeng
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5
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Qiang Zhang
series ordinal
6
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Ming-Ming Zhou
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7
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language of work or name
English
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publication date
February 2003
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published in
Structure
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volume
11
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issue
2
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page(s)
155-164
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cites work
Mammalian MAP kinase signalling cascades
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https://api.crossref.org/works/10.1016%2FS0969-2126%2802%2900943-7
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7 January 2021
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Signal transduction through MAP kinase cascades
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https://api.crossref.org/works/10.1016%2FS0969-2126%2802%2900943-7
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Mitogen-activated protein kinase pathways
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https://api.crossref.org/works/10.1016%2FS0969-2126%2802%2900943-7
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7 January 2021
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Identification of the regulatory phosphorylation sites in pp42/mitogen-activated protein kinase (MAP kinase)
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Protein phosphatases and the regulation of mitogen-activated protein kinase signalling.
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Dual specificity phosphatases: a gene family for control of MAP kinase function.
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Parallel signal processing among mammalian MAPKs
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Specificity of receptor tyrosine kinase signaling: transient versus sustained extracellular signal-regulated kinase activation
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Control of MAP kinase activation by the mitogen-induced threonine/tyrosine phosphatase PAC1
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https://api.crossref.org/works/10.1016%2FS0969-2126%2802%2900943-7
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MKP-3, a novel cytosolic protein-tyrosine phosphatase that exemplifies a new class of mitogen-activated protein kinase phosphatase
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7 January 2021
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The dual specificity phosphatases M3/6 and MKP-3 are highly selective for inactivation of distinct mitogen-activated protein kinases
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7 January 2021
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The mitogen-activated protein kinase phosphatase-3 N-terminal noncatalytic region is responsible for tight substrate binding and enzymatic specificity
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Catalytic Activation of the Phosphatase MKP-3 by ERK2 Mitogen-Activated Protein Kinase
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Discordance between the binding affinity of mitogen-activated protein kinase subfamily members for MAP kinase phosphatase-2 and their ability to activate the phosphatase catalytically
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Catalytic activation of mitogen-activated protein (MAP) kinase phosphatase-1 by binding to p38 MAP kinase: critical role of the p38 C-terminal domain in its negative regulation
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Distinct binding determinants for ERK2/p38alpha and JNK map kinases mediate catalytic activation and substrate selectivity of map kinase phosphatase-1
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Solution structure of ERK2 binding domain of MAPK phosphatase MKP-3: structural insights into MKP-3 activation by ERK2
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A conserved docking motif in MAP kinases common to substrates, activators and regulators
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Substrate Recognition Domains within Extracellular Signal-regulated Kinase Mediate Binding and Catalytic Activation of Mitogen-activated Protein Kinase Phosphatase-3
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Multiple regions of MAP kinase phosphatase 3 are involved in its recognition and activation by ERK2.
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Mechanistic basis for catalytic activation of mitogen-activated protein kinase phosphatase 3 by extracellular signal-regulated kinase
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The mechanism of dephosphorylation of extracellular signal-regulated kinase 2 by mitogen-activated protein kinase phosphatase 3.
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Crystal structure of the tyrosine phosphatase SHP-2
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Crystal structure of the MAPK phosphatase Pyst1 catalytic domain and implications for regulated activation
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Structural basis for phosphotyrosine peptide recognition by protein tyrosine phosphatase 1B
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Molecular basis for the dephosphorylation of the activation segment of the insulin receptor by protein tyrosine phosphatase 1B
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Heteronuclear multidimensional NMR experiments for the structure determination of proteins in solution employing pulsed field gradients
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Reconstitution of mitogen-activated protein kinase phosphorylation cascades in bacteria. Efficient synthesis of active protein kinases
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Activation mechanism of the MAP kinase ERK2 by dual phosphorylation
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10.1016/S0969-2126(02)00943-7
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