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Oligomerization-induced modulation of TPR-MET tyrosine kinase activity
John L. Hays,
Stanley J. Watowich
Biochemistry & Molecular Biology
Research output
:
Contribution to journal
›
Article
›
peer-review
22
Scopus citations
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Dive into the research topics of 'Oligomerization-induced modulation of TPR-MET tyrosine kinase activity'. Together they form a unique fingerprint.
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Keyphrases
Receptor Tyrosine Kinase
100%
Oligomerization
100%
Tyrosine Kinase Activity
100%
Peptide Substrate
50%
Phosphorylation
33%
Conformational Change
33%
C-Met
33%
Cytoplasmic Domain
33%
Oncoprotein
33%
Enzymatic Analysis
33%
Regulatory Mechanism
16%
Recombinant
16%
Kinase Activation
16%
Kinetic Properties
16%
Catalytic Efficiency
16%
Enzymatic Activity
16%
Dissociation Constant
16%
Coiled-coil Motif
16%
Km Value
16%
Mechanistic Model
16%
Kinetic Changes
16%
Substrate Binding
16%
Kcat
16%
Structure-based Design
16%
Nuclear Pore Complex
16%
Activation Loop
16%
Binding Efficiency
16%
ATP-competitive Inhibitors
16%
Receptor Tyrosine Kinase Inhibitor
16%
Receptor Heteromers
16%
Biochemistry, Genetics and Molecular Biology
Receptor Tyrosine Kinase
100%
Oligomerization
100%
Tyrosine Kinase
100%
Adenosine Triphosphate
71%
Conformational Change
28%
Enzyme
14%
Protein Kinase C
14%
Catalytic Efficiency
14%
Enzyme Activity
14%
Coiled Coil
14%
Competitive Inhibition
14%
Dissociation Constant
14%
Turnover Number
14%
Nuclear Pore Complex
14%
Enzyme Phosphorylation
14%
Receptor Tyrosine Kinase Inhibitors
14%