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Characterization of Lys-698-to-Met substitution in human plasminogen catalytic domain.
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Characterization of Lys-698-to-Met substitution in human plasminogen catalytic domain.
Characterization of Lys-698-to-Met substitution in human plasminogen catalytic domain. Proteins. 2004 Aug 01; 56(2):277-84.
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PubMed
subject areas
Amino Acid Substitution
Amino Acid Substitution
Binding Sites
Binding Sites
Catalysis
Catalysis
Chromogenic Compounds
Chromogenic Compounds
Crystallography, X-Ray
Crystallography, X-Ray
Enzyme Activation
Enzyme Activation
Humans
Humans
Lysine
Lysine
Macromolecular Substances
Macromolecular Substances
Methionine
Methionine
Models, Molecular
Models, Molecular
Molecular Sequence Data
Molecular Sequence Data
Mutation, Missense
Mutation, Missense
Plasminogen
Plasminogen
Pliability
Pliability
Protein Binding
Protein Binding
Protein Conformation
Protein Conformation
Protein Folding
Protein Folding
Protein Interaction Mapping
Protein Interaction Mapping
Protein Structure, Tertiary
Protein Structure, Tertiary
Recombinant Fusion Proteins
Recombinant Fusion Proteins
Streptokinase
Streptokinase
Structure-Activity Relationship
Structure-Activity Relationship
Surface Plasmon Resonance
Surface Plasmon Resonance
authors with profiles
Karla K Rodgers