Her4 and Her2/neu tyrosine kinase domains dimerize and activate in a reconstituted in vitro system.
Monsey, John
Her4 and Her2/neu tyrosine kinase domains dimerize and activate in a reconstituted in vitro system. [electronic resource] - The Journal of biological chemistry Mar 2010 - 7035-44 p. digital
Publication Type: Journal Article; Research Support, N.I.H., Extramural
1083-351X
10.1074/jbc.M109.096032 doi
Amino Acid Sequence
Animals
Cations, Divalent--metabolism
Cell Line
Cell-Free System
Enzyme Activation
ErbB Receptors--chemistry
Humans
Liposomes--chemistry
Models, Molecular
Molecular Sequence Data
Mutation
Nickel--chemistry
Protein Multimerization
Protein Structure, Quaternary
Protein Structure, Tertiary
Receptor, ErbB-2--chemistry
Receptor, ErbB-3--genetics
Receptor, ErbB-4
Sequence Alignment
Her4 and Her2/neu tyrosine kinase domains dimerize and activate in a reconstituted in vitro system. [electronic resource] - The Journal of biological chemistry Mar 2010 - 7035-44 p. digital
Publication Type: Journal Article; Research Support, N.I.H., Extramural
1083-351X
10.1074/jbc.M109.096032 doi
Amino Acid Sequence
Animals
Cations, Divalent--metabolism
Cell Line
Cell-Free System
Enzyme Activation
ErbB Receptors--chemistry
Humans
Liposomes--chemistry
Models, Molecular
Molecular Sequence Data
Mutation
Nickel--chemistry
Protein Multimerization
Protein Structure, Quaternary
Protein Structure, Tertiary
Receptor, ErbB-2--chemistry
Receptor, ErbB-3--genetics
Receptor, ErbB-4
Sequence Alignment