Monobromobimane occupies a distinct xenobiotic substrate site in glutathione S-transferase pi.
about
GST pi modulates JNK activity through a direct interaction with JNK substrate, ATF2.Catalytically active monomer of glutathione S-transferase pi and key residues involved in the electrostatic interaction between subunits.Delineation of xenobiotic substrate sites in rat glutathione S-transferase M1-1.Glutathione S-transferase Pi has at least three distinguishable xenobiotic substrate sites close to its glutathione-binding site.A conserved N-capping motif contributes significantly to the stabilization and dynamics of the C-terminal region of class Alpha glutathione S-transferases.
P2860
Monobromobimane occupies a distinct xenobiotic substrate site in glutathione S-transferase pi.
description
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2003年の論文
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name
Monobromobimane occupies a dis ...... glutathione S-transferase pi.
@en
type
label
Monobromobimane occupies a dis ...... glutathione S-transferase pi.
@en
prefLabel
Monobromobimane occupies a dis ...... glutathione S-transferase pi.
@en
P2860
P356
P1433
P1476
Monobromobimane occupies a dis ...... glutathione S-transferase pi.
@en
P2093
Luis A Ralat
P2860
P304
P356
10.1110/PS.03249303
P577
2003-11-01T00:00:00Z