نتایج جستجو برای: substrate inhibition

تعداد نتایج: 456722  

Journal: :The Journal of biological chemistry 1986
P F Weller E J Corey K F Austen R A Lewis

Arylsulfatase B, purified to homogeneity from human eosinophils, is a tetrameric enzyme whose activity varied in accordance with the state of association of its monomeric subunits. The rate of dissociation of oligomeric forms was slow relative to the rate of the enzymatic reaction so that the kinetic properties of the enzyme depended on the concentration of the enzyme before assay. For concentr...

Journal: :Cell biology international 2003
K Koumanov A Momchilova C Wolf

Melittin and phospholipase A2-activating protein (PLAP) are known as efficient activators of secretory phospholipase A2(sPLA2) types I, II, and III when phospholipid liposomes are used as substrate. The present study demonstrates that both peptides can either inhibit or activate sPLA2 depending on the peptide/phospholipid ratio when erythrocyte membranes serve as a biologically relevant substra...

Journal: :Cell 2001
Stefan J. Riedl Martin Renatus Robert Schwarzenbacher Qiao Zhou Chaohong Sun Stephen W. Fesik Robert C. Liddington Guy S. Salvesen

The molecular mechanism(s) that regulate apoptosis by caspase inhibition remain poorly understood. The main endogenous inhibitors are members of the IAP family and are exemplified by XIAP, which regulates the initiator caspase-9, and the executioner caspases-3 and -7. We report the crystal structure of the second BIR domain of XIAP (BIR2) in complex with caspase-3, at a resolution of 2.7 A, rev...

Journal: :Journal of Pharmacology and Experimental Therapeutics 2013

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