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NPI-0052 inhibits proteasome actinhibits covalently modifying the active site threonine residues of the 20S proteasome (Corey activity1999).
Wang, M., Rada, C. & Neuberger, M. S. Altering the spectrum of immunoglobulin V gene somatic hypermutation by modifying the active site of AID.
The V67L mutation is proposed to activate splicing by reducing the ensemble distribution of the intein structure and by modifying the active sites.
High energy mechanical milling (HEMM) was found to effectively improve the reversible capacity associated with the electrochemical kinetics by modifying the active hosts' morphology characteristics.
The edge functionalization by –H, –F, –OH, –NH2, and –COOH groups could significantly alter gas permeability by modifying the active surface area of the pore and tuning attractive and/or repulsive interaction with molecules at the entrance of channel.
The post annealing process was employed for modifying the active layer and PEDOT PSS, which was at 140°C for 5 min and at 130°C for 20 min, respectively.
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The co-crystal structure reveals that the inhibitor binds in the active-site cleft, irreversibly modifying the active-site cysteine; however, the catalytic histidine is still misaligned as seen in the native structure, suggesting that the inhibitor binds to an inactive form of the enzyme.
On the basis of these analyses, we propose that the ancestral RNase-encoding gene adopted its new metabolic role in the context of L-ascorbate metabolism by grafting both N and C-terminal motifs onto the RNase scaffold while extensively modifying the active-site loops responsible for binding the metal and substrate(s) and exerting the catalytic function(s).
Assuming that any of the newly discovered pathways are used at a frequency that is at least 10-fold lower than for the common pathways to WS, it is possible to estimate that only one in one thousand activating mutations would directly modify the active site.
Here, we designed fluorophore or biotin-coupled activity based-probes (ABP) that covalently modify the active center of MALT1.
The most effective TG2 inhibitors to date are small-molecule peptidomimetics featuring electrophilic warheads that irreversibly modify the active site catalytic cysteine (CYS277).
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