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1 r Arg90Cit and Glu52Ala mutants, and the 1F7 catalytic antibody.
2 Cope rearrangement compared to the germ line catalytic antibody.
3 tes in conjunction with a unique broad-scope catalytic antibody.
4 state stabilization in the evolution of this catalytic antibody.
5 r effect on reactions promoted by engineered catalytic antibodies.
6 erate the germline and affinity-matured AZ28 catalytic antibodies.
7 splay to generate a panel of closely related catalytic antibodies.
8 low the procurement of a wide range of novel catalytic antibodies.
11 antigen binding loops from a murine-derived catalytic antibody, 17E8, onto a human antibody framewor
12 steroids to antibody DB3 and of a hapten to catalytic antibody 1E9 are computed and compared to expe
13 ight into the evolution of the redox active, catalytic antibody 28B4, the germline genes used by the
14 graphic structure of the Fab fragment of the catalytic antibody, 29G11, complexed with an (S)-norleuc
15 ivities (% ee) derived from an enamine-based catalytic antibody 33F12 and a chiral organocatalyst.
16 Furthermore, this is the first example of catalytic antibody 38C2 displaying regioselectivity on a
19 tivation using the prohormone insulin(D) and catalytic antibody 38C2 with potential therapeutic appli
22 to the substrate (the compound on which the catalytic antibody acts) lead to dramatic differences in
23 Here we demonstrate a novel CocH form, a catalytic antibody analog, which is a fragment crystalli
25 fficiency of natural enzymes evolve, but the catalytic antibodies are much more accepting of a wide r
28 tic receptor fulfils a role reminiscent of a catalytic antibody by stabilizing the planar transition
32 assical immunization methods do not generate catalytic antibodies (catabodies), but recent findings s
35 inogen activator inhibitor, addition of anti-catalytic antibodies directed against urokinase plasmino
36 of four related Fab fragments of a family of catalytic antibodies displaying differential levels of e
38 by antibodies 13G5 and 4D5 as well as other catalytic antibodies elicited in the same immunizations
41 s indicate the power of initial selection of catalytic antibodies from a biased antibody library in b
53 t catalysts for related reactions, including catalytic antibodies (kcat/kuncat=10(6) to 10(8)) and an
55 To provide a new approach, the high-activity catalytic antibody mAb 15A10 was elicited using a transi
56 aine hydrolysis catalyzed by an anti-cocaine catalytic antibody, mAb15A10, were studied by using a no
61 cellular fibrinogen-binding protein (Efb) by catalytic antibodies produced with no exposure to the ba
62 erent from that induced by the antibody; the catalytic antibody produces a distortion which is simila
63 and structural data are consistent with the catalytic antibody providing oxyanion stabilization as i
64 cloning and kinetic analysis of a family of catalytic antibodies raised against a common transition
67 n as one of the few systems where the mature catalytic antibody shows a negative correlation between
68 une system and reveals that the evolution of catalytic antibodies significantly predates their ration
69 putative site was found in 14 of 63 (22.2%) catalytic antibody structures and 119 of 1602 (7.4%) ant
70 these structures are the highest resolution catalytic antibody structures to date and provide insigh
71 within the hydrophobic environments of this catalytic antibody than speculated for natural aldolase
73 n criteria of the immune system are changed, catalytic antibodies that have the efficiency of natural
76 body 38C2 is the prototype of a new class of catalytic antibodies that were generated by reactive imm
77 the key lessons learned from the science of catalytic antibodies--that binding energy can be convert
79 arginally higher active site burial than non-catalytic antibodies, these values are generally smaller
80 defense function for constitutively produced catalytic antibodies to a putative superantigenic site o
82 s can be readily used to optimize binding of catalytic antibodies to transition-state analogs, and wh
85 ese prodrugs are selectively unmasked by the catalytic antibody when it is applied at therapeutically
86 nues for the improvement of first generation catalytic antibodies with chorismate mutase activity.
88 rationally designed cocaine antagonist and a catalytic antibody with potential for medicinal use.
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