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1 rmed cleft using a convex binding interface (paratope).
2 only A2 contributes to the canonical Hib PS paratope.
3 ill" and VH "valley" shape of the grooved E8 paratope.
4 een this peptide and the monoclonal antibody paratope.
5 bclasses and IgA, consistent with an altered paratope.
6 icity with conformational versatility of the paratope.
7 sequence information on the location of the paratope.
8 nce-based information on the location of the paratope.
9 d in order to map the structural epitope and paratope.
10 al of 16 amino acid residues in the antibody paratope.
11 seven amino acids form part of the CAT-2200 paratope.
12 ed the affinity limit achievable with a flat paratope.
13 dues suggested that this is not an optimized paratope.
14 ties via their unusually long, convex-shaped paratopes.
15 es, mimicking the energetic core of antibody paratopes.
16 he minor portion of the predicted functional paratopes.
17 opes whose cognate mAbs have electropositive paratopes.
18 t a source for human antibodies with genuine paratopes.
19 nt in combination with other nonneutralizing paratopes.
20 m pneumococcal capsular PS (PPS) 6B-specific paratopes.
24 nt of SCV therapeutics based on the antibody paratope and epitope, and a retrovaccinology approach fo
25 remarkable feature revealed lies within the paratope and is a novel six-amino-acid alpha-helix that
26 Surprisingly, Tyr still dominates the YSX paratope and the additional amino acid types are primari
27 he antibody molecules reducing the hiding of paratopes, and (ii) maintained the activity of the captu
29 ith orientation control for site-positioning paratopes (antigen binding site) of the antibody molecul
31 on average, complete structural epitopes and paratopes are equal in size to each other and similar in
33 site thus comprises antibodies with distinct paratopes arrayed about two optimal geometric orientatio
34 The peptide structures differed, and the two paratopes attained discrete conformations, leading to di
36 ucture at 3.2 A resolution reveals a contact paratope composed almost entirely of tryptophan and seri
37 studies, the findings indicate that a hybrid paratope consisting of quinine and reconfigured antibody
38 , VH-V1a recognizes VEGF by using an unusual paratope consisting predominantly of CDR3 but with signi
41 nd use a combination of structural analysis, paratope dissection, and neutralization assessment to de
43 density comparisons were used to analyze the paratope-epitope interface and demonstrated that the ant
45 e polar atomistic contacts in the structural paratope-epitope interfaces; more that 80% these polar c
47 lonal within the individual, with one or two paratope families accounting for the majority of express
50 othesize that the hydrophobic surface of the paratope functions as a "trap" for the viral sequences,
52 LIPH (grouping of lymphocyte interactions by paratope hotspots) to cluster TCRs with a high probabili
53 quence protected from proteolysis by the 2F5 paratope; (ii) downstream residues postulated to establi
55 the size of a complete structural epitope or paratope, inclusive of CR and the minimum set of support
56 s could be used as specific non-covalent and paratope-independent handles in targeted drug delivery,
57 ntarity-determining regions that are driving paratope interactions; the variable light complementarit
59 nesis experiments reveal that the functional paratope is dominated by Tyr, which represents 11 of the
60 contact between the B2.1 peptide and the b12 paratope is unlikely to mimic the discontinuous key bind
61 finity is engineered outside of the antibody paratope, it can complement affinity maturation strategi
64 ; (iii) antigen selection increased antibody paratope net charge and solvent-accessible surface area;
68 an and tyrosine residues highly populate the paratope of the antibody but not the epitope of the anti
70 ction-linked (PL) biopanning," probes the Ab paratopes of protected vaccinees versus those with vacci
71 variability of antigenic epitopes, where the paratope on the antibody binds specifically to a given e
72 employed thiophene-3-boronic acid (T3BA) as paratope orientation controller, (i) enabled site orient
77 structurally important positions within the paratope region and (b) tailored amino acid composition
78 Structurally important positions within the paratope region were identified through stability, struc
80 sity to the light chain, by diversifying non-paratope residues that may influence CDR conformations,
82 ing potential developability issues; predict paratope residues; and predict epitope patches on protei
83 led molecular comparison of an anti-idiotype paratope specific for a human antibody with its analogou
84 traints on the variable (V) region to affect paratope structure in a V region identical IgG(1), IgG(2
85 omparable to those of mammalian TCR in basic paratope structure; additionally, nurse shark TCRdelta C
88 yranosonic acid), displays a germ-line-coded paratope that differs significantly from previously char
90 ey are significantly less common among those paratopes that bind to the immunodominant amino-terminal
92 odify the V region structure to alter the Ab paratope, thus providing an explanation for how isotype
94 y crystallography has shown that an antibody paratope typically binds 15-22 amino acids (aa) of an ep
96 the parent 10E8 was the most soluble, with a paratope we showed crystallographically to be virtually
97 structures of large protein Ag epitopes and paratopes were analyzed to inform the process of eliciti
100 ecifically to a distinct conformation of the paratope, which was also different from that of the Ag-f
101 hich conformational convergence of different paratopes while binding to a common epitope in a similar
102 novel approach to the problem by probing the paratope with (15)N label peptide mimetics followed by N
103 nal residues located at the periphery of the paratope with a concomitant loss of the so-called "O-rin
104 t a limited repertoire of antibodies bearing paratopes with diverse structural contours enriched with
106 methods were used to predict the functional paratopes with the 3D antibody variable domain structure
107 hain V region gene products to form specific paratopes, with no apparent tendency for conservation of
108 e the major part of the predicted functional paratopes, with short-chain hydrophilic residues forming
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