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1 rmed cleft using a convex binding interface (paratope).
2 specific lipid binding sites of the antibody paratope.
3 ed the affinity limit achievable with a flat paratope.
4 dues suggested that this is not an optimized paratope.
5 only A2 contributes to the canonical Hib PS paratope.
6 ill" and VH "valley" shape of the grooved E8 paratope.
7 een this peptide and the monoclonal antibody paratope.
8 dated by structurally-similar changes in the paratope.
9 bclasses and IgA, consistent with an altered paratope.
10 icity with conformational versatility of the paratope.
11 sequence information on the location of the paratope.
12 nce-based information on the location of the paratope.
13 d in order to map the structural epitope and paratope.
14 al of 16 amino acid residues in the antibody paratope.
15 seven amino acids form part of the CAT-2200 paratope.
16 m pneumococcal capsular PS (PPS) 6B-specific paratopes.
17 tively charged amino acid residues in bNAbs' paratopes.
18 ties via their unusually long, convex-shaped paratopes.
19 es, mimicking the energetic core of antibody paratopes.
20 he minor portion of the predicted functional paratopes.
21 opes whose cognate mAbs have electropositive paratopes.
22 t a source for human antibodies with genuine paratopes.
23 nt in combination with other nonneutralizing paratopes.
27 nt of SCV therapeutics based on the antibody paratope and epitope, and a retrovaccinology approach fo
28 idating the role of C domains in shaping the paratope and influencing specificity is a critical area
29 remarkable feature revealed lies within the paratope and is a novel six-amino-acid alpha-helix that
30 Surprisingly, Tyr still dominates the YSX paratope and the additional amino acid types are primari
31 utralizing antibodies (bnAbs) with conserved paratopes and mutations, and in some cases, the same Ig-
33 b segment reveals a well-defined polyanionic paratope, and the docking studies indicate that the poly
34 he antibody molecules reducing the hiding of paratopes, and (ii) maintained the activity of the captu
37 ith orientation control for site-positioning paratopes (antigen binding site) of the antibody molecul
39 on average, complete structural epitopes and paratopes are equal in size to each other and similar in
42 site thus comprises antibodies with distinct paratopes arrayed about two optimal geometric orientatio
44 to these three rotations positioning the Fab paratopes at a proper distance and orientation required
45 The peptide structures differed, and the two paratopes attained discrete conformations, leading to di
48 und surrogates of the intracellular antibody paratope (called antibody-derived [Abd] compounds) have
50 ucture at 3.2 A resolution reveals a contact paratope composed almost entirely of tryptophan and seri
51 studies, the findings indicate that a hybrid paratope consisting of quinine and reconfigured antibody
52 , VH-V1a recognizes VEGF by using an unusual paratope consisting predominantly of CDR3 but with signi
54 l quality attribute for biotherapeutics with paratopes containing potential cis proline amide bonds.
55 omain (d7) to the membrane, and the antibody paratope contains electrostatic surfaces compatible with
57 olding elements that physically separate the paratope-defining variable (V) region from the effector
58 nd use a combination of structural analysis, paratope dissection, and neutralization assessment to de
60 f antibody responses is inherently linked to paratope diversity, as generated through V(D)J recombina
61 simultaneously via nonoverlapping epitopes-"paratope duality." One mode involved paratope gullying,
64 density comparisons were used to analyze the paratope-epitope interface and demonstrated that the ant
67 e polar atomistic contacts in the structural paratope-epitope interfaces; more that 80% these polar c
68 data provide a mechanistic insight into the paratope-epitope relationship between an alloantibody an
69 results highlight the importance not only of paratope/epitope complementarity but also the topologica
71 tural analyses demonstrate that the improved paratope expands the FP binding groove to accommodate di
72 2, with a large reorientation of the binding paratope facilitating increases in contact surface and s
73 lonal within the individual, with one or two paratope families accounting for the majority of express
76 othesize that the hydrophobic surface of the paratope functions as a "trap" for the viral sequences,
78 itopes-"paratope duality." One mode involved paratope gullying, whereas the other involved only CDRs,
80 ng by grouping of lymphocyte interactions by paratope hotspots (GLIPH2) in a South African longitudin
82 LIPH (grouping of lymphocyte interactions by paratope hotspots) to cluster TCRs with a high probabili
84 edict mutational effects on antigen binding, paratope identification, and other key antibody properti
85 quence protected from proteolysis by the 2F5 paratope; (ii) downstream residues postulated to establi
87 the size of a complete structural epitope or paratope, inclusive of CR and the minimum set of support
88 s could be used as specific non-covalent and paratope-independent handles in targeted drug delivery,
89 of EEEV by these mAbs including the epitope-paratope interaction surface, occupancy, and kinetic dif
93 nding site structure and the presence of key paratope interactions, which can occur even when their s
95 ntarity-determining regions that are driving paratope interactions; the variable light complementarit
96 velopment we identified sites on the epitope-paratope interface that are the focus of affinity optimi
99 e have developed a method to introduce novel paratopes into the human antibody repertoire by modifyin
102 nesis experiments reveal that the functional paratope is dominated by Tyr, which represents 11 of the
103 contact between the B2.1 peptide and the b12 paratope is unlikely to mimic the discontinuous key bind
105 finity is engineered outside of the antibody paratope, it can complement affinity maturation strategi
109 ; (iii) antigen selection increased antibody paratope net charge and solvent-accessible surface area;
116 an and tyrosine residues highly populate the paratope of the antibody but not the epitope of the anti
119 e molecular binding interactions between the paratopes of antibodies and the epitopes of food allerge
120 ction-linked (PL) biopanning," probes the Ab paratopes of protected vaccinees versus those with vacci
121 variability of antigenic epitopes, where the paratope on the antibody binds specifically to a given e
122 plications such as the evolution of multiple paratopes or shelf-stable diagnostics and therapeutics.
123 employed thiophene-3-boronic acid (T3BA) as paratope orientation controller, (i) enabled site orient
127 ynamics simulations which revealed increased paratope plasticity in the scFv relative to the correspo
130 We present Paragraph, a structure-based paratope prediction tool that outperforms current state-
131 he epitope, while graph models are better in paratope prediction, both achieving significant performa
135 structurally important positions within the paratope region and (b) tailored amino acid composition
136 Structurally important positions within the paratope region were identified through stability, struc
137 d "peptide matrix," inspired by the antibody paratope region, was fabricated on a surface plasmon res
138 ing sites in the GP trimer, and separate 1C3 paratope regions interact differently with identical res
140 utagenesis to map the functional epitope and paratope residues that govern the antigen-antibody inter
141 sity to the light chain, by diversifying non-paratope residues that may influence CDR conformations,
143 ing potential developability issues; predict paratope residues; and predict epitope patches on protei
144 bodies simultaneously, and identification of paratope sequence determinants for binding recognition f
147 led molecular comparison of an anti-idiotype paratope specific for a human antibody with its analogou
148 1C3 is of particular interest because its paratope strongly binds with unique stoichiometry to the
149 ow protein topology, parental framework, and paratope structure and location all impact scaffold perf
150 traints on the variable (V) region to affect paratope structure in a V region identical IgG(1), IgG(2
151 omparable to those of mammalian TCR in basic paratope structure; additionally, nurse shark TCRdelta C
154 yranosonic acid), displays a germ-line-coded paratope that differs significantly from previously char
155 ive bnAbs can be generated by human antibody paratopes that accommodate the conserved glycan differen
157 ey are significantly less common among those paratopes that bind to the immunodominant amino-terminal
160 odify the V region structure to alter the Ab paratope, thus providing an explanation for how isotype
161 ombined with alanine scanning of epitope and paratope to predict a model of FGF23-Burosumab interacti
162 four or five diverse, structurally distinct paratopes, to elucidate their impact on evolvability and
164 y crystallography has shown that an antibody paratope typically binds 15-22 amino acids (aa) of an ep
165 tures and these patterns of naive repertoire paratope usage are highly conserved across subjects.
168 the parent 10E8 was the most soluble, with a paratope we showed crystallographically to be virtually
169 nies the removal of C domains from identical paratopes, we performed molecular dynamics simulations w
170 structures of large protein Ag epitopes and paratopes were analyzed to inform the process of eliciti
173 ecifically to a distinct conformation of the paratope, which was also different from that of the Ag-f
174 ue features, including small size and convex paratopes, which provide enhanced targeting of concave e
175 hich conformational convergence of different paratopes while binding to a common epitope in a similar
176 novel approach to the problem by probing the paratope with (15)N label peptide mimetics followed by N
177 nal residues located at the periphery of the paratope with a concomitant loss of the so-called "O-rin
178 t a limited repertoire of antibodies bearing paratopes with diverse structural contours enriched with
180 methods were used to predict the functional paratopes with the 3D antibody variable domain structure
181 hain V region gene products to form specific paratopes, with no apparent tendency for conservation of
182 e the major part of the predicted functional paratopes, with short-chain hydrophilic residues forming