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1 mapping with a SU C-terminal domain-specific antigen binding fragment.
2 e interdomain conformational dynamics of the antigen-binding fragment.
3 eractions with a striking WWDDD motif of the antigen binding fragments.
4 es (sdAbs); they comprise the smallest known antigen binding fragments.
5  plasmon resonance, were recloned as IgE and antigen-binding fragments.
6 lated with the bioactivity of its individual antigen-binding fragments.
7 ion (1.55 A) crystal structure of the KD-247 antigen binding fragment and examined the potential inte
8 inding proteins, a single chain antibody, an antigen binding fragment, and a fragment of a bacterial
9        We also show that a blocking antibody antigen-binding fragment binds to the extracellular surf
10                                        A b12 antigen-binding fragment blocked both cell-free and mDC-
11 tructure of a ternary complex of onartuzumab antigen-binding fragment bound to a MET extracellular do
12 shion to rapidly improve the affinity of the antigen binding fragment by greater than 90-fold.
13 uman tissue-derived protein macroarrays with antigen-binding fragments derived from 47 consecutive ca
14 Ms using nanobodies, which are single-domain antigen-binding fragments derived from Camelidae heavy-c
15 chain-only antibody (VHH), are single-domain antigen-binding fragments derived from heavy-chain antib
16  of an antibody (monoclonal antibody and the antigen binding fragments F(ab')2 and Fab) targeting epi
17                                          The antigen-binding fragment Fab-YADS2 recognizes vascular e
18 s work, we selected DNA aptamers against the antigen binding fragment (Fab) of antivesicular stomatit
19               A model of AO complexed to the antigen binding fragment (Fab) of mAb 26-10 which was ge
20 cetylphenylalanine (pAcPhe) into an antibody antigen binding fragment (Fab) targeting HER2 (human epi
21      From an anti-AahII mAb, we generated an antigen binding fragment (Fab) with high affinity and se
22 th single-chain variable fragment (scFv) and antigen binding fragment (Fab).
23 of the immature virus complexed with the 2H2 antigen binding fragments (Fab) at different concentrati
24                                              Antigen binding fragments (Fab), variable region fragmen
25 ein the antigen-binding site residing in the antigen-binding fragment (Fab or Fv) is an autonomous an
26  the in vitro and in vivo pharmacology of an antigen-binding fragment (Fab) antidote for ticagrelor.
27 ure of the E2 core domain in complex with an antigen-binding fragment (Fab) at 2.4 A resolution.
28  and human HER2 complexed with the Herceptin antigen-binding fragment (Fab) at 2.5 A.
29 en-binding site relative to the conventional antigen-binding fragment (Fab) from which it was derived
30 ance, we constructed monovalent and bivalent antigen-binding fragment (Fab) libraries, and explored d
31                                          The antigen-binding fragment (Fab) of a monospecific peptide
32 vealed by crystallographic structures of the antigen-binding fragment (Fab) of E8 bound to cyt c (Fab
33                 The crystal structure of the antigen-binding fragment (Fab) of PG16 at 2.5 A resoluti
34  complexed trimeric BG505 SOSIP.664 with the antigen-binding fragment (Fab) of PGT145, a broadly neut
35 erial expression, and crystallization of the antigen-binding fragment (Fab) of the anti-hen egg white
36 .664 trimer and the same trimer bound to the antigen-binding fragment (Fab) of the PGT145 antibody, a
37                Although the influence of the antigen-binding fragment (Fab) on FcRn interactions has
38 region loops of a full-length antibody or an antigen-binding fragment (Fab).
39 s C in the melting temperature (T(m)) of the antigen-binding fragment (Fab).
40 tion of combinatorial libraries of bovine Ig antigen-binding fragments (Fab) of native sequence.
41 ribution, two differently modified alphaCD20 antigen-binding fragments (Fab), prepared by PASylation
42 ay, utilizing a pair of recombinant antibody antigen-binding fragments (Fab), that is specific for HT
43                  When reformatted as soluble antigen-binding fragments (Fab), these clones expressed
44 racterize the binding kinetics of a panel of antigen binding fragments (Fabs) directed against the Pc
45 ils, and fibrils and the structures of their antigen binding fragments (Fabs) in complex with the Abe
46                 Here, we have used synthetic antigen-binding fragments (Fabs) as crystallographic cha
47 ture of human TRAAK in complex with antibody antigen-binding fragments (Fabs) at 2.75-A resolution.
48 onstant domains of different murine antibody antigen-binding fragments (Fabs) by reactive species gen
49  of selection and antiselection for antibody antigen-binding fragments (Fabs) displayed on phage.
50                                              Antigen-binding fragments (Fabs) of antibodies with mode
51 d or eliminated, and ligands such as CD4 and antigen-binding fragments (Fabs) of monoclonal antibodie
52                        Crystal structures of antigen-binding fragments (Fabs) PGT 127 and 128 with Ma
53 tic phage-display library to select specific antigen-binding fragments (Fabs) targeting a large funct
54  the ability of several recombinant antibody antigen-binding fragments (Fabs) to inhibit prion propag
55             Five gammaDPGA-specific antibody antigen-binding fragments (Fabs) were generated from imm
56        Using phage display technology, human antigen-binding fragments (Fabs) were selected against S
57                                              Antigen-binding fragments (Fabs) with synthetic antigen-
58 omologous 1a strain of HCV were recovered as antigen-binding fragments (FAbs).
59 We have determined crystal structures of the antigen-binding fragment for one of these antibodies, 2F
60                            The structures of antigen-binding fragments for two homologous mAbs specif
61 is seed extract, we cloned the single-domain antigen-binding fragments from their heavy-chain only an
62             The crystal structure of another antigen binding fragment in complex with its antigen (hu
63               Crystal structures of the 101F antigen-binding fragment in complex with peptides from t
64     The KD for each of a six-member fragment antigen-binding fragment library is reported using ~25-f
65 , approximately 1.5x10(10)) human naive Fab (antigen-binding fragment) library against an Env and fou
66 mats, as well as the shuttling display of an antigen-binding fragment molecule on phage coat proteins
67                         The structure of the antigen binding fragment of mAb S25-26, determined to 1.
68    The crystal structure of ustekinumab Fab (antigen binding fragment of mAb), in complex with human
69 th a two-domain fragment of human CD4 and an antigen-binding fragment of a neutralizing antibody that
70 ructures of PfCyRPA and its complex with the antigen-binding fragment of a parasite growth inhibitory
71 ptides that bind in a specific pocket in the antigen-binding fragment of a therapeutic antibody such
72                                          The antigen-binding fragment of functional heavy chain antib
73 ibe the use of combinatorial immunoglobulin [antigen-binding fragment of immunoglobulin molecule (Fab
74         Here we present the structure of the antigen-binding fragment of PG16 in monoclinic and ortho
75                                          The antigen-binding fragment of the broadly neutralizing hum
76 ain antibodies (dAbs) are the smallest known antigen-binding fragments of antibodies, ranging from 11
77 -induced basophil degranulation, and IgG1 or antigen-binding fragments of each anti-SEE enhanced degr
78 A into clinical potential, the structures of antigen-binding fragments of mAbs S1-15 and A6 have been
79  p19-p40 IL-23 and its complex with the Fab (antigen-binding fragment) of a neutralizing antibody at
80  target protein (a single chain antibody, an antigen binding fragment, or a fragment of a bacterial t
81  this work, we hypothesize that the bivalent antigen-binding fragment regions of immunoglobulin G are
82            The intact IgG1 antibody with two antigen-binding fragments was also much more active in s
83 munoglobulins (IgGs) composed of independent antigen-binding fragments with a common Fc region.

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