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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
11 tructure of a ternary complex of onartuzumab antigen-binding fragment bound to a MET extracellular do
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
18 s work, we selected DNA aptamers against the antigen binding fragment (Fab) of antivesicular stomatit
20 cetylphenylalanine (pAcPhe) into an antibody antigen binding fragment (Fab) targeting HER2 (human epi
23 of the immature virus complexed with the 2H2 antigen binding fragments (Fab) at different concentrati
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.
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
32 vealed by crystallographic structures of the antigen-binding fragment (Fab) of E8 bound to cyt c (Fab
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
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
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
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
51 d or eliminated, and ligands such as CD4 and antigen-binding fragments (Fabs) of monoclonal antibodie
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
59 We have determined crystal structures of the antigen-binding fragment for one of these antibodies, 2F
61 is seed extract, we cloned the single-domain antigen-binding fragments from their heavy-chain only an
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
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
73 ibe the use of combinatorial immunoglobulin [antigen-binding fragment of immunoglobulin molecule (Fab
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
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