ライフサイエンスコーパス: antigen-binding fragment

1 mapping with a SU C-terminal domain-specific antigen binding fragment.

2 s the smallest known recombinant independent antigen-binding fragment.

3 e interdomain conformational dynamics of the antigen-binding fragment.

4 eractions with a striking WWDDD motif of the antigen binding fragments.

5 es (sdAbs); they comprise the smallest known antigen binding fragments.

6 plasmon resonance, were recloned as IgE and antigen-binding fragments.

7 lated with the bioactivity of its individual antigen-binding fragments.

8 e crystal structure of E2 in complex with an antigen-binding fragment (2A12) and CD81-LEL (E2-2A12-CD

9 One 1C3 antigen-binding fragment anchors simultaneously to the t

10 ion (1.55 A) crystal structure of the KD-247 antigen binding fragment and examined the potential inte

11 tween two and six Ig monomers, each with two antigen binding fragments and one fragment crystallizati

12 ment crystallizable) and F(ab')(2) (fragment antigen-binding) fragments and protects the bacteria aga

13 inding proteins, a single chain antibody, an antigen binding fragment, and a fragment of a bacterial

14 We also show that a blocking antibody antigen-binding fragment binds to the extracellular surf

15 A b12 antigen-binding fragment blocked both cell-free and mDC-

16 tructure of a ternary complex of onartuzumab antigen-binding fragment bound to a MET extracellular do

17 shion to rapidly improve the affinity of the antigen binding fragment by greater than 90-fold.

18 d homogeneous dual-labeled anti-MMP-14 Fabs (antigen-binding fragments) conjugated to monomethyl auri

19 uman tissue-derived protein macroarrays with antigen-binding fragments derived from 47 consecutive ca

20 Ms using nanobodies, which are single-domain antigen-binding fragments derived from Camelidae heavy-c

21 chain-only antibody (VHH), are single-domain antigen-binding fragments derived from heavy-chain antib

22 the CD19-CD81 complex bound to a therapeutic antigen-binding fragment, determined by cryo-electron mi

23 In class (B1), the antigen binding fragment distorted significantly, and we

24 of an antibody (monoclonal antibody and the antigen binding fragments F(ab')2 and Fab) targeting epi

25 e, two Fc-silenced variants, or the bivalent antigen-binding fragment F(ab')(2)), administered either

26 ential administration of a pair of anti-EGFR antigen binding fragments, F(ab')(2), conjugated to eith

27 cancer using (211)At conjugated to MX35, the antigen-binding fragments-F(ab')(2)-of a mouse monoclona

28 The antigen-binding fragment Fab-YADS2 recognizes vascular e

29 s work, we selected DNA aptamers against the antigen binding fragment (Fab) of antivesicular stomatit

30 A model of AO complexed to the antigen binding fragment (Fab) of mAb 26-10 which was ge

31 cetylphenylalanine (pAcPhe) into an antibody antigen binding fragment (Fab) targeting HER2 (human epi

32 From an anti-AahII mAb, we generated an antigen binding fragment (Fab) with high affinity and se

33 and a newly determined structure of the OKT9 antigen binding fragment (Fab), suggests that OKT9 and t

34 th single-chain variable fragment (scFv) and antigen binding fragment (Fab).

35 of the immature virus complexed with the 2H2 antigen binding fragments (Fab) at different concentrati

36 Antigen binding fragments (Fab), variable region fragmen

37 ein the antigen-binding site residing in the antigen-binding fragment (Fab or Fv) is an autonomous an

38 y variable domain shuffling and converted to antigen-binding fragment (Fab) antibodies.

39 the in vitro and in vivo pharmacology of an antigen-binding fragment (Fab) antidote for ticagrelor.

40 ure of the E2 core domain in complex with an antigen-binding fragment (Fab) at 2.4 A resolution.

41 and human HER2 complexed with the Herceptin antigen-binding fragment (Fab) at 2.5 A.

42 e a 2.85 angstrom co-crystal structure of J2 antigen-binding fragment (Fab) bound to dsRNA.

43 the high-resolution cryo-EM structure of its antigen-binding fragment (Fab) bound to the virion of a

44 core mechanisms of protection: an antibody's antigen-binding fragment (Fab) can bind and neutralize v

45 FHTR2163 is a novel antigen-binding fragment (Fab) directed against high-tem

46 Here, we report crystal structures of a S9.6 antigen-binding fragment (Fab) free and bound to a 13-bp

47 en-binding site relative to the conventional antigen-binding fragment (Fab) from which it was derived

48 ance, we constructed monovalent and bivalent antigen-binding fragment (Fab) libraries, and explored d

49 applied to a 12 standard monoclonal antibody antigen-binding fragment (Fab) mixture, demonstrating th

50 virus-like particle (VLP) complexed with the antigen-binding fragment (Fab) of a human neutralizing a

51 The antigen-binding fragment (Fab) of a monospecific peptide

52 vealed by crystallographic structures of the antigen-binding fragment (Fab) of E8 bound to cyt c (Fab

53 The crystal structure of the antigen-binding fragment (Fab) of PG16 at 2.5 A resoluti

54 complexed trimeric BG505 SOSIP.664 with the antigen-binding fragment (Fab) of PGT145, a broadly neut

55 erial expression, and crystallization of the antigen-binding fragment (Fab) of the anti-hen egg white

56 .664 trimer and the same trimer bound to the antigen-binding fragment (Fab) of the PGT145 antibody, a

57 Although the influence of the antigen-binding fragment (Fab) on FcRn interactions has

58 ted IbpA construct in complex with mouse VH5 antigen-binding fragment (Fab) shows a binding of Ig hea

59 get membrane-proximal CD21 epitopes using an antigen-binding fragment (Fab)-CAR design, we demonstrat

60 region loops of a full-length antibody or an antigen-binding fragment (Fab).

61 s C in the melting temperature (T(m)) of the antigen-binding fragment (Fab).

62 tion of combinatorial libraries of bovine Ig antigen-binding fragments (Fab) of native sequence.

63 ribution, two differently modified alphaCD20 antigen-binding fragments (Fab), prepared by PASylation

64 ay, utilizing a pair of recombinant antibody antigen-binding fragments (Fab), that is specific for HT

65 When reformatted as soluble antigen-binding fragments (Fab), these clones expressed

66 Here, to address this, we developed an antigen-binding fragment (Fab7) that recognizes both act

67 racterize the binding kinetics of a panel of antigen binding fragments (Fabs) directed against the Pc

68 ils, and fibrils and the structures of their antigen binding fragments (Fabs) in complex with the Abe

69 imits the possible positions of both sets of antigen-binding fragments (Fabs) and preserves steric ac

70 Here, we have used synthetic antigen-binding fragments (Fabs) as crystallographic cha

71 ture of human TRAAK in complex with antibody antigen-binding fragments (Fabs) at 2.75-A resolution.

72 onstant domains of different murine antibody antigen-binding fragments (Fabs) by reactive species gen

73 of selection and antiselection for antibody antigen-binding fragments (Fabs) displayed on phage.

74 ated a library of Fc variants with identical antigen-binding fragments (Fabs) from an EBOV neutralizi

75 Antigen-binding fragments (Fabs) of antibodies with mode

76 d or eliminated, and ligands such as CD4 and antigen-binding fragments (Fabs) of monoclonal antibodie

77 ture of trimeric human STEAP1 bound to three antigen-binding fragments (Fabs) of the clinically used

78 e the structure of prefusion Gc bound to the antigen-binding fragments (Fabs) of two neutralizing ant

79 Crystal structures of antigen-binding fragments (Fabs) PGT 127 and 128 with Ma

80 tic phage-display library to select specific antigen-binding fragments (Fabs) targeting a large funct

81 Here we identified synthetic antigen-binding fragments (Fabs) that inhibit the quinol

82 ological applications, there is a demand for antigen-binding fragments (Fabs) that specifically and t

83 the ability of several recombinant antibody antigen-binding fragments (Fabs) to inhibit prion propag

84 ated common ancestors (UCAs), and monovalent antigen-binding fragments (Fabs) to investigate how affi

85 Five gammaDPGA-specific antibody antigen-binding fragments (Fabs) were generated from imm

86 Using phage display technology, human antigen-binding fragments (Fabs) were selected against S

87 Antigen-binding fragments (Fabs) with synthetic antigen-

88 we coupled bivalent low-affinity anti-LYPD1 antigen-binding fragments (Fabs) with the anti-CD3 scFv.

89 compact double-barrel dimer bound by two RTX antigen-binding fragments (Fabs), each of which engages

90 d a panel of sperm-binding IgGs with 6 to 10 antigen-binding fragments (Fabs), isolated from a health

91 s either immunoglobulins (IgGs) or monomeric antigen-binding fragments (Fabs), which was consistent w

92 omologous 1a strain of HCV were recovered as antigen-binding fragments (FAbs).

93 We have determined crystal structures of the antigen-binding fragment for one of these antibodies, 2F

94 The structures of antigen-binding fragments for two homologous mAbs specif

95 by employing nanobodies (Nbs), single domain antigen binding fragments from camelid heavy chain-only

96 is seed extract, we cloned the single-domain antigen-binding fragments from their heavy-chain only an

97 inhibitor molecule SN-38, with a trastuzumab antigen binding fragment (HER2-Fab), has been used to ta

98 The crystal structure of another antigen binding fragment in complex with its antigen (hu

99 Crystal structures of the 101F antigen-binding fragment in complex with peptides from t

100 The KD for each of a six-member fragment antigen-binding fragment library is reported using ~25-f

101 , approximately 1.5x10(10)) human naive Fab (antigen-binding fragment) library against an Env and fou

102 , understanding the functional impact of CD3 antigen-binding fragment modifications is of utmost impo

103 mats, as well as the shuttling display of an antigen-binding fragment molecule on phage coat proteins

104 of the microelectrode surface and HT-2 toxin antigen binding fragment of antibody (anti-HT2 (10) Fab)

105 The structure of the antigen binding fragment of mAb S25-26, determined to 1.

106 The crystal structure of ustekinumab Fab (antigen binding fragment of mAb), in complex with human

107 th a two-domain fragment of human CD4 and an antigen-binding fragment of a neutralizing antibody that

108 ructures of PfCyRPA and its complex with the antigen-binding fragment of a parasite growth inhibitory

109 ptides that bind in a specific pocket in the antigen-binding fragment of a therapeutic antibody such

110 The antigen-binding fragment of functional heavy chain antib

111 The cryo-EM structure of the antigen-binding fragment of HmAb64 in complex with a CNE

112 ibe the use of combinatorial immunoglobulin [antigen-binding fragment of immunoglobulin molecule (Fab

113 p120 core in complex with rhesus CD4 and the antigen-binding fragment of ITS90.03 at 2.5- angstrom re

114 Here we present the structure of the antigen-binding fragment of PG16 in monoclinic and ortho

115 The antigen-binding fragment of the broadly neutralizing hum

116 ain antibodies (dAbs) are the smallest known antigen-binding fragments of antibodies, ranging from 11

117 -induced basophil degranulation, and IgG1 or antigen-binding fragments of each anti-SEE enhanced degr

118 A into clinical potential, the structures of antigen-binding fragments of mAbs S1-15 and A6 have been

119 f the complex of Bet v 1 with immunoglobulin antigen-binding fragments of REGN5713 or REGN5715 show d

120 p19-p40 IL-23 and its complex with the Fab (antigen-binding fragment) of a neutralizing antibody at

121 With nanomolar affinity for hTfR1, the OKT9 antigen binding fragment (OKT9-Fab) sterically blocks cl

122 target protein (a single chain antibody, an antigen binding fragment, or a fragment of a bacterial t

123 this work, we hypothesize that the bivalent antigen-binding fragment regions of immunoglobulin G are

124 Here, we used a synthetic antigen-binding fragment (sFab) library to discover two

125 single-particle cryo-electron microscopy and antigen-binding fragment technology.

126 y, we screened and characterized a synthetic antigen-binding fragment, termed sAB-K29, that can speci

127 ll proteins, merely consisting of two linked antigen-binding fragments, to large immunoglobulin G (Ig

128 reatment of primed neutrophils with purified antigen-binding fragments used as competitor significant

129 The intact IgG1 antibody with two antigen-binding fragments was also much more active in s

130 eloped the FORCETM platform consisting of an antigen-binding fragment, which binds the transferrin re

131 otype 8 vector that expresses an anti-VEGF-A antigen-binding fragment, which provides potential for c

132 munoglobulins (IgGs) composed of independent antigen-binding fragments with a common Fc region.

133 crystal structures of COV44-62 and COV44-79 antigen-binding fragments with the SARS-CoV-2 fusion pep