戻る
「早戻しボタン」を押すと検索画面に戻ります。 [閉じる]

コーパス検索結果 (１語後でソート)

通し番号をクリックするとPubMedの該当ページを表示します
1 ses to differentiate big and small body size camelids.
2 g with terrestrial animals, notably domestic camelids.
3 at are composed of the heavy chain only from camelids.
4 n antibodies that occur naturally in sera of camelids.
5 haemolamae," an endemic red-cell pathogen of camelids.
6 , or CDR2 was also observed, as described in camelids.
7                                              Camelid alpha-lactalbumin is the only known protein that
8 l proteins of the adaptive immune systems of camelid and shark species, complementing conventional an
9 eet dyes, single-domain antibodies, found in camelids and a few other species, are highly specific, a
10   H chain-only Igs are naturally produced in camelids and sharks.
11                  The study of South American camelids and their domestication is a highly debated top
12 cordis has been described in some ruminants, camelids, and otters, but never in great apes.
13  receptor potential vanilloid 1 (TRPV1) by a camelid anti-GFP antibody (anti-GFP-TRPV1).
14  The ferritin nanoparticles associate with a camelid anti-GFP-transient receptor potential vanilloid
15    Here, we describe a panel of single-chain camelid antibodies (nanobodies) directed against differe
16 tified and characterized three single domain camelid antibodies (VHH) against cluster II.
17 el of neutralizing Nanobodies (single domain camelid antibodies fragment) directed against several ch
18 IL-6 with two Fabs derived from conventional camelid antibodies that antagonize the interaction betwe
19    Nanobodies are single-domain fragments of camelid antibodies that are emerging as versatile tools
20      Using GFP-binding proteins derived from Camelid antibodies, we co-opted GFP as a scaffold for in
21 correspond to the antigen-binding domains of camelid antibodies.
22 t also rival the cleft binding properties of camelid antibodies.
23 ed from naturally occurring heavy chain-only camelids antibodies, represent new biological tools to e
24  experiments using a diverse naive synthetic camelid antibody fragment (nanobody) library to enable m
25  to enrich for GPCR ligands from a synthetic camelid antibody fragment (nanobody) library.
26                               We generated a camelid antibody fragment (nanobody) to the human beta(2
27 e receptor stabilized by a G-protein mimetic camelid antibody fragment isolated by conformational sel
28 nt and a crystal structure in complex with a camelid antibody fragment show that the doublecortin C-t
29                               A single chain camelid antibody fragment specific for the C-terminal do
30 ted evolution, we engineered a high-affinity camelid antibody fragment that stabilizes the active sta
31 rphinan agonist BU72 and a G protein mimetic camelid antibody fragment.
32 s the issue of selectivity, here we generate camelid antibody fragments (nanobodies) against the TREK
33 using a yeast-displayed library of synthetic camelid antibody fragments called "nanobodies." Using th
34 eavychain binders (nanobodies) obtained from camelid antibody libraries hold a great promise for immu
35 we report that a single-domain fragment of a camelid antibody raised against wild-type human lysozyme
36 e an investigation involving a single-domain camelid antibody, NbSyn2, selected by phage display tech
37  was found to stabilize the framework of the camelid antibody.
38                                 Single chain camelid antigen binding domains, often called nanobodies
39                                              Camelids are an exception, expressing homodimeric IgGs,
40 avy domain of heavy chain (VHH) domains from camelids, are an attractive platform for therapeutic pur
41 anobodies, a subclass of antibodies found in camelids, are versatile molecular binding scaffolds comp
42 rus HCoV-229E may constitute a descendant of camelid-associated viruses.
43 phic analyses are consistent with Isla Mocha camelids being sourced from Southern Chilean guanaco pop
44 y 17th century, they found that domesticated camelids called "chilihueque" played a major role in the
45  properties of single-domain antibodies from camelids (camels and llamas) can circumvent both these o
46 functional heavy chain antibodies (HCAbs) in camelids comprises a single domain, named the variable d
47                                      Sera of camelids contain both conventional heterotetrameric anti
48 ndrial genomes for 61 ancient South American camelids dated between 3,500 and 2,400 years before the
49                       Gomphothere, equid and camelid delta(13)C records show a broad variability poin
50 l trivalent nanobody comprised of monovalent camelid-derived (ie, from the Camelidae family of mammal
51                                              Camelid-derived and synthetic single-domain antibodies (
52 lected a single N-terminal domain functional camelid-derived heavy (H)-chain antibody fragments (VHH,
53 bodies, a minimalist scaffold generated from camelid-derived heavy-chain IgGs, are one such example.
54                                              Camelid-derived single domain antibodies (VHHs) exhibit
55                                              Camelid-derived single-domain antibody fragments (VHHs o
56                      We generated a panel of camelid-derived single-domain antibody fragments (VHHs)
57                               We generated a camelid-derived single-domain antibody specific for huma
58                                              Camelid-derived VHH single-domain Abs specific for human
59    Single domain antibody fragments, such as camelid-derived VHHs, can serve as inhibitors or activat
60 ly reminiscent of what has been observed for camelid domains.
61 c single-domain antibody (nanobody) from the Camelid family was recently found to allosterically bind
62 ique heavy chain-only immunoglobulins of the camelid family, and have broad applications in bioscienc
63 ough immunization of llamas, a member of the camelid family, whose members generate conventional heav
64 ntrogression signatures within both domestic camelid genomes may reflect post-conquest changes in agr
65                                              Camelids have a special type of Ab, known as heavy chain
66                 Single-chain antibodies from camelids have served as powerful tools ranging from diag
67   Heavy chain-only antibodies, discovered in camelids, have been truncated to yield single-domain ant
68                   Relative to classical Abs, camelid heavy chain Abs (cAbs) have comparable immunogen
69     Unlike the monomeric variable domains of camelid heavy chain antibodies (V(H)H domains), in which
70 robust single domain antibodies derived from camelid heavy chain antibodies.
71  With the B1 domain of protein G (GB1) and a camelid heavy chain antibody as model systems, we are us
72 r Ly-6C/Ly-6G-specific variable fragments of camelid heavy chain-only antibodies (VHH) conjugated to
73                          Variable domains of camelid heavy chain-only antibodies (VHHs) with affinity
74 single domain antigen binding fragments from camelid heavy chain-only antibodies.
75 erface to reduce hydrophobicity by mimicking camelid heavy chains naturally devoid of light chains.
76 ntly expressed variable domains derived from camelid heavy-chain antibodies known as single-domain an
77 -domain antibodies (nanobodies) derived from camelid heavy-chain antibodies specific to Toxocara cani
78 odies, single-domain antibodies derived from camelid heavy-chain antibodies, are known for their high
79 bodies), derived from the variable domain of camelid heavy-chain antibodies, to modulate the function
80 tope limited to two loops found in a natural camelid heavy-chain antibody (VHH) that binds to ribonuc
81    A single-domain fragment, cAb-HuL22, of a camelid heavy-chain antibody specific for the active sit
82 nstructs consisting of two or more different camelid heavy-chain only antibodies (VHHs) joined via pe
83 bodies") derived from the variable region of camelid heavy-chain only antibody variants have proven t
84 ly label VHHs [the variable domain (VH) of a camelid heavy-chain only antibody] with (18)F or (64)Cu.
85 only a single immunoglobulin domain, akin to camelid heavy-chain V domains.
86 tigen receptors of cartilaginous fish and in camelid heavy-chain variable domains.
87 brary of non-immune llama single-domain VHH (camelid heavy-chain variable region derived from heavy-c
88 gainst BoNT/A1 termed ciA-C2, derived from a camelid heavy-chain-only antibody (VHH).
89                    More recently, the use of camelid heavy-chain-only antibody fragments (nanobodies)
90 we describe herein the development of SG4, a camelid heavy-chain-only derived nanobody that was selec
91 usly that the production and evaluation of a camelid heavy-chain-only VH domain (VHH)-based neutraliz
92 therapeutic proteins based on single-domain, camelid, heavy-chain-only antibodies.
93 uring the domestication process by the early camelid herders in the Atacama during the Early Formativ
94 arly consumed camel meat and milk, therefore camelid HEV, which is genotype 7, might infect human bei
95       We found the patient to be infected by camelid HEV.
96 y chain antibodies are naturally produced by camelids, however the structure of their VHH regions can
97 , most nanobodies are produced by immunizing camelids; however, platforms for animal-free production
98                                Previously, a camelid-human chimeric heavy chain antibody VHH-B11-Fc t
99 is unusual feature is analogous to bona fide camelid IgG in which modifications of Ig heavy chain V (
100                       In this study, we used camelid immunization and proteomics to identify a large
101                                 By combining camelid immunization with yeast surface display, we were
102 ditional nanobody generation methods rely on camelid immunization, which can be costly and time-consu
103                                           In camelids, immunization with viral epitopes generates hig
104  chain altogether, as is the case in natural camelid immunoglobulins.
105 rategies, we reviewed the structure of known camelid inhibitory antibodies, which block enzyme activi
106   The origin and taxonomy of these enigmatic camelids is unclear and controversial.
107                            We have generated camelid (Lama pacos) heavy chain-only variable VH domain
108 ote ASV richness was significantly higher in camelid latrines than in controls.
109 ific support that rewilding of native Andean camelids may favor adaptation to glacier retreat and inf
110 Tulan-54 and Tulan-85), as well as 66 modern camelid mitogenomes and 815 modern mitochondrial control
111              We have developed single-domain camelid nanobodies (Nbs) against a LacY mutant in an out
112                                Single-domain camelid nanobodies (Nbs) developed against a LacY mutant
113         Here, we characterized single-domain camelid nanobodies for the 3D quantitative multiplex ima
114 dinary intracellular binding capabilities of camelid nanobodies fused to the UBX domain of the p97 ad
115                                              Camelid nanobodies have been used as a 'one tool, one re
116          We developed and characterized four camelid nanobodies that bind holo-TC (TC in complex with
117                                              Camelid nanobodies, expressed in plants, may offer a sol
118 can be achieved by the in vivo expression of camelid nanobodies.
119                      We employed a synthetic camelid nanobody library expressed in yeast to identify
120 uitin E3 ligase RNF4 with a protein-specific camelid nanobody mediates target destruction by the ubiq
121 ibodies (i.e., nanobody), Nanosota-1, from a camelid nanobody phage display library.
122  We show that ribosomes can be tagged with a camelid nanobody raised against GFP and that this system
123 munal dung deposition by wild, native Andean camelids on soil abiotic and biotic properties and plant
124 nobodies, small single-chain antibodies from camelids or sharks.
125   Nanobodies are single-domain antibodies of camelid origin.
126 ssociated HEV in ungulates such as swine and camelids (posterior probability 0.8), whereas the nonrec
127                                              Camelids produce functional antibodies devoid of light c
128 conventional heavy chain antibodies found in camelids, provide stable, well-expressed binding element
129 versy through genetic analyses of Isla Mocha camelid remains dating from pre-Columbian to early histo
130 site P21-3 on Isla Mocha yielded a number of camelid remains.
131 -chain antibodies or nanobodies, produced by camelids, represent an exciting antiviral approach; they
132                                            A camelid sdAb complex also reveals the molecular structur
133 sdAb heterohexamers in which each of the six camelid sdAb components (VHHs) can neutralize one of thr
134 t transfer into glacier forefields by native camelids shortcuts a 100+ year lag between glacier retre
135 e the "junctional epitope" nature of VHH6, a camelid single domain antibody recognizing the IL-6-gp80
136 ation of this backbone-modified peptide to a camelid single-domain Ab fragment specific for MHC-II en
137 thod that uses phage displaying, engineered, camelid single-domain antibodies ('nanobodies') for simu
138                    This approach also yields camelid single-domain antibodies that recognize key P. a
139                                              Camelid single-domain antibodies, also known as nanobodi
140               Here we develop a radiolabeled camelid single-domain antibody (anti-PD-L1 VHH) to track
141 s can be realized by designing (18)F-labeled camelid single-domain antibody fragments (sdAbs) specifi
142 urther demonstrates the unique properties of camelid single-domain antibody fragments as structural p
143 e populations from small volumes blood using camelid single-domain antibodyfragments (VHHs) as captur
144 ain other key kinetic states, here we raised camelid single-domain nanobodies (Nbs) and carried out a
145 h conquest of South America that resulted in camelids slaughtered en masse.
146                                              Camelid species (llama and camel) were selected for immu
147  virus resistance based on the expression of camelid specific nanobodies against Broad bean mottle vi
148  mutations, which differ from those found in camelid V(H)H domains.
149  and are even more thermostable than typical camelid V(H)H domains.
150 domain antibody specific for fentanyl from a camelid variable-heavy-heavy (VHH) domain phage display
151   When exposed to elevated temperatures, the camelid VHH antibodies retained more reactivity than a p
152 e among alternates is demonstrated for three camelid VHH domain-porcine alpha-amylase interactions.
153  interacts with PCSK9 at low affinity, while camelid VHH exhibits some immunogenicity.
154  binding thermodynamics for an anti-caffeine camelid (VHH) antibody.
155 s of antigen recognition and, in particular, camelid (VHH) domains.
156 sualized in complexes with four 80S-specific camelid VHHs (Nanobodies).
157 ernative to avert viral escape is the use of camelid VHHs (variable heavy chain domains of heavy chai
158 ion between pumas (Puma concolor) and native camelids (Vicugna vicugna and Lama guanicoe) for the per
159 ased in size over a succession starting from camelid viruses via old human viruses to contemporary hu
160                               South American camelids were even found on remote and hard to reach isl
161    In South American societies, domesticated camelids were of great cultural importance and subject t
162 , small single-chain antibodies derived from camelids with numerous advantageous properties and the p

 
Page Top