ライフサイエンスコーパス: camelid

1 n antibodies that occur naturally in sera of camelids.

2 haemolamae," an endemic red-cell pathogen of camelids.

3 , or CDR2 was also observed, as described in camelids.

4 receptor potential vanilloid 1 (TRPV1) by a camelid anti-GFP antibody (anti-GFP-TRPV1).

5 The ferritin nanoparticles associate with a camelid anti-GFP-transient receptor potential vanilloid

6 tified and characterized three single domain camelid antibodies (VHH) against cluster II.

7 el of neutralizing Nanobodies (single domain camelid antibodies fragment) directed against several ch

8 IL-6 with two Fabs derived from conventional camelid antibodies that antagonize the interaction betwe

9 Nanobodies are single-domain fragments of camelid antibodies that are emerging as versatile tools

10 Using GFP-binding proteins derived from Camelid antibodies, we co-opted GFP as a scaffold for in

11 t also rival the cleft binding properties of camelid antibodies.

12 correspond to the antigen-binding domains of camelid antibodies.

13 ed from naturally occurring heavy chain-only camelids antibodies, represent new biological tools to e

14 We generated a camelid antibody fragment (nanobody) to the human beta(2

15 e receptor stabilized by a G-protein mimetic camelid antibody fragment isolated by conformational sel

16 nt and a crystal structure in complex with a camelid antibody fragment show that the doublecortin C-t

17 A single chain camelid antibody fragment specific for the C-terminal do

18 ted evolution, we engineered a high-affinity camelid antibody fragment that stabilizes the active sta

19 rphinan agonist BU72 and a G protein mimetic camelid antibody fragment.

20 eavychain binders (nanobodies) obtained from camelid antibody libraries hold a great promise for immu

21 we report that a single-domain fragment of a camelid antibody raised against wild-type human lysozyme

22 e an investigation involving a single-domain camelid antibody, NbSyn2, selected by phage display tech

23 was found to stabilize the framework of the camelid antibody.

24 Camelids are an exception, expressing homodimeric IgGs,

25 rus HCoV-229E may constitute a descendant of camelid-associated viruses.

26 phic analyses are consistent with Isla Mocha camelids being sourced from Southern Chilean guanaco pop

27 y 17th century, they found that domesticated camelids called "chilihueque" played a major role in the

28 properties of single-domain antibodies from camelids (camels and llamas) can circumvent both these o

29 functional heavy chain antibodies (HCAbs) in camelids comprises a single domain, named the variable d

30 Sera of camelids contain both conventional heterotetrameric anti

31 bodies, a minimalist scaffold generated from camelid-derived heavy-chain IgGs, are one such example.

32 Camelid-derived single-domain antibody fragments (VHHs o

33 We generated a panel of camelid-derived single-domain antibody fragments (VHHs)

34 We generated a camelid-derived single-domain antibody specific for huma

35 Single domain antibody fragments, such as camelid-derived VHHs, can serve as inhibitors or activat

36 ly reminiscent of what has been observed for camelid domains.

37 c single-domain antibody (nanobody) from the Camelid family was recently found to allosterically bind

38 Camelids have a special type of Ab, known as heavy chain

39 Relative to classical Abs, camelid heavy chain Abs (cAbs) have comparable immunogen

40 Unlike the monomeric variable domains of camelid heavy chain antibodies (V(H)H domains), in which

41 robust single domain antibodies derived from camelid heavy chain antibodies.

42 With the B1 domain of protein G (GB1) and a camelid heavy chain antibody as model systems, we are us

43 r Ly-6C/Ly-6G-specific variable fragments of camelid heavy chain-only antibodies (VHH) conjugated to

44 Variable domains of camelid heavy chain-only antibodies (VHHs) with affinity

45 erface to reduce hydrophobicity by mimicking camelid heavy chains naturally devoid of light chains.

46 tope limited to two loops found in a natural camelid heavy-chain antibody (VHH) that binds to ribonuc

47 A single-domain fragment, cAb-HuL22, of a camelid heavy-chain antibody specific for the active sit

48 nstructs consisting of two or more different camelid heavy-chain only antibodies (VHHs) joined via pe

49 ly label VHHs [the variable domain (VH) of a camelid heavy-chain only antibody] with (18)F or (64)Cu.

50 only a single immunoglobulin domain, akin to camelid heavy-chain V domains.

51 tigen receptors of cartilaginous fish and in camelid heavy-chain variable domains.

52 brary of non-immune llama single-domain VHH (camelid heavy-chain variable region derived from heavy-c

53 gainst BoNT/A1 termed ciA-C2, derived from a camelid heavy-chain-only antibody (VHH).

54 usly that the production and evaluation of a camelid heavy-chain-only VH domain (VHH)-based neutraliz

55 arly consumed camel meat and milk, therefore camelid HEV, which is genotype 7, might infect human bei

56 We found the patient to be infected by camelid HEV.

57 is unusual feature is analogous to bona fide camelid IgG in which modifications of Ig heavy chain V (

58 In camelids, immunization with viral epitopes generates hig

59 chain altogether, as is the case in natural camelid immunoglobulins.

60 rategies, we reviewed the structure of known camelid inhibitory antibodies, which block enzyme activi

61 The origin and taxonomy of these enigmatic camelids is unclear and controversial.

62 We have generated camelid (Lama pacos) heavy chain-only variable VH domain

63 We have developed single-domain camelid nanobodies (Nbs) against a LacY mutant in an out

64 Single-domain camelid nanobodies (Nbs) developed against a LacY mutant

65 Camelid nanobodies, expressed in plants, may offer a sol

66 can be achieved by the in vivo expression of camelid nanobodies.

67 We show that ribosomes can be tagged with a camelid nanobody raised against GFP and that this system

68 Nanobodies are single-domain antibodies of camelid origin.

69 Camelids produce functional antibodies devoid of light c

70 versy through genetic analyses of Isla Mocha camelid remains dating from pre-Columbian to early histo

71 site P21-3 on Isla Mocha yielded a number of camelid remains.

72 -chain antibodies or nanobodies, produced by camelids, represent an exciting antiviral approach; they

73 A camelid sdAb complex also reveals the molecular structur

74 e the "junctional epitope" nature of VHH6, a camelid single domain antibody recognizing the IL-6-gp80

75 Here we develop a radiolabeled camelid single-domain antibody (anti-PD-L1 VHH) to track

76 s can be realized by designing (18)F-labeled camelid single-domain antibody fragments (sdAbs) specifi

77 urther demonstrates the unique properties of camelid single-domain antibody fragments as structural p

78 e populations from small volumes blood using camelid single-domain antibodyfragments (VHHs) as captur

79 Camelid species (llama and camel) were selected for immu

80 virus resistance based on the expression of camelid specific nanobodies against Broad bean mottle vi

81 mutations, which differ from those found in camelid V(H)H domains.

82 and are even more thermostable than typical camelid V(H)H domains.

83 When exposed to elevated temperatures, the camelid VHH antibodies retained more reactivity than a p

84 e among alternates is demonstrated for three camelid VHH domain-porcine alpha-amylase interactions.

85 binding thermodynamics for an anti-caffeine camelid (VHH) antibody.

86 s of antigen recognition and, in particular, camelid (VHH) domains.

87 sualized in complexes with four 80S-specific camelid VHHs (Nanobodies).

88 ased in size over a succession starting from camelid viruses via old human viruses to contemporary hu

89 South American camelids were even found on remote and hard to reach isl

90 In South American societies, domesticated camelids were of great cultural importance and subject t