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1 stant domains and a structural model of this heavy chain-only antibody.
2 ause of their potential to make heat-stable, heavy-chain-only antibodies.
3 Here we report identification of a panel of heavy-chain-only antibody (Ab) V(H) (VHH) domains that n
5 tion allostery in integrins and in isolating heavy chain-only antibodies against botulinum neurotoxin
6 functional fragments of naturally occurring heavy chain-only antibodies and represent an attractive
7 lid heavy-chain variable region derived from heavy-chain-only antibody) antibodies displayed on the s
8 Nanobodies, which are derived from unique heavy-chain-only antibodies, are the smallest antigen-bi
9 brary derived from variable regions of llama heavy chain-only antibodies, as fusions with a hyperacti
10 new antigen receptor (IgNAR), a homodimeric heavy chain-only antibody, as a major part of their humo
12 ell-known Ig fold, but apart from that, this heavy chain-only antibody employs unique ways for dimeri
13 lated and characterized a caffeine-specific, heavy-chain-only antibody fragment (V(HH)) from llama th
15 applications, nanobodies (VHH) derived from heavy chain only antibodies from Camelidae, may be bette
16 -domain antigen-binding fragments from their heavy-chain only antibodies in a phage display vector an
17 GPI-anchored variable regions (VHHs) of two heavy chain-only antibodies, JM2 and JM4, from immunized
19 igen-recognizing domains of the minimalistic heavy chain-only antibodies produced by camels and llama
21 aracterized a collection of epitopic tagged, heavy chain-only antibody VH domains (VHHs) specific for
22 Ly-6G-specific variable fragments of camelid heavy chain-only antibodies (VHH) conjugated to Pseudomo
23 s), also known as the variable domain of the heavy-chain-only antibody (VHH), are single-domain antig
25 tibodies by fusing variable domains of llama heavy chain-only antibodies (VHHs) against ETEC to the F
27 consisting of two or more different camelid heavy-chain only antibodies (VHHs) joined via peptide li
28 duction, the recombinant variable domains of heavy-chain-only antibodies (VHHs) are becoming a salien
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