Alpaca (Lama pacos) as a convenient source of recombinant camelid heavy chain antibodies (VHHs).
about
Isolation of alpaca anti-idiotypic heavy-chain single-domain antibody for the aflatoxin immunoassayNanobody-derived nanobiotechnology tool kits for diverse biomedical and biotechnology applicationsSingle domain antibodies: promising experimental and therapeutic tools in infection and immunityIsolation of alpaca anti-hapten heavy chain single domain antibodies for development of sensitive immunoassayThe breadth of cross sub-type neutralisation activity of a single domain antibody to influenza hemagglutinin can be increased by antibody valency.Physico-chemical determinants of soluble intrabody expression in mammalian cell cytoplasm.Design and testing of PCR primers for the construction of scFv libraries representing the immunoglobulin repertoire of rats.A single VHH-based toxin-neutralizing agent and an effector antibody protect mice against challenge with Shiga toxins 1 and 2.Camelid single domain antibodies (VHHs) as neuronal cell intrabody binding agents and inhibitors of Clostridium botulinum neurotoxin (BoNT) proteasesDetermination of Aspergillus pathogens in agricultural products by a specific nanobody-polyclonal antibody sandwich ELISA.Development and utilization of camelid VHH antibodies from alpaca for 2,2',4,4'-tetrabrominated diphenyl ether detection.A novel strategy for development of recombinant antitoxin therapeutics tested in a mouse botulism model.Adenoviral targeting using genetically incorporated camelid single variable domains.A novel multivalent, single-domain antibody targeting TcdA and TcdB prevents fulminant Clostridium difficile infection in mice.Antiviral activity of a single-domain antibody immunotoxin binding to glycoprotein D of herpes simplex virus 2.A general protocol for the generation of Nanobodies for structural biologyIntracellular expression of camelid single-domain antibodies specific for influenza virus nucleoprotein uncovers distinct features of its nuclear localization.Single-domain antibodies and their utility.A heterodimer of a VHH (variable domains of camelid heavy chain-only) antibody that inhibits anthrax toxin cell binding linked to a VHH antibody that blocks oligomer formation is highly protective in an anthrax spore challenge model.How lamina-associated polypeptide 1 (LAP1) activates Torsin.Monoclonal and Single Domain Antibodies Targeting β-Integrin Subunits Block Sexual Transmission of HIV-1 in In Vitro and In Vivo Model SystemsIsolation and characterization of antigen-specific alpaca (Lama pacos) VHH antibodies by biopanning followed by high-throughput sequencing.Structural biology. Structural basis for chemokine recognition and activation of a viral G protein-coupled receptor.Allosteric activation of apicomplexan calcium-dependent protein kinases.Ricin detection using phage displayed single domain antibodies.Camelid Ig V genes reveal significant human homology not seen in therapeutic target genes, providing for a powerful therapeutic antibody platform.Nanobodies: site-specific labeling for super-resolution imaging, rapid epitope-mapping and native protein complex isolation.A single domain antibody fragment that recognizes the adaptor ASC defines the role of ASC domains in inflammasome assemblyCrystal structure of a substrate-engaged SecY protein-translocation channelDurable antitumor responses to CD47 blockade require adaptive immune stimulation.Evaluation of antidiphtheria toxin nanobodies.Phenotypic lentivirus screens to identify functional single domain antibodiesA Tetraspecific VHH-Based Neutralizing Antibody Modifies Disease Outcome in Three Animal Models of Clostridium difficile Infection.Yeast surface two-hybrid for quantitative in vivo detection of protein-protein interactions via the secretory pathway.Bioengineering of bacteria to assemble custom-made polyester affinity resinsSingle-domain antibodies pinpoint potential targets within Shigella invasion plasmid antigen D of the needle tip complex for inhibition of type III secretion.Generation of Immunity against Pathogens via Single-Domain Antibody-Antigen Constructs.Development and Characterization of a Camelid Single Domain Antibody-Urease Conjugate That Targets Vascular Endothelial Growth Factor Receptor 2.PD-L1 is an activation-independent marker of brown adipocytes.Nanobody-based enzyme immunoassay for ochratoxin A in cereal with high resistance to matrix interference.
P2860
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P2860
Alpaca (Lama pacos) as a convenient source of recombinant camelid heavy chain antibodies (VHHs).
description
2007 nî lūn-bûn
@nan
2007 թուականի Մայիսին հրատարակուած գիտական յօդուած
@hyw
2007 թվականի մայիսին հրատարակված գիտական հոդված
@hy
2007年の論文
@ja
2007年論文
@yue
2007年論文
@zh-hant
2007年論文
@zh-hk
2007年論文
@zh-mo
2007年論文
@zh-tw
2007年论文
@wuu
name
Alpaca (Lama pacos) as a conve ...... heavy chain antibodies (VHHs).
@ast
Alpaca (Lama pacos) as a conve ...... heavy chain antibodies (VHHs).
@en
Alpaca
@nl
type
label
Alpaca (Lama pacos) as a conve ...... heavy chain antibodies (VHHs).
@ast
Alpaca (Lama pacos) as a conve ...... heavy chain antibodies (VHHs).
@en
Alpaca
@nl
prefLabel
Alpaca (Lama pacos) as a conve ...... heavy chain antibodies (VHHs).
@ast
Alpaca (Lama pacos) as a conve ...... heavy chain antibodies (VHHs).
@en
Alpaca
@nl
P2093
P2860
P1476
Alpaca (Lama pacos) as a conve ...... heavy chain antibodies (VHHs).
@en
P2093
Anton Pernthaner
Charles B Shoemaker
David R Maass
Jorge Sepulveda
P2860
P356
10.1016/J.JIM.2007.04.008
P577
2007-05-15T00:00:00Z