Alpaca (Lama pacos) as a convenient source of recombinant camelid heavy chain antibodies (VHHs). - Wikidata - wikimedia - TriplyDB

Alpaca (Lama pacos) as a convenient source of recombinant camelid heavy chain antibodies (VHHs).

Alpaca (Lama pacos) as a convenient source of recombinant camelid heavy chain antibodies (VHHs).

http://www.wikidata.org/entity/Q33287667

about

Isolation of alpaca anti-idiotypic heavy-chain single-domain antibody for the aflatoxin immunoassay Nanobody-derived nanobiotechnology tool kits for diverse biomedical and biotechnology applications Single domain antibodies: promising experimental and therapeutic tools in infection and immunity Isolation of alpaca anti-hapten heavy chain single domain antibodies for development of sensitive immunoassay The 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) proteases Determination 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 biology Intracellular 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 Systems Isolation 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 assembly Crystal structure of a substrate-engaged SecY protein-translocation channel Durable antitumor responses to CD47 blockade require adaptive immune stimulation.Evaluation of antidiphtheria toxin nanobodies.Phenotypic lentivirus screens to identify functional single domain antibodies A 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 resins Single-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.

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Alpaca (Lama pacos) as a convenient source of recombinant camelid heavy chain antibodies (VHHs).

http://www.wikidata.org/entity/Q33287667

description

2007 nî lūn-bûn

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2007 թուականի Մայիսին հրատարակուած գիտական յօդուած

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2007 թվականի մայիսին հրատարակված գիտական հոդված

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2007年の論文

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2007年論文

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2007年論文

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2007年論文

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2007年論文

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2007年论文

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Alpaca (Lama pacos) as a conve ...... heavy chain antibodies (VHHs).

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Alpaca (Lama pacos) as a conve ...... heavy chain antibodies (VHHs).

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Alpaca (Lama pacos) as a conve ...... heavy chain antibodies (VHHs).

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Alpaca (Lama pacos) as a conve ...... heavy chain antibodies (VHHs).

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P356

J.JIM.2007.04.008

P1433

Journal of Immunological Methods

P1476

Alpaca (Lama pacos) as a conve ...... heavy chain antibodies (VHHs).

@en

P2093

Anton Pernthaner

http://www.w3.org/2001/XMLSchema#string

Charles B Shoemaker

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David R Maass

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Jorge Sepulveda

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P2860

Canonical antigen-binding loop structures in immunoglobulins: more structures, more canonical classes?

Tight regulation, modulation, and high-level expression by vectors containing the arabinose PBAD promoter

Comparison of physical chemical properties of llama VHH antibody fragments and mouse monoclonal antibodies

Selection and identification of single domain antibody fragments from camel heavy-chain antibodies

Naturally occurring antibodies devoid of light chains

Targeting and tracing antigens in live cells with fluorescent nanobodies

TNF-alpha neutralization ameliorates the severity of murine Crohn's-like ileitis by abrogation of intestinal epithelial cell apoptosis.

Loss of splice consensus signal is responsible for the removal of the entire C(H)1 domain of the functional camel IGG2A heavy-chain antibodies.

The structure of the llama heavy chain constant genes reveals a mechanism for heavy-chain antibody formation.

Molecular cloning, expression and characterization of ovine TNF alpha.

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13-25

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scholarly article

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10.1016/J.JIM.2007.04.008

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1-2

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324

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2007-05-15T00:00:00Z

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6267788

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17568607

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2014515

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