Literature DB >> 22886243

Introduction to heavy chain antibodies and derived Nanobodies.

Cécile Vincke1, Serge Muyldermans.   

Abstract

The immune response of infected or immunized dromedaries contains a diverse repertoire of conventional and heavy chain-only antibodies, both functional in antigen binding. By definition, a heavy chain antibody is devoid of a light chain and in the case of the heavy chain antibodies in camelids the CH1 domain is also missing. Consequently a camelid heavy chain antibody associates with its cognate antigen via a single domain, the variable heavy chain domain of a heavy chain antibody or VHH. An antigen-specific VHH, also known as Nanobody, with excellent biochemical properties can be obtained in various ways. Their recombinant expression provides access to user-friendly tools for a wide variety of applications.

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Year:  2012        PMID: 22886243     DOI: 10.1007/978-1-61779-968-6_2

Source DB:  PubMed          Journal:  Methods Mol Biol        ISSN: 1064-3745


  32 in total

1.  Intracellular Delivery of Nanobodies for Imaging of Target Proteins in Live Cells.

Authors:  Ruth Röder; Jonas Helma; Tobias Preiß; Joachim O Rädler; Heinrich Leonhardt; Ernst Wagner
Journal:  Pharm Res       Date:  2016-10-31       Impact factor: 4.200

Review 2.  The actin-bundling protein L-plastin supports T-cell motility and activation.

Authors:  Sharon Celeste Morley
Journal:  Immunol Rev       Date:  2013-11       Impact factor: 12.988

Review 3.  β2 Adrenergic Receptor Complexes with the L-Type Ca2+ Channel CaV1.2 and AMPA-Type Glutamate Receptors: Paradigms for Pharmacological Targeting of Protein Interactions.

Authors:  Kwun Nok Mimi Man; Manuel F Navedo; Mary C Horne; Johannes W Hell
Journal:  Annu Rev Pharmacol Toxicol       Date:  2019-09-27       Impact factor: 13.820

4.  Identification of Nanobodies Blocking Intimate Adherence of Shiga Toxin-Producing Escherichia coli to Epithelial Cells.

Authors:  David Ruano-Gallego; Luis Ángel Fernández
Journal:  Methods Mol Biol       Date:  2021

5.  Regulation of β2-adrenergic receptor function by conformationally selective single-domain intrabodies.

Authors:  Dean P Staus; Laura M Wingler; Ryan T Strachan; Soren G F Rasmussen; Els Pardon; Seungkirl Ahn; Jan Steyaert; Brian K Kobilka; Robert J Lefkowitz
Journal:  Mol Pharmacol       Date:  2013-12-06       Impact factor: 4.436

6.  Magic bullets from llamas.

Authors:  Daniel J Leahy
Journal:  Structure       Date:  2013-07-02       Impact factor: 5.006

Review 7.  Subcellular functions of proteins under fluorescence single-cell microscopy.

Authors:  Casey L Kohnhorst; Danielle L Schmitt; Anand Sundaram; Songon An
Journal:  Biochim Biophys Acta       Date:  2015-05-27

Review 8.  IgA nephropathy enigma.

Authors:  Jiri Mestecky; Jan Novak; Zina Moldoveanu; Milan Raska
Journal:  Clin Immunol       Date:  2016-07-18       Impact factor: 3.969

Review 9.  VHH antibodies: emerging reagents for the analysis of environmental chemicals.

Authors:  Candace S Bever; Jie-Xian Dong; Natalia Vasylieva; Bogdan Barnych; Yongliang Cui; Zhen-Lin Xu; Bruce D Hammock; Shirley J Gee
Journal:  Anal Bioanal Chem       Date:  2016-05-21       Impact factor: 4.142

10.  Characterization of camel nanobodies specific for superfolder GFP fusion proteins.

Authors:  Aya Twair; Souad Al-Okla; Moutaz Zarkawi; Abdul Qader Abbady
Journal:  Mol Biol Rep       Date:  2014-08-02       Impact factor: 2.316

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