ArticleNature protocols2010
Protocol for the selection of single-domain antibody fragments by third generation intracellular antibody capture.
Article in Nature protocols, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
What it found
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The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
20 citing papers in PubMed, 43 citations in OpenAlex.
- Tiny tools closing the gap: nanobodies in research and therapy.Function (Oxford, England) · 2026Review
- Intracellular Antibodies for Drug Discovery and as Drugs of the Future.Antibodies (Basel, Switzerland) · 2023Review
- Single-domain antibody screening byLife science alliance · 2022Article
- Pan RAS-binding compounds selected from a chemical library by inhibiting interaction between RAS and a reduced affinity intracellular antibody.Scientific reports · 2021Article
- RAS Function in cancer cells: translating membrane biology and biochemistry into new therapeutics.The Biochemical journal · 2020Review
- Construction of Antibody Phage Libraries and Their Application in Veterinary Immunovirology.Antibodies (Basel, Switzerland) · 2020Review
- A genetically encoded probe for imaging nascent and mature HA-tagged proteins in vivo.Nature communications · 2019Article
- Cancer cell killing by target antigen engagement with engineered complementary intracellular antibody single domains fused to pro-caspase3.Scientific reports · 2019Article
- Small molecule inhibitors of RAS-effector protein interactions derived using an intracellular antibody fragment.Nature communications · 2018Article
- Cloning, purification and structure determination of the HIV integrase-binding domain of lens epithelium-derived growth factor.Acta crystallographica. Section F, Structural biology communications · 2018Article
- Intracellular immunization against HIV infection with an intracellular antibody that mimics HIV integrase binding to the cellular LEDGF protein.Scientific reports · 2017Article
- Single domain antibodies for the knockdown of cytosolic and nuclear proteins.Protein science : a publication of the Protein Society · 2017Review
- Efficient affinity maturation of antibody variable domains requires co-selection of compensatory mutations to maintain thermodynamic stability.Scientific reports · 2017Article
- Assessment of antibody library diversity through next generation sequencing and technical error compensation.PloS one · 2017Article
- Article
- LMO2 at 25 years: a paradigm of chromosomal translocation proteins.Open biology · 2015Review
- Conformational flexibility of the oncogenic protein LMO2 primes the formation of the multi-protein transcription complex.Scientific reports · 2014Article
- Immunosympathectomy as the first phenotypic knockout with antibodies.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- Changing the subcellular location of the oncoprotein Bcr-Abl using rationally designed capture motifs.Pharmaceutical research · 2012Article
- Single domain intracellular antibodies from diverse libraries: emphasizing dual functions of LMO2 protein interactions using a single VH domain.The Journal of biological chemistry · 2011Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors at 2 institutions in 1 country.
Funding
Abstract
Single-domain intracellular antibodies are antibody variable segments that bind to specific target proteins inside cells. These antigen-binding variable regions can interfere with protein function or perturb protein-protein interactions and can be used as tools for research, especially functional genomics and proteomics and interfering with the protein interactome. This protocol (Intracellular Antibody Capture, IAC(3)) describes the isolation of functional variable heavy (VH) or variable light (VL) segments from diverse libraries. The protocol comprises four principle steps: validation of a bait antigen; initial screening in yeast of a single domain library; generation of sub-libraries after the initial screen; and finally confirmation of the positive clones interaction with antigen in yeast and mammalian cells. Each library (initial, second and third) screening takes upto 2 weeks and the overall procedure <3 months. This third generation IAC method has many advantages, including isolation of single domain intracellular antibodies with high affinity and specificity by direct in vivo genetic selection.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.