Evidence map›Paper›PMID 12595572›Full record

ArticleNucleic acids research2003

De novo production of diverse intracellular antibody libraries.

Tomoyuki Tanaka, Grace T Y Chung, Alan Forster, M Natividad Lobato, Terence H Rabbitts

Open access · greenAbstract read
In one paragraph

Article in Nucleic acids research, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
3.8field-weighted citation impact, top 7% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

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.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

14 citing papers in PubMed, 40 citations in OpenAlex.

  1. Article
  2. Article
  3. The modular nature of bradykinin-potentiating peptides isolated from snake venoms.The journal of venomous animals and toxins including tropical diseases · 2017
    Review
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Intrabody expression in eukaryotic cells.Methods in molecular biology (Clifton, N.J.) · 2009
    Article
  11. Expression of single-chain Fv fragments in E. coli cytoplasm.Methods in molecular biology (Clifton, N.J.) · 2009
    Article
  12. Intracellular antibodies for proteomics.Journal of immunological methods · 2004
    Review
  13. Article
  14. Review
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

5 authors at 1 institution in 1 country.

Tomoyuki TanakaMRC Laboratory of Molecular Biology, Hills Road, Cambridge CB2 2QH, UK.
Grace T Y Chung
Alan Forster
M Natividad Lobato
Terence H Rabbitts
MRC Laboratory of Molecular Biology · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Many therapeutic targets are intracellular proteins and molecules designed to interact with them must effectively bind to their target inside the cell. Intracellular antibodies (intrabodies) recognise and bind to proteins in cells and various methods have been developed to produce such molecules. Intracellular antibody capture (IAC) is based on a genetic screening approach and is a facile methodology with which effective intracellular antibodies can be obtained. During the development of the IAC technology, consensus immunoglobulin variable frameworks were identified which can form the basis of intrabody libraries for direct screening. In this paper, we describe the de novo synthesis of intrabody libraries based on the IAC consensus sequence. The procedure comprises in vitro production of a single antibody gene fragment from oligonucleotides and diversification of CDRs of the immunoglobulin variable domain by mutagenic PCR. Completely de novo intrabody libraries can be rapidly generated in vitro by these approaches. As an example, a single immunoglobulin VH domain intrabody library was screened directly in yeast with an oncogenic BCR-ABL antigen bait and distinct antigen binders were isolated illustrating the functional utility of the library. This second generation IAC approach (IAC2) has many practical advantages, in particular the ability to isolate intrabodies by direct genetic selection, which obviates the need for in vitro production of antigen for pre-selection of antibody fragments.

Indexed as

Peptide LibraryAmino Acid SequenceAnimalsAntibodiesBase SequenceCloning, MolecularComplementarity Determining RegionsHumansMolecular Sequence DataMutationSequence Homology, Amino AcidAntibodiesComplementarity Determining RegionsPeptide Library

Identifiers

PMID12595572
PMCPMC149845
OpenAlexW2135670700

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

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.