Evidence map›Paper›PMID 9246635›Full record

ArticleJournal of protein chemistry1997

A phage display technique for a fast, sensitive, and systematic investigation of protein-protein interactions.

S Rossenu, D Dewitte, J Vandekerckhove, C Ampe

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Article in Journal of protein chemistry, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
–field-weighted citation impact
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

4 citing papers in PubMed.

  1. Article
  2. Review
  3. Article
  4. Article
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

4 authors.

S RossenuFlanders Interuniversity Institute for Biotechnology, Department of Biochemistry, Faculty of Medicine, University of Ghent, Belgium.
D Dewitte
J Vandekerckhove
C Ampe

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Phage display is a technique in which a foreign protein or peptide is presented at the surface of a (filamentous) bacteriophage. This system, developed by Smith [(1985), Science 228, 1315-1317], was originally used to create large libraries of antibodies for the purpose of selecting those that strongly bound a particular antigen. More recently it was also employed to present peptides, domains of proteins, or intact proteins at the surface of phages, again to identify high-affinity interactions with ligands. Here we want to illustrate the use of phage display, in combination with PCR saturation mutagenesis, for the study of protein-protein interactions. Rather than selecting for mutants having high affinity, we systematically investigate the binding of every variant with its natural ligand. Via a modified ELISA we can calculate a relative affinity. As a model system we chose to display thymosin beta 4 on the phage surface in order to study its interaction with actin.

Indexed as

BacteriophagesActinsAmino Acid SequenceBinding SitesEnzyme-Linked Immunosorbent AssayKineticsMolecular Sequence DataMutagenesisMutationPolymerase Chain ReactionProteinsSensitivity and SpecificityThymosinThymosin beta(4)ActinsProteinsThymosinThymosin beta(4)

Identifiers

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.