Evidence map›Paper›PMID 29605911›Full record

ArticleMethods in molecular biology (Clifton, N.J.)2018

Characterizing Protein-Protein Interactions Using Deep Sequencing Coupled to Yeast Surface Display.

Angelica V Medina-Cucurella, Timothy A Whitehead

Abstract read
In one paragraph

Article in Methods in molecular biology (Clifton, N.J.), 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing 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

29 citing papers in PubMed.

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  9. Retrospective SARS-CoV-2 human antibody development trajectories are largely sparse and permissive.Proceedings of the National Academy of Sciences of the United States of America · 2025
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  17. Incorporating, Quantifying, and Leveraging Noncanonical Amino Acids in Yeast.Methods in molecular biology (Clifton, N.J.) · 2022
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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

2 authors.

Angelica V Medina-CucurellaDepartment of Chemical Engineering and Materials Science, Michigan State University, East Lansing, MI, USA.
Timothy A WhiteheadDepartment of Chemical Engineering and Materials Science, Michigan State University, East Lansing, MI, USA. taw@egr.msu.edu.

Funding

Plant Biotechnology for Health and SustainabilityT32GM110523 · NIGMS · MICHIGAN STATE UNIVERSITY · PI LAST, ROBERT LOUIS · 2014 to 2023
$2.2M
NIGMS NIH HHS T32 GM110523
6 · The paper itself

Abstract

In this chapter, we discuss a method to determine the affinity and specificity of nearly all single-point mutants for a full-length protein binder. This method combines deep sequencing, comprehensive mutagenesis, yeast surface display, and fluorescence-activated cell sorting. This approach has been used to study sequence-function relationships for protein-protein interactions. The data can be used to determine the fine conformational epitope on the protein binder.

Indexed as

Protein Interaction Domains and MotifsBinding SitesCell Adhesion MoleculesCell SeparationEpitope MappingEpitopesFlow CytometryHigh-Throughput Nucleotide SequencingMutagenesisPeptide LibraryProtein BindingSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsCell Adhesion MoleculesEpitopesPeptide LibrarySaccharomyces cerevisiae ProteinsConformational epitope mappingDeep sequencingFACSNicking mutagenesisYeast surface display

Identifiers

PMID29605911
PMCPMC6664802

What OpenQuestion holds

Textmetadata
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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.