Evidence map›Paper›PMID 42569891›Full record

ArticleCurrent protocols2026

Profiling Protein-Peptide Interactions by Yeast Surface Display.

Joseph D Hurley, Andrew C Kruse

Abstract read
In one paragraph

Article in Current protocols, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing 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

1 citing paper in PubMed.

  1. 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

2 authors.

Joseph D HurleyDepartment of Biological Chemistry and Molecular Pharmacology, Blavatnik Institute, Harvard Medical School, Boston, MA, USA.
Andrew C KruseDepartment of Biological Chemistry and Molecular Pharmacology, Blavatnik Institute, Harvard Medical School, Boston, MA, USA.

Funding

Molecular, Cellular, & Developmental Dynamics PhD ProgramT32GM007226 · NIGMS · HARVARD UNIVERSITY (MEDICAL SCHOOL) · PI VAN VACTOR, DAVID L. · 1985 to 2021
$14.4M
Making antibody generation rapid, scalable, and democratic through machine learning and continuous evolutionR01CA260415 · NCI · UNIVERSITY OF CALIFORNIA-IRVINE · PI KRUSE, ANDREW, LIU, CHANG C · 2020 to 2024
$8.4M
NCI NIH HHS R01 CA260415NIGMS NIH HHS T32 GM007226NIH HHS
6 · The paper itself

Abstract

Protein-peptide interactions are central to many biological processes and form the basis for many techniques in basic research and therapeutic discovery. A common research challenge is to identify specific peptide ligands or binding motifs where no initial hit is known. Here we describe a protocol for discovering protein-binding peptides using a very large, target-agnostic yeast surface display library containing approximately 6.1 × 10

Indexed as

Cell Surface Display TechniquesPeptidesProteinsSaccharomyces cerevisiaeFlow CytometryHigh-Throughput Nucleotide SequencingPeptide LibraryProtein BindingPeptide LibraryPeptidesProteinsflow cytometryfluorescence‐activated cell sortingmagnetic‐activated cell sortingnext‐generation sequencingPeptidesprotein‐peptide interactionsyeast surface display

Identifiers

PMID42569891
PMCPMC13452087

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.