Evidence map›Paper›PMID 33984330›Full record

ArticleThe Journal of biological chemistry

Unlocking the PIP-box: A peptide library reveals interactions that drive high-affinity binding to human PCNA.

Aimee J Horsfall, Beth A Vandborg, Wioleta Kowalczyk, Theresa Chav, Denis B Scanlon, Andrew D Abell, John B Bruning

Open access · goldAbstract read
In one paragraph

Article in The Journal of biological chemistry. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
1.1field-weighted citation impact, top 24% 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

16 citing papers in PubMed, 19 citations in OpenAlex.

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  7. X-ray crystal structure of proliferating cell nuclear antigen 1 from Aeropyrum pernix.Acta crystallographica. Section F, Structural biology communications · 2024
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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

7 authors at 2 institutions in 1 country.

Aimee J HorsfallARC Centre of Excellence for Nanoscale BioPhotonics, Institute of Photonics and Advanced Sensing, School of Physical Sciences, The University of Adelaide, Adelaide, South Australia, Australia.
Beth A VandborgInstitute of Photonics and Advanced Sensing, School of Biological Sciences, The University of Adelaide, Adelaide, South Australia, Australia.
Wioleta KowalczykCSIRO Manufacturing, Clayton South, Victoria, Australia.
Theresa ChavARC Centre of Excellence for Nanoscale BioPhotonics, Institute of Photonics and Advanced Sensing, School of Physical Sciences, The University of Adelaide, Adelaide, South Australia, Australia.
Denis B ScanlonARC Centre of Excellence for Nanoscale BioPhotonics, Institute of Photonics and Advanced Sensing, School of Physical Sciences, The University of Adelaide, Adelaide, South Australia, Australia.
Andrew D AbellARC Centre of Excellence for Nanoscale BioPhotonics, Institute of Photonics and Advanced Sensing, School of Physical Sciences, The University of Adelaide, Adelaide, South Australia, Australia. Electronic address: andrew.abell@adelaide.edu.au.
John B BruningInstitute of Photonics and Advanced Sensing, School of Biological Sciences, The University of Adelaide, Adelaide, South Australia, Australia. Electronic address: john.bruning@adelaide.edu.au.
The University of Adelaide · AUCSIRO Manufacturing · AU

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The human sliding clamp, Proliferating Cell Nuclear Antigen (hPCNA), interacts with over 200 proteins through a conserved binding motif, the PIP-box, to orchestrate DNA replication and repair. It is not clear how changes to the features of a PIP-box modulate protein binding and thus how they fine-tune downstream processes. Here, we present a systematic study of each position within the PIP-box to reveal how hPCNA-interacting peptides bind with drastically varied affinities. We synthesized a series of 27 peptides derived from the native protein p21 with small PIP-box modifications and another series of 19 peptides containing PIP-box binding motifs from other proteins. The hPCNA-binding affinity of all peptides, characterized as K

Indexed as

Binding SitesHumansModels, MolecularPeptide LibraryPeptidesProliferating Cell Nuclear AntigenProtein BindingProtein Interaction MapsProteinsPCNA protein, humanPeptide LibraryPeptidesProliferating Cell Nuclear AntigenProteinscrystallographypeptidesproliferating cell nuclear antigen (PCNA)structural biologysurface plasmon resonance (SPR)

Identifiers

PMID33984330
PMCPMC8191301
OpenAlexW3160642445

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.