Evidence map›Paper›PMID 39328775›Full record

ArticleAdvanced nanobiomed research2024

A Multivalent DNA Nanoparticle/Peptide Hybrid Molecular Modality for the Modulation of Protein-Protein Interactions in the Tumor Microenvironment.

Jessica A Roman, Michael Y Girgis, Rocìo S Prisby, Robyn P Araujo, Paul Russo, Esra Oktay, Alessandra Luchini, Lance A Liotta, Remi Veneziano, Amanda Haymond

Abstract read
In one paragraph

Article in Advanced nanobiomed research, 2024. 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. Laser capture microdissection.Nature reviews. Methods primers · 2025
    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

10 authors.

Jessica A RomanCenter for Applied Proteomics and Molecular Medicine, 19020 George Mason Circle, Manassas, VA, 20110, USA.
Michael Y GirgisDepartment of Bioengineering, 19020 George Mason Circle, Manassas, VA, 20110, USA.
Rocìo S PrisbyCenter for Applied Proteomics and Molecular Medicine, 19020 George Mason Circle, Manassas, VA, 20110, USA.
Robyn P AraujoSchool of Mathematical Sciences, Queensland University of Technology, Brisbane, Queensland, Australia.
Paul RussoCenter for Applied Proteomics and Molecular Medicine, 19020 George Mason Circle, Manassas, VA, 20110, USA.
Esra OktayDepartment of Bioengineering, 19020 George Mason Circle, Manassas, VA, 20110, USA.
Alessandra LuchiniCenter for Applied Proteomics and Molecular Medicine, 19020 George Mason Circle, Manassas, VA, 20110, USA.
Lance A LiottaCenter for Applied Proteomics and Molecular Medicine, 19020 George Mason Circle, Manassas, VA, 20110, USA.
Remi VenezianoDepartment of Bioengineering, 19020 George Mason Circle, Manassas, VA, 20110, USA.
Amanda HaymondCenter for Applied Proteomics and Molecular Medicine, 19020 George Mason Circle, Manassas, VA, 20110, USA.

Funding

New Hybrid Molecular Modalities Comprised of DNA-Origami and Interfering Peptides as Inhibitors of Protein-Protein InteractionsR21CA251015 · NCI · GEORGE MASON UNIVERSITY · PI STILL, AMANDA NICOLE HAYMOND · 2021 to 2023
$522k
NCI NIH HHS R21 CA251015
6 · The paper itself

Abstract

Despite success in the treatment of some blood cancers and melanoma, positive response to immunotherapies remains disappointingly low in the treatment of solid tumors. The context of the molecular crosstalk within the tumor microenvironment can result in dysfunctional immune cell activation, leading to tumor tolerance and progression. Although modulating these protein-protein interactions (PPIs) is vital for appropriate immune cell activation and recognition, targeting nonenzymatic PPIs has proven to be fraught with challenges. To address this, we introduce a synthetic, multivalent molecular modality comprised of small interfering peptides precisely hybridized to a semi-rigid DNA scaffold. Herein, we describe a prototype of this modality that targets the IL-33/ST2 signaling axis, which is associated with tumor tolerance and immunotherapy treatment failure. Using peptides that mimic the specific high energy "hotspot" residues with which the IL-33/ST2 co-receptor, IL-1RAcP, interacts with the initial binary complex, we show this platform to effectively bind IL-33/ST2 with a

Indexed as

DNA nanoparticlesinteraction modulatorsmultivalencyprotein-protein interactions

Identifiers

PMID39328775
PMCPMC11423619

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Registered trials

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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.