Evidence map›Paper›PMID 39705005›Full record

ArticleACS synthetic biology2025

Extracellular Peptide-Ligand Dimerization Actuator Receptor Design for Reversible and Spatially Dosed 3D Cell-Material Communication.

Matthias Recktenwald, Ritankar Bhattacharya, Mohammed Mehdi Benmassaoud, James MacAulay, Varun M Chauhan, Leah Davis, Evan Hutt, Peter A Galie, Mary M Staehle, Nichole M Daringer and 2 more

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in ACS synthetic biology, 2025. 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

12 authors.

Matthias RecktenwaldDepartment of Biomedical Engineering, Rowan University, 201 Mullica Hill Rd, Glassboro, New Jersey 08028, United States.
Ritankar BhattacharyaDepartment of Chemical Engineering, Auburn University, Auburn, Alabama 36849, United States.
Mohammed Mehdi BenmassaoudDepartment of Biomedical Engineering, Rowan University, 201 Mullica Hill Rd, Glassboro, New Jersey 08028, United States.
James MacAulayDepartment of Biomedical Engineering, Rowan University, 201 Mullica Hill Rd, Glassboro, New Jersey 08028, United States.
Varun M ChauhanDepartment of Chemical Engineering, Auburn University, Auburn, Alabama 36849, United States.
Leah DavisDepartment of Biomedical Engineering, Rowan University, 201 Mullica Hill Rd, Glassboro, New Jersey 08028, United States.
Evan HuttDepartment of Biomedical Engineering, Rowan University, 201 Mullica Hill Rd, Glassboro, New Jersey 08028, United States.
Peter A GalieDepartment of Biomedical Engineering, Rowan University, 201 Mullica Hill Rd, Glassboro, New Jersey 08028, United States.
Mary M StaehleDepartment of Biomedical Engineering, Rowan University, 201 Mullica Hill Rd, Glassboro, New Jersey 08028, United States.ORCID 0000-0001-6708-9378
Nichole M DaringerDepartment of Biomedical Engineering, Rowan University, 201 Mullica Hill Rd, Glassboro, New Jersey 08028, United States.
Robert J PantazesDepartment of Chemical Engineering, Auburn University, Auburn, Alabama 36849, United States.ORCID 0000-0002-0994-007X
Sebastián L VegaDepartment of Biomedical Engineering, Rowan University, 201 Mullica Hill Rd, Glassboro, New Jersey 08028, United States.ORCID 0000-0002-7669-1552

Funding

The Development and Experimental Verification of Computational Methods to Design and Predict the Properties of Therapeutic ProteinsR35GM138220 · NIGMS · AUBURN UNIVERSITY AT AUBURN · PI PANTAZES, ROBERT J · 2020 to 2024
$1.7M
NIGMS NIH HHS R35 GM138220NIH HHS MIRA R35GM138220
6 · The paper itself

Abstract

Transmembrane receptors that endow mammalian cells with the ability to sense and respond to biomaterial-bound ligands will prove instrumental in bridging the fields of synthetic biology and biomaterials. Materials formed with thiol-norbornene chemistry are amenable to thiol-peptide patterning, and this study reports the rational design of synthetic receptors that reversibly activate cellular responses based on peptide-ligand recognition. This transmembrane receptor platform, termed Extracellular Peptide-ligand Dimerization Actuator (EPDA), consists of stimulatory or inhibitory receptor pairs that come together upon extracellular peptide dimer binding with corresponding monobody receptors. Intracellularly,

Indexed as

Cell CommunicationPeptidesGreen Fluorescent ProteinsHumansLigandsNorbornanesGreen Fluorescent ProteinsLigandsNorbornanesPeptidesbiomaterialscomputational protein designpeptidessynthetic biologytransmembrane receptors

Identifiers

PMID39705005
PMCPMC12281622

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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.