Evidence map›Paper›PMID 37315694›Full record

ArticleJournal of controlled release : official journal of the Controlled Release Society2023

Fibronectin-targeted FUD and PEGylated FUD peptides for fibrotic diseases.

Hye Jin Lee, Bianca R Tomasini-Johansson, Nikesh Gupta, Glen S Kwon

Open access · greenAbstract read
In one paragraph

Article in Journal of controlled release : official journal of the Controlled Release Society, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing papers in PubMed
2.3field-weighted citation impact, top 11% 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

6 citing papers in PubMed, 10 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Review
  5. [Science advances · 2024
    Article
  6. Mechanotransductive receptorFrontiers in molecular biosciences · 2023
    Review
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

4 authors at 1 institution in 1 country.

Hye Jin LeePharmaceutical Sciences Division, School of Pharmacy, University of Wisconsin - Madison, 777 Highland Avenue, Madison, WI 53705, USA.
Bianca R Tomasini-JohanssonDepartment of Cell and Regenerative Biology, School of Medicine and Public Health, University of Wisconsin - Madison, 1111 Highland Avenue, WIMRII, Madison, WI 53705, USA.
Nikesh GuptaPharmaceutical Sciences Division, School of Pharmacy, University of Wisconsin - Madison, 777 Highland Avenue, Madison, WI 53705, USA.
Glen S KwonPharmaceutical Sciences Division, School of Pharmacy, University of Wisconsin - Madison, 777 Highland Avenue, Madison, WI 53705, USA; Carbone Cancer Center, University of Wisconsin - Madison, 600 Highland Avenue, Madison, WI 53705, USA. Electronic address: glen.kwon@wisc.edu.
University of Wisconsin–Madison · US

Funding

Oligo(lactic acid)n-Prodrug Nanomedicines for Combination TherapyR01CA257837 · NCI · UNIVERSITY OF WISCONSIN-MADISON · PI KWON, GLEN S. · 2021 to 2024
$1.4M
Direct therapeutic intervention of the tumor microenvironment with a potent inhibitor of fibronectin assemblyR21CA252579 · NCI · UNIVERSITY OF WISCONSIN-MADISON · PI KWON, GLEN S., PONIK, SUZANNE MARIE · 2021 to 2022
$386k
NCI NIH HHS R01 CA257837NCI NIH HHS R21 CA252579
6 · The paper itself

Abstract

Tissue fibrosis is characterized by excessive deposition of extracellular matrix (ECM) molecules. Fibronectin (FN) is a glycoprotein found in the blood and tissues, a key player in the assembly of ECM through interaction with cellular and extracellular components. Functional Upstream Domain (FUD), a peptide derived from an adhesin protein of bacteria, has a high binding affinity for the N-terminal 70-kDa domain of FN that plays a crucial role in FN polymerization. In this regard, FUD peptide has been characterized as a potent inhibitor of FN matrix assembly, reducing excessive ECM accumulation. Furthermore, PEGylated FUD was developed to prevent rapid elimination of FUD and enhance its systemic exposure in vivo. Herein, we summarize the development of FUD peptide as a potential anti-fibrotic agent and its application in experimental fibrotic diseases. In addition, we discuss how modification of the FUD peptide via PEGylation impacts pharmacokinetic profiles of the FUD peptide and can potentially contribute to anti-fibrosis therapy.

Indexed as

Adhesins, BacterialFibronectinsPeptidesExtracellular MatrixFibrosisPolyethylene GlycolsAdhesins, BacterialFibronectinsFUD peptidePeptidesPolyethylene GlycolsExtracellular matrixFibronectinFibrosisFunctional upstream domainPEGylation

Identifiers

PMID37315694
PMCPMC10527082
OpenAlexW4380730258

What OpenQuestion holds

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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.