Evidence map›Paper›PMID 32435424›Full record

ArticleACS medicinal chemistry letters2020

HOPPI-NMR: Hot-Peptide-Based Screening Assay for Inhibitors of Protein-Protein Interactions by NMR.

Diego Brancaccio, Salvatore Di Maro, Linda Cerofolini, Stefano Giuntini, Marco Fragai, Claudio Luchinat, Stefano Tomassi, Antonio Limatola, Pasquale Russomanno, Francesco Merlino and 2 more

Open access · greenAbstract read
In one paragraph

Article in ACS medicinal chemistry letters, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
0.3field-weighted citation impact, top 44% 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

3 citing papers in PubMed, 5 citations in OpenAlex.

  1. Article
  2. Applications of Solution NMR in Drug Discovery.Molecules (Basel, Switzerland) · 2021
    Review
  3. 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

12 authors at 4 institutions in 2 countries.

Diego BrancaccioDepartment of Pharmacy, University of Naples "Federico II", 80131 Naples, Italy.
Salvatore Di MaroDISTABIF, University of Campania "Luigi Vanvitelli", 81100 Caserta, Italy.
Linda CerofoliniCERM, University of Florence, 50019 Sesto Fiorentino, Italy.
Stefano GiuntiniCERM, University of Florence, 50019 Sesto Fiorentino, Italy.
Marco FragaiCERM, University of Florence, 50019 Sesto Fiorentino, Italy.
Claudio LuchinatCERM, University of Florence, 50019 Sesto Fiorentino, Italy.
Stefano TomassiDepartment of Pharmacy, University of Naples "Federico II", 80131 Naples, Italy.
Antonio LimatolaDepartment of Biology, Stanford University, Stanford, California 94305-5430, United States.
Pasquale RussomannoDepartment of Pharmacy, University of Naples "Federico II", 80131 Naples, Italy.
Francesco MerlinoDepartment of Pharmacy, University of Naples "Federico II", 80131 Naples, Italy.
Ettore NovellinoDepartment of Pharmacy, University of Naples "Federico II", 80131 Naples, Italy.
Alfonso CarotenutoDepartment of Pharmacy, University of Naples "Federico II", 80131 Naples, Italy.
University of Naples Federico II · ITInteruniversity Consortium for Magnetic Resonance · ITStanford University · USUniversity of Campania "Luigi Vanvitelli" · IT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Protein-protein interactions (PPIs) contribute to the onset and/or progression of several diseases, especially cancer, and this discovery has paved the way for considering disruption of the PPIs as an attractive anti-tumor strategy. In this regard, simple and efficient biophysical methods for detecting the interaction of the inhibitors with the protein counterpart are still in high demand. Herein, we describe a convenient NMR method for the screening of putative PPI inhibitors based on the use of "hot peptides" (HOPPI-NMR). As a case study, HOPPI-NMR was successful applied to the well-known p53/MDM2 system. Our outcomes highlight the main advantages of the method, including the use of a small amount of unlabeled proteins, the minimization of the risk of protein aggregation, and the ability to identify weak binders. The last leaves open the possibility for application of HOPPI-NMR in tandem with fragment-based drug discovery as a valid strategy for the identification of novel chemotypes acting as PPI inhibitors.

Identifiers

PMID32435424
PMCPMC7236535
OpenAlexW3008047893

What OpenQuestion holds

Textmetadata
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.