Evidence map›Paper›PMID 34692637›Full record

ReviewFrontiers in chemistry2021

Mapping, Structure and Modulation of PPI.

Elisa Martino, Sara Chiarugi, Francesco Margheriti, Gianpiero Garau

Open access · goldAbstract readReview
In one paragraph

Review in Frontiers in chemistry, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.

0numbers the graph read from it
0cells of the map it votes in
35citing papers in PubMed
3.8field-weighted citation impact, top 5% 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

35 citing papers in PubMed, 62 citations in OpenAlex.

  1. Article
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  18. Estrogen: the forgotten player in metaflammation.Frontiers in pharmacology · 2024
    Review
  19. Potential candidates from a functional foodFrontiers in endocrinology · 2024
    Article
  20. 3International journal of molecular sciences · 2023
    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

4 authors at 3 institutions in 1 country.

Elisa MartinoLaboratorio NEST, Scuola Normale Superiore, Pisa, Italy.
Sara ChiarugiLaboratorio NEST, Scuola Normale Superiore, Pisa, Italy.
Francesco MargheritiLaboratorio NEST, Scuola Normale Superiore, Pisa, Italy.
Gianpiero GarauBioStructures Lab, Istituto Italiano di Tecnologia (IIT@NEST), Pisa, Italy.
Scuola Normale Superiore · ITItalian Institute of Technology · ITNational Enterprise for NanoScience and NanoTechnology · IT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Because of the key relevance of protein-protein interactions (PPI) in diseases, the modulation of protein-protein complexes is of relevant clinical significance. The successful design of binding compounds modulating PPI requires a detailed knowledge of the involved protein-protein system at molecular level, and investigation of the structural motifs that drive the association of the proteins at the recognition interface. These elements represent hot spots of the protein binding free energy, define the complex lifetime and possible modulation strategies. Here, we review the advanced technologies used to map the PPI involved in human diseases, to investigate the structure-function features of protein complexes, and to discover effective ligands that modulate the PPI for therapeutic intervention.

Indexed as

ligand interaction5modulation strategies3PPI in disease1protein-protein4target structure2

Identifiers

PMID34692637
PMCPMC8529325
OpenAlexW3207244478

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.