Evidence map›Paper›PMID 30150415›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2018

Molecular strategy for blocking isopeptide bond formation in nascent pilin proteins.

Jaime Andrés Rivas-Pardo, Carmen L Badilla, Rafael Tapia-Rojo, Álvaro Alonso-Caballero, Julio M Fernández

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
1.7field-weighted citation impact, top 15% 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

10 citing papers in PubMed, 35 citations in OpenAlex.

  1. A global survey of intramolecular isopeptide bonds.Protein science : a publication of the Protein Society · 2025
    Article
  2. Modulating Antimicrobial Activity and Structure of the Peptide Esc(1-21) via Site-Specific Isopeptide Bond Formation.Journal of peptide science : an official publication of the European Peptide Society · 2025
    Article
  3. Article
  4. De Novo Design of Proteins for Autocatalytic Isopeptide Bond Formation.Journal of the American Chemical Society · 2025
    Article
  5. Article
  6. A tethered ligand assay to probe SARS-CoV-2:ACE2 interactions.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  7. Article
  8. Review
  9. Article
  10. Frontiers in microbiology · 2021
    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

5 authors at 1 institution in 1 country.

Jaime Andrés Rivas-PardoDepartment of Biological Sciences, Columbia University, NY 10027 rivas.pardo@gmail.com jfernandez@columbia.edu.ORCID 0000-0002-8304-3238
Carmen L BadillaDepartment of Biological Sciences, Columbia University, NY 10027.
Rafael Tapia-RojoDepartment of Biological Sciences, Columbia University, NY 10027.
Álvaro Alonso-CaballeroDepartment of Biological Sciences, Columbia University, NY 10027.
Julio M FernándezDepartment of Biological Sciences, Columbia University, NY 10027 rivas.pardo@gmail.com jfernandez@columbia.edu.
Columbia University · US

Funding

Single Molecule Studies of Titin ElasticityR01HL061228 · NHLBI · MAYO CLINIC COLL OF MEDICINE, ROCHESTER · PI FERNANDEZ, JULIO M · 1999 to 2017
$7.4M
Nanomechanics of bacterial adhesionR01GM116122 · NIGMS · COLUMBIA UNIV NEW YORK MORNINGSIDE · PI FERNANDEZ, JULIO M · 2015 to 2018
$1.4M
NHLBI NIH HHS R01 HL061228NIGMS NIH HHS R01 GM116122
6 · The paper itself

Abstract

Bacteria anchor to their host cells through their adhesive pili, which must resist the large mechanical stresses induced by the host as it attempts to dislodge the pathogens. The pili of gram-positive bacteria are constructed as a single polypeptide made of hundreds of pilin repeats, which contain intramolecular isopeptide bonds strategically located in the structure to prevent their unfolding under force, protecting the pilus from degradation by extant proteases and oxygen radicals. Here, we demonstrate the design of a short peptide that blocks the formation of the isopeptide bond present in the pilin Spy0128 from the human pathogen

Indexed as

Protein FoldingAnti-Bacterial AgentsFimbriae ProteinsHumansPeptidesProtein DomainsProtein StabilityStreptococcus pyogenesAnti-Bacterial AgentsFimbriae ProteinsPeptidesantibiotic peptideisopeptide bondprotein foldingprotein mechanicssingle-molecule force spectroscopy

Identifiers

PMID30150415
PMCPMC6140542
OpenAlexW2888955436

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.