Evidence map›Paper›PMID 36494904›Full record

ArticleJournal of peptide science : an official publication of the European Peptide Society2023

N

Lindsey O Calabretta, Jinyi Yang, Ronald T Raines

Abstract read
In one paragraph

Article in Journal of peptide science : an official publication of the European Peptide Society, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing 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

4 citing papers in PubMed.

  1. Reductive Methylation: An Alternative to Lysine → Arginine Mutagenesis.Journal of peptide science : an official publication of the European Peptide Society · 2026
    Article
  2. Article
  3. Article
  4. 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

3 authors.

Lindsey O CalabrettaDepartment of Chemistry, Massachusetts Institute of Technology, Cambridge, Massachusetts, USA.ORCID https://orcid.org/0000-0002-5747-5803
Jinyi YangDepartment of Chemistry, Massachusetts Institute of Technology, Cambridge, Massachusetts, USA.ORCID https://orcid.org/0000-0002-9694-1838
Ronald T RainesDepartment of Chemistry, Massachusetts Institute of Technology, Cambridge, Massachusetts, USA.ORCID https://orcid.org/0000-0001-7164-1719

Funding

STRUCTURE--FUNCTION ANALYSIS OF RIBONUCLEASE AR01GM044783 · NIGMS · UNIVERSITY OF WISCONSIN-MADISON · PI RAINES, RONALD T · 1990 to 2021
$7.1M
NIGMS NIH HHS R01 GM044783NIH HHS R01 GM044783
6 · The paper itself

Abstract

The field of cell-penetrating peptides is dominated by the use of oligomers of arginine residues. Octanol-water partitioning in the presence of an anionic lipid is a validated proxy for cell-penetrative efficacy. Here, we add one, two, or three N-methyl groups to Ac-Arg-NH

Indexed as

Cell-Penetrating PeptidesArginineLipidsMethylationOctanolsWaterArginineCell-Penetrating PeptidesLipidsOctanolsWaterguanidino groupoctanol-water partitioningpeptoidtopological polar surface area

Identifiers

PMID36494904
PMCPMC10073267

What OpenQuestion holds

Textmetadata
LicenceTDM
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.