Evidence map›Paper›PMID 30307621›Full record

ReviewMedicinal research reviews2019

Recent structural advances in constrained helical peptides.

Kornelia J Skowron, Thomas E Speltz, Terry W Moore

Open access · greenAbstract readReview
In one paragraph

Review in Medicinal research reviews, 2019. 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
1.2field-weighted citation impact, top 21% 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, 31 citations in OpenAlex.

  1. Article
  2. Review
  3. Review
  4. Article
  5. Peptide Stapling Applied to Antimicrobial Peptides.Antibiotics (Basel, Switzerland) · 2023
    Review
  6. Review
  7. Review
  8. Article
  9. Photochemical Methods for Peptide Macrocyclisation.Chemistry (Weinheim an der Bergstrasse, Germany) · 2021
    Review
  10. 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

3 authors at 2 institutions in 1 country.

Kornelia J SkowronDepartment of Medicinal Chemistry and Pharmacognosy, College of Pharmacy, University of Illinois at Chicago, Chicago, Illinois.ORCID 0000-0002-0846-6134
Thomas E SpeltzDepartment of Medicinal Chemistry and Pharmacognosy, College of Pharmacy, University of Illinois at Chicago, Chicago, Illinois.ORCID 0000-0001-9551-9080
Terry W MooreDepartment of Medicinal Chemistry and Pharmacognosy, College of Pharmacy, University of Illinois at Chicago, Chicago, Illinois.ORCID 0000-0002-5410-306X
University of Illinois Chicago · USUniversity of Illinois Urbana-Champaign · US

Funding

Research Training in Natural Product Complementary and Integrative HealthT32AT007533 · NCCIH · UNIVERSITY OF ILLINOIS AT CHICAGO · PI Joanna E Burdette, JIMMY ORJALA · 2013 to 2026
$4.3M
NCCIH NIH HHS T32 AT007533
6 · The paper itself

Abstract

Given the ubiquity of the ⍺-helix in the proteome, there has been much research in developing mimics of ⍺-helices, and most of this study has been toward developing protein-protein interaction inhibitors. A common strategy for mimicking ⍺-helices has been through the use of constrained, helical peptides. The addition of a constraint typically provides for conformational and proteolytic stability and, in some cases, cell permeability. Some of the most well-known strategies included are lactam formation and hydrocarbon "stapling." Beyond those strategies, there have been many recent advances in developing constrained peptides. The purpose of this review is to highlight recent advances in the development of new helix-stabilizing technologies, constraint diversification strategies, tether diversification strategies, and combination strategies that create new bicyclic helical peptides.

Indexed as

AnimalsChemistry, PharmaceuticalCross-Linking ReagentsCysteineGlucuronatesHumansHydrocarbonsIsocyanatesLactamsMethionineNitrogenPeptidesPermeabilityProtein ConformationProteomePyrazolesCross-Linking ReagentsCysteineGlucuronatesHydrocarbonsIsocyanatesLactamsMethionineNitrogenPeptidesProteomePyrazolesSelenocysteineSulfhydryl Compoundsalpha helixhelical peptidespeptide chemistryprotein-protein interactions

Identifiers

PMID30307621
PMCPMC7395366
OpenAlexW2897833298

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.