Evidence map›Paper›PMID 38062770›Full record

ArticleJournal of the American Chemical Society2023

Conformations of Macrocyclic Peptides Sampled by Nuclear Magnetic Resonance: Models for Cell-Permeability.

Simon H Rüdisser, Emmanuel Matabaro, Lukas Sonderegger, Peter Güntert, Markus Künzler, Alvar D Gossert

Abstract read
In one paragraph

Article in Journal of the American Chemical Society, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing 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

8 citing papers in PubMed.

  1. Pulse Programme Considerations for Quantitative NOE Analysis.Magnetic resonance in chemistry : MRC · 2026
    Article
  2. Article
  3. Article
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  6. Review
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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

6 authors.

Simon H RüdisserDepartment of Biology, ETH Zürich, Zürich 8093, Switzerland.ORCID 0000-0002-1107-6196
Emmanuel MatabaroDepartment of Biology, ETH Zürich, Zürich 8093, Switzerland.
Lukas SondereggerDepartment of Biology, ETH Zürich, Zürich 8093, Switzerland.
Peter GüntertDepartment of Chemistry and Applied Biosciences, ETH Zürich, Zürich 8093, Switzerland.ORCID 0000-0002-2911-7574
Markus KünzlerDepartment of Biology, ETH Zürich, Zürich 8093, Switzerland.ORCID 0000-0003-1275-0629
Alvar D GossertDepartment of Biology, ETH Zürich, Zürich 8093, Switzerland.ORCID 0000-0001-7732-495X

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The biological activities and pharmacological properties of peptides and peptide mimetics are determined by their conformational states. Therefore, a detailed understanding of the conformational landscape is crucial for rational drug design. Nuclear magnetic resonance (NMR) is the only method for structure determination in solution. However, it remains challenging to determine the structures of peptides using NMR because of very weak nuclear Overhauser effects (NOEs), the semiquantitative nature of the rotating frame Overhauser effect (ROE), and the low number of NOEs/ROEs in

Indexed as

Magnetic Resonance ImagingPeptidesCyclosporineMagnetic Resonance SpectroscopyProtein ConformationSolventsCyclosporinePeptidesSolvents

Identifiers

PMID38062770
PMCPMC10739998

What OpenQuestion holds

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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.