Evidence map›Paper›PMID 30551606›Full record

ReviewBiomedicines2018

Structural Features and Binding Modes of Thioether-Cyclized Peptide Ligands.

Manuel E Otero-Ramirez, Toby Passioura, Hiroaki Suga

Abstract readReview
In one paragraph

Review in Biomedicines, 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
–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

10 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Review
  7. Article
  8. Cyclic peptides can engage a single binding pocket through highly divergent modes.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  9. Article
  10. 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.

Manuel E Otero-RamirezDepartment of Chemistry, Graduate School of Science, The University of Tokyo, 7-3-1 Hongo, 113-0033 Tokyo, Bunkyo-ku, Japan. motero@chem.s.u-tokyo.ac.jp.
Toby PassiouraDepartment of Chemistry, Graduate School of Science, The University of Tokyo, 7-3-1 Hongo, 113-0033 Tokyo, Bunkyo-ku, Japan. toby@chem.s.u-tokyo.ac.jp.ORCID 0000-0002-6089-5067
Hiroaki SugaDepartment of Chemistry, Graduate School of Science, The University of Tokyo, 7-3-1 Hongo, 113-0033 Tokyo, Bunkyo-ku, Japan. hsuga@chem.s.u-tokyo.ac.jp.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Macrocyclic peptides are an emerging class of bioactive compounds for therapeutic use. In part, this is because they are capable of high potency and excellent target affinity and selectivity. Over the last decade, several biochemical techniques have been developed for the identification of bioactive macrocyclic peptides, allowing for the rapid isolation of high affinity ligands to a target of interest. A common feature of these techniques is a general reliance on thioether formation to effect macrocyclization. Increasingly, the compounds identified using these approaches have been subjected to x-ray crystallographic analysis bound to their respective targets, providing detailed structural information about their conformation and mechanism of target binding. The present review provides an overview of the target bound thioether-closed macrocyclic peptide structures that have been obtained to date.

Indexed as

crystallographymacrocyclicpeptide

Identifiers

PMID30551606
PMCPMC6316662

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.