Evidence map›Paper›PMID 39394908›Full record

ReviewJournal of molecular recognition : JMR2025

Toward Understanding the Mechanism of Client-Selective Small Molecule Inhibitors of the Sec61 Translocon.

Nidhi Sorout, Volkhard Helms

Erratum issuedAbstract readReview
In one paragraph

Review in Journal of molecular recognition : JMR, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing 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

1 citing paper in PubMed.

  1. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

2 authors.

Nidhi SoroutCenter for Bioinformatics, Saarland University, Saarbrücken, Saarland, Germany.
Volkhard HelmsCenter for Bioinformatics, Saarland University, Saarbrücken, Saarland, Germany.ORCID https://orcid.org/0000-0002-2180-9154

Funding

Deutsche Forschungsgemeinschaft He3875/15-1
6 · The paper itself

Abstract

The Sec61 translocon mediates the translocation of numerous, newly synthesized precursor proteins into the lumen of the endoplasmic reticulum or their integration into its membrane. Recently, structural biology revealed conformations of idle or substrate-engaged Sec61, and likewise its interactions with the accessory membrane proteins Sec62, Sec63, and TRAP, respectively. Several natural and synthetic small molecules have been shown to block Sec61-mediated protein translocation. Since this is a key step in protein biogenesis, broad inhibition is generally cytotoxic, which may be problematic for a putative drug target. Interestingly, several compounds exhibit client-selective modes of action, such that only translocation of certain precursor proteins was affected. Here, we discuss recent advances of structural biology, molecular modelling, and molecular screening that aim to use Sec61 as feasible drug target.

Indexed as

SEC Translocation ChannelsSmall Molecule LibrariesAnimalsEndoplasmic ReticulumHumansModels, MolecularProtein TransportSEC Translocation ChannelsSmall Molecule Libraries

Identifiers

PMID39394908
PMCPMC11695074

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.