Evidence map›Paper›PMID 30543669›Full record

ArticlePloS one2018

Use of a sequential high throughput screening assay to identify novel inhibitors of the eukaryotic SRP-Sec61 targeting/translocation pathway.

Wolfgang Klein, Claudia Rutz, Jamina Eckhard, Becky Provinciael, Edgar Specker, Martin Neuenschwander, Gunnar Kleinau, Patrick Scheerer, Jens-Peter von Kries, Marc Nazaré and 2 more

Abstract read
In one paragraph

Article in PloS one, 2018. 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. Article
  2. Article
  3. Lipid Scrambling Pathways in the Sec61 Translocon Complex.Journal of the American Chemical Society · 2025
    Article
  4. Article
  5. Review
  6. Article
  7. Article
  8. 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

12 authors.

Wolfgang KleinLeibniz-Forschungsinstitut für Molekulare Pharmakologie (FMP), Berlin, Germany.
Claudia RutzLeibniz-Forschungsinstitut für Molekulare Pharmakologie (FMP), Berlin, Germany.
Jamina EckhardLeibniz-Forschungsinstitut für Molekulare Pharmakologie (FMP), Berlin, Germany.
Becky ProvinciaelKU Leuven, Department of Microbiology and Immunology, Rega Institute, Laboratory of Virology and Chemotherapy, Leuven, Belgium.
Edgar SpeckerLeibniz-Forschungsinstitut für Molekulare Pharmakologie (FMP), Berlin, Germany.
Martin NeuenschwanderLeibniz-Forschungsinstitut für Molekulare Pharmakologie (FMP), Berlin, Germany.
Gunnar KleinauCharité-Universitätsmedizin Berlin, Campus Charité Mitte, Charité Centrum Grundlagenmedizin CC2, Institut für Medizinische Physik und Biophysik, Group Protein X-ray Crystallography & Signal Transduction, Berlin, Germany.
Patrick ScheererCharité-Universitätsmedizin Berlin, Campus Charité Mitte, Charité Centrum Grundlagenmedizin CC2, Institut für Medizinische Physik und Biophysik, Group Protein X-ray Crystallography & Signal Transduction, Berlin, Germany.
Jens-Peter von KriesLeibniz-Forschungsinstitut für Molekulare Pharmakologie (FMP), Berlin, Germany.
Marc NazaréLeibniz-Forschungsinstitut für Molekulare Pharmakologie (FMP), Berlin, Germany.
Kurt VermeireKU Leuven, Department of Microbiology and Immunology, Rega Institute, Laboratory of Virology and Chemotherapy, Leuven, Belgium.ORCID 0000-0003-1123-1907
Ralf SchüleinLeibniz-Forschungsinstitut für Molekulare Pharmakologie (FMP), Berlin, Germany.ORCID 0000-0001-5921-9486

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The SRP-Sec61 targeting/translocation pathway of eukaryotic cells targets nascent protein chains to the membrane of the endoplasmic reticulum. Using this machinery, secretory proteins are translocated across this membrane whereas membrane proteins are integrated into the lipid bilayer. One of the key players of the pathway is the protein-conducting Sec61 (translocon) complex of the endoplasmic reticulum. The Sec61 complex has no enzymatic activity, is expressed only intracellularly and is difficult to purify and to reconstitute. Screening for small molecule inhibitors impairing its functions is thus notoriously difficult. Such inhibitors may not only be valuable tools for cell biology, they may also represent novel anti-tumor drugs. Here we have developed a two-step, sequential screening assay for inhibitors of the whole SRP-Sec61 targeting/translocation pathway which might include molecules affecting Sec61 complex functions. The resulting hit compounds were analyzed using a whole cell biosynthesis assay and a cell free transcription/translation/translocation assay. Using this methodology, we identified novel compounds inhibiting this pathway. Following structure-based back screening, one of these substances was analyzed in more detail and we could show that it indeed impairs translocation at the level of the Sec61 complex. A slightly modified methodology may be used in the future to screen for substances affecting SecYEG, the bacterial ortholog of the Sec61 complex in order to derive novel antibiotic drugs.

Indexed as

Cell-Free SystemEndoplasmic ReticulumGreen Fluorescent ProteinsHEK293 CellsHigh-Throughput Screening AssaysHumansInhibitory Concentration 50PyrazolesPyrimidinesSEC Translocation Channelsenhanced green fluorescent proteinGreen Fluorescent ProteinsPyrazolespyrazolo(1,5-a)pyrimidinePyrimidinesSEC Translocation Channels

Identifiers

PMID30543669
PMCPMC6292634

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Registered trials

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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.