Evidence map›Paper›PMID 27551685›Full record

ArticleScience advances2016

Structural analysis of a signal peptide inside the ribosome tunnel by DNP MAS NMR.

Sascha Lange, W Trent Franks, Nandhakishore Rajagopalan, Kristina Döring, Michel A Geiger, Arne Linden, Barth-Jan van Rossum, Günter Kramer, Bernd Bukau, Hartmut Oschkinat

Open access · goldAbstract read
In one paragraph

Article in Science advances, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
3.1field-weighted citation impact, top 8% 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

16 citing papers in PubMed, 46 citations in OpenAlex.

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  8. Advances in studying protein disorder with solid-state NMR.Solid state nuclear magnetic resonance · 2020
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  10. Sensitivity boosts by the CPMAS CryoProbe for challenging biological assemblies.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2020
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  11. Review
  12. Electron decoupling with cross polarization and dynamic nuclear polarization below 6 K.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2018
    Article
  13. Article
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  15. New applications of solid-state NMR in structural biology.Emerging topics in life sciences · 2018
    Article
  16. 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

10 authors at 2 institutions in 1 country.

Sascha LangeLeibniz Institut für Molekulare Pharmakologie im Forschungsverbund Berlin e.V. (FMP), Campus Berlin-Buch, Robert-Roessle-Str. 10, D-13125 Berlin, Germany.; Freie Universität Berlin, Fachbereich BCP, Takustr. 3, 14195 Berlin, Germany.
W Trent FranksLeibniz Institut für Molekulare Pharmakologie im Forschungsverbund Berlin e.V. (FMP), Campus Berlin-Buch, Robert-Roessle-Str. 10, D-13125 Berlin, Germany.ORCID 0000-0003-4111-8868
Nandhakishore RajagopalanCenter for Molecular Biology of the University of Heidelberg (ZMBH), Im Neuenheimer Feld 282, Heidelberg D-69120, Germany.; DKFZ-ZMBH Alliance and German Cancer Research Center (DKFZ), Im Neuenheimer Feld 280, Heidelberg D-69120, Germany.
Kristina DöringCenter for Molecular Biology of the University of Heidelberg (ZMBH), Im Neuenheimer Feld 282, Heidelberg D-69120, Germany.; DKFZ-ZMBH Alliance and German Cancer Research Center (DKFZ), Im Neuenheimer Feld 280, Heidelberg D-69120, Germany.ORCID 0000-0002-1465-6882
Michel A GeigerLeibniz Institut für Molekulare Pharmakologie im Forschungsverbund Berlin e.V. (FMP), Campus Berlin-Buch, Robert-Roessle-Str. 10, D-13125 Berlin, Germany.; Freie Universität Berlin, Fachbereich BCP, Takustr. 3, 14195 Berlin, Germany.
Arne LindenLeibniz Institut für Molekulare Pharmakologie im Forschungsverbund Berlin e.V. (FMP), Campus Berlin-Buch, Robert-Roessle-Str. 10, D-13125 Berlin, Germany.; Freie Universität Berlin, Fachbereich BCP, Takustr. 3, 14195 Berlin, Germany.
Barth-Jan van RossumLeibniz Institut für Molekulare Pharmakologie im Forschungsverbund Berlin e.V. (FMP), Campus Berlin-Buch, Robert-Roessle-Str. 10, D-13125 Berlin, Germany.
Günter KramerCenter for Molecular Biology of the University of Heidelberg (ZMBH), Im Neuenheimer Feld 282, Heidelberg D-69120, Germany.; DKFZ-ZMBH Alliance and German Cancer Research Center (DKFZ), Im Neuenheimer Feld 280, Heidelberg D-69120, Germany.
Bernd BukauCenter for Molecular Biology of the University of Heidelberg (ZMBH), Im Neuenheimer Feld 282, Heidelberg D-69120, Germany.; DKFZ-ZMBH Alliance and German Cancer Research Center (DKFZ), Im Neuenheimer Feld 280, Heidelberg D-69120, Germany.
Hartmut OschkinatLeibniz Institut für Molekulare Pharmakologie im Forschungsverbund Berlin e.V. (FMP), Campus Berlin-Buch, Robert-Roessle-Str. 10, D-13125 Berlin, Germany.; Freie Universität Berlin, Fachbereich BCP, Takustr. 3, 14195 Berlin, Germany.
Leibniz-Forschungsinstitut für Molekulare Pharmakologie · DEGerman Cancer Research Center · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Proteins are synthesized in cells by ribosomes and, in parallel, prepared for folding or targeting. While ribosomal protein synthesis is progressing, the nascent chain exposes amino-terminal signal sequences or transmembrane domains that mediate interactions with specific interaction partners, such as the signal recognition particle (SRP), the SecA-adenosine triphosphatase, or the trigger factor. These binding events can set the course for folding in the cytoplasm and translocation across or insertion into membranes. A distinction of the respective pathways depends largely on the hydrophobicity of the recognition sequence. Hydrophobic transmembrane domains stabilize SRP binding, whereas less hydrophobic signal sequences, typical for periplasmic and outer membrane proteins, stimulate SecA binding and disfavor SRP interactions. In this context, the formation of helical structures of signal peptides within the ribosome was considered to be an important factor. We applied dynamic nuclear polarization magic-angle spinning nuclear magnetic resonance to investigate the conformational states of the disulfide oxidoreductase A (DsbA) signal peptide stalled within the exit tunnel of the ribosome. Our results suggest that the nascent chain comprising the DsbA signal sequence adopts an extended structure in the ribosome with only minor populations of helical structure.

Indexed as

Protein Sorting SignalsAmino Acid SequenceMagnetic Resonance ImagingRecombinant ProteinsRibosomesProtein Sorting SignalsRecombinant Proteinsco-translational foldingdynamic nuclear polarisationMAS NMRProtein structureribosomesignal peptide

Identifiers

PMID27551685
PMCPMC4991931
OpenAlexW2512638401

What OpenQuestion holds

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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.