Evidence map›Paper›PMID 27890920›Full record

ReviewNature reviews. Microbiology2017

Protein export through the bacterial Sec pathway.

Alexandra Tsirigotaki, Jozefien De Geyter, Nikolina Šoštaric, Anastassios Economou, Spyridoula Karamanou

Abstract readReview
PubMed Publisher
In one paragraph

Review in Nature reviews. Microbiology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 234 papers.

0numbers the graph read from it
0cells of the map it votes in
234citing papers in PubMed
41.7field-weighted citation impact, top 1% 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

234 citing papers in PubMed, 440 citations in OpenAlex.

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174 more citing papers are in PubMed but not listed here.

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

5 authors at 2 institutions in 1 country.

Alexandra TsirigotakiLaboratory of Molecular Bacteriology, Department of Microbiology and Immunology, Rega Institute for Medical Research, Katholieke Universiteit Leuven (KU Leuven), B-3000 Leuven, Belgium.
Jozefien De GeyterLaboratory of Molecular Bacteriology, Department of Microbiology and Immunology, Rega Institute for Medical Research, Katholieke Universiteit Leuven (KU Leuven), B-3000 Leuven, Belgium.
Nikolina ŠoštaricLaboratory of Molecular Bacteriology, Department of Microbiology and Immunology, Rega Institute for Medical Research, Katholieke Universiteit Leuven (KU Leuven), B-3000 Leuven, Belgium.
Anastassios EconomouLaboratory of Molecular Bacteriology, Department of Microbiology and Immunology, Rega Institute for Medical Research, Katholieke Universiteit Leuven (KU Leuven), B-3000 Leuven, Belgium.
Spyridoula KaramanouLaboratory of Molecular Bacteriology, Department of Microbiology and Immunology, Rega Institute for Medical Research, Katholieke Universiteit Leuven (KU Leuven), B-3000 Leuven, Belgium.
KU Leuven · BERega Institute for Medical Research · BE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The general secretory (Sec) pathway comprises an essential, ubiquitous and universal export machinery for most proteins that integrate into, or translocate through, the plasma membrane. Sec exportome polypeptides are synthesized as pre-proteins that have cleavable signal peptides fused to the exported mature domains. Recent advances have re-evaluated the interaction networks of pre-proteins with chaperones that are involved in pre-protein targeting from the ribosome to the SecYEG channel and have identified conformational signals as checkpoints for high-fidelity targeting and translocation. The recent structural and mechanistic insights into the channel and its ATPase motor SecA are important steps towards the elucidation of the allosteric crosstalk that mediates secretion. In this Review, we discuss recent biochemical, structural and mechanistic insights into the consecutive steps of the Sec pathway - sorting and targeting, translocation and release - in both co-translational and post-translational modes of export. The architecture and conformational dynamics of the SecYEG channel and its regulation by ribosomes, SecA and pre-proteins are highlighted. Moreover, we present conceptual models of the mechanisms and energetics of the Sec-pathway dependent secretion process in bacteria.

Indexed as

Adenosine TriphosphatasesBacterial ProteinsCell MembraneEscherichia coliEscherichia coli ProteinsProtein ConformationProtein Sorting SignalsProtein TransportSecA ProteinsSEC Translocation ChannelsSignal TransductionAdenosine TriphosphatasesBacterial ProteinsEscherichia coli ProteinsProtein Sorting SignalsSecA ProteinsSEC Translocation Channels

Identifiers

PMID27890920
OpenAlexW2559192784

What OpenQuestion holds

Textmetadata
Read underepoch 390

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.