Evidence map›Paper›PMID 34769302›Full record

ReviewInternational journal of molecular sciences2021

Take Me Home, Protein Roads: Structural Insights into Signal Peptide Interactions during ER Translocation.

A Manuel Liaci, Friedrich Förster

Abstract readReview
In one paragraph

Review in International journal of molecular sciences, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 48 papers.

0numbers the graph read from it
0cells of the map it votes in
48citing 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

48 citing papers in PubMed.

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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

2 authors.

A Manuel LiaciBijvoet Centre for Biomolecular Research, Structural Biochemistry Group, Utrecht University, Universiteitsweg 99, 3584 CG Utrecht, The Netherlands.
Friedrich FörsterBijvoet Centre for Biomolecular Research, Structural Biochemistry Group, Utrecht University, Universiteitsweg 99, 3584 CG Utrecht, The Netherlands.ORCID 0000-0002-6044-2746

Funding

European Research Council 724425
6 · The paper itself

Abstract

Cleavable endoplasmic reticulum (ER) signal peptides (SPs) and other non-cleavable signal sequences target roughly a quarter of the human proteome to the ER. These short peptides, mostly located at the N-termini of proteins, are highly diverse. For most proteins targeted to the ER, it is the interactions between the signal sequences and the various ER targeting and translocation machineries such as the signal recognition particle (SRP), the protein-conducting channel Sec61, and the signal peptidase complex (SPC) that determine the proteins' target location and provide translocation fidelity. In this review, we follow the signal peptide into the ER and discuss the recent insights that structural biology has provided on the governing principles of those interactions.

Indexed as

EndopeptidasesEndoplasmic ReticulumHumansProtein Sorting SignalsProtein TransportProteomeSEC Translocation ChannelsSignal Recognition ParticleEndopeptidasesProtein Sorting SignalsProteomeSEC Translocation ChannelsSignal Recognition Particlechaperonesendoplasmic reticulumER transloconprotein targetingprotein translocationsignal peptidasesignal peptide

Identifiers

PMID34769302
PMCPMC8584900

What Socratic holds

Textmetadata
LicenceCC BY
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 Socratic graph.