Evidence map›Paper›PMID 34884562›Full record

ReviewInternational journal of molecular sciences2021

Emerging View on the Molecular Functions of Sec62 and Sec63 in Protein Translocation.

Sung-Jun Jung, Hyun Kim

Open access · goldAbstract 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 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
2.5field-weighted citation impact, top 11% 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

19 citing papers in PubMed, 32 citations in OpenAlex.

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  17. Mechanisms of ER Protein Import.International journal of molecular sciences · 2022
    Article
  18. Review
  19. 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

2 authors at 1 institution in 1 country.

Sung-Jun JungSchool of Biological Sciences and Institute of Microbiology, Seoul National University, Seoul 08826, Korea.ORCID 0000-0002-9050-0433
Hyun KimSchool of Biological Sciences and Institute of Microbiology, Seoul National University, Seoul 08826, Korea.
Seoul National University · KR

Funding

National Research Foundation of Korea 2019R1A2C2087701 and 2021R1H1A2009879
6 · The paper itself

Abstract

Most secreted and membrane proteins are targeted to and translocated across the endoplasmic reticulum (ER) membrane through the Sec61 protein-conducting channel. Evolutionarily conserved Sec62 and Sec63 associate with the Sec61 channel, forming the Sec complex and mediating translocation of a subset of proteins. For the last three decades, it has been thought that ER protein targeting and translocation occur via two distinct pathways: signal recognition particle (SRP)-dependent co-translational or SRP-independent, Sec62/Sec63 dependent post-translational translocation pathway. However, recent studies have suggested that ER protein targeting and translocation through the Sec translocon are more intricate than previously thought. This review summarizes the current understanding of the molecular functions of Sec62/Sec63 in ER protein translocation.

Indexed as

Protein Processing, Post-TranslationalProtein TransportEndoplasmic ReticulumHeat-Shock ProteinsMembrane Transport ProteinsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSEC Translocation ChannelsHeat-Shock ProteinsMembrane Transport ProteinsSaccharomyces cerevisiae ProteinsSEC62 protein, S cerevisiaeSEC63 protein, S cerevisiaeSEC Translocation Channelsendoplasmic reticulumprotein translocationSec61Sec62Sec63

Identifiers

PMID34884562
PMCPMC8657602
OpenAlexW3216794324

What OpenQuestion 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 OpenQuestion graph.