Evidence map›Paper›PMID 30635083›Full record

ReviewAdvances in protein chemistry and structural biology2019

The roles of cytosolic quality control proteins, SGTA and the BAG6 complex, in disease.

Rashi Benarroch, Jennifer M Austin, Fahmeda Ahmed, Rivka L Isaacson

Open access · greenAbstract readReview
In one paragraph

Review in Advances in protein chemistry and structural biology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
6.8field-weighted citation impact, top 3% 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

18 citing papers in PubMed, 32 citations in OpenAlex.

  1. Transfer of chloroplastSynthetic and systems biotechnology · 2027
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  7. Biomolecules · 2025
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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

4 authors at 1 institution in 1 country.

Rashi BenarrochDepartment of Chemistry, King's College London, London, United Kingdom.
Jennifer M AustinDepartment of Chemistry, King's College London, London, United Kingdom.
Fahmeda AhmedDepartment of Chemistry, King's College London, London, United Kingdom.
Rivka L IsaacsonDepartment of Chemistry, King's College London, London, United Kingdom. Electronic address: rivka.isaacson@kcl.ac.uk.
King's College London · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

SGTA is a co-chaperone that, in collaboration with the complex of BAG6/UBL4A/TRC35, facilitates the biogenesis and quality control of hydrophobic proteins, protecting them from the aqueous cytosolic environment. This work includes targeting tail-anchored proteins to their resident membranes, sorting of membrane and secretory proteins that mislocalize to the cytoplasm and endoplasmic reticulum-associated degradation of misfolded proteins. Since these functions are all vital for the cell's continued proteostasis, their disruption poses a threat to the cell, with a particular risk of protein aggregation, a phenomenon that underpins many diseases. Although the specific disease implications of machinery involved in quality control of hydrophobic substrates are poorly understood, here we summarize much of the available information on this topic.

Indexed as

AnimalsCarrier ProteinsCytosolFemaleHumansMolecular ChaperonesNeoplasmsNeurodegenerative DiseasesPolycystic Ovary SyndromeVirus DiseasesBAG6 protein, humanCarrier ProteinsMolecular ChaperonesSGTA protein, humanBAG6ChaperonesCo-chaperonesHydrophobic proteinsProteostasisQuality controlSGTATail-anchored proteinsTRC35UBL4A

Identifiers

PMID30635083
PMCPMC7102839
OpenAlexW2904184044

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.