Evidence map›Paper›PMID 24867671›Full record

ReviewCurrent opinion in cell biology2014

Recent technical developments in the study of ER-associated degradation.

Kunio Nakatsukasa, Takumi Kamura, Jeffrey L Brodsky

Abstract readReview
In one paragraph

Review in Current opinion in cell biology, 2014. 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
–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

18 citing papers in PubMed.

  1. Review
  2. AVirulence · 2024
    Article
  3. Article
  4. Article
  5. Role of the HSP70 Co-Chaperone SIL1 in Health and Disease.International journal of molecular sciences · 2021
    Review
  6. Article
  7. Article
  8. The Integrated UPR and ERAD in Oligodendrocytes Maintain Myelin Thickness in Adults by Regulating Myelin Protein Translation.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2020
    Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Review
  14. Article
  15. Glycosylation-directed quality control of protein folding.Nature reviews. Molecular cell biology · 2015
    Review
  16. Article
  17. Article
  18. The biology of proteostasis in aging and disease.Annual review of biochemistry · 2015
    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

3 authors.

Kunio NakatsukasaDivision of Biological Sciences, Graduate School of Science, Nagoya University, Nagoya, Aichi 464-8602, Japan. Electronic address: z47875a@cc.nagoya-u.ac.jp.
Takumi KamuraDivision of Biological Sciences, Graduate School of Science, Nagoya University, Nagoya, Aichi 464-8602, Japan.
Jeffrey L BrodskyDepartment of Biological Sciences, University of Pittsburgh, Pittsburgh, PA 15260, USA. Electronic address: jbrodsky@pitt.edu.

Funding

Single Nephron and MetabolomicsP30DK079307 · NIDDK · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI KLEYMAN, THOMAS R · 2008 to 2022
$13.4M
ER Associated Degradation of Membrane Proteins in YeastR01GM075061 · NIGMS · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI BRODSKY, JEFFREY L. · 2006 to 2019
$3.2M
NIDDK NIH HHS DK79307NIDDK NIH HHS P30 DK079307NIGMS NIH HHS GM75061NIGMS NIH HHS R01 GM075061
6 · The paper itself

Abstract

Endoplasmic reticulum-associated degradation (ERAD) is a mechanism during which native and misfolded proteins are recognized and retrotranslocated across the ER membrane to the cytosol for degradation by the ubiquitin-proteasome system. Like other cellular pathways, the factors required for ERAD have been analyzed using both conventional genetic and biochemical approaches. More recently, however, an integrated top-down approach has identified a functional network that underlies the ERAD system. In turn, bottom-up reconstitution has become increasingly sophisticated and elucidated the molecular mechanisms underlying substrate recognition, ubiquitylation, retrotranslocation, and degradation. In addition, a live cell imaging technique and a site-specific in vivo photo-crosslinking approach have further dissected specific steps during ERAD. These technical developments have revealed an unexpected dynamicity of the membrane-associated ERAD complex. In this article, we will discuss how these technical developments have improved our understanding of the ERAD pathway and have led to new questions.

Indexed as

Endoplasmic Reticulum-Associated DegradationAnimalsEndoplasmic ReticulumHumansProteasome Endopeptidase ComplexProtein BindingProteinsUbiquitinationProteasome Endopeptidase ComplexProteins

Identifiers

PMID24867671
PMCPMC4130770

What OpenQuestion holds

Textmetadata
LicenceTDM
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.