Evidence map›Paper›PMID 33019542›Full record

ReviewCells2020

Adaptation of Proteasomes and Lysosomes to Cellular Environments.

Yohannes Afework Mebratu, Zerihun Hailemariam Negasi, Saugata Dutta, Joselyn Rojas-Quintero, Yohannes Tesfaigzi

Open access · goldAbstract readReview
In one paragraph

Review in Cells, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
0.5field-weighted citation impact, top 37% 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

4 citing papers in PubMed, 8 citations in OpenAlex.

  1. Review
  2. Review
  3. Review
  4. Article
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 1 institution in 1 country.

Yohannes Afework MebratuPulmonary and Critical Care Medicine Division, Department of Medicine, Brigham and Women's Hospital, Harvard Medical School, Boston, MA 01255, USA.
Zerihun Hailemariam NegasiPulmonary and Critical Care Medicine Division, Department of Medicine, Brigham and Women's Hospital, Harvard Medical School, Boston, MA 01255, USA.ORCID 0000-0002-4028-4269
Saugata DuttaPulmonary and Critical Care Medicine Division, Department of Medicine, Brigham and Women's Hospital, Harvard Medical School, Boston, MA 01255, USA.
Joselyn Rojas-QuinteroPulmonary and Critical Care Medicine Division, Department of Medicine, Brigham and Women's Hospital, Harvard Medical School, Boston, MA 01255, USA.
Yohannes TesfaigziPulmonary and Critical Care Medicine Division, Department of Medicine, Brigham and Women's Hospital, Harvard Medical School, Boston, MA 01255, USA.ORCID 0000-0002-3997-5839
Brigham and Women's Hospital · US

Funding

Resolution of Epithelial Cell Hyperplasia in AsthmaR01HL068111 · NHLBI · LOVELACE BIOMEDICAL & ENVIRONMENTAL RESEARCH INSTITUTE · PI TESFAIGZI, YOHANNES · 2003 to 2021
$10.9M
Wood Smoke and Chronic Mucous HypersecretionR01HL140839 · NHLBI · LOVELACE BIOMEDICAL & ENVIRONMENTAL RESEARCH INSTITUTE · PI TESFAIGZI, YOHANNES · 2018 to 2021
$2.8M
NHLBI NIH HHS R01 HL068111NHLBI NIH HHS R01 HL140839
6 · The paper itself

Abstract

Protein degradation is important for proper cellular physiology as it removes malfunctioning proteins or can provide a source for energy. Proteasomes and lysosomes, through the regulatory particles or adaptor proteins, respectively, recognize proteins destined for degradation. These systems have developed mechanisms to allow adaptation to the everchanging environment of the cell. While the complex recognition of proteins to be degraded is somewhat understood, the mechanisms that help switch the proteasomal regulatory particles or lysosomal adaptor proteins to adjust to the changing landscape of degrons, during infections or inflammation, still need extensive exploration. Therefore, this review is focused on describing the protein degradation systems and the possible sensors that may trigger the rapid adaptation of the protein degradation machinery.

Indexed as

HomeostasisHumansLysosomesProteasome Endopeptidase ComplexProteasome Endopeptidase Complexaggresomeautophagycore particleendosomeprotein degradationregulatory particle

Identifiers

PMID33019542
PMCPMC7600607
OpenAlexW3090718867

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.