Evidence map›Paper›PMID 31142026›Full record

ArticleBiomolecules2019

Effect of Protein Denaturation and Enzyme Inhibitors on Proteasomal-Mediated Production of Peptides in Human Embryonic Kidney Cells.

Sayani Dasgupta, Michael A Fishman, Leandro M Castro, Alexandre K Tashima, Emer S Ferro, Lloyd D Fricker

Open access · goldAbstract read
In one paragraph

Article in Biomolecules, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing papers in PubMed
0.6field-weighted citation impact, top 33% 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

5 citing papers in PubMed, 8 citations in OpenAlex.

  1. Article
  2. Application ofInternational journal of molecular sciences · 2020
    Article
  3. Review
  4. Review
  5. 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

6 authors at 4 institutions in 2 countries.

Sayani DasguptaDepartment of Molecular Pharmacology, Albert Einstein College of Medicine, Bronx, NY 10461, USA. sayani.dasgupta@einstein.yu.edu.
Michael A FishmanDepartment of Molecular Pharmacology, Albert Einstein College of Medicine, Bronx, NY 10461, USA. michael.fishman@einstein.yu.edu.
Leandro M CastroBioscience Institute, Coastal Campus, São Paulo State University, São Vicente, 11330-900, SP, Brazil. leandro.mantovani@unesp.br.
Alexandre K TashimaDepartment of Biochemistry, Escola Paulista de Medicina, Federal University of Sao Paulo, Sao Paulo, SP, 04023-901, SP, Brazil. aktashima@unifesp.br.
Emer S FerroDepartment of Pharmacology, Biomedical Science Institute, University of São Paulo, São Paulo, 05508-000, SP, Brazil. emersferro@gmail.com.
Lloyd D FrickerDepartment of Molecular Pharmacology, Albert Einstein College of Medicine, Bronx, NY 10461, USA. lloyd.fricker@einstein.yu.edu.
Albert Einstein College of Medicine · USUniversidade de São Paulo · BRUniversidade Estadual Paulista (Unesp) · BRUniversidade Federal de São Paulo · BR

Funding

Einstein Postbaccalaureate Research Education ProgramR25GM104547 · NIGMS · ALBERT EINSTEIN COLLEGE OF MEDICINE, INC · PI AKABAS, MYLES H. · 2013 to 2023
$4.0M
NIGMS NIH HHS R25 GM104547
6 · The paper itself

Abstract

Peptides produced by the proteasome have been proposed to function as signaling molecules that regulate a number of biological processes. In the current study, we used quantitative peptidomics to test whether conditions that affect protein stability, synthesis, or turnover cause changes in the levels of peptides in Human Embryonic Kidney 293T (HEK293T) cells. Mild heat shock (42 °C for 1 h) or treatment with the deubiquitinase inhibitor b-AP15 led to higher levels of ubiquitinated proteins but did not significantly increase the levels of intracellular peptides. Treatment with cycloheximide, an inhibitor of protein translation, did not substantially alter the levels of intracellular peptides identified herein. Cells treated with a combination of epoxomicin and bortezomib showed large increases in the levels of most peptides, relative to the levels in cells treated with either compound alone. Taken together with previous studies, these results support a mechanism in which the proteasome cleaves proteins into peptides that are readily detected in our assays (i.e., 6-37 amino acids) and then further degrades many of these peptides into smaller fragments.

Indexed as

Protein DenaturationAmino Acid SequenceCycloheximideEnzyme InhibitorsHEK293 CellsHumansIntracellular SpacePeptidesProteasome Endopeptidase ComplexProteomicsUbiquitinationCycloheximideEnzyme InhibitorsPeptidesProteasome Endopeptidase Complexbortezomibepoxomicinmass spectrometrypeptidepeptidomicsProteasome

Identifiers

PMID31142026
PMCPMC6627375
OpenAlexW2947410299

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.