Evidence map›Paper›PMID 34726906›Full record

ArticleACS chemical biology2021

Proteome-Wide Profiling of Cellular Targets Modified by Dopamine Metabolites Using a Bio-Orthogonally Functionalized Catecholamine.

Alexander K Hurben, Luke N Erber, Natalia Y Tretyakova, Todd M Doran

Open access · greenAbstract read
In one paragraph

Article in ACS chemical biology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
1.7field-weighted citation impact, top 13% 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

13 citing papers in PubMed, 21 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Review
  9. Article
  10. Article
  11. Review
  12. Review
  13. 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

4 authors at 1 institution in 1 country.

Alexander K HurbenDepartment of Medicinal Chemistry, University of Minnesota, Minneapolis, Minnesota 55455, United States.ORCID 0000-0002-4016-1103
Luke N ErberDepartment of Medicinal Chemistry, University of Minnesota, Minneapolis, Minnesota 55455, United States.
Natalia Y TretyakovaDepartment of Medicinal Chemistry, University of Minnesota, Minneapolis, Minnesota 55455, United States.ORCID 0000-0002-0621-6860
Todd M DoranDepartment of Medicinal Chemistry, University of Minnesota, Minneapolis, Minnesota 55455, United States.ORCID 0000-0003-1457-6476
University of Minnesota · US

Funding

Training Research Educators in Minnesota (TREM) whilst increasing diversityK12GM119955 · NIGMS · UNIVERSITY OF MINNESOTA · PI David Irwin Greenstein, Julia Willett · 2017 to 2026
$6.5M
DNA Protein Cross-Links:Cellular Effects and Repair MechanismsR01ES023350 · NIEHS · UNIVERSITY OF MINNESOTA · PI CAMPBELL, COLIN R, TRETYAKOVA, NATALIA Y · 2014 to 2023
$5.0M
Chromatin regions, genes and pathways that confer susceptibility to chemical-induced DNA damageR01ES029911 · NIEHS · TEXAS A&M AGRILIFE RESEARCH · PI RUSYN, IVAN, THREADGILL, DAVID W. · 2019 to 2023
$3.3M
Training the Next Generation of Chemical BiologistsT32GM132029 · NIGMS · UNIVERSITY OF MINNESOTA · PI Erin Elizabeth Carlson, William Charles Krause Pomerantz · 2019 to 2026
$2.7M
NIEHS NIH HHS R01 ES023350NIEHS NIH HHS R01 ES029911NIGMS NIH HHS K12 GM119955NIGMS NIH HHS T32 GM132029
6 · The paper itself

Abstract

Selective death of midbrain dopaminergic neurons is a hallmark pathology of Parkinson's disease (PD), but the molecular mechanisms that initiate the cascade of events resulting in neurodegeneration in PD remain unclear. Compelling evidence suggests that dysregulation of dopamine (DA) induces neuronal stress and damage responses that are operative processes in striatal degeneration preceding PD-like symptoms. Improper DA sequestration to vesicles raises cytosolic DA levels, which is rapidly converted into electrophilic dopaquinone species (DQs) that react readily with protein nucleophiles forming covalent modifications that alter the native structure and function of proteins. These so-called DA-protein adducts (DPAs) have been reported to play a role in neurotoxicity, and their abundance with respect to neurodegeneration has been linked to clinical and pathological features of PD that suggest that they play a causal role in PD pathogenesis. Therefore, characterizing DPAs is a critical first step in understanding the susceptibility of midbrain dopaminergic neurons during PD. To help achieve this goal, we report here a novel DA-mimetic (DA

Indexed as

ProteomeCatecholaminesDopamineDopaminergic NeuronsEndoplasmic Reticulum StressHumansOxidation-ReductionParkinson DiseaseProtein Disulfide-IsomerasesProteomicsCatecholaminesDopamineProtein Disulfide-IsomerasesProteome

Identifiers

PMID34726906
PMCPMC9872492
OpenAlexW3210718752

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.