Evidence map›Paper›PMID 33450959›Full record

ArticleInternational journal of molecular sciences2021

Tyrosinase Nanoparticles: Understanding the Melanogenesis Pathway by Isolating the Products of Tyrosinase Enzymatic Reaction.

Paul K Varghese, Mones Abu-Asab, Emilios K Dimitriadis, Monika B Dolinska, George P Morcos, Yuri V Sergeev

Open access · goldAbstract read
In one paragraph

Article in International journal of molecular sciences, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
1.8field-weighted citation impact, top 16% 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

11 citing papers in PubMed, 23 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Pharmaceuticals (Basel, Switzerland) · 2024
    Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. 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 1 institution in 1 country.

Paul K VargheseNational Eye Institute, National Institutes of Health, Bethesda, MD 20892, USA.
Mones Abu-AsabNational Eye Institute, National Institutes of Health, Bethesda, MD 20892, USA.ORCID 0000-0002-4047-1232
Emilios K DimitriadisNIH Shared Resources on Biomedical Engineering and Physical Science, National Institute of Biomedical Imaging and Bioengineering, National Institutes of Health, Bethesda, MD 20892, USA.
Monika B DolinskaNational Eye Institute, National Institutes of Health, Bethesda, MD 20892, USA.
George P MorcosNational Eye Institute, National Institutes of Health, Bethesda, MD 20892, USA.
Yuri V SergeevNational Eye Institute, National Institutes of Health, Bethesda, MD 20892, USA.ORCID 0000-0002-7204-6572
National Institutes of Health · US

Funding

Scanning Probe Microscopy for the Intramural Research CommunityZICEB000085 · NIBIB · NATIONAL INSTITUTE OF BIOMEDICAL IMAGING AND BIOENGINEERING · PI DIMITRIADIS, EMILIOS K · 2013 to 2025
$24.1M
Proteins From Hereditary Eye Diseases: In-silico and Experimental StudiesZIAEY000476 · NEI · NATIONAL EYE INSTITUTE · PI SERGEEV, YURI · 2009 to 2025
$16.8M
Intramural NIH HHS ZIA EY000476Intramural Program, National Eye Institute ZIA EY000476-10
6 · The paper itself

Abstract

Human Tyrosinase (Tyr) is the rate-limiting enzyme of the melanogenesis pathway. Tyr catalyzes the oxidation of the substrate L-DOPA into dopachrome and melanin. Currently, the characterization of dopachrome-related products is difficult due to the absence of a simple way to partition dopachrome from protein fraction. Here, we immobilize catalytically pure recombinant human Tyr domain (residues 19-469) containing 6xHis tag to Ni-loaded magnetic beads (MB). Transmission electron microscopy revealed Tyr-MB were within limits of 168.2 ± 24.4 nm while the dark-brown melanin images showed single and polymerized melanin with a diameter of 121.4 ± 18.1 nm. Using Hill kinetics, we show that Tyr-MB has a catalytic activity similar to that of intact Tyr. The diphenol oxidase reactions of L-DOPA show an increase of dopachrome formation with the number of MB and with temperature. At 50 °C, Tyr-MB shows some residual catalytic activity suggesting that the immobilized Tyr has increased protein stability. In contrast, under 37 °C, the dopachrome product, which is isolated from Tyr-MB particles, shows that dopachrome has an orange-brown color that is different from the color of the mixture of L-DOPA, Tyr, and dopachrome. In the future, Tyr-MB could be used for large-scale productions of dopachrome and melanin-related products and finding a treatment for oculocutaneous albinism-inherited diseases.

Indexed as

Biosynthetic PathwaysCatalysisChemical FractionationGene ExpressionMelaninsMicroscopy, Atomic ForceMonophenol MonooxygenaseNanoparticlesMelaninsMonophenol Monooxygenasedopachrome/melanin purificationoculocutaneous albinismprotein purificationtyrosinasetyrosinase nanoparticles

Identifiers

PMID33450959
PMCPMC7828394
OpenAlexW3120944669

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.