Evidence map›Paper›PMID 27551823›Full record

ArticlePloS one2016

Large-Scale Recombinant Expression and Purification of Human Tyrosinase Suitable for Structural Studies.

Xuelei Lai, Montserrat Soler-Lopez, Harry J Wichers, Bauke W Dijkstra

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.

0numbers the graph read from it
0cells of the map it votes in
30citing papers in PubMed
4.5field-weighted citation impact, top 5% 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

30 citing papers in PubMed, 67 citations in OpenAlex.

  1. Molecular Targets in Modern Cosmetic Science.Molecules (Basel, Switzerland) · 2026
    Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Tyrosinase Inhibitors: A Perspective.Molecules (Basel, Switzerland) · 2023
    Review
  11. Article
  12. Article
  13. Review
  14. Recycled Sericin Hydrolysates Modified by AlcalaseInternational journal of molecular sciences · 2022
    Article
  15. Article
  16. Review
  17. Article
  18. Phenylthiourea Binding to Human Tyrosinase-Related Protein 1.International journal of molecular sciences · 2020
    Article
  19. FunctionalJournal of analytical & pharmaceutical research · 2020
    Article
  20. 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 3 institutions in 2 countries.

Xuelei LaiLaboratory of Biophysical Chemistry, University of Groningen, Groningen, The Netherlands.
Montserrat Soler-LopezESRF-The European Synchrotron, Grenoble, France.
Harry J WichersLaboratory of Food Chemistry, Wageningen University, Wageningen, The Netherlands.
Bauke W DijkstraLaboratory of Biophysical Chemistry, University of Groningen, Groningen, The Netherlands.ORCID http://orcid.org/0000-0001-9731-6586
University of Groningen · NLEuropean Synchrotron Radiation Facility · FRWageningen University & Research · NL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Human tyrosinase (TYR) is a glycoprotein that initiates the first two reactions in the melanin biosynthesis pathway. Mutations in its encoding gene cause Oculocutaneous Albinism type I (OCA1), the most severe form of albinism, which is a group of autosomal recessive disorders characterized by reduced or absent production of melanin in skin, hair and eyes. Despite extensive structural and characterization studies of its homologues in lower eukaryotic organisms, the catalytic mechanism of human TYR and the molecular basis of OCA1 are largely unknown. In this work, we have carried out a large-scale recombinant expression of TYR that has enabled us to obtain high yields of pure and active protein, required for crystallization trials and screening of skin whitening agents, which is highly demanded in the cosmetic industry. Addition of an N-terminal honeybee melittin signal peptide for secretion of the produced protein into the (protein-free) medium, as well as a cleavable His-tag at the C-terminus, was crucial for increasing the yield of pure protein. We have successfully crystallized two TYR variants, in both glycosylated and deglycosylated forms, showing preliminary X-ray diffraction patterns at 3.5 Å resolution. Hence, we have established an expression and purification protocol suitable for the crystal structure determination of human TYR, which will give unique atomic insight into the nature and conformation of the residues that shape the substrate binding pocket that will ultimately lead to efficient compound design.

Indexed as

Recombinant ProteinsAmino Acid SequenceAnimalsChromatographyGene ExpressionGlycosylationHumansMonophenol MonooxygenaseProtein StabilityStructure-Activity RelationshipTemperatureX-Ray DiffractionMonophenol MonooxygenaseRecombinant Proteins

Identifiers

PMID27551823
PMCPMC4994950
OpenAlexW2518186484

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.