Evidence map›Paper›PMID 14690249›Full record

ArticleJournal of protein chemistry2003

Kinetic inactivation study of mushroom tyrosinase: intermediate detection by denaturants.

Yong-Doo Park, Jae-Yong Jung, Do-Won Kim, Won-Serk Kim, Myong-Joon Hahn, Jun-Mo Yang

Abstract read
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In one paragraph

Article in Journal of protein chemistry, 2003. 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
0.6field-weighted citation impact, top 36% 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, 22 citations in OpenAlex.

  1. Denaturation of proteins by SDS and tetraalkylammonium dodecyl sulfates.Langmuir : the ACS journal of surfaces and colloids · 2011
    Article
  2. Article
  3. Differentiation of proteins based on characteristic patterns of association and denaturation in solutions of SDS.Proceedings of the National Academy of Sciences of the United States of America · 2006
    Article
  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

6 authors at 2 institutions in 1 country.

Yong-Doo ParkClinical Research Center, Samsung Biomedical Research Institute, Seoul 135-710, Korea.
Jae-Yong Jung
Do-Won Kim
Won-Serk Kim
Myong-Joon Hahn
Jun-Mo Yang
Samsung (South Korea) · KRSungkyunkwan University · KR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The unfolding and inhibition study of mushroom tyrosinase have been studied in the presence of different denaturants such as sodium dodecyl sulfate (SDS), guanidine hydrochloride (GdnHCl), and urea. The kinetic two-phase rate constants were commonly measured from semilogarithmic plots of the activity versus time, which resolved into two straight lines, indicating that the inactivation process consisted of fast and slow phases as a first-order reaction. This result also implied that transient partially folded intermediate existed during tyrosinase unfolding pathway. Mushroom tyrosinase had different behaviors to denaturants in regard with: noncooperative binding manner by SDS while cooperative interactions by GdnHCl and urea; in equilibrium state, SDS-micelle never completely inactivated enzyme activity while GdnHCl has single step denaturation and urea induced a typical transition-like process. Various kinetic parameters for each denaturant were calculated and the possible unfolding pathway scheme was discussed.

Indexed as

AgaricusCatalysisGuanidineKineticsMonophenol MonooxygenaseProtein DenaturationProtein FoldingSodium Dodecyl SulfateThermodynamicsUreaGuanidineMonophenol MonooxygenaseSodium Dodecyl SulfateUrea

Identifiers

PMID14690249
OpenAlexW2070335438

What OpenQuestion holds

Textmetadata
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.