Evidence map›Paper›PMID 32052243›Full record

ArticleJournal of fluorescence2020

Study of the Interaction of Novel Nonprotein Amino Acids with Trypsin by Steady-State Fluorescence Spectroscopy.

Gohar A Shahinyan, Ani S Dadayan, Nelli A Hovhannisyan, Shiraz A Markarian

Abstract read
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In one paragraph

Article in Journal of fluorescence, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing papers in PubMed
0.2field-weighted citation impact, top 51% 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

0 citing papers in PubMed, 5 citations in OpenAlex.

No citing paper in PubMed yet.

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 2 institutions in 1 country.

Gohar A ShahinyanDepartment of Chemistry, Yerevan State University, 0025, Yerevan, Armenia.
Ani S DadayanInstitute of Pharmacy, Yerevan State University, 0025, Yerevan, Armenia.
Nelli A Hovhannisyan"Armbiotechnology" Scientific and Production Center NAS RA, 0056, Yerevan, Armenia.
Shiraz A MarkarianDepartment of Chemistry, Yerevan State University, 0025, Yerevan, Armenia. shmarkar@ysu.am.
Yerevan State University · AMNational Academy of Sciences of Armenia · AM

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The interaction of (2R, 3S)-hydroxyleucine (trypsin inhibitor) and β-hydroxyvaline with trypsin has been studied by the steady-state fluorescence spectroscopy. The analysis of fluorescence spectra has revealed the mechanism of binding of these nonprotein amino acids to trypsin. According to the docking (2R, 3S)-hydroxyleucine form hydrogen bonds with trypsin having little effect on tryptophan and tyrosine residues in enzyme molecule. The results obtained in this study indicate that fluorescence of trypsin is quenched at high concentrations of amino acids. Thus fluorescence spectra analysis confirms data obtained by molecular docking.

Indexed as

Amino AcidsEnzyme InhibitorsLeucineMolecular Docking SimulationMolecular StructureSpectrometry, FluorescenceTrypsinAmino AcidsEnzyme InhibitorsLeucineTrypsinFluorescence quenchingSerine protease trypsinβ-Hydroxyleucineβ-Hydroxyvaline

Identifiers

PMID32052243
OpenAlexW3006453228

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.