Evidence map›Paper›PMID 31758489›Full record

ArticleMolecular biotechnology2020

Cloning, Purification, and Characterization of the Catalytic C-Terminal Domain of the Human 3-Hydroxy-3-methyl glutaryl-CoA Reductase: An Effective, Fast, and Easy Method for Testing Hypocholesterolemic Compounds.

Rosita Curcio, Donatella Aiello, Angelo Vozza, Luigina Muto, Emanuela Martello, Anna Rita Cappello, Loredana Capobianco, Giuseppe Fiermonte, Carlo Siciliano, Anna Napoli and 1 more

Open access · greenAbstract read
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In one paragraph

Article in Molecular biotechnology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing papers in PubMed
2.0field-weighted citation impact, top 14% 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

5 citing papers in PubMed, 13 citations in OpenAlex.

  1. Article
  2. Citrate Regulates theJournal of fungi (Basel, Switzerland) · 2022
    Article
  3. International journal of molecular sciences · 2022
    Article
  4. Article
  5. 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

11 authors at 3 institutions in 1 country.

Rosita CurcioDepartment of Pharmacy, Health, and Nutritional Sciences, University of Calabria, 87036, Arcavacata di Rende, Cosenza, Italy.
Donatella AielloDepartment of Chemistry and Chemical Technologies, University of Calabria, 87036, Arcavacata di Rende, Cosenza, Italy.
Angelo VozzaLaboratory of Biochemistry and Molecular Biology, Department of Biosciences, Biotechnologies and Biopharmaceutics, University of Bari, 70125, Bari, Italy.
Luigina MutoDepartment of Pharmacy, Health, and Nutritional Sciences, University of Calabria, 87036, Arcavacata di Rende, Cosenza, Italy.
Emanuela MartelloDepartment of Pharmacy, Health, and Nutritional Sciences, University of Calabria, 87036, Arcavacata di Rende, Cosenza, Italy.
Anna Rita CappelloDepartment of Pharmacy, Health, and Nutritional Sciences, University of Calabria, 87036, Arcavacata di Rende, Cosenza, Italy.
Loredana CapobiancoDepartment of Biological and Environmental Sciences and Technologies, University of Salento, 73100, Lecce, Italy.
Giuseppe FiermonteLaboratory of Biochemistry and Molecular Biology, Department of Biosciences, Biotechnologies and Biopharmaceutics, University of Bari, 70125, Bari, Italy.
Carlo SicilianoDepartment of Pharmacy, Health, and Nutritional Sciences, University of Calabria, 87036, Arcavacata di Rende, Cosenza, Italy.
Anna NapoliDepartment of Chemistry and Chemical Technologies, University of Calabria, 87036, Arcavacata di Rende, Cosenza, Italy. amc.napoli@unical.it.
Vincenza DolceDepartment of Pharmacy, Health, and Nutritional Sciences, University of Calabria, 87036, Arcavacata di Rende, Cosenza, Italy. vincenza.dolce@unical.it.ORCID http://orcid.org/0000-0003-2966-4866
University of Calabria · ITUniversity of Bari Aldo Moro · ITUniversity of Salento · IT

Funding

Associazione Italiana per la Ricerca sul Cancro 15404/2014
6 · The paper itself

Abstract

3-hydroxy-3-methyl glutaryl-CoA reductase, also known as HMGR, plays a crucial role in regulating cholesterol biosynthesis and represents the main pharmacological target of statins. In mammals, this enzyme localizes to the endoplasmic reticulum membrane. HMGR includes different regions, an integral N-terminal domain connected by a linker-region to a cytosolic C-terminal domain, the latter being responsible for enzymatic activity. The aim of this work was to design a simple strategy for cloning, expression, and purification of the catalytic C-terminal domain of the human HMGR (cf-HMGR), in order to spectrophotometrically test its enzymatic activity. The recombinant cf-HMGR protein was heterologously expressed in Escherichia coli, purified by Ni

Indexed as

Amino Acid SequenceCatalytic DomainChromatography, AffinityCloning, MolecularDrug Evaluation, PreclinicalEnzyme AssaysEscherichia coliGene ExpressionHumansHydroxymethylglutaryl-CoA Reductase InhibitorsHydroxymethylglutaryl CoA ReductasesRecombinant ProteinsTandem Mass SpectrometryHydroxymethylglutaryl-CoA Reductase InhibitorsHydroxymethylglutaryl CoA ReductasesRecombinant ProteinsAffinity chromatographyBacterial expressionEnzymatic activityHMGRMALDI MS and MS/MSScreening of statin-like molecules

Identifiers

PMID31758489
OpenAlexW2990334959

What OpenQuestion holds

Textmetadata
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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.