An Engineered Version of Human PON2 Opens the Way to Understand the Role of Its Post-Translational Modifications in Modulating Catalytic Activity (Q35866267)

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scientific article published on 10 December 2015

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English	An Engineered Version of Human PON2 Opens the Way to Understand the Role of Its Post-Translational Modifications in Modulating Catalytic Activity	scientific article published on 10 December 2015

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scholarly article

1 reference

Europe PubMed Central

PMC publication ID

10 August 2017

An Engineered Version of Human PON2 Opens the Way to Understand the Role of Its Post-Translational Modifications in Modulating Catalytic Activity (English)

1 reference

Europe PubMed Central

PMC publication ID

10 August 2017

object named as

Luigi Mandrich

1

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author name string

Mariangela Cerreta

2

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Europe PubMed Central

PMC publication ID

10 August 2017

Giuseppe Manco

3

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Europe PubMed Central

PMC publication ID

10 August 2017

language of work or name

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publication date

10 December 2015

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Europe PubMed Central

PMC publication ID

10 August 2017

1 reference

Europe PubMed Central

PMC publication ID

10 August 2017

10

1 reference

Europe PubMed Central

PMC publication ID

10 August 2017

12

1 reference

Europe PubMed Central

PMC publication ID

10 August 2017

e0144579

1 reference

Europe PubMed Central

PMC publication ID

10 August 2017

copyright license

Creative Commons Attribution 4.0 International

10 December 2015

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April 2022 Public Data File from Crossref

copyright status

0 references

Regulation of human MutYH DNA glycosylase by the E3 ubiquitin ligase mule

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Early adipogenesis is regulated through USP7-mediated deubiquitination of the histone acetyltransferase TIP60.

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The evolutionary origins of detoxifying enzymes: the mammalian serum paraoxonases (PONs) relate to bacterial homoserine lactonases

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Paraoxonase 1 (PON1) as a genetic determinant of susceptibility to organophosphate toxicity

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Harnessing glycosylation to improve cellulase activity

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One enzyme, two functions: PON2 prevents mitochondrial superoxide formation and apoptosis independent from its lactonase activity

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Engineering human PON1 in an E. coli expression system

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Paraoxonase 2 is down-regulated by the Pseudomonas aeruginosa quorumsensing signal N-(3-oxododecanoyl)-L-homoserine lactone and attenuates oxidative stress induced by pyocyanin.

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A common mutation in paraoxonase-2 results in impaired lactonase activity.

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Dominant role of paraoxonases in inactivation of the Pseudomonas aeruginosa quorum-sensing signal N-(3-oxododecanoyl)-L-homoserine lactone

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Human paraoxonases (PON1, PON2, and PON3) are lactonases with overlapping and distinct substrate specificities

1 reference

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The role of pyocyanin in Pseudomonas aeruginosa infection

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Structure and evolution of the serum paraoxonase family of detoxifying and anti-atherosclerotic enzymes

1 reference

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Paraoxonase-2 is a ubiquitously expressed protein with antioxidant properties and is capable of preventing cell-mediated oxidative modification of low density lipoprotein

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Effect of a low concentration of a cationic steroid antibiotic (CSA-13) on the formation of a biofilm by Pseudomonas aeruginosa

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Two alleles of the human paraoxonase gene produce different amounts of mRNA. An explanation for differences in serum concentrations of paraoxonase associated with the (Leu-Met54) polymorphism

1 reference

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Identifiers

10.1371/JOURNAL.PONE.0144579

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Europe PubMed Central

PMC publication ID

10 August 2017

2015PLoSO..1044579M

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24 November 2022

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PMC publication ID

1 reference

Europe PubMed Central

PMC publication ID

10 August 2017

PubMed publication ID

1 reference

Europe PubMed Central

PMC publication ID

10 August 2017

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