Evidence map›Paper›PMID 25688920›Full record

ArticleArchives of biochemistry and biophysics2015

Inactivation of myeloperoxidase by benzoic acid hydrazide.

Jiansheng Huang, Forrest Smith, Jennifer R Panizzi, Douglas C Goodwin, Peter Panizzi

Open access · greenAbstract read
In one paragraph

Article in Archives of biochemistry and biophysics, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
0.8field-weighted citation impact, top 28% 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

10 citing papers in PubMed, 20 citations in OpenAlex.

  1. The potential ofJournal of integrative bioinformatics · 2024
    Article
  2. Review
  3. Myeloperoxidase Inhibitory and Antioxidant Activities of (Pharmaceuticals (Basel, Switzerland) · 2021
    Article
  4. Article
  5. Review
  6. Review
  7. Article
  8. Review
  9. Article
  10. Review
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

5 authors at 1 institution in 1 country.

Jiansheng HuangDepartment of Drug Discovery and Development, Harrison School of Pharmacy, Auburn University, Auburn, AL 36849, United States.
Forrest SmithDepartment of Drug Discovery and Development, Harrison School of Pharmacy, Auburn University, Auburn, AL 36849, United States.
Jennifer R PanizziDepartment of Anatomy, Physiology and Pharmacology, College of Veterinary Medicine, Auburn University, Auburn, AL 36849, United States.
Douglas C GoodwinDepartment of Chemistry and Biochemistry, College of Science and Mathematics, Auburn University, Auburn, AL 36849, United States.
Peter PanizziDepartment of Drug Discovery and Development, Harrison School of Pharmacy, Auburn University, Auburn, AL 36849, United States. Electronic address: panizzi@auburn.edu.
Auburn University · US

Funding

Random Shear Shuttle BAC Libraries for Antimicrobial Discovery from Soil MetagenoR44AI085840 · NIAID · LUCIGEN CORPORATION · PI LI, XING-CONG, LILES, MARK R · 2012 to 2014
$2.6M
Pathogen specific imaging of endocarditisR01HL114477 · NHLBI · MASSACHUSETTS GENERAL HOSPITAL · PI NAHRENDORF, MATTHIAS, PANIZZI, PETER ROLF · 2013 to 2016
$1.7M
Pathobiology of Staphyloccocus areus EndocarditisR00HL094533 · NHLBI · AUBURN UNIVERSITY AT AUBURN · PI PANIZZI, PETER ROLF · 2011 to 2013
$719k
NHLBI NIH HHS R00 HL094533NHLBI NIH HHS R00HL094533NHLBI NIH HHS R01 HL114477NHLBI NIH HHS R01HL114477NIAID NIH HHS 2R44AI085840-02NIAID NIH HHS R44 AI085840
6 · The paper itself

Abstract

Myeloperoxidase (MPO) is expressed by myeloid cells for the purpose of catalyzing the formation of hypochlorous acid, from chloride ions and reaction with a hydrogen peroxide-charged heme covalently bound to the enzyme. Most peroxidase enzymes both plant and mammalian are inhibited by benzoic acid hydrazide (BAH)-containing compounds, but the mechanism underlying MPO inhibition by BAH compounds is largely unknown. Recently, we reported MPO inhibition by BAH and 4-(trifluoromethyl)-BAH was due to hydrolysis of the ester bond between MPO heavy chain glutamate 242 ((HC)Glu(242)) residue and the heme pyrrole A ring, freeing the heme linked light chain MPO subunit from the larger remaining heavy chain portion. Here we probed the structure and function relationship behind this ester bond cleavage using a panel of BAH analogs to gain insight into the constraints imposed by the MPO active site and channel leading to the buried protoporphyrin IX ring. In addition, we show evidence that destruction of the heme ring does not occur by tracking the heme prosthetic group and provide evidence that the mechanism of hydrolysis follows a potential attack of the (HC)Glu(242) carbonyl leading to a rearrangement causing the release of the vinyl-sulfonium linkage between (HC)Met(243) and the pyrrole A ring.

Indexed as

Amino Acid SequenceAniline CompoundsAnimalsBenzoic AcidCarbocyaninesCatalytic DomainCattleElectronsEnzyme InhibitorsFluorescent DyesFree RadicalsGlutamic AcidHemeHumansHydrogen PeroxideInflammation4-aminobenzhydrazideAniline CompoundsBenzoic AcidCarbocyaninescyanine dye 5Enzyme InhibitorsFluorescent DyesFree RadicalsGlutamic AcidHemeHydrogen PeroxideLysineMethionineOxygenPeroxidaseBenzoic acid hydrazideInflammationMyeloperoxidase

Identifiers

PMID25688920
PMCPMC4779370
OpenAlexW2045532378

What OpenQuestion holds

Textmetadata
LicenceTDM
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.