ReviewInternational journal of biochemistry and molecular biology2013
Lactoperoxidase: structural insights into the function,ligand binding and inhibition.
Review in International journal of biochemistry and molecular biology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers, 1 of them a synthesis that pooled 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.
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.
Who cites it
42 citing papers in PubMed, 1 synthesis or guideline pooled it, 78 citations in OpenAlex.
- The relationship between thyroid peroxidase antibody and differentiated thyroid cancer: a systematic review and meta-analysis.Frontiers in endocrinology · 2024Pooled it
- Trial
- Lipid droplets and major metabolic disorders.Molecular biology reports · 2026Review
- Major Antioxidants and Methods for Studying Their Total Activity in Milk: A Review.Methods and protocols · 2025Review
- Discovery of Surface-Engineered Nanoparticles That Boost Enzyme Activity via High-Throughput Screening and Machine Learning.Small (Weinheim an der Bergstrasse, Germany) · 2025Article
- Lactoperoxidase: Properties, Functions, and Potential Applications.International journal of molecular sciences · 2025Review
- Biochemical and Structural Characterisation of a Bacterial Lactoperoxidase.Chembiochem : a European journal of chemical biology · 2025Article
- Article
- Alginate-modified graphene oxide anchored with lactoperoxidase as a novel bioactive nanocombination for colorectal cancer therapy.Scientific reports · 2024Article
- The skimmed milk proteome of dairy cows is affected by the stage of lactation and by supplementation with polyunsaturated fatty acids.Scientific reports · 2024Article
- Impact of a Functional Dairy Powder and Its Primary Component on the Growth of Pathogenic and Probiotic Gut Bacteria and Human Coronavirus 229E.International journal of molecular sciences · 2024Article
- Lactoperoxidase catalytically oxidize hydrogen sulfide via intermediate formation of sulfheme derivatives.Redox biochemistry and chemistry · 2024Article
- Use of Lactoperoxidase Inhibitory Effects to Extend the Shelf Life of Meat and Meat Products.Microorganisms · 2024Article
- A Bacterial Myeloperoxidase with Antimicrobial Properties.Biotech (Basel (Switzerland)) · 2023Article
- Halogenation Activity of Mammalian Heme Peroxidases.Antioxidants (Basel, Switzerland) · 2022Review
- Essential Protective Role of Catalytically Active Antibodies (Abzymes) with Redox Antioxidant Functions in Animals and Humans.International journal of molecular sciences · 2022Review
- Antimicrobial Activity of Films and Coatings Containing Lactoperoxidase System: A Review.Frontiers in nutrition · 2022Review
- Pulmonary toxicity and gene expression changes in response to whole-body inhalation exposure to multi-walled carbon nanotubes in rats.Inhalation toxicology · 2022Article
- Reverse Ordered Sequential Mechanism for Lactoperoxidase with Inhibition by Hydrogen Peroxide.Antioxidants (Basel, Switzerland) · 2021Article
- Potassium-induced partial inhibition of lactoperoxidase: structure of the complex of lactoperoxidase with potassium ion at 2.20 Å resolution.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2021Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
9 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Lactoperoxidase (LPO) is a member of a large group of mammalian heme peroxidases that include myeloperoxidase (MPO), eosinophil peroxidase (EPO) and thyroid peroxidase (TPO). The LPO is found in exocrine secretions including milk. It is responsible for the inactivation of a wide range of micro-organisms and hence, is an important component of defense mechanism in the body. With the help of hydrogen peroxide, it catalyzes the oxidation of halides, pseudohalides and organic aromatic molecules. Historically, LPO was isolated in 1943, nearly seventy years ago but its three-dimensional crystal structure has been elucidated only recently. This review provides various details of this protein from its discovery to understanding its structure, function and applications. In order to highlight species dependent variations in the structure and function of LPO, a detailed comparison of sequence, structure and function of LPO from various species have been made. The structural basis of ligand binding and distinctions in the modes of binding of substrates and inhibitors have been analyzed extensively.
Indexed as
Identifiers
24049667PMC3776144W83847820What OpenQuestion holds
Registered trials
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.