About: Haem detoxification by an insect

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scientific article published in Nature

Attributes	Values
rdf:type	Item
description	artículu científicu (ast) wetenschappelijk artikel (nl) article publié dans la revue scientifique Nature (fr) im August 1999 veröffentlichter wissenschaftlicher Artikel (de) নেচারে প্রকাশিত বৈজ্ঞানিক প্রবন্ধ (bn) scientific article published in Nature (en) наукова стаття, опублікована в Nature в серпні 1999 (uk)
publication date	wds:Q57001169-CB7F82FC-D0B5-4E4F-BB58-A936F7C36C05
publication date	1999-08-01 00:00:00Z (xsd:dateTime)
language of work or name	wds:Q57001169-86C3CAA1-AB02-4C2E-87BC-38B9AAEE5CBB
language of work or name	English
exact match	wds:Q57001169-5E2B983C-989A-43BB-A7D8-A1631BCAACBD
exact match	https://scigraph.springernature.com/pub.10.1038/22910
author name string	wds:Q57001169-16152532-D4F4-4DE0-8F2B-2F142DAA84D0 wds:Q57001169-6DC62B8B-40BE-4433-837A-D42E955AEBC4 wds:Q57001169-7B06708E-087B-4696-8CC1-6BD5D69543BA wds:Q57001169-C79F1AF1-2DF0-444B-A814-FFFC4B49BCC3 wds:Q57001169-CFB0184F-EA5A-4B8C-A6D7-EC1F35719525 wds:Q57001169-F1CF1368-C5B8-4F87-897B-7C1C7F1C928A
author name string	Hatisaburo Masuda Marílvia Dansa-Petretski Pedro L. Oliveira Cláudia M. S. Braga José R. Silva Marcus F. Oliveira
rdfs:label	Haem detoxification by an insect (en) Haem detoxification by an insect (nl)
skos:prefLabel	Haem detoxification by an insect (en) Haem detoxification by an insect (nl)
name	Haem detoxification by an insect (en) Haem detoxification by an insect (nl)
author	wds:Q57001169-3359ADE2-8F35-46FA-AD7C-592CFC3BA3C2 wds:Q57001169-581E6327-BE5C-4283-83C7-1C099C3004D3
author	Wanderley de Souza Ulysses Lins
title	wds:Q57001169-27768DDF-75B9-4534-8704-C71F67FDA13D
title	Haem detoxification by an insect (en)
page(s)	wds:Q57001169-1D9EA1B8-22A8-49F7-8D36-65961FF041CA
page(s)	517-518
instance of	wds:Q57001169-A0D0984D-D01A-4C74-8F97-0658DACCB926
instance of	scholarly article
main subject	wds:Q57001169-4307564F-23CA-43FE-AE68-C1DA77E25E0E
main subject	insect
PubMed ID	wds:Q57001169-D17A4A61-7FB8-4BB2-B42E-3C0D93E5E912
PubMed ID	http://rdf.ncbi.nlm.nih.gov/pubchem/reference/10448851
PubMed ID	10448851
published in	wds:Q57001169-1E30EC9A-B172-4358-99FC-D16D00BAF46A
published in	Nature
issue	wds:Q57001169-59CCCC98-6247-4021-8C6B-BC58FC0D776A
volume	wds:Q57001169-D4378B25-7989-420C-A4AE-080DF818F68E
issue	6744
volume	400
DOI	wds:Q57001169-3584886B-4BAA-4528-9078-9CCB7A94C73E
DOI	http://dx.doi.org/10.1038/22910
DOI	10.1038/22910
Dimensions Publication ID	wds:Q57001169-74F374CE-B2E9-42B9-9CC1-CB37A03A49C5
Dimensions Publication ID	1009353517
is about of	https://www.wikidata.org/wiki/Special:EntityData/Q57001169
is cites work of	Interference with hemozoin formation represents an important mechanism of schistosomicidal action of antimalarial quinoline methanols Haemozoin in Schistosoma mansoni. Anti-tick vaccines On the pro-oxidant effects of haemozoin Heme on innate immunity and inflammation The heme synthesis and degradation pathways: role in oxidant sensitivity. Heme oxygenase has both pro- and antioxidant properties Haemoproteus and Schistosoma synthesize heme polymers similar to Plasmodium hemozoin and beta-hematin Blood meal-derived heme decreases ROS levels in the midgut of Aedes aegypti and allows proliferation of intestinal microbiota Alpha-glucosidase promotes hemozoin formation in a blood-sucking bug: an evolutionary history Speciation and structure of ferriprotoporphyrin IX in aqueous solution: spectroscopic and diffusion measurements demonstrate dimerization, but not mu-oxo dimer formation. Theories on malarial pigment formation and quinoline action Identification and mapping of the promoter for the gene encoding the ferritin heavy-chain homologue of the yellow fever mosquito Aedes aegypti Developmental profile, isolation, and biochemical characterization of a novel lipoglycoheme-carrier protein from the American dog tick, Dermacentor variabilis (Acari: Ixodidae) and observations on a similar protein in the soft tick, Ornithodoros par Aedes aegypti peritrophic matrix and its interaction with heme during blood digestion On the mechanisms involved in biological heme crystallization Extracellular lipid droplets promote hemozoin crystallization in the gut of the blood fluke Schistosoma mansoni. Haemozoin (beta-haematin) biomineralization occurs by self-assembly near the lipid/water interface Haemozoin formation in the midgut of the blood-sucking insect Rhodnius prolixus Hydrogen peroxide detoxification in the midgut of the blood-sucking insect, Rhodnius prolixus Structural and morphological characterization of hemozoin produced by Schistosoma mansoni and Rhodnius prolixus A heme-degradation pathway in a blood-sucking insect The nematode polyprotein allergens/antigens Biglutaminyl-biliverdin IX alpha as a heme degradation product in the dengue fever insect-vector Aedes aegypti Environmental signals generate a differential and coordinated expression of the heme receptor gene family of Bartonella quintana Transcriptional regulation of the heme binding protein gene family of Bartonella quintana is accomplished by a novel promoter element and iron response regulator An insight into the transcriptome of the digestive tract of the bloodsucking bug, Rhodnius prolixus Wolbachia and the insect immune system: what reactive oxygen species can tell us about the mechanisms of Wolbachia-host interactions Neutral lipids associated with haemozoin mediate efficient and rapid β-haematin formation at physiological pH, temperature and ionic composition The polyprotein lipid binding proteins of nematodes Immunopathological effects of malaria pigment or hemozoin and other crystals Tissue distribution and characterization of predominant hemolymph carrier proteins from Dermacentor variabilis and Ornithodoros parkeri Hemozoin: oil versus water Potential biomarkers and their applications for rapid and reliable detection of malaria Vampires, Pasteur and reactive oxygen species. Is the switch from aerobic to anaerobic metabolism a preventive antioxidant defence in blood-feeding parasites? Hemozoin "knobs" in Opisthorchis felineus infected liver. Heme binding proteins of Bartonella henselae are required when undergoing oxidative stress during cell and flea invasion Resonance Raman spectroscopy in malaria research A heme-binding aspartic proteinase from the eggs of the hard tick Boophilus microplus. Kinetics of beta-haematin formation from suspensions of haematin in aqueous benzoic acid Heme biosynthesis and oogenesis in the blood-sucking bug, Rhodnius prolixus Plasmodium falciparum: nitric oxide modulates heme speciation in isolated food vacuoles

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