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Involvement of Nod2 in the innate immune response elicited by malarial pigment hemozoin

https://doi.org/10.1016/j.micinf.2014.11.001
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What this work says

Outgoing claims: the papers this work cites, builds on, or argues with.

inferredcites →https://doi.org/10.1002/path.2271openalex-snapshot
Nod‐like proteins in inflammation and disease
inferredcites →https://doi.org/10.1016/j.celrep.2013.12.014openalex-snapshot
Dual Engagement of the NLRP3 and AIM2 Inflammasomes by Plasmodium-Derived Hemozoin and DNA during Malaria
inferredcites →https://doi.org/10.1016/j.febslet.2006.08.043openalex-snapshot
Haemozoin (β‐haematin) biomineralization occurs by self‐assembly near the lipid/water interface
inferredcites →https://doi.org/10.1016/j.immuni.2011.05.016openalex-snapshot
Innate Immune Recognition of an AT-Rich Stem-Loop DNA Motif in the Plasmodium falciparum Genome
inferredcites →https://doi.org/10.1016/j.jhep.2010.04.026openalex-snapshot
Hepatocytes express functional NOD1 and NOD2 receptors: A role for NOD1 in hepatocyte CC and CXC chemokine production
inferredcites →https://doi.org/10.1016/j.jinorgbio.2007.12.004openalex-snapshot
Recent advances in understanding the mechanism of hemozoin (malaria pigment) formation
inferredcites →https://doi.org/10.1016/j.pt.2005.07.002openalex-snapshot
Nitric oxide bioavailability in malaria
inferredcites →https://doi.org/10.1016/j.pt.2007.09.003openalex-snapshot
TLR-mediated cell signaling by malaria GPIs
inferredcites →https://doi.org/10.1016/s0140-6736(02)11474-7openalex-snapshot
A new NOS2 promoter polymorphism associated with increased nitric oxide production and protection from severe malaria in Tanzanian and Kenyan children
inferredcites →https://doi.org/10.1016/s0140-6736(13)60024-0openalex-snapshot
Malaria
inferredcites →https://doi.org/10.1016/s0162-0134(02)00372-0openalex-snapshot
Physico-chemical aspects of hemozoin (malaria pigment) structure and formation
inferredcites →https://doi.org/10.1016/s1995-7645(10)60041-7openalex-snapshot
Higher production of tumor necrosis factor alpha in hemozoin-fed—human adherent monocytes is dependent on lipidic component of malarial pigment: new evidences on cytokine regulation in Plasmodium falciparum malaria
inferredcites →https://doi.org/10.1021/cg4009416openalex-snapshot
Synthetic Hemozoin (β-Hematin) Crystals Nucleate at the Surface of Neutral Lipid Droplets that Control Their Sizes
inferredcites →https://doi.org/10.1038/35005132openalex-snapshot
The structure of malaria pigment β-haematin
inferredcites →https://doi.org/10.1038/35079107openalex-snapshot
Association of NOD2 leucine-rich repeat variants with susceptibility to Crohn's disease
inferredcites →https://doi.org/10.1038/416194aopenalex-snapshot
RICK/Rip2/CARDIAK mediates signalling for receptors of the innate and adaptive immune systems
inferredcites →https://doi.org/10.1038/ni.1631openalex-snapshot
Silica crystals and aluminum salts activate the NALP3 inflammasome through phagosomal destabilization
inferredcites →https://doi.org/10.1038/ni.1782openalex-snapshot
Activation of innate immune antiviral responses by Nod2
inferredcites →https://doi.org/10.1038/ni.1816openalex-snapshot
T cell–intrinsic role of Nod2 in promoting type 1 immunity to Toxoplasma gondii
inferredcites →https://doi.org/10.1073/pnas.0608745104openalex-snapshot
Malaria hemozoin is immunologically inert but radically enhances innate responses by presenting malaria DNA to Toll-like receptor 9
inferredcites →https://doi.org/10.1074/jbc.m413541200openalex-snapshot
Induction of Proinflammatory Responses in Macrophages by the Glycosylphosphatidylinositols of Plasmodium falciparum
inferredcites →https://doi.org/10.1093/bioinformatics/btg157openalex-snapshot
Q-Gene: processing quantitative real-time RT–PCR data
inferredcites →https://doi.org/10.1093/nar/gkr1013openalex-snapshot
PrimerBank: a PCR primer database for quantitative gene expression analysis, 2012 update
inferredcites →https://doi.org/10.1111/j.1365-3024.2006.00775.xopenalex-snapshot
Regulating immunity to malaria
inferredcites →https://doi.org/10.1111/j.1462-5822.2010.01508.xopenalex-snapshot
Role of the NF-κB transcription pathway in the haemozoin- and 15-HETE-mediated activation of matrix metalloproteinase-9 in human adherent monocytes
inferredcites →https://doi.org/10.1111/j.1462-5822.2011.01620.xopenalex-snapshot
Natural haemozoin modulates matrix metalloproteinases and induces morphological changes in human microvascular endothelium
inferredcites →https://doi.org/10.1111/j.1469-0691.2008.02270.xopenalex-snapshot
Role of the cytoplasmic pattern recognition receptor Nod2 in Coxiella burnetii infection
inferredcites →https://doi.org/10.1126/science.781840openalex-snapshot
Human Malaria Parasites in Continuous Culture
inferredcites →https://doi.org/10.1128/iai.01070-13openalex-snapshot
NOS2 Variants Reveal a Dual Genetic Control of Nitric Oxide Levels, Susceptibility to Plasmodium Infection, and Cerebral Malaria
inferredcites →https://doi.org/10.1128/iai.06033-11openalex-snapshot
Experimental Cerebral Malaria Develops Independently of Caspase Recruitment Domain-Containing Protein 9 Signaling
inferredcites →https://doi.org/10.1128/iai.67.9.4977-4981.1999openalex-snapshot
Blood Mononuclear Cell Nitric Oxide Production and Plasma Cytokine Levels in Healthy Gabonese Children with Prior Mild or Severe Malaria
inferredcites →https://doi.org/10.1128/iai.72.8.4868-4873.2004openalex-snapshot
Elevated Nitric Oxide Production in Children with Malarial Anemia: Hemozoin-Induced Nitric Oxide Synthase Type 2 Transcripts and Nitric Oxide in Blood Mononuclear Cells
inferredcites →https://doi.org/10.1155/2012/861426openalex-snapshot
Nucleotide-Binding Oligomerization Domain-1 and -2 Play No Role in ControllingBrucella abortusInfection in Mice
inferredcites →https://doi.org/10.1182/blood-2002-03-0979openalex-snapshot
Malaria-parasitized erythrocytes and hemozoin nonenzymatically generate large amounts of hydroxy fatty acids that inhibit monocyte functions
inferredcites →https://doi.org/10.1182/blood-2010-03-272781openalex-snapshot
Inhibition of erythropoiesis in malaria anemia: role of hemozoin and hemozoin-generated 4-hydroxynonenal
inferredcites →https://doi.org/10.1182/blood-2010-10-312413openalex-snapshot
Host fibrinogen stably bound to hemozoin rapidly activates monocytes via TLR-4 and CD11b/CD18-integrin: a new paradigm of hemozoin action
inferredcites →https://doi.org/10.1371/annotation/abca067d-b82b-4de6-93c5-0fcc38e3df05openalex-snapshot
Correction: Malarial Hemozoin Activates the NLRP3 Inflammasome through Lyn and Syk Kinases
inferredcites →https://doi.org/10.1371/journal.pone.0006510openalex-snapshot
Malarial Hemozoin Is a Nalp3 Inflammasome Activating Danger Signal
inferredcites →https://doi.org/10.1371/journal.pone.0039497openalex-snapshot
Haemozoin Induces Early Cytokine-Mediated Lysozyme Release from Human Monocytes through p38 MAPK- and NF-kappaB- Dependent Mechanisms
inferredcites →https://doi.org/10.1371/journal.ppat.1000559openalex-snapshot
Malarial Hemozoin Activates the NLRP3 Inflammasome through Lyn and Syk Kinases
inferredcites →https://doi.org/10.3389/fimmu.2012.00328openalex-snapshot
NOD1 and NOD2 Signaling in Infection and Inflammation
inferredcites →https://doi.org/10.4049/jimmunol.0903824openalex-snapshot
Protein–DNA Complex Is the Exclusive Malaria Parasite Component That Activates Dendritic Cells and Triggers Innate Immune Responses
inferredcites →https://doi.org/10.4049/jimmunol.171.10.5396openalex-snapshot
Activation of a Subset of Human NK Cells upon Contact with Plasmodium falciparum -Infected Erythrocytes
inferredcites →https://doi.org/10.4049/jimmunol.171.8.4243openalex-snapshot
Hemozoin Increases IFN-γ-Inducible Macrophage Nitric Oxide Generation Through Extracellular Signal-Regulated Kinase- and NF-κB-Dependent Pathways
inferredcites →https://doi.org/10.4049/jimmunol.176.8.4804openalex-snapshot
IFN-γ Enhances Production of Nitric Oxide from Macrophages via a Mechanism That Depends on Nucleotide Oligomerization Domain-2
inferredcites →https://doi.org/10.4269/ajtmh.2009.80.718openalex-snapshot
Disruption of Nod-like Receptors Alters Inflammatory Response to Infection but Does Not Confer Protection in Experimental Cerebral Malaria
inferredcites →https://doi.org/10.7150/ijbs.7.1427openalex-snapshot
Severe Malarial Anemia: Innate Immunity and Pathogenesis

What points at this work

Incoming claims: where this work appears in other papers’ reference lists and arguments.

inferred← citeshttps://doi.org/10.2139/ssrn.4568190openalex-extracted
inferred← citeshttps://doi.org/10.1007/s10571-019-00713-4openalex-snapshot
Induction of Neuroinflammation and Neurotoxicity by Synthetic Hemozoin
inferred← citeshttps://doi.org/10.1007/s40588-021-00166-8openalex-snapshot
Hemozoin: a Complex Molecule with Complex Activities
inferred← citeshttps://doi.org/10.1016/j.actatropica.2017.05.002openalex-snapshot
Malaria pigment stimulates chemokine production by human microvascular endothelium
inferred← citeshttps://doi.org/10.1016/j.celrep.2018.11.059openalex-snapshot
Organ-Specific Fate, Recruitment, and Refilling Dynamics of Tissue-Resident Macrophages during Blood-Stage Malaria
inferred← citeshttps://doi.org/10.1016/j.it.2017.07.004openalex-snapshot
NOD1 and NOD2: Beyond Peptidoglycan Sensing
inferred← citeshttps://doi.org/10.1016/j.micinf.2014.12.010openalex-snapshot
Crystal myth
inferred← citeshttps://doi.org/10.1016/j.saa.2024.123902openalex-snapshot
Hematin anhydride (β-hematin): An analogue to malaria pigment hemozoin possesses nonlinearity
inferred← citeshttps://doi.org/10.1016/j.semcdb.2020.08.005openalex-snapshot
The diverse roles of RIP kinases in host-pathogen interactions
inferred← citeshttps://doi.org/10.1038/s41598-025-30231-xopenalex-snapshot
Malaria pigment hemozoin drives M1 pro-inflammatory macrophage polarization in vitro
inferred← citeshttps://doi.org/10.1038/srep29289openalex-snapshot
Nucleotide-binding oligomerization domain-containing protein 2 prompts potent inflammatory stimuli during Neospora caninum infection
inferred← citeshttps://doi.org/10.1038/srep36193openalex-snapshot
Heme-mediated apoptosis and fusion damage in BeWo trophoblast cells
inferred← citeshttps://doi.org/10.1111/imr.12902openalex-snapshot
NOD1 and NOD2 in inflammatory and infectious diseases
inferred← citeshttps://doi.org/10.1128/iai.00898-19openalex-snapshot
NOD1 and NOD2 Activation by Diverse Stimuli: a Possible Role for Sensing Pathogen-Induced Endoplasmic Reticulum Stress
inferred← citeshttps://doi.org/10.1128/jb.00689-19openalex-snapshot
NOD2/c-Jun NH 2 -Terminal Kinase Triggers Mycoplasma ovipneumoniae-Induced Macrophage Autophagy
inferred← citeshttps://doi.org/10.1186/s12936-018-2602-0openalex-snapshot
Interplay between Plasmodium falciparum haemozoin and l-arginine: implication for nitric oxide production
inferred← citeshttps://doi.org/10.1186/s12936-021-03589-2openalex-snapshot
Phagocytosis and activation of bone marrow‐derived macrophages by Plasmodium falciparum gametocytes
inferred← citeshttps://doi.org/10.1186/s13071-024-06529-6openalex-snapshot
Role of inflammasomes in Toxoplasma and Plasmodium infections
inferred← citeshttps://doi.org/10.15252/embj.2020106272openalex-snapshot
Cellular stress promotes NOD1/2‐dependent inflammation via the endogenous metabolite sphingosine‐1‐phosphate
inferred← citeshttps://doi.org/10.32657/10220/48099openalex-snapshot
Modulation of adaptive and innate immune responses by myeloid cells during malaria
inferred← citeshttps://doi.org/10.3389/fimmu.2016.00463openalex-snapshot
Malaria Parasites: The Great Escape
inferred← citeshttps://doi.org/10.3389/fitd.2022.874081openalex-snapshot
Have We Ignored Vector-Associated Microbiota While Characterizing the Function of Langerhans Cells in Experimental Cutaneous Leishmaniasis?
inferred← citeshttps://doi.org/10.4172/2470-6965.1000s1-004openalex-snapshot
Effect of Nelumbo nucifera Stamen Extract on Phagocytosis and Malaria Parasite Growth Against Plasmodium Berghei Infected Mice
inferred← citeshttps://doi.org/10.70675/d05fc6cfz307bz4484za408z43ec7e8427c4openalex-snapshot
The inflammatory response of primary epithelial cells of the female genital tract to Chlamydia trachomatis infection, and its exacerbation by type-I interferon
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