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Journal ArticleDOI

Formyl peptide receptors: a promiscuous subfamily of G protein-coupled receptors controlling immune responses.

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TLDR
The physiological role of the FPR family is still incompletely understood, due in part to the large variety of ligands, the redundancy with other chemoattractant agents, and the lack of clear orthologs between human and mouse receptors.
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This article is published in Cytokine & Growth Factor Reviews.The article was published on 2006-12-01. It has received 417 citations till now. The article focuses on the topics: Formyl peptide receptor & Rhodopsin-like receptors.

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Microbes in Gastrointestinal Health and Disease

TL;DR: Gaining a fuller understanding of both partners in the normal gut-microbiota interaction may shed light on how the relationship can go awry and contribute to a spectrum of immune, inflammatory, and metabolic disorders and may reveal mechanisms by which this relationship could be manipulated toward therapeutic ends.
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International Union of Basic and Clinical Pharmacology. LXXIII. Nomenclature for the formyl peptide receptor (FPR) family.

TL;DR: An International Union of Basic and Clinical Pharmacology (IUPHAR)-recommended nomenclature is introduced and unmet challenges are discussed, including the mechanisms used by these receptors to bind diverse ligands and mediate different biological functions.
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Emerging role of damage-associated molecular patterns derived from mitochondria in inflammation.

TL;DR: The significance of mitochondrial DAMPs is highlighted and their contribution to inflammation and development of human pathologies is discussed.
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Neutrophil cell surface receptors and their intracellular signal transduction pathways

TL;DR: The various cell surface receptors trigger very diverse signal transduction pathways including activation of heterotrimeric and monomeric G-proteins, receptor-induced and store-operated Ca2 + signals, protein and lipid kinases, adapter proteins and cytoskeletal rearrangement.
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Neutrophils to the ROScue: Mechanisms of NADPH Oxidase Activation and Bacterial Resistance.

TL;DR: Mechanisms of oxidative burst in PMNs in response to bacterial infections, as well as the mechanisms by which bacterial pathogens thwart restriction by ROS to survive under conditions of oxidative stress are reviewed.
References
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Journal ArticleDOI

Ll-37, the Neutrophil Granule–And Epithelial Cell–Derived Cathelicidin, Utilizes Formyl Peptide Receptor–Like 1 (Fprl1) as a Receptor to Chemoattract Human Peripheral Blood Neutrophils, Monocytes, and T Cells

TL;DR: The results suggest that, in addition to its microbicidal activity, LL-37 may contribute to innate and adaptive immunity by recruiting neutrophils, monocytes, and T cells to sites of microbial invasion by interacting with FPRL1.
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Neurodegenerative diseases: a decade of discoveries paves the way for therapeutic breakthroughs.

TL;DR: Understanding of mechanisms regulating protein processing and aggregation, as well as of the toxic effects of misfolded neurodegenerative disease proteins, will facilitate development of rationally designed therapies to treat and prevent these disorders.
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Formyl-peptide receptors revisited

TL;DR: This work has shown that the formyl-peptide receptor and its variant FPRL1 (FPR-like 1) are involved in host defense against bacterial infection and in the clearance of damaged cells, and suggests that these receptors contribute to disease pathogenesis and host defense.
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Humanin peptide suppresses apoptosis by interfering with Bax activation

TL;DR: This work shows that Bax interacts with humanin (HN), an anti-apoptotic peptide of 24 amino acids encoded in mammalian genomes, providing a mechanism for protecting these organelles from Bax.
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