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Search results 101 to 200 out of 350 for Fpr2

0.045s
Type Details Score
Publication
First Author: Moreno C
Year: 2013
Journal: J Immunol
Title: Modulation of voltage-dependent and inward rectifier potassium channels by 15-epi-lipoxin-A4 in activated murine macrophages: implications in innate immunity.
Volume: 191
Issue: 12
Pages: 6136-46
Publication
First Author: Wantha S
Year: 2013
Journal: Circ Res
Title: Neutrophil-derived cathelicidin promotes adhesion of classical monocytes.
Volume: 112
Issue: 5
Pages: 792-801
Publication
First Author: Lämmermann T
Year: 2013
Journal: Nature
Title: Neutrophil swarms require LTB4 and integrins at sites of cell death in vivo.
Volume: 498
Issue: 7454
Pages: 371-5
Publication
First Author: Liu X
Year: 2016
Journal: BMC Immunol
Title: Decreased expression levels of Ifi genes is associated to the increased resistance to spontaneous arthritis disease in mice deficiency of IL-1RA.
Volume: 17
Issue: 1
Pages: 25
Publication        
First Author: UniProt-GOA
Year: 2012
Title: Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping, accompanied by conservative changes to GO terms applied by UniProt
Publication        
First Author: Mouse Genome Informatics Scientific Curators
Year: 2002
Title: Chromosome assignment of mouse genes using the Mouse Genome Sequencing Consortium (MGSC) assembly and the ENSEMBL Database
Publication        
First Author: The Gene Ontology Consortium
Year: 2010
Title: Automated transfer of experimentally-verified manual GO annotation data to mouse-human orthologs
Publication        
First Author: Marc Feuermann, Huaiyu Mi, Pascale Gaudet, Dustin Ebert, Anushya Muruganujan, Paul Thomas
Year: 2010
Title: Annotation inferences using phylogenetic trees
Publication      
First Author: Mouse Genome Database and National Center for Biotechnology Information
Year: 2000
Journal: Database Release
Title: Entrez Gene Load
Publication      
First Author: Bairoch A
Year: 1999
Journal: Database Release
Title: SWISS-PROT Annotated protein sequence database
Publication        
First Author: Mouse Genome Informatics Scientific Curators
Year: 2005
Title: Obtaining and Loading Genome Assembly Coordinates from Ensembl Annotations
Publication        
First Author: Mouse Genome Informatics Scientific Curators
Year: 2005
Title: Obtaining and loading genome assembly coordinates from NCBI annotations
Publication        
First Author: The Gene Ontology Consortium
Year: 2014
Title: Automated transfer of experimentally-verified manual GO annotation data to mouse-rat orthologs
Publication        
First Author: Mouse Genome Informatics Scientific Curators
Year: 2003
Title: MGI Sequence Curation Reference
Publication      
First Author: Mouse Genome Informatics Scientific Curators
Year: 2010
Journal: Database Download
Title: Mouse Microarray Data Integration in Mouse Genome Informatics, the Affymetrix GeneChip Mouse Genome U74 Array Platform (A, B, C v2).
Publication        
First Author: GemPharmatech
Year: 2020
Title: GemPharmatech Website.
Publication      
First Author: Mouse Genome Informatics (MGI) and The National Center for Biotechnology Information (NCBI)
Year: 2010
Journal: Database Download
Title: Consensus CDS project
Publication      
First Author: Velocigene
Year: 2008
Journal: MGI Direct Data Submission
Title: Alleles produced for the KOMP project by Velocigene (Regeneron Pharmaceuticals)
Publication      
First Author: Wellcome Trust Sanger Institute
Year: 2009
Journal: MGI Direct Data Submission
Title: Alleles produced for the KOMP project by the Wellcome Trust Sanger Institute
Publication      
First Author: Wellcome Trust Sanger Institute
Year: 2010
Journal: MGI Direct Data Submission
Title: Alleles produced for the EUCOMM and EUCOMMTools projects by the Wellcome Trust Sanger Institute
Publication      
First Author: Allen Institute for Brain Science
Year: 2004
Journal: Allen Institute
Title: Allen Brain Atlas: mouse riboprobes
Publication      
First Author: Mouse Genome Informatics Group
Year: 2003
Journal: Database Procedure
Title: Automatic Encodes (AutoE) Reference
Publication      
First Author: Mouse Genome Informatics Scientific Curators
Year: 2009
Journal: Database Download
Title: Mouse Microarray Data Integration in Mouse Genome Informatics, the Affymetrix GeneChip Mouse Genome 430 2.0 Array Platform
Publication        
First Author: MGD Nomenclature Committee
Year: 1995
Title: Nomenclature Committee Use
Publication      
First Author: Shanghai Model Organisms Center
Year: 2017
Journal: MGI Direct Data Submission
Title: Information obtained from the Shanghai Model Organisms Center (SMOC), Shanghai, China
Publication
First Author: Diez-Roux G
Year: 2011
Journal: PLoS Biol
Title: A high-resolution anatomical atlas of the transcriptome in the mouse embryo.
Volume: 9
Issue: 1
Pages: e1000582
Publication
First Author: Skarnes WC
Year: 2011
Journal: Nature
Title: A conditional knockout resource for the genome-wide study of mouse gene function.
Volume: 474
Issue: 7351
Pages: 337-42
Publication        
First Author: Cyagen Biosciences Inc.
Year: 2022
Title: Cyagen Biosciences Website.
Publication
First Author: Okazaki Y
Year: 2002
Journal: Nature
Title: Analysis of the mouse transcriptome based on functional annotation of 60,770 full-length cDNAs.
Volume: 420
Issue: 6915
Pages: 563-73
Protein
Organism: Mus musculus/domesticus
Length: 351  
Fragment?: false
Publication
First Author: Cao T
Year: 2017
Journal: Cell Biol Toxicol
Title: FAM3D inhibits glucagon secretion via MKP1-dependent suppression of ERK1/2 signaling.
Volume: 33
Issue: 5
Pages: 457-466
Publication
First Author: de Wit NJ
Year: 2012
Journal: J Nutr Biochem
Title: Oit1/Fam3D, a gut-secreted protein displaying nutritional status-dependent regulation.
Volume: 23
Issue: 11
Pages: 1425-33
Protein Domain
Type: Family
Description: This entry represents a group of animal proteins, including TAFA-5 from mammals. TAFA-5 is a secreted protein distantly related to the CC-chemokine family. It has been shown to inhibit postinjury neointima formation via sphingosine-1-phosphate receptor 2-G12/13-RhoA signaling []. Together with its target receptor FPR2 can negatively regulate osteoclast formation [].
Protein Domain
Type: Family
Description: FAM3D inhibits glucagon secretion via MKP1-dependent suppression of ERK1/2 signaling. As dysregulated glucagon secretion is a characteristic of type 2 diabetes, FAM3D could have a therapeutic potential []. FAM3D is constitutively expressed in the gastrointestinal tract []and could play a role in gastrointestinal homeostasis and inflammation through its receptors FPR1 and FPR2 [].
Publication
First Author: Su SB
Year: 1999
Journal: J Exp Med
Title: A seven-transmembrane, G protein-coupled receptor, FPRL1, mediates the chemotactic activity of serum amyloid A for human phagocytic cells.
Volume: 189
Issue: 2
Pages: 395-402
Publication
First Author: Gao JL
Year: 1999
Journal: J Exp Med
Title: Impaired antibacterial host defense in mice lacking the N-formylpeptide receptor.
Volume: 189
Issue: 4
Pages: 657-62
Publication
First Author: Schiffmann E
Year: 1975
Journal: Proc Natl Acad Sci U S A
Title: N-formylmethionyl peptides as chemoattractants for leucocytes.
Volume: 72
Issue: 3
Pages: 1059-62
Publication
First Author: Kindzelskii AL
Year: 1994
Journal: J Struct Biol
Title: Imaging the spatial distribution of membrane receptors during neutrophil phagocytosis.
Volume: 113
Issue: 3
Pages: 191-8
Publication
First Author: Schepetkin IA
Year: 2008
Journal: Mol Pharmacol
Title: Identification of novel formyl peptide receptor-like 1 agonists that induce macrophage tumor necrosis factor alpha production.
Volume: 74
Issue: 2
Pages: 392-402
Publication
First Author: Browning DD
Year: 1997
Journal: J Biol Chem
Title: Cell type- and developmental stage-specific activation of NF-kappaB by fMet-Leu-Phe in myeloid cells.
Volume: 272
Issue: 12
Pages: 7995-8001
Publication
First Author: Zhou Y
Year: 2005
Journal: J Natl Cancer Inst
Title: Formylpeptide receptor FPR and the rapid growth of malignant human gliomas.
Volume: 97
Issue: 11
Pages: 823-35
Publication
First Author: Chen DL
Year: 2009
Journal: Biochem Biophys Res Commun
Title: Downregulating FPR restrains xenograft tumors by impairing the angiogenic potential and invasive capability of malignant glioma cells.
Volume: 381
Issue: 3
Pages: 448-52
Publication
First Author: Karlsson J
Year: 2005
Journal: J Leukoc Biol
Title: Neutrophil NADPH-oxidase activation by an annexin AI peptide is transduced by the formyl peptide receptor (FPR), whereas an inhibitory signal is generated independently of the FPR family receptors.
Volume: 78
Issue: 3
Pages: 762-71
Publication
First Author: Svensson L
Year: 2007
Journal: Eur J Immunol
Title: House dust mite allergen activates human eosinophils via formyl peptide receptor and formyl peptide receptor-like 1.
Volume: 37
Issue: 7
Pages: 1966-77
Publication
First Author: Bena S
Year: 2012
Journal: J Biol Chem
Title: Annexin A1 interaction with the FPR2/ALX receptor: identification of distinct domains and downstream associated signaling.
Volume: 287
Issue: 29
Pages: 24690-7
Publication
First Author: Ye RD
Year: 1992
Journal: Biochem Biophys Res Commun
Title: Isolation of a cDNA that encodes a novel granulocyte N-formyl peptide receptor.
Volume: 184
Issue: 2
Pages: 582-9
Publication
First Author: Rabiet MJ
Year: 2005
Journal: Eur J Immunol
Title: Human mitochondria-derived N-formylated peptides are novel agonists equally active on FPR and FPRL1, while Listeria monocytogenes-derived peptides preferentially activate FPR.
Volume: 35
Issue: 8
Pages: 2486-95
Publication
First Author: Rabiet MJ
Year: 2011
Journal: J Biol Chem
Title: N-formyl peptide receptor 3 (FPR3) departs from the homologous FPR2/ALX receptor with regard to the major processes governing chemoattractant receptor regulation, expression at the cell surface, and phosphorylation.
Volume: 286
Issue: 30
Pages: 26718-31
Publication
First Author: Cattaneo F
Year: 2013
Journal: Int J Mol Sci
Title: Distinct signaling cascades elicited by different formyl peptide receptor 2 (FPR2) agonists.
Volume: 14
Issue: 4
Pages: 7193-230
Publication
First Author: Iribarren P
Year: 2005
Journal: Immunol Res
Title: Role of formyl peptide receptor-like 1 (FPRL1/FPR2) in mononuclear phagocyte responses in Alzheimer disease.
Volume: 31
Issue: 3
Pages: 165-76
Publication
First Author: Forsman H
Year: 2013
Journal: Biochim Biophys Acta
Title: The leukocyte chemotactic receptor FPR2, but not the closely related FPR1, is sensitive to cell-penetrating pepducins with amino acid sequences descending from the third intracellular receptor loop.
Volume: 1833
Issue: 8
Pages: 1914-23
Protein Domain
Type: Family
Description: Formyl peptide receptors (FPR) are members of the rhodopsin-like G-protein coupled receptor family and are involved in chemotaxis [, ]. They were originally identified by their ability to bind N-formyl peptides (typified by fMet-Leu-Phe (fMLP)), produced by the degradation of either bacterial or host cells [, ]but subsequent ligands have been discovered, containing many microbial agonists derived from both bacteria and viruses [, ].FPRs were initially found on leukocytes, but they are expressed in other cells, for example, immature dendritic cells, platelets, microglial cells, astrocytes, fibroblasts and platelets [, ]. FPRs are expressed at high levels on polymorphonuclear and mononuclear phagocytes. Formyl peptide receptors are not only involved in mediating immune cell response to infection, but also act to suppress the immune system under certain conditions []. The main responses elicited upon ligation of formylated peptides, are those of morphological polarization, locomotion, production of reactive-oxygen species and release of proteolytic enzymes []. There are three formyl peptide receptor subtypes, FPR1, FPR2 and FPR3 [, ]. The sequence similarity between FPR1 and FPR2 is high (69%), and although there is a large sequence similarity also between FPR2 and FPR3 (83%), FPR3 can not bind formylated peptides [, ]. This entry represents formyl peptide receptor 1 (FPR1) and Formyl peptide receptor 2 (FPR2).Formyl peptide receptor 1 (FPR1, also known as fMet-Leu-Phe receptor) plays an important role for host defence. This is shown in mice that are devoid of receptor expression, are unable to respond to an infection by Listeria monocytogenes []. The interaction between formyl-methionyl-leucyl phenylalanine (fMLF) and FPR1 triggers a cascade of multiple second messengers through the activation of phospholipase C, phospholipase D and phospholipase A2. This signalling cascade culminates in cell chemotaxis [], phagocytosis [], production of proinflammatory mediators []and activation of transcription factors []. The characterisation of FPR1 function has focused on cells involved in brain function and disease and research indicates that FPR1 is expressed in highly malignant human glioma cells, and is thought to be responsible for mediating motility, growth and angiogenesis of the glioblastoma [, ]. The number of ligands for FPRs is immense, and includes many microbial agonists derived from both bacteria and viruses [, ]. However, unlike FPR2 and FPR3, ligands for FPR1 include endogenous substances, such as annexin AI peptide (Ac9-25) [], and allergens, such as the house mite allergen [].Formyl peptide receptor 2 (FPR2), also known as formyl peptide receptor-like 1 (FPRL1) []and ALXR [], interacts with formylated peptides at a much lower affinity than FPR1 [, ]. However, FPR2 has been found to be a promiscuous receptor, and binds ligands of great diversity in origin and structure, including both lipids and proteins [, ]. It has also been found that mitochondria-derived formyl peptides are potent agonists for FPR2 [], suggesting that its primary function may be to recognise host-driven mitochondrial peptides or possibly other bacterially derived formyl peptides []. FPR2 is also sensitive to cell-penetrating pepducins, unlike FPR1 [].The characterisation of FPR2 function has focused on cells involved in brain function and disease. Research indicates that peptides derived from the protein amyloid beta, which have been shown to stimulate the release of neurotoxic substances from monocytes, do so via FPR2. This suggests that FPR2 is at least partly responsible for proinflammatory destructive activity in brain tissue during Alzheimer's disease [, ]. FPR2 is also critical in mediating homeostasis, inflammation, and epithelial repair processes in the colon [].
Publication
First Author: Migeotte I
Year: 2006
Journal: Cytokine Growth Factor Rev
Title: Formyl peptide receptors: a promiscuous subfamily of G protein-coupled receptors controlling immune responses.
Volume: 17
Issue: 6
Pages: 501-19
Publication
First Author: Ye RD
Year: 2009
Journal: Pharmacol Rev
Title: International Union of Basic and Clinical Pharmacology. LXXIII. Nomenclature for the formyl peptide receptor (FPR) family.
Volume: 61
Issue: 2
Pages: 119-61
Publication
First Author: Le Y
Year: 2002
Journal: Trends Immunol
Title: Formyl-peptide receptors revisited.
Volume: 23
Issue: 11
Pages: 541-8
Publication
First Author: Panaro MA
Year: 2006
Journal: Immunopharmacol Immunotoxicol
Title: Biological role of the N-formyl peptide receptors.
Volume: 28
Issue: 1
Pages: 103-27
Publication
First Author: Braun MC
Year: 2001
Journal: Blood
Title: Activation of the formyl peptide receptor by the HIV-derived peptide T-20 suppresses interleukin-12 p70 production by human monocytes.
Volume: 97
Issue: 11
Pages: 3531-6
Publication
First Author: He HQ
Year: 2013
Journal: Mol Pharmacol
Title: Functional characterization of three mouse formyl peptide receptors.
Volume: 83
Issue: 2
Pages: 389-98
Publication
First Author: Fu H
Year: 2006
Journal: J Leukoc Biol
Title: Ligand recognition and activation of formyl peptide receptors in neutrophils.
Volume: 79
Issue: 2
Pages: 247-56
Publication
First Author: Gantz I
Year: 1996
Journal: Cytogenet Cell Genet
Title: Molecular cloning of a novel receptor (CMKLR1) with homology to the chemotactic factor receptors.
Volume: 74
Issue: 4
Pages: 286-90
Protein Domain
Type: Family
Description: Formyl peptide receptors (FPR) are members of the rhodopsin-like G-protein coupled receptor family and are involved in chemotaxis [, ]. They were originally identified by their ability to bind N-formyl peptides (typified by fMet-Leu-Phe (fMLP)), produced by the degradation of either bacterial or host cells [, ]but subsequent ligands have been discovered, containing many microbial agonists derived from both bacteria and viruses [, ].FPRs were initially found on leukocytes, but they are expressed in other cells, for example, immature dendritic cells, platelets, microglial cells, astrocytes, fibroblasts and platelets [, ]. FPRs are expressed at high levels on polymorphonuclear and mononuclear phagocytes. Formyl peptide receptors are not only involved in mediating immune cell response to infection, but also act to suppress the immune system under certain conditions []. The main responses elicited upon ligation of formylated peptides, are those of morphological polarization, locomotion, production of reactive-oxygen species and release of proteolytic enzymes []. There are three formyl peptide receptor subtypes, FPR1, FPR2 and FPR3 [, ]. The sequence similarity between FPR1 and FPR2 is high (69%), and although there is a large sequence similarity also between FPR2 and FPR3 (83%), FPR3 can not bind formylated peptides [, ]. This entry includes the formyl peptide receptors and other related receptors such as C3a and C5a anaphylatoxin chemotactic receptors []and G-protein-coupled receptor CMKlR1 [].
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein Coding Gene
Type: protein_coding_gene
Organism: Mus caroli
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein Coding Gene
Type: protein_coding_gene
Organism: Mus caroli
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein Coding Gene
Type: protein_coding_gene
Organism: Mus caroli
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory