|  Help  |  About  |  Contact Us

Search our database by keyword

Examples

  • Search this entire website. Enter identifiers, names or keywords for genes, diseases, strains, ontology terms, etc. (e.g. Pax6, Parkinson, ataxia)
  • Use OR to search for either of two terms (e.g. OR mus) or quotation marks to search for phrases (e.g. "dna binding").
  • Boolean search syntax is supported: e.g. Balb* for partial matches or mus AND NOT embryo to exclude a term

Search results 101 to 182 out of 182 for Fpr1

<< First    < Previous  |  Next >    Last >>
0.025s
Type Details Score
Publication        
First Author: GemPharmatech
Year: 2020
Title: GemPharmatech Website.
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: 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: MGI Genome Annotation Group and UniGene Staff
Year: 2015
Journal: Database Download
Title: MGI-UniGene Interconnection Effort
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: 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 NCBI annotations
Publication      
First Author: Mouse Genome Informatics Group
Year: 2003
Journal: Database Procedure
Title: Automatic Encodes (AutoE) Reference
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: Mouse Genome Informatics
Year: 2010
Journal: Database Release
Title: Protein Ontology Association Load.
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: 2009
Journal: Database Download
Title: Mouse Microarray Data Integration in Mouse Genome Informatics, the Affymetrix GeneChip Mouse Gene 1.0 ST Array Platform
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 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: Le Naour J
Year: 2021
Journal: Cancer Discov
Title: A TLR3 Ligand Reestablishes Chemotherapeutic Responses in the Context of FPR1 Deficiency.
Volume: 11
Issue: 2
Pages: 408-423
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: 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: Alvarez V
Year: 1996
Journal: Immunogenetics
Title: Molecular evolution of the N-formyl peptide and C5a receptors in non-human primates.
Volume: 44
Issue: 6
Pages: 446-52
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: 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: Liu X
Year: 2012
Journal: Nat Immunol
Title: Bidirectional regulation of neutrophil migration by mitogen-activated protein kinases.
Volume: 13
Issue: 5
Pages: 457-64
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: Steinckwich N
Year: 2015
Journal: FASEB J
Title: Role of the store-operated calcium entry protein, STIM1, in neutrophil chemotaxis and infiltration into a murine model of psoriasis-inflamed skin.
Volume: 29
Issue: 7
Pages: 3003-13
Publication
First Author: Seidel S
Year: 2012
Journal: Am J Physiol Renal Physiol
Title: Annexin A1 modulates macula densa function by inhibiting cyclooxygenase 2.
Volume: 303
Issue: 6
Pages: F845-54
Publication  
First Author: Hu Y
Year: 2023
Journal: Metabolism
Title: Hepatocyte-secreted FAM3D ameliorates hepatic steatosis by activating FPR1-hnRNP U-GR-SCAD pathway to enhance lipid oxidation.
Volume: 146
Pages: 155661
Publication
First Author: He L
Year: 2018
Journal: Arterioscler Thromb Vasc Biol
Title: Deficiency of FAM3D (Family With Sequence Similarity 3, Member D), A Novel Chemokine, Attenuates Neutrophil Recruitment and Ameliorates Abdominal Aortic Aneurysm Development.
Volume: 38
Issue: 7
Pages: 1616-1631
Publication
First Author: Cooray SN
Year: 2013
Journal: Proc Natl Acad Sci U S A
Title: Ligand-specific conformational change of the G-protein-coupled receptor ALX/FPR2 determines proresolving functional responses.
Volume: 110
Issue: 45
Pages: 18232-7
Protein
Organism: Mus musculus/domesticus
Length: 364  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 351  
Fragment?: false
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 [].
Publication  
First Author: Lebtig M
Year: 2023
Journal: Front Immunol
Title: Keratinocytes use FPR2 to detect Staphylococcus aureus and initiate antimicrobial skin defense.
Volume: 14
Pages: 1188555
Protein
Organism: Mus musculus/domesticus
Length: 223  
Fragment?: false
Publication
First Author: Yang D
Year: 2002
Journal: J Leukoc Biol
Title: Human dendritic cells express functional formyl peptide receptor-like-2 (FPRL2) throughout maturation.
Volume: 72
Issue: 3
Pages: 598-607
Publication
First Author: Migeotte I
Year: 2005
Journal: J Exp Med
Title: Identification and characterization of an endogenous chemotactic ligand specific for FPRL2.
Volume: 201
Issue: 1
Pages: 83-93
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 [, ]. Formyl peptide receptor 3 (FPR3) is primarily a receptor of monocytes, macrophages and dendritic cells. It is also expressed on mouse, but not human, neutrophils [, , ]. Although FPR3 is found in human monocytes, studies have shown that approximately one third of individuals lack cell surface expression of this receptor [, ]. The functions of FPR3, other than directing cell migration, remain to be characterised [, ].
Publication
First Author: Crass T
Year: 1996
Journal: Eur J Immunol
Title: Expression cloning of the human C3a anaphylatoxin receptor (C3aR) from differentiated U-937 cells.
Volume: 26
Issue: 8
Pages: 1944-50
Protein
Organism: Mus musculus/domesticus
Length: 343  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 339  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 323  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 351  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 339  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 338  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 339  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 351  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 344  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 477  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 371  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 477  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 358  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 301  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 181  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 193  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 477  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 301  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 371  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 226  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 358  
Fragment?: false