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Search results 101 to 184 out of 184 for Fpr1

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Type Details Score
Publication
- | J:326541
       
First Author: Cyagen Biosciences Inc.
Year: 2022
Title: Cyagen Biosciences Website.
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Publication
- | J:342605
       
First Author: GOA curators
Year: 2016
Title: Automatic transfer of experimentally verified manual GO annotation data to orthologs using Ensembl Compara
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Publication
- | J:164563
       
First Author: The Gene Ontology Consortium
Year: 2010
Title: Automated transfer of experimentally-verified manual GO annotation data to mouse-human orthologs
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Publication
21267068 | J:153498
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
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Publication
- | J:157972
     
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).
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Publication
- | J:57747
     
First Author: MGI Genome Annotation Group and UniGene Staff
Year: 2015
Journal: Database Download
Title: MGI-UniGene Interconnection Effort
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Publication
- | J:161428
       
First Author: Marc Feuermann, Huaiyu Mi, Pascale Gaudet, Dustin Ebert, Anushya Muruganujan, Paul Thomas
Year: 2010
Title: Annotation inferences using phylogenetic trees
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Publication
- | J:63103
     
First Author: Mouse Genome Database and National Center for Biotechnology Information
Year: 2000
Journal: Database Release
Title: Entrez Gene Load
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Publication
- | J:262123
     
First Author: Allen Institute for Brain Science
Year: 2004
Journal: Allen Institute
Title: Allen Brain Atlas: mouse riboprobes
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Publication
- | J:144086
     
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
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Publication
- | J:155721
     
First Author: Mouse Genome Informatics (MGI) and The National Center for Biotechnology Information (NCBI)
Year: 2010
Journal: Database Download
Title: Consensus CDS project
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Publication
- | J:85324
     
First Author: Mouse Genome Informatics Group
Year: 2003
Journal: Database Procedure
Title: Automatic Encodes (AutoE) Reference
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Publication
- | J:53168
     
First Author: Bairoch A
Year: 1999
Journal: Database Release
Title: SWISS-PROT Annotated protein sequence database
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Publication
- | J:91388
       
First Author: Mouse Genome Informatics Scientific Curators
Year: 2005
Title: Obtaining and Loading Genome Assembly Coordinates from Ensembl Annotations
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Publication
- | J:155221
     
First Author: Mouse Genome Informatics
Year: 2010
Journal: Database Release
Title: Protein Ontology Association Load.
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Publication
- | J:90438
       
First Author: Mouse Genome Informatics Scientific Curators
Year: 2005
Title: Obtaining and loading genome assembly coordinates from NCBI annotations
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Publication
- | J:144087
     
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
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Publication
33046534 | J:301327
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
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Publication
28247283 | -
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
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Publication
22226334 | J:241065
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
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Protein Domain
IPR039240 | FAM3D
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 [].
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Publication
8824156 | J:36504
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
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Publication
9892621 | -
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
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Publication
1093163 | -
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
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Publication
7734243 | -
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
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Publication
18458054 | -
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
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Publication
9065470 | -
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
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Publication
15928303 | -
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
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Publication
19233142 | -
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
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Publication
15951351 | -
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
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Publication
17559171 | -
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
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Publication
22610094 | -
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
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Publication
1374236 | -
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
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Publication
16025565 | -
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
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Publication
21543323 | -
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
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Publication
23549262 | -
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
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Publication
15888909 | -
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
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Publication
23562731 | -
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
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Protein Domain
IPR027345 | Formyl_pep_1/2_rcpt
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 [].
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Publication
22447027 | J:185374
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
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Publication
17084101 | -
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
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Publication
19498085 | -
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
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Publication
12401407 | -
First Author: Le Y
Year: 2002
Journal: Trends Immunol
Title: Formyl-peptide receptors revisited.
Volume: 23
Issue: 11
Pages: 541-8
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Publication
16684671 | -
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
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Publication
11369647 | -
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
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Publication
23160941 | -
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
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Publication
16365159 | -
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
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Publication
37454871 | J:338854
 
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
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Publication
25837581 | J:225467
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
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Publication
22791338 | J:188531
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
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Publication
34494308 | J:357865
First Author: Liu W
Year: 2022
Journal: J Leukoc Biol
Title: Mitofusin-2 regulates leukocyte adhesion and β2 integrin activation.
Volume: 111
Issue: 4
Pages: 771-791
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Publication
24108355 | J:202942
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
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Publication
29853563 | J:304594
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
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Protein
P33766
Organism: Mus musculus/domesticus
Length: 364  
Fragment?: false
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Protein
O88536
Organism: Mus musculus/domesticus
Length: 351  
Fragment?: false
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Publication
8976386 | -
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
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Protein Domain
IPR000826 | Formyl_rcpt-rel
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 [].
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Publication
37325619 | J:346933
 
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
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Protein
P97805
Organism: Mus musculus/domesticus
Length: 223  
Fragment?: false
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Publication
12223529 | -
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
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Publication
15623572 | -
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
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Protein Domain
IPR027347 | Formyl_pep_3_rcpt
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 [, ].
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Publication
8765043 | -
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
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Protein
O88537
Organism: Mus musculus/domesticus
Length: 343  
Fragment?: false
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Protein
O88416
Organism: Mus musculus/domesticus
Length: 339  
Fragment?: false
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Protein
A4FUQ5
Organism: Mus musculus/domesticus
Length: 323  
Fragment?: false
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Protein
O08790
Organism: Mus musculus/domesticus
Length: 351  
Fragment?: false
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Protein
Q3SXG2
Organism: Mus musculus/domesticus
Length: 339  
Fragment?: false
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Protein
Q71MR7
Organism: Mus musculus/domesticus
Length: 338  
Fragment?: false
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Protein
D8VER2
Organism: Mus musculus/domesticus
Length: 339  
Fragment?: false
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Protein
P30993
Organism: Mus musculus/domesticus
Length: 351  
Fragment?: false
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Protein
Q8BW93
Organism: Mus musculus/domesticus
Length: 344  
Fragment?: false
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Protein
O09047
Organism: Mus musculus/domesticus
Length: 477  
Fragment?: false
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Protein
P97468
Organism: Mus musculus/domesticus
Length: 371  
Fragment?: false
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Protein
Q5U7A4
Organism: Mus musculus/domesticus
Length: 477  
Fragment?: false
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Protein
E9QQ21
Organism: Mus musculus/domesticus
Length: 358  
Fragment?: false
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Protein
Q3UCS9
Organism: Mus musculus/domesticus
Length: 301  
Fragment?: true
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Protein
A0A1B0GT01
Organism: Mus musculus/domesticus
Length: 181  
Fragment?: true
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Protein
Q3TYR0
Organism: Mus musculus/domesticus
Length: 193  
Fragment?: true
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Protein
Q8C6R2
Organism: Mus musculus/domesticus
Length: 477  
Fragment?: false
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Protein
E9Q8N2
Organism: Mus musculus/domesticus
Length: 301  
Fragment?: true
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Protein
Q497D3
Organism: Mus musculus/domesticus
Length: 371  
Fragment?: false
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Protein
Q3U4N3
Organism: Mus musculus/domesticus
Length: 226  
Fragment?: true
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Protein
E9PVQ2
Organism: Mus musculus/domesticus
Length: 358  
Fragment?: false
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MouseMine is a collaboration between MGI at The Jackson Laboratory and the InterMine project at the Cambridge Systems Biology Centre. MouseMine is funded through a grant from the NIH/NHGRI.The Jackson Laboratory makes no representation about the suitability or accuracy of this software or data for any purpose, and makes no warranties, either express or implied, including merchantability and fitness for a particular purpose or that the use of this software or data will not infringe any third party patents, copyrights, trademarks, or other rights. the software and data are provided "as is". This software and data are provided to enhance knowledge and encourage progress in the scientific community and are to be used only for research and educational purposes. Any reproduction or use for commercial purpose is prohibited without the prior express written permission of the Jackson Laboratory.

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