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Search results 401 to 500 out of 530 for Cd22

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Hits by Strain

Type Details Score
Gene Segment
Type: gene_segment
Organism: mouse, laboratory
Gene Segment
Type: gene_segment
Organism: mouse, laboratory
Gene Segment
Type: gene_segment
Organism: mouse, laboratory
Gene Segment
Type: gene_segment
Organism: mouse, laboratory
Gene Segment
Type: gene_segment
Organism: mouse, laboratory
Gene Segment
Type: gene_segment
Organism: mouse, laboratory
Gene Segment
Type: gene_segment
Organism: mouse, laboratory
Gene Segment
Type: gene_segment
Organism: mouse, laboratory
Gene Segment
Type: gene_segment
Organism: mouse, laboratory
Gene Segment
Type: gene_segment
Organism: mouse, laboratory
Gene Segment
Type: gene_segment
Organism: mouse, laboratory
Gene Segment
Type: gene_segment
Organism: mouse, laboratory
Gene Segment
Type: gene_segment
Organism: mouse, laboratory
Gene Segment
Type: gene_segment
Organism: mouse, laboratory
Gene Segment
Type: gene_segment
Organism: mouse, laboratory
Gene Segment
Type: gene_segment
Organism: mouse, laboratory
Gene Segment
Type: gene_segment
Organism: mouse, laboratory
Gene Segment
Type: gene_segment
Organism: mouse, laboratory
Gene Segment
Type: gene_segment
Organism: mouse, laboratory
Gene Segment
Type: gene_segment
Organism: mouse, laboratory
Gene Segment
Type: gene_segment
Organism: mouse, laboratory
Protein
Organism: Mus musculus/domesticus
Length: 116  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 108  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 104  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 117  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 104  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 209  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 120  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 595  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 101  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 116  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 116  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 99  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 113  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 98  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 120  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 120  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 116  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 100  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 119  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 120  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 119  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 118  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 117  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 100  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 119  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 116  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 98  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 115  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 105  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 119  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 116  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 119  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 117  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 120  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 119  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 117  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 119  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 120  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 120  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 131  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 119  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 106  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 100  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 116  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 118  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 120  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 99  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 120  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 117  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 119  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 117  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 114  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 117  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 119  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 117  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 116  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 119  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 99  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 117  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 120  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 119  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 120  
Fragment?: true
Publication
First Author: Briscoe CP
Year: 2003
Journal: J Biol Chem
Title: The orphan G protein-coupled receptor GPR40 is activated by medium and long chain fatty acids.
Volume: 278
Issue: 13
Pages: 11303-11
Publication
First Author: Itoh Y
Year: 2003
Journal: Nature
Title: Free fatty acids regulate insulin secretion from pancreatic beta cells through GPR40.
Volume: 422
Issue: 6928
Pages: 173-6
Protein Domain
Type: Family
Description: G protein-coupled receptors (GPCRs) constitute a vast protein family that encompasses a wide range of functions (including various autocrine, paracrine and endocrine processes). They show considerable diversity at the sequence level, on the basis of which they can be separated into distinct groups. We use the term clan to describe the GPCRs, as they embrace a group of families for which there are indications of evolutionary relationship, but between which there is no statistically significant similarity in sequence []. The currently known clan members include the rhodopsin-like GPCRs, the secretin-like GPCRs, the cAMP receptors, the fungal mating pheromone receptors, and the metabotropic glutamate receptor family. The rhodopsin-like GPCRs themselves represent a widespread protein family that includes hormone, neurotransmitter and light receptors, all of which transduce extracellular signals through interaction with guanine nucleotide-binding (G) proteins. Although their activating ligands vary widely in structure and character, the amino acid sequences of the receptors are very similar and are believed to adopt a common structural framework comprising 7 transmembrane (TM) helices [, , ]. A cluster of four intronless GPCR genes, sharing significant sequence similarity with one another, have been identified on human chromosome 19q13.1, downstream from the CD22 gene []. The receptors have been named GPR40, GPR41, GPR42 and GPR43. The GPR42 protein sequence shares more than 98% amino acid identity with GPR41 and is located on a possible polymorphic insert []. GPR40 has recently been shown to bind long-chain free fatty acids, molecules that have a role in various cellular processes, including regulation of insulin secretion [, ]. Expression of GPR40 is restricted to the pancreas, with high levels in the islets and pancreatic beta cell lines []. Upon activation, GPR40 appears to couple predominantly to Gq and partially to Gi proteins, and has been shown to amplify glucose-stimulated insulin secretion from pancreatic beta cells. The receptor may therefore be a potential target for anti-diabetic drugs [].
Publication
First Author: Pfrengle F
Year: 2013
Journal: J Immunol
Title: Copresentation of antigen and ligands of Siglec-G induces B cell tolerance independent of CD22.
Volume: 191
Issue: 4
Pages: 1724-31
Publication
First Author: Hutzler S
Year: 2014
Journal: J Immunol
Title: The ligand-binding domain of Siglec-G is crucial for its selective inhibitory function on B1 cells.
Volume: 192
Issue: 11
Pages: 5406-14
Publication
First Author: Crocker PR
Year: 1994
Journal: EMBO J
Title: Sialoadhesin, a macrophage sialic acid binding receptor for haemopoietic cells with 17 immunoglobulin-like domains.
Volume: 13
Issue: 19
Pages: 4490-503
Publication
First Author: Bökers S
Year: 2014
Journal: J Immunol
Title: Siglec-G deficiency leads to more severe collagen-induced arthritis and earlier onset of lupus-like symptoms in MRL/lpr mice.
Volume: 192
Issue: 7
Pages: 2994-3002
Publication
First Author: Lim AK
Year: 2010
Journal: Diabetologia
Title: Lymphocytes promote albuminuria, but not renal dysfunction or histological damage in a mouse model of diabetic renal injury.
Volume: 53
Issue: 8
Pages: 1772-82
Publication
First Author: Zhou M
Year: 2021
Journal: J Immunol
Title: Integrin CD11b Negatively Regulates B Cell Receptor Signaling to Shape Humoral Response during Immunization and Autoimmunity.
Volume: 207
Issue: 7
Pages: 1785-1797
Publication
First Author: Xu Y
Year: 2002
Journal: J Immunol
Title: The activation and subsequent regulatory roles of Lyn and CD19 after B cell receptor ligation are independent.
Volume: 169
Issue: 12
Pages: 6910-8
Publication
First Author: Li X
Year: 2001
Journal: J Immunol
Title: Antigen receptor proximal signaling in splenic B-2 cell subsets.
Volume: 166
Issue: 5
Pages: 3122-9
Publication  
First Author: Irons EE
Year: 2020
Journal: Front Immunol
Title: Blood-Borne ST6GAL1 Regulates Immunoglobulin Production in B Cells.
Volume: 11
Pages: 617
Publication
First Author: Naito Y
Year: 2007
Journal: Mol Cell Biol
Title: Germinal center marker GL7 probes activation-dependent repression of N-glycolylneuraminic acid, a sialic acid species involved in the negative modulation of B-cell activation.
Volume: 27
Issue: 8
Pages: 3008-22
Publication
First Author: Ennerfelt H
Year: 2023
Journal: Proc Natl Acad Sci U S A
Title: CARD9 attenuates Aβ pathology and modifies microglial responses in an Alzheimer's disease mouse model.
Volume: 120
Issue: 24
Pages: e2303760120
Publication
First Author: Wei H
Year: 2013
Journal: J Biol Chem
Title: A modified form of diphthamide causes immunotoxin resistance in a lymphoma cell line with a deletion of the WDR85 gene.
Volume: 288
Issue: 17
Pages: 12305-12
Publication
First Author: Fujimoto M
Year: 2001
Journal: J Biol Chem
Title: CD19 amplification of B lymphocyte Ca2+ responses: a role for Lyn sequestration in extinguishing negative regulation.
Volume: 276
Issue: 48
Pages: 44820-7
Publication
First Author: Manzano M
Year: 2002
Journal: J Nutr
Title: Absolute counts and distribution of lymphocyte subsets in small intestine of BALB/c mice change during weaning.
Volume: 132
Issue: 9
Pages: 2757-62