Identification and characterization of S2V, a novel putative siglec that contains two V set Ig-like domains and recruits protein-tyrosine phosphatases SHPs (Q33944757)

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English	Identification and characterization of S2V, a novel putative siglec that contains two V set Ig-like domains and recruits protein-tyrosine phosphatases SHPs	scientific article

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scholarly article

1 reference

Europe PubMed Central

30 July 2017

Identification and characterization of S2V, a novel putative siglec that contains two V set Ig-like domains and recruits protein-tyrosine phosphatases SHPs (English)

1 reference

Europe PubMed Central

30 July 2017

author name string

Yu Z

1

1 reference

Europe PubMed Central

30 July 2017

Lai CM

2

1 reference

Europe PubMed Central

30 July 2017

Maoui M

3

1 reference

Europe PubMed Central

30 July 2017

Banville D

4

1 reference

Europe PubMed Central

30 July 2017

Shen SH

5

1 reference

Europe PubMed Central

30 July 2017

language of work or name

0 references

publication date

27 April 2001

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Europe PubMed Central

30 July 2017

Journal of Biological Chemistry

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Europe PubMed Central

30 July 2017

276

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Europe PubMed Central

30 July 2017

23816-23824

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Europe PubMed Central

30 July 2017

26

1 reference

Europe PubMed Central

30 July 2017

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Cytoplasmic protein tyrosine phosphatases SHP-1 and SHP-2: regulators of B cell signal transduction.

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Mutations at the murine motheaten locus are within the hematopoietic cell protein-tyrosine phosphatase (Hcph) gene.

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Cloning, characterization, and phylogenetic analysis of siglec-9, a new member of the CD33-related group of siglecs. Evidence for co-evolution with sialic acid synthesis pathways

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The amino-terminal immunoglobulin-like domain of sialoadhesin contains the sialic acid binding site. Comparison with CD22.

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Characterization of the sialic acid-binding site in sialoadhesin by site-directed mutagenesis

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Myelin-associated glycoprotein interacts with neurons via a sialic acid binding site at ARG118 and a distinct neurite inhibition site

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A role in B cell activation for CD22 and the protein tyrosine phosphatase SHP

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The sialoadhesin CD33 is a myeloid-specific inhibitory receptor

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The myeloid-specific sialic acid-binding receptor, CD33, associates with the protein-tyrosine phosphatases, SHP-1 and SHP-2

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A protein-tyrosine phosphatase with sequence similarity to the SH2 domain of the protein-tyrosine kinases

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PILRalpha, a novel immunoreceptor tyrosine-based inhibitory motif-bearing protein, recruits SHP-1 upon tyrosine phosphorylation and is paired with the truncated counterpart PILRbeta

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LAIR-1, a novel inhibitory receptor expressed on human mononuclear leukocytes

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The tyrosine phosphatase PTP1C associates with Vav, Grb2, and mSos1 in hematopoietic cells

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The B-cell antigen CD22 mediates monocyte and erythrocyte adhesion

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SHP-1 associates with both platelet-derived growth factor receptor and the p85 subunit of phosphatidylinositol 3-kinase

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mSiglec-E, a novel mouse CD33-related siglec (sialic acid-binding immunoglobulin-like lectin) that recruits Src homology 2 (SH2)-domain-containing protein tyrosine phosphatases SHP-1 and SHP-2

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Identifiers

10.1074/JBC.M102394200

1 reference

Europe PubMed Central

30 July 2017

1 reference

Europe PubMed Central

30 July 2017

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