Within the hemopoietic system, LAR phosphatase is a T cell lineage-specific adhesion receptor-like protein whose phosphatase activity appears dispensable for T cell development, repertoire selection and function (Q32159773)

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English	Within the hemopoietic system, LAR phosphatase is a T cell lineage-specific adhesion receptor-like protein whose phosphatase activity appears dispensable for T cell development, repertoire selection and function	scientific article

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scholarly article

1 reference

Europe PubMed Central

PubMed publication ID

6 July 2017

Within the hemopoietic system, LAR phosphatase is a T cell lineage-specific adhesion receptor-like protein whose phosphatase activity appears dispensable for T cell development, repertoire selection and function (English)

1 reference

Europe PubMed Central

PubMed publication ID

6 July 2017

author name string

Terszowski G

1

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Europe PubMed Central

PubMed publication ID

6 July 2017

Jankowski A

2

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Europe PubMed Central

PubMed publication ID

6 July 2017

Hendriks WJ

3

1 reference

Europe PubMed Central

PubMed publication ID

6 July 2017

Rolink AG

4

1 reference

Europe PubMed Central

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6 July 2017

Kisielow P

5

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Europe PubMed Central

PubMed publication ID

6 July 2017

language of work or name

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publication date

1 March 2001

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Europe PubMed Central

PubMed publication ID

6 July 2017

European Journal of Immunology

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Europe PubMed Central

PubMed publication ID

6 July 2017

31

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Europe PubMed Central

PubMed publication ID

6 July 2017

3

1 reference

Europe PubMed Central

PubMed publication ID

6 July 2017

832-840

1 reference

Europe PubMed Central

PubMed publication ID

6 July 2017

The next wave: protein tyrosine phosphatases enter T cell antigen receptor signalling

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A new member of the immunoglobulin superfamily that has a cytoplasmic region homologous to the leukocyte common antigen

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Form, function, and regulation of protein tyrosine phosphatases and their involvement in human diseases.

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Neural cell adhesion molecule: structure, immunoglobulin-like domains, cell surface modulation, and alternative RNA splicing

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Crystal structure of the tandem phosphatase domains of RPTP LAR

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Association between a transmembrane protein tyrosine phosphatase and the cadherin-catenin complex.

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The laminin-nidogen complex is a ligand for a specific splice isoform of the transmembrane protein tyrosine phosphatase LAR

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Deficient LAR expression decreases basal forebrain cholinergic neuronal size and hippocampal cholinergic innervation

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Impaired mammary gland development and function in mice lacking LAR receptor-like tyrosine phosphatase activity.

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The transmembrane protein-tyrosine phosphatase LAR modulates signaling by multiple receptor tyrosine kinases

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Overexpression of the transmembrane tyrosine phosphatase LAR activates the caspase pathway and induces apoptosis

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Transmembrane tyrosine phosphatase LAR induces apoptosis by dephosphorylating and destabilizing p130Cas

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Developmental expression of the cell adhesion molecule-like protein tyrosine phosphatases LAR, RPTPdelta and RPTPsigma in the mouse

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The LAR/PTP delta/PTP sigma subfamily of transmembrane protein-tyrosine-phosphatases: multiple human LAR, PTP delta, and PTP sigma isoforms are expressed in a tissue-specific manner and associate with the LAR-interacting protein LIP.1

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Identifiers

10.1002/1521-4141(200103)31:3<832::AID-IMMU832>3.0.CO;2-D

1 reference

Europe PubMed Central

PubMed publication ID

6 July 2017

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

6 July 2017

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