Dominique Davidson

发表

Genetic evidence linking SAP, the X-linked lymphoproliferative gene product, to Src-related kinase FynT in T(H)2 cytokine regulation.

Hao Wang, Y. Yanagi, A. Veillette, 2004, Immunity.

Negative regulation of T-cell receptor signalling by tyrosine protein kinase p50csk

M. Fournel, A. Veillette, L. Chow, 1993, Nature.

Inhibitory Tyrosine Protein Kinase p50 csk Is Associated with Protein-tyrosine Phosphatase PTP-PEST in Hemopoietic and Non-hemopoietic Cells*

J. Cloutier, A. Gregorieff, A. Veillette, 1997, The Journal of Biological Chemistry.

Clnk, a Novel Slp-76–Related Adaptor Molecule Expressed in Cytokine-Stimulated Hemopoietic Cells

M. Cao, S. Latour, A. Veillette, 1999, The Journal of experimental medicine.

Synergistic Regulation of Immunoreceptor Signaling by SLP-76-Related Adaptor Clnk and Serine/Threonine Protein Kinase HPK-1

C. Riou, A. Veillette, Jie Yu, 2001, Molecular and Cellular Biology.

Raft-Associated Transmembrane Adaptor T-Cell Activation by PAG/Cbp, a Lipid Phosphorylation-Dependent Regulation of

A. Veillette, Marcin Bakinowski, V. Hořejší, 2014 .

Negative regulation of immunoreceptor signaling.

S. Latour, D. Davidson, A. Veillette, 2002, Annual review of immunology.

Cis interactions between CD2 and its ligands on T cells are required for T cell activation

B. Malissen, R. Roncagalli, Yan Lu, 2022, Science Immunology.

Protein Tyrosine Phosphatase α Regulates Fyn Activity and Cbp/PAG Phosphorylation in Thymocyte Lipid Rafts1

C. Pallen, A. Veillette, H. T. Le, 2005, The Journal of Immunology.

SAP expression in T cells, not in B cells, is required for humoral immunity

A. Veillette, Xiaochu Shi, Zhongjun Dong, 2008, Proceedings of the National Academy of Sciences.

Combined mTOR and MEK inhibition is an effective therapy in a novel mouse model for angiosarcoma

E. Boscolo, Yi Zheng, Anita Gupta, 2018, Oncotarget.

AXL confers cell migration and invasion by hijacking a PEAK1-regulated focal adhesion protein network

A. Gingras, Marie-Anne Goyette, R. Daly, 2020, Nature Communications.

PTP-PEST/PTPN12Protein Tyrosine Phosphatase Macrophage Fusion Is Controlled by the

J. Vacher, C. M. Souza, Inmoo Rhee, 2014 .

Macrophage Fusion Is Controlled by the Cytoplasmic Protein Tyrosine Phosphatase PTP-PEST/PTPN12

J. Vacher, C. M. Souza, Inmoo Rhee, 2013, Molecular and Cellular Biology.

The Noncatalytic Domain of Protein-tyrosine Phosphatase-PEST Targets Paxillin for Dephosphorylation in Vivo *

M. Schaller, A. Veillette, Patrick D. Lyons, 2000, The Journal of Biological Chemistry.

Differential Requirement for the SAP-Fyn Interaction during NK T Cell Development and Function1

K. Nichols, M. Juntilla, G. Koretzky, 2008, The Journal of Immunology.

Binding of SAP SH2 domain to FynT SH3 domain reveals a novel mechanism of receptor signalling in immune regulation

P. Schwartzberg, S. Latour, R. Roncagalli, 2003, Nature Cell Biology.

Critical Role of Lipid Scramblase TMEM16F in Phosphatidylserine Exposure and Repair of Plasma Membrane after Pore Formation.

H. McBride, Shanshan Luo, Ning Wu, 2020, Cell reports.

PEST family phosphatases in immunity, autoimmunity, and autoinflammatory disorders

C. M. Souza, Inmoo Rhee, A. Veillette, 2009, Immunological reviews.

Inflammatory macrophages exploit unconventional pro-phagocytic integrins for phagocytosis and anti-tumor immunity.

D. Davidson, A. Veillette, Jin Qian, 2021, Cell reports.

SLAMF7 is critical for phagocytosis of haematopoietic tumour cells via Mac-1 integrin

J. Danska, D. Vinh, Inmoo Rhee, 2017, Nature.

DNAM-1 controls NK cell activation via an ITT-like motif

M. Colonna, Ning Wu, Yan Lu, 2015, The Journal of experimental medicine.

Deletion of Slam locus in mice reveals inhibitory role of SLAM family in NK cell responses regulated by cytokines and LFA-1

Ning Wu, Yan Lu, S. Waggoner, 2016, The Journal of experimental medicine.

Correction: Deletion of Slam locus in mice reveals inhibitory role of SLAM family in NK cell responses regulated by cytokines and LFA-1

Ning Wu, Yan Lu, S. Waggoner, 2016, The Journal of experimental medicine.

Dok-3, a Novel Adapter Molecule Involved in the Negative Regulation of Immunoreceptor Signaling

S. Latour, A. Veillette, S. Lemay, 2000, Molecular and Cellular Biology.

The Csk-Associated Adaptor PAG Inhibits Effector T Cell Activation in Cooperation with Phosphatase PTPN22 and Dok Adaptors.

Brian Seed, Pier Paolo Pandolfi, R. Xavier, 2016, Cell reports.

Chk, a Csk Family Tyrosine Protein Kinase, Exhibits Csk-like Activity in Fibroblasts, but Not in an Antigen-specific T-cell Line*

A. Veillette, L. Chow, D. Davidson, 1997, The Journal of Biological Chemistry.

The phosphatase PTP-PEST promotes secondary T cell responses by dephosphorylating the protein tyrosine kinase Pyk2.

Inmoo Rhee, D. Davidson, A. Veillette, 2010, Immunity.

Phosphorylation-Dependent Regulation of T-Cell Activation by PAG/Cbp, a Lipid Raft-Associated Transmembrane Adaptor

V. Horejsi, D. Davidson, A. Veillette, 2003, Molecular and Cellular Biology.

Interactions of CD45-associated Protein with the Antigen Receptor Signaling Machinery in T-lymphocytes*

S. Latour, A. Veillette, F. Gervais, 1999, The Journal of Biological Chemistry.

PAG-Associated FynT Regulates Calcium Signaling and Promotes Anergy in T Lymphocytes

B. Schraven, D. Davidson, A. Veillette, 2007, Molecular and Cellular Biology.

Lck-dependent Fyn Activation Requires C Terminus-dependent Targeting of Kinase-active Lck to Lipid Rafts*

A. Veillette, M. Julius, O. Ballek, 2008, Journal of Biological Chemistry.

Inhibition of the Jun N-Terminal Protein Kinase Pathway by SHIP-1, a Lipid Phosphatase That Interacts with the Adaptor Molecule Dok-3

D. Davidson, A. Veillette, Jeffrey D. Robson, 2004, Molecular and Cellular Biology.

PTP‐PEST, a scaffold protein tyrosine phosphatase, negatively regulates lymphocyte activation by targeting a unique set of substrates

A. Veillette, D. Davidson, Dominique Davidson, 2001, The EMBO journal.

The adaptor SAP controls NK cell activation by regulating the enzymes Vav-1 and SHIP-1 and by enhancing conjugates with target cells.

W. Swat, T. Kurosaki, D. Davidson, 2012, Immunity.

EAT-2, a SAP-like adaptor, controls NK cell activation through phospholipase Cγ, Ca++, and Erk, leading to granule polarization

S. Latour, A. Veillette, Luis-Alberto Pérez-Quintero, 2014, The Journal of experimental medicine.

The Phosphatase PTP-PEST/PTPN12 Regulates Endothelial Cell Migration and Adhesion, but Not Permeability, and Controls Vascular Development and Embryonic Viability*

J. Gratton, C. M. Souza, Inmoo Rhee, 2012, The Journal of Biological Chemistry.

Loss of PTPN12 Stimulates Progression of ErbB2-Dependent Breast Cancer by Enhancing Cell Survival, Migration, and Epithelial-to-Mesenchymal Transition

Morag Park, W. Muller, Morag Park, 2015, Molecular and Cellular Biology.

Developing combination immunotherapies against cancer that make sense

A. Veillette, Dominique Davidson, 2018, Science Immunology.

Immunology: When lymphocytes run out of steam

A. Veillette, Dominique Davidson, 2014, Nature.

A. Veillette, D. Davidson, Dominique Davidson, 1992, Trends in genetics : TIG.

Differential regulation of T cell antigen responsiveness by isoforms of the src-related tyrosine protein kinase p59fyn

M. Fournel, A. Veillette, L. Chow, 1992, The Journal of experimental medicine.

The adaptor SAP controls NK cell activation by regulating the enzymes Vav-1 and SHIP-1 and by enhancing conjugates with target cells.

W. Swat, T. Kurosaki, A. Veillette, 2012, Immunity.

Unique catalytic properties dictate the enhanced function of p59fynT, the hemopoietic cell-specific isoform of the Fyn tyrosine protein kinase, in T cells

A. Veillette, J. Viallet, D. Davidson, 1994, Molecular and cellular biology.

CD47 masks pro-phagocytic ligands in cis on tumor cells to suppress antitumor immunity

A. Veillette, E. Hui, Yunlong Zhao, 2023, Nature Immunology.

Oncogenic activation of p59fyn tyrosine protein kinase by mutation of its carboxyl-terminal site of tyrosine phosphorylation, tyrosine 528.

M. Fournel, A. Veillette, D Davidson, 1994, The Journal of biological chemistry.