S. Fischer

发表

The tyrosine kinase activity of p56lck is increased in human T cells activated via CD2

A. Alcover, O. Acuto, R. Fagard, 1991, European journal of immunology.

Endothelin induces tyrosine phosphorylation and GRB2 association of Shc in astrocytes.

A. Strosberg, F. Schweighoffer, S. Cazaubon, 1994, The Journal of biological chemistry.

Correlation between phosphorylation and kinase activity of a tyrosine protein kinase: p56lck.

R. Fagard, I. Boulet, S. Fischer, 1987, Biochemical and biophysical research communications.

hSiah 2 Is a New Vav Binding Protein Which Inhibits Vav-Mediated Signaling Pathways

N. Varin‐Blank, J. Camonis, F. Romero, 1999 .

hSiah2 Is a New Vav Binding Protein Which Inhibits Vav-Mediated Signaling Pathways

N. Varin‐Blank, J. Camonis, F. Romero, 1999, Molecular and Cellular Biology.

Erythropoietin induces the association of phosphatidylinositol 3'-kinase with a tyrosine-phosphorylated protein complex containing the erythropoietin receptor.

W. Vainchenker, B. Druker, I. Dusanter-Fourt, 1993, European journal of biochemistry.

Erythropoietin induces the tyrosine phosphorylation of its own receptor in human erythropoietin-responsive cells.

N. Casadevall, I. Dusanter-Fourt, C. Lacombe, 1992, The Journal of biological chemistry.

p95 Associates with the Nuclear Protein Ku-70

J. Camonis, C. Dargemont, F. Romero, 1995 .

Activation of p56lck by p72syk through physical association and N-terminal tyrosine phosphorylation

A. Altman, G. Baier, S. Williams, 1994, Molecular and cellular biology.

Functional implications of tyrosine protein phosphorylation in platelets. Simultaneous studies with different agonists and inhibitors.

B. Druker, E. Cano, F. Rendu, 1992, The Biochemical journal.

Activation of p 561 ck by p 72 , k through Physical Association and N-Terminal Tyrosine Phosphorylationt

Gabriele, A. Altman, G. Baier, 2022 .

CSF-1 stimulation induces the formation of a multiprotein complex including CSF-1 receptor, c-Cbl, PI 3-kinase, Crk-II and Grb2

H. Husson, B. Mograbi, B. Rossi, 1997, Oncogene.

The proline-rich region of Vav binds to Grb2 and Grb3-3.

J. Camonis, F. Schweighoffer, G. Bismuth, 1995, Oncogene.

Vav binds to several SH2/SH3 containing proteins in activated lymphocytes.

B. Druker, F. Ramos-Morales, S. Fischer, 1994, Oncogene.

Activation and internalization of p56lck upon CD45 triggering of Jurkat cells

I. Maridonneau-Parini, A. Marie-Cardine, S. Fischer, 1994, European journal of immunology.

Purification of the LSTRA tyrosine protein kinase (p56lck).

R. Fagard, S. Fischer, H. Van Tan, 1988, European journal of biochemistry.

Both T cell receptor (TcR)‐CD3 complex and CD2 increase the tyrosine kinase activity of p56lck. CD2 can mediate TcR‐CD3‐independent and CD45‐dependent activation of p56lck

A. Alcover, O. Acuto, R. Fagard, 1992, European journal of immunology.

Recruitment of Activated p56lck on Endosomes of CD2-triggered T Cells, Colocalization with ZAP-70*

J. Gorvel, I. Maridonneau-Parini, A. Marie-Cardine, 1996, The Journal of Biological Chemistry.

Phosphorylation of the N and M1 proteins of rabies virus.

C. Tuffereau, A. Flamand, S. Fischer, 1985, The Journal of general virology.

The amino terminal region of the p56 lck from LSTRA exerts negative modulation on the tyrosine kinase activity.

R. Fagard, I. Boulet, J. Gesquiere, 1987, Biochemical and biophysical research communications.

Tyr394 and Tyr505 are autophosphorylated in recombinant Lck protein-tyrosine kinase expressed in Escherichia coli.

R. Benarous, L. Camoin, H. Durand, 1994, European journal of biochemistry.

The lymphocyte‐specific protein tyrosine kinase p56lck is hyperphosphorylated on serine and tyrosine residues within minutes after activation via T cell receptor or CD2

A. Alcover, O. Acuto, R. Fagard, 1989, European journal of immunology.

Synthesis and phosphorylation of cytoskeleton components in foetal, regenerating and adult normal rat hepatocytes during culture

G. Baffet, B. Clement, S. Fischer, 1985, Molecular and Cellular Biochemistry.

Structure and function of vav.

F. Romero, S. Fischer, 1996, Cellular signalling.

Detection of a Physical and Functional Interaction between Csk and Lck Which Involves the SH2 Domain of Csk and Is Mediated by Autophosphorylation of Lck on Tyrosine 394 (*)

H. Hanafusa, R. Benarous, H. Sabe, 1996, The Journal of Biological Chemistry.

Identification of JAK protein tyrosine kinases as signaling molecules for prolactin. Functional analysis of prolactin receptor and prolactin‐erythropoietin receptor chimera expressed in lymphoid cells.

A. Wilks, I. Dusanter-Fourt, A. Ziemiecki, 1994, The EMBO journal.

Grb2 and Its Apoptotic Isoform Grb3-3 Associate with Heterogeneous Nuclear Ribonucleoprotein C, and These Interactions Are Modulated by Poly(U) RNA*

B. Tocqué, F. Schweighoffer, F. Ramos-Morales, 1998, The Journal of Biological Chemistry.

Vav Binding to Heterogeneous Nuclear Ribonucleoprotein (hnRNP) C

N. Varin‐Blank, J. Camonis, F. Romero, 1998, The Journal of Biological Chemistry.

p 95 vav Associates with the Nuclear Protein Ku-70

J. Camonis, C. Dargemont, F. Romero, 1995 .

The multiple endocrine neoplasia type 2B point mutation switches the specificity of the Ret tyrosine kinase towards cellular substrates that are susceptible to interact with Crk and Nck

M. Borrello, M. Pierotti, B. Pasini, 1997, Oncogene.

Recombinant Csk expressed in Escherichia coli is autophosphorylated on tyrosine residue(s).

R. Benarous, C. Bougeret, R Benarous, 1993, Oncogene.

Association of the protein tyrosine phosphatase PTP1C with the protein tyrosine kinase c‐Src in human platelets

F. Ramos-Morales, F. Rendu, H. Falet, 1996, FEBS letters.

The src-family protein-tyrosine kinase p59hck is located on the secretory granules in human neutrophils and translocates towards the phagosome during cell activation.

I. Maridonneau-Parini, V. Le Cabec, S. Fischer, 1995, The Biochemical journal.

P56lck A lymphocyte specific protein tyrosine kinase: activation, regulation and signal transduction.

R. Benarous, F. Ramos-Morales, I. Maridonneau-Parini, 1994, Cellular and molecular biology.

Recombinant CSK Expressed in E.Coli is Phosphorylated on Tyrosine Residue(s) and Undergoes in Vitro Phosphorylation

R. Benarous, C. Bougeret, S. Fischer, 1993 .

Structure of the human lck gene: differences in genomic organisation within src-related genes affect only N-terminal exons.

R. Benarous, E. Rouer, M. Lang, 1989, Gene.

Naturally occurring anti-idiotypic antibodies to anti-phosphotyrosine in systemic lupus erythematosus interact with SRC-homology 2 domains.

F. Ramos-Morales, A. Onu, M. Stefănescu, 1995, Autoimmunity.

Spleen protein tyrosine kinases TPK‐IIB and CSK display different immunoreactivity and opposite specificities toward c‐src‐derived peptides

Stefan Fischer, R. Benarous, A. Brunati, 1992, FEBS letters.

p95vav associates with the nuclear protein Ku-70

J. Camonis, C. Dargemont, F. Romero, 1996, Molecular and Cellular Biology.