M. Šuša

M. Šuša, M. Brandi, M. Jeschke, 1998, Journal of bone and mineral research : the official journal of the American Society for Bone and Mineral Research.

Localization of G-proteins in macrophages and E. coli during phagocytosis.

M. Šuša, I. Buchwalow, K. Augsten, 1996, Acta Histochemica.

Follicle-Stimulating Hormone Does Not Impact Male Bone Mass In Vivo or Human Male Osteoclasts In Vitro

M. Šuša, B. Fournier, F. Morvan, 2008, Calcified Tissue International.

In vitro evidence for modification of rat liver glucocorticoid receptor binding properties and transformation by hyperthermia.

M. Šuša, S. Damjanovic, G. Matić, 1989, Journal of steroid biochemistry.

PI 3-kinase activation in BCR/abl-transformed hematopoietic cells does not require interaction of p85 SH2 domains with p210 BCR/abl

B. Druker, M. Šuša, M. Keeler, 1996 .

Active recombinant human tyrosine kinase c-Yes: expression in baculovirus system, purification, comparison to c-Src, and inhibition by a c-Src inhibitor.

M. Šuša, G. Mcmaster, M. Missbach, 2000, Protein expression and purification.

Studying gene expression in bone by in situ hybridization.

Rishard Salie, M. Šuša, M. Kneissel, 2012, Methods in molecular biology.

Ubiquitous overexpression of Hey1 transcription factor leads to osteopenia and chondrocyte hypertrophy in bone.

Rishard Salie, M. Šuša, Matthias Mueller, 2010, Bone.

Transcriptional Program of Mouse Osteoclast Differentiation Governed by the Macrophage Colony-stimulating Factor and the Ligand for the Receptor Activator of NFκB*

Sandrine Bongiovanni, David Cappellen, M. Šuša, 2002, The Journal of Biological Chemistry.

Role of PI 3-kinase in mitogenesis.

M. Šuša, M. Keeler, L. Varticovski, 1994, Biochimica et biophysica acta.

Fluoroaluminate induces pertussis toxin-sensitive protein phosphorylation: differences in MC3T3-E1 osteoblastic and NIH3T3 fibroblastic cells.

M. Šuša, D. Rohner, M. Jeschke, 1997, Biochemical and biophysical research communications.

Coordinated Activation of Notch, Wnt, and Transforming Growth Factor-β Signaling Pathways in Bone Morphogenic Protein 2-induced Osteogenesis

M. Šuša, D. Cappellen, N. Zamurović, 2004, Journal of Biological Chemistry.

EGF receptor‐mediated, c‐Src‐dependent, activation of Stat5b is downregulated in mitogenically responsive hepatocytes

M. Šuša, J. Ødegård, G. H. Thoresen, 2003, Journal of cellular physiology.

PI 3-kinase activation in BCR/abl-transformed hematopoietic cells does not require interaction of p85 SH2 domains with p210 BCR/abl.

S. Jain, B. Druker, M. Šuša, 1996, Blood.

Inhibition of Protein Kinase c-Src Reduces the Incidence of Breast Cancer Metastases and Increases Survival in Mice: Implications for Therapy

D. Fabbro, A. Angelucci, M. Šuša, 2006, Journal of Pharmacology and Experimental Therapeutics.

EGF induces biphasic S6 kinase activation: Late phase is protein kinase C-dependent and contributes to mitogenicity

D. Fabbro, M. Šuša, G. Thomas, 1989, Cell.

Identical Mr 70,000 S6 kinase is activated biphasically by epidermal growth factor: a phosphopeptide that characterizes the late phase.

M. Šuša, G. Thomas, 1990, Proceedings of the National Academy of Sciences of the United States of America.

Fluoroaluminate Induces Activation and Association of Src and Pyk2 Tyrosine Kinases in Osteoblastic MC3T3-E1 Cells*

M. Šuša, M. Jeschke, G. Standke, 1998, The Journal of Biological Chemistry.

A novel inhibitor of the tyrosine kinase Src suppresses phosphorylation of its major cellular substrates and reduces bone resorption in vitro and in rodent models in vivo.

M. Šuša, J. Green, J. Feyen, 1999, Bone.

Coordinated activation of Notch, Wnt and TGF-β signaling pathways in BMP-2 induced osteogenesis: Notch target gene Hey1 inhibits mineralization and Runx2 transcriptional activity

M. Šuša, D. Cappellen, N. Zamurović, 2004 .

7-Alkyl- and 7-cycloalkyl-5-aryl-pyrrolo[2,3-d]pyrimidines--potent inhibitors of the tyrosine kinase c-Src.

E. Altmann, M. Šuša, J. Green, 2001, Bioorganic & medicinal chemistry letters.

Differences in binding of PI 3-kinase to the src-homology domains 2 and 3 of p56 lck and p59 fyn tyrosine kinases.

M. Šuša, S. Bichsel, D. Rohner, 1996, Biochemical and biophysical research communications.

Src as a Target for Pharmaceutical Intervention

M. Šuša, T. O'reilly, A. Teti, 2006 .

Reduction of c-Src activity by substituted 5,7-diphenyl-pyrrolo[2,3-d]-pyrimidines induces osteoclast apoptosis in vivo and in vitro. Involvement of ERK1/2 pathway.

D. Fabbro, M. Šuša, A. Teti, 2004, Bone.

Phosphatidylinositol 3-kinase activity in murine erythroleukemia cells during DMSO-induced differentiation.

Z Ai, M. Šuša, L. Varticovski, 1995, Experimental cell research.

7-Pyrrolidinyl- and 7-piperidinyl-5-aryl-pyrrolo[2,3-d]pyrimidines--potent inhibitors of the tyrosine kinase c-Src.

E. Altmann, M. Šuša, J. Green, 2001, Bioorganic & medicinal chemistry letters.

Substituted 5,7-diphenyl-pyrrolo[2,3d]pyrimidines: potent inhibitors of the tyrosine kinase c-Src.

E. Altmann, M. Šuša, J. Green, 2000, Bioorganic & medicinal chemistry letters.