Marius Sudol mainly investigates WW domain, Cell biology, Peptide sequence, Biochemistry and Genetics. The various areas that Marius Sudol examines in his WW domain study include Protein structure, Transcription factor, Dystrophin and Binding site. His Transcription factor research includes themes of Molecular biology, Cytoplasm, Nuclear localization sequence and Signal transducing adaptor protein.
Marius Sudol has researched Binding site in several fields, including Plasma protein binding, Computational biology and Phosphotyrosine binding. His Cell biology research is multidisciplinary, incorporating perspectives in Actin cytoskeleton, Cell membrane and Utrophin. His research integrates issues of Src homology domain, Proto-oncogene tyrosine-protein kinase Src and Homology in his study of Peptide sequence.
His scientific interests lie mostly in Cell biology, WW domain, Hippo signaling pathway, Signal transduction and Cancer research. His studies deal with areas such as VP40 and Transcription factor as well as Cell biology. The WW domain study combines topics in areas such as Peptide sequence, Computational biology and Protein domain.
Marius Sudol combines subjects such as Molecular biology, Binding site and Homology with his study of Peptide sequence. His study in Hippo signaling pathway is interdisciplinary in nature, drawing from both Endocrinology, Bioinformatics and Transcription Coactivator. His Genetics study combines topics in areas such as Protein structure and Plasma protein binding.
His primary areas of study are Cell biology, Hippo signaling pathway, Cancer research, VP40 and WW domain. His research brings together the fields of Cell growth and Cell biology. The subject of his Hippo signaling pathway research is within the realm of Genetics.
His Cancer research research includes elements of Cancer, Suppressor, EZH2, Transforming growth factor and Lung cancer. He integrates WW domain with Neurodegeneration in his research. The concepts of his Signal transduction study are interwoven with issues in GTPase, Metastasis, Circulating tumor cell, Cytoskeleton and Phosphorylation.
The scientist’s investigation covers issues in Cell biology, Hippo signaling pathway, Signal transduction, WW domain and RHOA. Marius Sudol combines topics linked to VP40 with his work on Cell biology. His Hippo signaling pathway study combines topics from a wide range of disciplines, such as Epithelial–mesenchymal transition, RUNX2, Transcription factor and Phenotype.
His biological study spans a wide range of topics, including PDZ domain, Threonine Phosphorylation Site, Protein phosphorylation and 14-3-3 protein, Phosphorylation. The various areas that Marius Sudol examines in his WW domain study include Human cell and Signaling proteins. His studies deal with areas such as Metastasis, Circulating tumor cell, Cytoskeleton and Actin as well as RHOA.
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The importance of being proline: the interaction of proline-rich motifs in signaling proteins with their cognate domains
Brian K. Kay;Michael P. Williamson;Marius Sudol.
The FASEB Journal (2000)
Signal transducing molecules and glycosyl-phosphatidylinositol-linked proteins form a caveolin-rich insoluble complex in MDCK cells
M. Sargiacomo;M. Sudol;Zhaolan Tang;M. P. Lisanti.
Journal of Cell Biology (1993)
Akt phosphorylates the Yes-associated protein, YAP, to induce interaction with 14-3-3 and attenuation of p73-mediated apoptosis.
Subham Basu;Nicholas F Totty;Meredith S Irwin;Marius Sudol.
Molecular Cell (2003)
The WW domain of Yes-associated protein binds a proline-rich ligand that differs from the consensus established for Src homology 3-binding modules
Henry I. Chen;Marius Sudol.
Proceedings of the National Academy of Sciences of the United States of America (1995)
WW and SH3 domains, two different scaffolds to recognize proline-rich ligands
Maria J. Macias;Silke Wiesner;Marius Sudol.
FEBS Letters (2002)
Structure of the WW domain of a kinase-associated protein complexed with a proline-rich peptide
Maria J. Macias;Marko Hyvönen;Elena Baraldi;Johan Schultz.
The WW domain: a signalling site in dystrophin?
Peer Bork;Marius Sudol.
Trends in Biochemical Sciences (1994)
WW domain-containing protein YAP associates with ErbB-4 and acts as a co-transcriptional activator for the carboxyl-terminal fragment of ErbB-4 that translocates to the nucleus
Akihiko Komuro;Makoto Nagai;Nicholas E. Navin;Marius Sudol.
Journal of Biological Chemistry (2003)
Physical interaction with Yes-associated protein enhances p73 transcriptional activity.
Sabrina Strano;Eliana Munarriz;Mario Rossi;Luisa Castagnoli.
Journal of Biological Chemistry (2001)
Yes-associated protein (YAP65) is a proline-rich phosphoprotein that binds to the SH3 domain of the Yes proto-oncogene product.
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