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Marius Sudol
Marius Sudol
Adjunct Associate Professor, Mount Sinai School of Medicine, NYC
Verified email at mssm.edu - Homepage
Title
Cited by
Cited by
Year
The importance of being proline: the interaction of proline‐rich motifs in signaling proteins with their cognate domains
BK Kay, MP Williamson, M Sudol
The FASEB journal 14 (2), 231-241, 2000
16022000
Signal transducing molecules and glycosyl-phosphatidylinositol-linked proteins form a caveolin-rich insoluble complex in MDCK cells
M Sargiacomo, M Sudol, ZL Tang, MP Lisanti
The Journal of cell biology 122 (4), 789-807, 1993
11961993
Akt phosphorylates the Yes-associated protein, YAP, to induce interaction with 14-3-3 and attenuation of p73-mediated apoptosis
S Basu, NF Totty, MS Irwin, M Sudol, J Downward
Molecular cell 11 (1), 11-23, 2003
10062003
The WW domain of Yes-associated protein binds a proline-rich ligand that differs from the consensus established for Src homology 3-binding modules.
HI Chen, M Sudol
Proceedings of the National Academy of Sciences 92 (17), 7819-7823, 1995
7181995
WW and SH3 domains, two different scaffolds to recognize proline-rich ligands
MJ Macias, S Wiesner, M Sudol
FEBS letters 513 (1), 30-37, 2002
6092002
Structure of the WW domain of a kinase-associated protein complexed with a proline-rich peptide
MJ Macias, M Hyv÷nen, E Baraldi, J Schultz, M Sudol, M Saraste, ...
Nature 382 (6592), 646-649, 1996
5651996
The WW domain: a signalling site in dystrophin?
P Bork, M Sudol
Trends in biochemical sciences 19 (12), 531-533, 1994
5381994
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
A Komuro, M Nagai, NE Navin, M Sudol
Journal of Biological Chemistry 278 (35), 33334-33341, 2003
5362003
Physical interaction with Yes-associated protein enhances p73 transcriptional activity
S Strano, E Munarriz, M Rossi, L Castagnoli, Y Shaul, A Sacchi, M Oren, ...
Journal of Biological Chemistry 276 (18), 15164-15173, 2001
5302001
Yes-associated protein (YAP65) is a proline-rich phosphoprotein that binds to the SH3 domain of the Yes proto-oncogene product.
M Sudol
Oncogene 9 (8), 2145-2152, 1994
5241994
Characterization of a novel protein-binding module—the WW domain
M Sudol, HI Chen, C Bougeret, A Einbond, P Bork
FEBS letters 369 (1), 67-71, 1995
4831995
YAP/TAZ as mechanosensors and mechanotransducers in regulating organ size and tumor growth
BC Low, CQ Pan, GV Shivashankar, A Bershadsky, M Sudol, M Sheetz
FEBS letters 588 (16), 2663-2670, 2014
4642014
NeW wrinkles for an old domain
M Sudol, T Hunter
Cell 103 (7), 1001-1004, 2000
4532000
Structure and function of the WW domain
M Sudol
Progress in biophysics and molecular biology 65 (1-2), 113-132, 1996
4271996
Characterization of the Mammalian YAP (Yes-associated Protein) Gene and Its Role in Defining a Novel Protein Module, the WW Domain∗
M Sudol, P Bork, A Einbond, K Kastury, T Druck, M Negrini, K Huebner, ...
Journal of Biological Chemistry 270 (24), 14733-14741, 1995
4031995
A proline-rich motif within the matrix protein of vesicular stomatitis virus and rabies virus interacts with WW domains of cellular proteins: implications for viral budding
RN Harty, J Paragas, M Sudol, P Palese
Journal of virology 73 (4), 2921-2929, 1999
3971999
Mst2 and Lats kinases regulate apoptotic function of Yes kinase-associated protein (YAP)
T Oka, V Mazack, M Sudol
Journal of Biological Chemistry 283 (41), 27534-27546, 2008
3862008
Structure of a WW domain containing fragment of dystrophin in complex with β-dystroglycan
X Huang, F Poy, R Zhang, A Joachimiak, M Sudol, MJ Eck
Nature structural biology 7 (8), 634-638, 2000
3602000
The WW domain of neural protein FE65 interacts with proline-rich motifs in Mena, the mammalian homolog of Drosophilaenabled
KS Ermekova, N Zambrano, H Linn, G Minopoli, F Gertler, T Russo, ...
Journal of Biological Chemistry 272 (52), 32869-32877, 1997
3451997
From Src Homology domains to other signaling modules: proposal of theprotein recognition code'
M Sudol
Oncogene 17 (11), 1469-1474, 1998
3151998
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