The WW module competes with the SH3 domain?

[1] WWP, A NEW AMINO-ACID MOTIF PRESENT IN SINGLE OR MULTIPLE COPIES IN VARIOUS PROTEINS INCLUDING DYSTROPHIN AND THE SH3-BINDING YES-ASSOCIATED PROTEIN YAP65 [J]. BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, 1994, 205 (02) : 1201 - 1205

[2] THE WW DOMAIN - A SIGNALING SITE IN DYSTROPHIN [J]. TRENDS IN BIOCHEMICAL SCIENCES, 1994, 19 (12) : 531 - 533

[3] Formin binding proteins bear WWP/WW domains that bind proline-rich peptides and functionally resemble SH3 domains [J]. EMBO JOURNAL, 1996, 15 (05) : 1045 - 1054

[4] THE WW DOMAIN OF YES-ASSOCIATED PROTEIN BINDS A PROLINE-RICH LIGAND THAT DIFFERS FROM THE CONSENSUS ESTABLISHED FOR SRC HOMOLOGY 3-BINDING MODULES [J]. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1995, 92 (17) : 7819 - 7823

[5] EINBOND A, IN PRESS FEBS LETT

[6] FLORE F, 1995, J BIOL CHEM, V270, P30853

[7] A DE-NOVO MISSENSE MUTATION OF THE BETA-SUBUNIT OF THE EPITHELIAL SODIUM-CHANNEL CAUSES HYPERTENSION AND LIDDLE SYNDROME, IDENTIFYING A PROLINE-RICH SEGMENT CRITICAL FOR REGULATION OF CHANNEL ACTIVITY [J]. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1995, 92 (25) : 11495 - 11499

[8] SITE-DIRECTED MUTAGENESIS OF THE SH2-CODING AND SH3-CODING DOMAINS OF C-SRC PRODUCES VARIED PHENOTYPES, INCLUDING ONCOGENIC ACTIVATION OF P60C-SRC [J]. MOLECULAR AND CELLULAR BIOLOGY, 1990, 10 (04) : 1307 - 1318

[9] THE RSP5-DOMAIN IS SHARED BY PROTEINS OF DIVERSE FUNCTIONS [J]. FEBS LETTERS, 1995, 358 (02) : 153 - 157

[10] A NOVEL VIRAL ONCOGENE WITH STRUCTURAL SIMILARITY TO PHOSPHOLIPASE-C [J]. NATURE, 1988, 332 (6161) : 272 - 275

[1] WWP, A NEW AMINO-ACID MOTIF PRESENT IN SINGLE OR MULTIPLE COPIES IN VARIOUS PROTEINS INCLUDING DYSTROPHIN AND THE SH3-BINDING YES-ASSOCIATED PROTEIN YAP65 [J]. BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, 1994, 205 (02) : 1201 - 1205

[2] THE WW DOMAIN - A SIGNALING SITE IN DYSTROPHIN [J]. TRENDS IN BIOCHEMICAL SCIENCES, 1994, 19 (12) : 531 - 533

[3] Formin binding proteins bear WWP/WW domains that bind proline-rich peptides and functionally resemble SH3 domains [J]. EMBO JOURNAL, 1996, 15 (05) : 1045 - 1054

[4] THE WW DOMAIN OF YES-ASSOCIATED PROTEIN BINDS A PROLINE-RICH LIGAND THAT DIFFERS FROM THE CONSENSUS ESTABLISHED FOR SRC HOMOLOGY 3-BINDING MODULES [J]. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1995, 92 (17) : 7819 - 7823

[5] EINBOND A, IN PRESS FEBS LETT

[6] FLORE F, 1995, J BIOL CHEM, V270, P30853

[7] A DE-NOVO MISSENSE MUTATION OF THE BETA-SUBUNIT OF THE EPITHELIAL SODIUM-CHANNEL CAUSES HYPERTENSION AND LIDDLE SYNDROME, IDENTIFYING A PROLINE-RICH SEGMENT CRITICAL FOR REGULATION OF CHANNEL ACTIVITY [J]. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1995, 92 (25) : 11495 - 11499

[8] SITE-DIRECTED MUTAGENESIS OF THE SH2-CODING AND SH3-CODING DOMAINS OF C-SRC PRODUCES VARIED PHENOTYPES, INCLUDING ONCOGENIC ACTIVATION OF P60C-SRC [J]. MOLECULAR AND CELLULAR BIOLOGY, 1990, 10 (04) : 1307 - 1318

[9] THE RSP5-DOMAIN IS SHARED BY PROTEINS OF DIVERSE FUNCTIONS [J]. FEBS LETTERS, 1995, 358 (02) : 153 - 157

[10] A NOVEL VIRAL ONCOGENE WITH STRUCTURAL SIMILARITY TO PHOSPHOLIPASE-C [J]. NATURE, 1988, 332 (6161) : 272 - 275