Nanopublications LDF server

Matches in Nanopublications for { ?s ?p "A number of ubiquitin-like proteins have been discovered recently that are attached to lysine residues of target proteins in a way analogous to that of ubiquitylation. Among them, SUMO-1, which is highly conserved from yeast to humans, has been shown to modify a number of proteins such as RanGAP1 (Matunis et al., 1996; Mahajan et al., 1997), the two nuclear body PML and SP100 proteins (Sternsdorf et al., 1997; Kamitani et al., 1998; Muller et al., 1998), p53 (Gostissa et al., 1999; Rodriguez et al., 1999; Muller et al., 2000), IkappaBalpha (Desterro et al., 1998) and a growing number of other proteins including viral proteins (for reviews see Melchior, 2000; Muller et al., 2001; Seeler and Dejean, 2001). Unlike ubiquitylation, sumoylation does not appear to promote protein degradation but rather was shown to be involved in mediating protein/protein interactions, subcellular compartmentalization and protein stability. Conjugation of SUMO-1 requires the E1-activating heterodimer Aos1/Uba2 and the single E2-conjugating Ubc9 enzyme. Very recently, two distinct families of SUMO E3 ligases have been identified. In yeast, the majority of SUMO conjugation requires the Siz1 and Siz2 proteins (Johnson and Gupta, 2001; Takahashi et al., 2001). The mammalian proteins to which Siz1 and Siz2 are most closely related are the PIAS (protein inhibitor of activated STAT) proteins, and PIAS1 and PIASy were shown to catalyse sumoylation of p53 and LEF-1, respectively (Kahyo et al., 2001; Sachdev et al., 2001; reviewed in Hochstrasser, 2001)." ?g. }

• _5 value "A number of ubiquitin-like proteins have been discovered recently that are attached to lysine residues of target proteins in a way analogous to that of ubiquitylation. Among them, SUMO-1, which is highly conserved from yeast to humans, has been shown to modify a number of proteins such as RanGAP1 (Matunis et al., 1996; Mahajan et al., 1997), the two nuclear body PML and SP100 proteins (Sternsdorf et al., 1997; Kamitani et al., 1998; Muller et al., 1998), p53 (Gostissa et al., 1999; Rodriguez et al., 1999; Muller et al., 2000), IkappaBalpha (Desterro et al., 1998) and a growing number of other proteins including viral proteins (for reviews see Melchior, 2000; Muller et al., 2001; Seeler and Dejean, 2001). Unlike ubiquitylation, sumoylation does not appear to promote protein degradation but rather was shown to be involved in mediating protein/protein interactions, subcellular compartmentalization and protein stability. Conjugation of SUMO-1 requires the E1-activating heterodimer Aos1/Uba2 and the single E2-conjugating Ubc9 enzyme. Very recently, two distinct families of SUMO E3 ligases have been identified. In yeast, the majority of SUMO conjugation requires the Siz1 and Siz2 proteins (Johnson and Gupta, 2001; Takahashi et al., 2001). The mammalian proteins to which Siz1 and Siz2 are most closely related are the PIAS (protein inhibitor of activated STAT) proteins, and PIAS1 and PIASy were shown to catalyse sumoylation of p53 and LEF-1, respectively (Kahyo et al., 2001; Sachdev et al., 2001; reviewed in Hochstrasser, 2001)." provenance.
• _5 value "A number of ubiquitin-like proteins have been discovered recently that are attached to lysine residues of target proteins in a way analogous to that of ubiquitylation. Among them, SUMO-1, which is highly conserved from yeast to humans, has been shown to modify a number of proteins such as RanGAP1 (Matunis et al., 1996; Mahajan et al., 1997), the two nuclear body PML and SP100 proteins (Sternsdorf et al., 1997; Kamitani et al., 1998; Muller et al., 1998), p53 (Gostissa et al., 1999; Rodriguez et al., 1999; Muller et al., 2000), IkappaBalpha (Desterro et al., 1998) and a growing number of other proteins including viral proteins (for reviews see Melchior, 2000; Muller et al., 2001; Seeler and Dejean, 2001). Unlike ubiquitylation, sumoylation does not appear to promote protein degradation but rather was shown to be involved in mediating protein/protein interactions, subcellular compartmentalization and protein stability. Conjugation of SUMO-1 requires the E1-activating heterodimer Aos1/Uba2 and the single E2-conjugating Ubc9 enzyme. Very recently, two distinct families of SUMO E3 ligases have been identified. In yeast, the majority of SUMO conjugation requires the Siz1 and Siz2 proteins (Johnson and Gupta, 2001; Takahashi et al., 2001). The mammalian proteins to which Siz1 and Siz2 are most closely related are the PIAS (protein inhibitor of activated STAT) proteins, and PIAS1 and PIASy were shown to catalyse sumoylation of p53 and LEF-1, respectively (Kahyo et al., 2001; Sachdev et al., 2001; reviewed in Hochstrasser, 2001)." provenance.
• _5 value "A number of ubiquitin-like proteins have been discovered recently that are attached to lysine residues of target proteins in a way analogous to that of ubiquitylation. Among them, SUMO-1, which is highly conserved from yeast to humans, has been shown to modify a number of proteins such as RanGAP1 (Matunis et al., 1996; Mahajan et al., 1997), the two nuclear body PML and SP100 proteins (Sternsdorf et al., 1997; Kamitani et al., 1998; Muller et al., 1998), p53 (Gostissa et al., 1999; Rodriguez et al., 1999; Muller et al., 2000), IkappaBalpha (Desterro et al., 1998) and a growing number of other proteins including viral proteins (for reviews see Melchior, 2000; Muller et al., 2001; Seeler and Dejean, 2001). Unlike ubiquitylation, sumoylation does not appear to promote protein degradation but rather was shown to be involved in mediating protein/protein interactions, subcellular compartmentalization and protein stability. Conjugation of SUMO-1 requires the E1-activating heterodimer Aos1/Uba2 and the single E2-conjugating Ubc9 enzyme. Very recently, two distinct families of SUMO E3 ligases have been identified. In yeast, the majority of SUMO conjugation requires the Siz1 and Siz2 proteins (Johnson and Gupta, 2001; Takahashi et al., 2001). The mammalian proteins to which Siz1 and Siz2 are most closely related are the PIAS (protein inhibitor of activated STAT) proteins, and PIAS1 and PIASy were shown to catalyse sumoylation of p53 and LEF-1, respectively (Kahyo et al., 2001; Sachdev et al., 2001; reviewed in Hochstrasser, 2001)." provenance.
• _5 value "A number of ubiquitin-like proteins have been discovered recently that are attached to lysine residues of target proteins in a way analogous to that of ubiquitylation. Among them, SUMO-1, which is highly conserved from yeast to humans, has been shown to modify a number of proteins such as RanGAP1 (Matunis et al., 1996; Mahajan et al., 1997), the two nuclear body PML and SP100 proteins (Sternsdorf et al., 1997; Kamitani et al., 1998; Muller et al., 1998), p53 (Gostissa et al., 1999; Rodriguez et al., 1999; Muller et al., 2000), IkappaBalpha (Desterro et al., 1998) and a growing number of other proteins including viral proteins (for reviews see Melchior, 2000; Muller et al., 2001; Seeler and Dejean, 2001). Unlike ubiquitylation, sumoylation does not appear to promote protein degradation but rather was shown to be involved in mediating protein/protein interactions, subcellular compartmentalization and protein stability. Conjugation of SUMO-1 requires the E1-activating heterodimer Aos1/Uba2 and the single E2-conjugating Ubc9 enzyme. Very recently, two distinct families of SUMO E3 ligases have been identified. In yeast, the majority of SUMO conjugation requires the Siz1 and Siz2 proteins (Johnson and Gupta, 2001; Takahashi et al., 2001). The mammalian proteins to which Siz1 and Siz2 are most closely related are the PIAS (protein inhibitor of activated STAT) proteins, and PIAS1 and PIASy were shown to catalyse sumoylation of p53 and LEF-1, respectively (Kahyo et al., 2001; Sachdev et al., 2001; reviewed in Hochstrasser, 2001)." provenance.