Prolyl isomerases and nuclear function

[11] The Drosophila melanogaster dodo (dod) gene, conserved in humans, is functionally interchangeable with the ESS1 cell division gene of Saccharomyces cerevisiae [J]. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1996, 93 (01) : 447 - 451

[12] Differential regulation of c-Myb-induced transcription activation by a phosphorylation site in the negative regulatory domain [J]. JOURNAL OF BIOLOGICAL CHEMISTRY, 1996, 271 (37) : 22697 - 22705

[13] The Myb oncoprotein: Regulating a regulator [J]. BIOCHIMICA ET BIOPHYSICA ACTA-REVIEWS ON CANCER, 1996, 1288 (03): : F123 - F139

[14] OGATA K, 1994, CELL, V79, P539

[15] CONFIRMATION OF THE EXISTENCE OF A 3RD FAMILY AMONG PEPTIDYL-PROLYL CIS/TRANS ISOMERASES - AMINO-ACID-SEQUENCE AND RECOMBINANT PRODUCTION OF PARVULIN [J]. FEBS LETTERS, 1994, 352 (02) : 180 - 184

[16] Structural and functional analysis of the mitotic rotamase Pin1 suggests substrate recognition is phosphorylation dependent [J]. CELL, 1997, 89 (06) : 875 - 886

[17] PROTEIN-FOLDING - PROLYL ISOMERASES JOIN THE FOLD [J]. CURRENT BIOLOGY, 1995, 5 (09) : 993 - 994

[18] Catalysis of protein folding by parvulin [J]. JOURNAL OF MOLECULAR BIOLOGY, 1997, 273 (03) : 752 - 762

[19] Cyclophilin active site mutants have native prolyl isomerase activity with a protein substrate [J]. FEBS LETTERS, 1997, 414 (01) : 69 - 73

[20] SHEN M, 1998, IN PRESS GENES DEV

[11] The Drosophila melanogaster dodo (dod) gene, conserved in humans, is functionally interchangeable with the ESS1 cell division gene of Saccharomyces cerevisiae [J]. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1996, 93 (01) : 447 - 451

[12] Differential regulation of c-Myb-induced transcription activation by a phosphorylation site in the negative regulatory domain [J]. JOURNAL OF BIOLOGICAL CHEMISTRY, 1996, 271 (37) : 22697 - 22705

[13] The Myb oncoprotein: Regulating a regulator [J]. BIOCHIMICA ET BIOPHYSICA ACTA-REVIEWS ON CANCER, 1996, 1288 (03): : F123 - F139

[14] OGATA K, 1994, CELL, V79, P539

[15] CONFIRMATION OF THE EXISTENCE OF A 3RD FAMILY AMONG PEPTIDYL-PROLYL CIS/TRANS ISOMERASES - AMINO-ACID-SEQUENCE AND RECOMBINANT PRODUCTION OF PARVULIN [J]. FEBS LETTERS, 1994, 352 (02) : 180 - 184

[16] Structural and functional analysis of the mitotic rotamase Pin1 suggests substrate recognition is phosphorylation dependent [J]. CELL, 1997, 89 (06) : 875 - 886

[17] PROTEIN-FOLDING - PROLYL ISOMERASES JOIN THE FOLD [J]. CURRENT BIOLOGY, 1995, 5 (09) : 993 - 994

[18] Catalysis of protein folding by parvulin [J]. JOURNAL OF MOLECULAR BIOLOGY, 1997, 273 (03) : 752 - 762

[19] Cyclophilin active site mutants have native prolyl isomerase activity with a protein substrate [J]. FEBS LETTERS, 1997, 414 (01) : 69 - 73

[20] SHEN M, 1998, IN PRESS GENES DEV