Year |
Citation |
Score |
2020 |
Negishi M, Kobayashi K, Sakuma T, Sueyoshi T. Nuclear receptor phosphorylation in xenobiotic signal transduction. The Journal of Biological Chemistry. PMID 32788213 DOI: 10.1074/jbc.rev120.007933 |
0.317 |
|
2020 |
Fashe M, Hashiguchi T, Negishi M, Sueyoshi T. Ser100-Phosphorylated ROR Orchestrates CAR and HNF4 to Form Active Chromatin Complex in Response to Phenobarbital to Regulate Induction of CYP2B6. Molecular Pharmacology. 97: 191-201. PMID 31924695 DOI: 10.1124/mol.119.118273 |
0.339 |
|
2019 |
Shizu R, Yokobori K, Perera L, Pedersen L, Negishi M. Ligand induced dissociation of the AR homodimer precedes AR monomer translocation to the nucleus. Scientific Reports. 9: 16734. PMID 31723170 DOI: 10.1038/S41598-019-53139-9 |
0.602 |
|
2017 |
Shizu R, Min J, Sobhany M, Pedersen LC, Mutoh S, Negishi M. Interaction of the phosphorylated DNA-binding domain in nuclear receptor CAR with its ligand binding domain regulates CAR activation. The Journal of Biological Chemistry. PMID 29133527 DOI: 10.1074/Jbc.M117.806604 |
0.311 |
|
2017 |
Shizu R, Osabe M, Perera L, Moore R, Sueyoshi T, Negishi M. Phosphorylated nuclear receptor CAR forms a homodimer to repress its constitutive activity for ligand activation. Molecular and Cellular Biology. PMID 28265001 DOI: 10.1128/Mcb.00649-16 |
0.554 |
|
2013 |
Mutoh S, Sobhany M, Moore R, Perera L, Pedersen L, Sueyoshi T, Negishi M. Phenobarbital indirectly activates the constitutive active androstane receptor (CAR) by inhibition of epidermal growth factor receptor signaling. Science Signaling. 6: ra31. PMID 23652203 DOI: 10.1126/Scisignal.2003705 |
0.595 |
|
2012 |
Sobhany M, Kakuta Y, Sugiura N, Kimata K, Negishi M. The structural basis for a coordinated reaction catalyzed by a bifunctional glycosyltransferase in chondroitin biosynthesis. The Journal of Biological Chemistry. 287: 36022-8. PMID 22936799 DOI: 10.1074/jbc.M112.375873 |
0.312 |
|
2012 |
Shindo S, Sakuma T, Negishi M, Squires J. Phosphorylation of serine 212 confers novel activity to human estrogen receptor α. Steroids. 77: 448-53. PMID 22266331 DOI: 10.1016/j.steroids.2012.01.001 |
0.314 |
|
2009 |
Mutoh S, Osabe M, Inoue K, Moore R, Pedersen L, Perera L, Rebolloso Y, Sueyoshi T, Negishi M. Dephosphorylation of threonine 38 is required for nuclear translocation and activation of human xenobiotic receptor CAR (NR1I3). The Journal of Biological Chemistry. 284: 34785-92. PMID 19858220 DOI: 10.1074/Jbc.M109.048108 |
0.62 |
|
2006 |
Hosseinpour F, Moore R, Negishi M, Sueyoshi T. Serine 202 regulates the nuclear translocation of constitutive active/androstane receptor. Molecular Pharmacology. 69: 1095-102. PMID 16377764 DOI: 10.1124/mol.105.019505 |
0.309 |
|
2005 |
Ferguson SS, Chen Y, LeCluyse EL, Negishi M, Goldstein JA. Human CYP2C8 is transcriptionally regulated by the nuclear receptors constitutive androstane receptor, pregnane X receptor, glucocorticoid receptor, and hepatic nuclear factor 4alpha. Molecular Pharmacology. 68: 747-57. PMID 15933212 DOI: 10.1124/Mol.105.013169 |
0.326 |
|
2005 |
Ueda A, Matsui K, Yamamoto Y, Pedersen LC, Sueyoshi T, Negishi M. Thr176 regulates the activity of the mouse nuclear receptor CAR and is conserved in the NR1I subfamily members PXR and VDR. The Biochemical Journal. 388: 623-30. PMID 15610065 DOI: 10.1042/Bj20041572 |
0.356 |
|
2004 |
Moon AF, Edavettal SC, Krahn JM, Munoz EM, Negishi M, Linhardt RJ, Liu J, Pedersen LC. Structural analysis of the sulfotransferase (3-o-sulfotransferase isoform 3) involved in the biosynthesis of an entry receptor for herpes simplex virus 1. The Journal of Biological Chemistry. 279: 45185-93. PMID 15304505 DOI: 10.1074/Jbc.M405013200 |
0.303 |
|
2004 |
Edavettal SC, Lee KA, Negishi M, Linhardt RJ, Liu J, Pedersen LC. Crystal structure and mutational analysis of heparan sulfate 3-O-sulfotransferase isoform 1. The Journal of Biological Chemistry. 279: 25789-97. PMID 15060080 DOI: 10.1074/Jbc.M401089200 |
0.322 |
|
2003 |
Lee KA, Fuda H, Lee YC, Negishi M, Strott CA, Pedersen LC. Crystal structure of human cholesterol sulfotransferase (SULT2B1b) in the presence of pregnenolone and 3'-phosphoadenosine 5'-phosphate. Rationale for specificity differences between prototypical SULT2A1 and the SULT2BG1 isoforms. The Journal of Biological Chemistry. 278: 44593-9. PMID 12923182 DOI: 10.1074/Jbc.M308312200 |
0.305 |
|
2003 |
Negishi M, Dong J, Darden TA, Pedersen LG, Pedersen LC. Glucosaminylglycan biosynthesis: what we can learn from the X-ray crystal structures of glycosyltransferases GlcAT1 and EXTL2. Biochemical and Biophysical Research Communications. 303: 393-8. PMID 12659829 DOI: 10.1016/S0006-291X(03)00356-5 |
0.517 |
|
2003 |
Kakuta Y, Li L, Pedersen LC, Pedersen LG, Negishi M. Heparan sulphate N-sulphotransferase activity: reaction mechanism and substrate recognition. Biochemical Society Transactions. 31: 331-4. PMID 12653630 DOI: 10.1042/Bst0310331 |
0.544 |
|
2003 |
Pedersen LC, Dong J, Taniguchi F, Kitagawa H, Krahn JM, Pedersen LG, Sugahara K, Negishi M. Crystal structure of an alpha 1,4-N-acetylhexosaminyltransferase (EXTL2), a member of the exostosin gene family involved in heparan sulfate biosynthesis. The Journal of Biological Chemistry. 278: 14420-8. PMID 12562774 DOI: 10.1074/Jbc.M210532200 |
0.537 |
|
2003 |
Gorokhov A, Negishi M, Johnson EF, Pedersen LC, Perera L, Darden TA, Pedersen LG. Explicit water near the catalytic I helix Thr in the predicted solution structure of CYP2A4. Biophysical Journal. 84: 57-68. PMID 12524265 DOI: 10.1016/S0006-3495(03)74832-2 |
0.634 |
|
2002 |
Pedersen LC, Petrotchenko E, Shevtsov S, Negishi M. Crystal structure of the human estrogen sulfotransferase-PAPS complex: evidence for catalytic role of Ser137 in the sulfuryl transfer reaction. The Journal of Biological Chemistry. 277: 17928-32. PMID 11884392 DOI: 10.1074/Jbc.M111651200 |
0.329 |
|
2001 |
Negishi M, Pedersen LG, Petrotchenko E, Shevtsov S, Gorokhov A, Kakuta Y, Pedersen LC. Structure and function of sulfotransferases. Archives of Biochemistry and Biophysics. 390: 149-57. PMID 11396917 DOI: 10.1006/Abbi.2001.2368 |
0.516 |
|
2001 |
Yoshinari K, Petrotchenko EV, Pedersen LC, Negishi M. Crystal structure-based studies of cytosolic sulfotransferase. Journal of Biochemical and Molecular Toxicology. 15: 67-75. PMID 11284047 DOI: 10.1002/Jbt.1 |
0.304 |
|
2000 |
Gorokhov A, Perera L, Darden TA, Negishi M, Pedersen LC, Pedersen LG. Heparan sulfate biosynthesis: a theoretical study of the initial sulfation step by N-deacetylase/N-sulfotransferase. Biophysical Journal. 79: 2909-17. PMID 11106599 DOI: 10.1016/S0006-3495(00)76528-3 |
0.621 |
|
2000 |
Pedersen LC, Tsuchida K, Kitagawa H, Sugahara K, Darden TA, Negishi M. Heparan/chondroitin sulfate biosynthesis. Structure and mechanism of human glucuronyltransferase I. The Journal of Biological Chemistry. 275: 34580-5. PMID 10946001 DOI: 10.1074/Jbc.M007399200 |
0.307 |
|
2000 |
Pedersen LC, Petrotchenko EV, Negishi M. Crystal structure of SULT2A3, human hydroxysteroid sulfotransferase. Febs Letters. 475: 61-4. PMID 10854859 DOI: 10.1016/S0014-5793(00)01479-4 |
0.323 |
|
1999 |
Bidwell LM, McManus ME, Gaedigk A, Kakuta Y, Negishi M, Pedersen L, Martin JL. Crystal structure of human catecholamine sulfotransferase. Journal of Molecular Biology. 293: 521-30. PMID 10543947 DOI: 10.1006/Jmbi.1999.3153 |
0.325 |
|
1999 |
Ong E, Yeh JC, Ding Y, Hindsgaul O, Pedersen LC, Negishi M, Fukuda M. Structure and function of HNK-1 sulfotransferase. Identification of donor and acceptor binding sites by site-directed mutagenesis. The Journal of Biological Chemistry. 274: 25608-12. PMID 10464296 DOI: 10.1074/Jbc.274.36.25608 |
0.359 |
|
1998 |
Sueyoshi T, Kakuta Y, Pedersen LC, Wall FE, Pedersen LG, Negishi M. A role of Lys614 in the sulfotransferase activity of human heparan sulfate N-deacetylase/N-sulfotransferase. Febs Letters. 433: 211-4. PMID 9744796 DOI: 10.1016/S0014-5793(98)00913-2 |
0.508 |
|
1998 |
Kakuta Y, Pedersen LG, Pedersen LC, Negishi M. Conserved structural motifs in the sulfotransferase family. Trends in Biochemical Sciences. 23: 129-30. PMID 9584614 DOI: 10.1016/S0968-0004(98)01182-7 |
0.432 |
|
1997 |
Kakuta Y, Pedersen LG, Carter CW, Negishi M, Pedersen LC. Crystal structure of estrogen sulphotransferase. Nature Structural Biology. 4: 904-8. PMID 9360604 DOI: 10.1038/Nsb1197-904 |
0.487 |
|
1996 |
Negishi M, Uno T, Honkakoski P, Sueyoshi T, Darden TA, Pedersen LP. The roles of individual amino acids in altering substrate specificity of the P450 2a4/2a5 enzymes. Biochimie. 78: 685-94. PMID 9010596 DOI: 10.1016/S0300-9084(97)82525-4 |
0.325 |
|
1996 |
Negishi M, Iwasaki M, Juvonen RO, Sueyoshi T, Darden TA, Pedersen LG. Structural flexibility and functional versatility of cytochrome P450 and rapid evolution. Mutation Research. 350: 43-50. PMID 8657195 DOI: 10.1016/0027-5107(95)00089-5 |
0.535 |
|
1996 |
Negishi M, Uno T, Darden TA, Sueyoshi T, Pedersen LG. Structural flexibility and functional versatility of mammalian P450 enzymes. Faseb Journal : Official Publication of the Federation of American Societies For Experimental Biology. 10: 683-9. PMID 8635685 DOI: 10.1096/Fasebj.10.7.8635685 |
0.53 |
|
1995 |
Iwasaki M, Davis DG, Darden TA, Pedersen LG, Negishi M. Multiple steroid-binding orientations: alteration of regiospecificity of dehydroepiandrosterone 2- and 7-hydroxylase activities of cytochrome P-450 2a-5 by mutation of residue 209. The Biochemical Journal. 306: 29-33. PMID 7864823 DOI: 10.1042/Bj3060029 |
0.506 |
|
1995 |
Iwasaki M, Darden TA, Pedersen LG, Negishi M. Altering the regiospecificity of androstenedione hydroxylase activity in P450s 2a-4/5 by a mutation of the residue at position 481. Biochemistry. 34: 5054-9. PMID 7711025 DOI: 10.1021/Bi00015A016 |
0.498 |
|
1992 |
Negishi M, Iwasaki M, Juvonen RO, Aida K. Alteration of the substrate specificity of mouse 2A P450s by the identity of residue-209: Steroid-binding site and orientation Journal of Steroid Biochemistry and Molecular Biology. 43: 1031-1036. PMID 22217847 DOI: 10.1016/0960-0760(92)90330-L |
0.358 |
|
1989 |
Lindberg RLP, Negishi M. Alteration of mouse cytochrome P450coh substrate specificity by mutation of a single amino-acid residue Nature. 339: 632-634. PMID 2733794 DOI: 10.1038/339632a0 |
0.328 |
|
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