| Year |
Citation |
Score |
| 2021 |
Romartinez-Alonso B, Agostini M, Jones H, McLellan J, Sood D, Tomkinson N, Marelli F, Gentile I, Visser WE, Schoenmakers E, Fairall L, Privalsky M, Moran C, Persani L, Chatterjee K, et al. Structure-guided approach to relieving transcriptional repression inResistance to Thyroid Hormone α. Molecular and Cellular Biology. MCB0036321. PMID 34871063 DOI: 10.1128/MCB.00363-21 |
0.437 |
|
| 2019 |
Privalsky ML, Goodson ML. Evolution of NCoR-1 and NCoR-2 corepressor alternative mRNA splicing in placental mammals. Bmc Research Notes. 12: 343. PMID 31208445 DOI: 10.1186/S13104-019-4384-Z |
0.337 |
|
| 2018 |
Harrus D, Déméné H, Vasquez EF, Boulahtouf A, Germain P, Figueira AC, Privalsky ML, Bourguet W, le Maire A. Pathological interactions between mutant thyroid hormone receptors and corepressors and their modulation by a thyroid hormone analogue with therapeutic potential. Thyroid : Official Journal of the American Thyroid Association. PMID 30235988 DOI: 10.1089/Thy.2017.0551 |
0.561 |
|
| 2017 |
Jimenez R, Privalsky ML. Title: A resistance to thyroid hormone syndrome mutant operates through the target gene repertoire of the wild-type thyroid hormone receptor. Molecular and Cellular Endocrinology. PMID 28257829 DOI: 10.1016/J.Mce.2017.02.044 |
0.521 |
|
| 2016 |
Privalsky ML, Snyder CA, Goodson ML. Corepressor diversification by alternative mRNA splicing is species specific. Bmc Evolutionary Biology. 16: 221. PMID 27756201 DOI: 10.1186/S12862-016-0781-2 |
0.494 |
|
| 2015 |
Snyder CA, Goodson ML, Schroeder AC, Privalsky ML. Regulation of corepressor alternative mRNA splicing by hormonal and metabolic signaling. Molecular and Cellular Endocrinology. 413: 228-35. PMID 26166430 DOI: 10.1016/J.Mce.2015.06.036 |
0.684 |
|
| 2014 |
Goodson ML, Young BM, Snyder CA, Schroeder AC, Privalsky ML. Alteration of NCoR corepressor splicing in mice causes increased body weight and hepatosteatosis without glucose intolerance. Molecular and Cellular Biology. 34: 4104-14. PMID 25182530 DOI: 10.1128/Mcb.00554-14 |
0.656 |
|
| 2014 |
Schroeder AC, Privalsky ML. Thyroid hormones, t3 and t4, in the brain. Frontiers in Endocrinology. 5: 40. PMID 24744751 DOI: 10.3389/Fendo.2014.00040 |
0.669 |
|
| 2014 |
Schroeder A, Jimenez R, Young B, Privalsky ML. The ability of thyroid hormone receptors to sense t4 as an agonist depends on receptor isoform and on cellular cofactors. Molecular Endocrinology (Baltimore, Md.). 28: 745-57. PMID 24673558 DOI: 10.1210/Me.2013-1335 |
0.711 |
|
| 2014 |
Hahm JB, Schroeder AC, Privalsky ML. The two major isoforms of thyroid hormone receptor, TRα1 and TRβ1, preferentially partner with distinct panels of auxiliary proteins Molecular and Cellular Endocrinology. 383: 80-95. PMID 24325866 DOI: 10.1016/J.Mce.2013.11.015 |
0.802 |
|
| 2013 |
Hahm JB, Privalsky ML. Research resource: Identification of novel coregulators specific for thyroid hormone receptor-β2 Molecular Endocrinology. 27: 840-859. PMID 23558175 DOI: 10.1210/Me.2012-1117 |
0.824 |
|
| 2012 |
Sinha RA, You SH, Zhou J, Siddique MM, Bay BH, Zhu X, Privalsky ML, Cheng SY, Stevens RD, Summers SA, Newgard CB, Lazar MA, Yen PM. Thyroid hormone stimulates hepatic lipid catabolism via activation of autophagy. The Journal of Clinical Investigation. 122: 2428-38. PMID 22684107 DOI: 10.1172/Jci60580 |
0.378 |
|
| 2012 |
Mengeling BJ, Goodson ML, Bourguet W, Privalsky ML. SMRTε, a corepressor variant, interacts with a restricted subset of nuclear receptors, including the retinoic acid receptors α and β. Molecular and Cellular Endocrinology. 351: 306-16. PMID 22266197 DOI: 10.1016/J.Mce.2012.01.006 |
0.548 |
|
| 2011 |
Goodson ML, Mengeling BJ, Jonas BA, Privalsky ML. Alternative mRNA splicing of corepressors generates variants that play opposing roles in adipocyte differentiation. The Journal of Biological Chemistry. 286: 44988-99. PMID 22065574 DOI: 10.1074/Jbc.M111.291625 |
0.474 |
|
| 2011 |
Rosen MD, Privalsky ML. Thyroid hormone receptor mutations in cancer and resistance to thyroid hormone: perspective and prognosis. Journal of Thyroid Research. 2011: 361304. PMID 21760978 DOI: 10.4061/2011/361304 |
0.657 |
|
| 2011 |
Rosen MD, Chan IH, Privalsky ML. Mutant thyroid hormone receptors (TRs) isolated from distinct cancer types display distinct target gene specificities: a unique regulatory repertoire associated with two renal clear cell carcinomas. Molecular Endocrinology (Baltimore, Md.). 25: 1311-25. PMID 21622534 DOI: 10.1210/Me.2010-0420 |
0.625 |
|
| 2011 |
Lee S, Young BM, Wan W, Chan IH, Privalsky ML. A mechanism for pituitary-resistance to thyroid hormone (PRTH) syndrome: a loss in cooperative coactivator contacts by thyroid hormone receptor (TR)beta2. Molecular Endocrinology (Baltimore, Md.). 25: 1111-25. PMID 21622532 DOI: 10.1210/Me.2010-0448 |
0.664 |
|
| 2011 |
Zhu XG, Kim DW, Goodson ML, Privalsky ML, Cheng SY. NCoR1 regulates thyroid hormone receptor isoform-dependent adipogenesis. Journal of Molecular Endocrinology. 46: 233-44. PMID 21389087 DOI: 10.1530/Jme-10-0163 |
0.441 |
|
| 2011 |
Mengeling BJ, Phan TQ, Goodson ML, Privalsky ML. Aberrant corepressor interactions implicated in PML-RAR(alpha) and PLZF-RAR(alpha) leukemogenesis reflect an altered recruitment and release of specific NCoR and SMRT splice variants. The Journal of Biological Chemistry. 286: 4236-47. PMID 21131350 DOI: 10.1074/Jbc.M110.200964 |
0.73 |
|
| 2011 |
Varlakhanova N, Hahm JB, Privalsky ML. Regulation of SMRT corepressor dimerization and composition by MAP kinase phosphorylation. Molecular and Cellular Endocrinology. 332: 180-8. PMID 20965228 DOI: 10.1016/J.Mce.2010.10.010 |
0.784 |
|
| 2010 |
Hsia EY, Goodson ML, Zou JX, Privalsky ML, Chen HW. Nuclear receptor coregulators as a new paradigm for therapeutic targeting. Advanced Drug Delivery Reviews. 62: 1227-37. PMID 20933027 DOI: 10.1016/J.Addr.2010.09.016 |
0.468 |
|
| 2010 |
Varlakhanova N, Snyder C, Jose S, Hahm JB, Privalsky ML. Estrogen receptors recruit SMRT and N-CoR corepressors through newly recognized contacts between the corepressor N terminus and the receptor DNA binding domain. Molecular and Cellular Biology. 30: 1434-45. PMID 20065040 DOI: 10.1128/Mcb.01002-09 |
0.815 |
|
| 2010 |
Chan IH, Privalsky ML. A conserved lysine in the thyroid hormone receptor-alpha1 DNA-binding domain, mutated in hepatocellular carcinoma, serves as a sensor for transcriptional regulation. Molecular Cancer Research : McR. 8: 15-23. PMID 20053725 DOI: 10.1158/1541-7786.Mcr-09-0425 |
0.585 |
|
| 2010 |
Phan TQ, Jow MM, Privalsky ML. DNA recognition by thyroid hormone and retinoic acid receptors: 3,4,5 rule modified. Molecular and Cellular Endocrinology. 319: 88-98. PMID 19945505 DOI: 10.1016/J.Mce.2009.11.010 |
0.744 |
|
| 2009 |
Chan IH, Privalsky ML. Thyroid hormone receptor mutants implicated in human hepatocellular carcinoma display an altered target gene repertoire. Oncogene. 28: 4162-74. PMID 19749797 DOI: 10.1038/Onc.2009.265 |
0.461 |
|
| 2009 |
Chan IH, Privalsky ML. Isoform-specific transcriptional activity of overlapping target genes that respond to thyroid hormone receptors alpha1 and beta1. Molecular Endocrinology (Baltimore, Md.). 23: 1758-75. PMID 19628582 DOI: 10.1210/Me.2009-0025 |
0.515 |
|
| 2009 |
Privalsky ML, Lee S, Hahm JB, Young BM, Fong RN, Chan IH. The p160 coactivator PAS-B motif stabilizes nuclear receptor binding and contributes to isoform-specific regulation by thyroid hormone receptors. The Journal of Biological Chemistry. 284: 19554-63. PMID 19487700 DOI: 10.1074/Jbc.M109.007542 |
0.829 |
|
| 2009 |
Rosen MD, Privalsky ML. Thyroid hormone receptor mutations found in renal clear cell carcinomas alter corepressor release and reveal helix 12 as key determinant of corepressor specificity. Molecular Endocrinology (Baltimore, Md.). 23: 1183-92. PMID 19407221 DOI: 10.1210/Me.2009-0126 |
0.683 |
|
| 2009 |
Goodson ML, Farboud B, Privalsky ML. High throughput analysis of nuclear receptor-cofactor interactions. Methods in Molecular Biology (Clifton, N.J.). 505: 157-69. PMID 19117144 DOI: 10.1007/978-1-60327-575-0_9 |
0.374 |
|
| 2008 |
Chan IH, Borowsky AD, Privalsky ML. A cautionary note as to the use of pBi-L and related luciferase/transgenic vectors in the study of thyroid endocrinology. Thyroid : Official Journal of the American Thyroid Association. 18: 665-6. PMID 18578620 DOI: 10.1089/Thy.2008.0013 |
0.377 |
|
| 2008 |
Mengeling BJ, Lee S, Privalsky ML. Coactivator recruitment is enhanced by thyroid hormone receptor trimers. Molecular and Cellular Endocrinology. 280: 47-62. PMID 18006144 DOI: 10.1016/J.Mce.2007.09.011 |
0.581 |
|
| 2008 |
Privalsky ML. Thyroid hormone receptors, coregulators, and disease Nr Coregulators and Human Diseases. 256-293. DOI: 10.1142/9789812819178_0006 |
0.498 |
|
| 2007 |
Jonas BA, Varlakhanova N, Hayakawa F, Goodson M, Privalsky ML. Response of SMRT (silencing mediator of retinoic acid and thyroid hormone receptor) and N-CoR (nuclear receptor corepressor) corepressors to mitogen-activated protein kinase kinase kinase cascades is determined by alternative mRNA splicing. Molecular Endocrinology (Baltimore, Md.). 21: 1924-39. PMID 17519355 DOI: 10.1210/Me.2007-0035 |
0.509 |
|
| 2007 |
Goodson ML, Farboud B, Privalsky ML. An improved high throughput protein-protein interaction assay for nuclear hormone receptors. Nuclear Receptor Signaling. 5: e002. PMID 17464356 DOI: 10.1621/Nrs.05002 |
0.377 |
|
| 2007 |
Jonas BA, Varlakhanova N, Hayakawa F, Goodson ML, Privalsky ML. KINASE SIGNALING AND ALTERNATIVE MESSENGER RIBONUCLEIC ACID SPLICING: TWO METHODS TO CUSTOMIZE SMRT AND N-COR FUNCTION WITHIN THE CELL. Journal of Investigative Medicine. 55: S140. DOI: 10.1097/00042871-200701010-00398 |
0.473 |
|
| 2006 |
Chan IH, Privalsky ML. Thyroid hormone receptors mutated in liver cancer function as distorted antimorphs. Oncogene. 25: 3576-88. PMID 16434963 DOI: 10.1038/Sj.Onc.1209389 |
0.435 |
|
| 2005 |
Lee S, Privalsky ML. Multiple mutations contribute to repression by the v-Erb A oncoprotein. Oncogene. 24: 6737-52. PMID 16007162 DOI: 10.1038/Sj.Onc.1208826 |
0.413 |
|
| 2005 |
Wan W, Farboud B, Privalsky ML. Pituitary resistance to thyroid hormone syndrome is associated with T3 receptor mutants that selectively impair beta2 isoform function. Molecular Endocrinology (Baltimore, Md.). 19: 1529-42. PMID 15802373 DOI: 10.1210/Me.2005-0014 |
0.604 |
|
| 2005 |
McKenzie GJ, Stevenson P, Ward G, Papadia S, Bading H, Chawla S, Privalsky M, Hardingham GE. Nuclear Ca2+ and CaM kinase IV specify hormonal- and Notch-responsiveness. Journal of Neurochemistry. 93: 171-85. PMID 15773917 DOI: 10.1111/J.1471-4159.2005.03010.X |
0.469 |
|
| 2005 |
Lee S, Privalsky ML. Heterodimers of retinoic acid receptors and thyroid hormone receptors display unique combinatorial regulatory properties. Molecular Endocrinology (Baltimore, Md.). 19: 863-78. PMID 15650024 DOI: 10.1210/Me.2004-0210 |
0.628 |
|
| 2005 |
Goodson ML, Jonas BA, Privalsky ML. Alternative mRNA splicing of SMRT creates functional diversity by generating corepressor isoforms with different affinities for different nuclear receptors. The Journal of Biological Chemistry. 280: 7493-503. PMID 15632172 DOI: 10.1074/Jbc.M411514200 |
0.58 |
|
| 2005 |
Mengeling BJ, Pan F, Privalsky ML. Novel mode of deoxyribonucleic acid recognition by thyroid hormone receptors: thyroid hormone receptor beta-isoforms can bind as trimers to natural response elements comprised of reiterated half-sites. Molecular Endocrinology (Baltimore, Md.). 19: 35-51. PMID 15459250 DOI: 10.1210/Me.2003-0289 |
0.531 |
|
| 2004 |
Jonas BA, Privalsky ML. SMRT and N-CoR corepressors are regulated by distinct kinase signaling pathways. The Journal of Biological Chemistry. 279: 54676-86. PMID 15491994 DOI: 10.1074/Jbc.M410128200 |
0.428 |
|
| 2004 |
Harper R, Xu C, Di P, Chen Y, Privalsky M, Wu R. Identification of a novel MAGE D2 antisense RNA transcript in human tissues. Biochemical and Biophysical Research Communications. 324: 199-204. PMID 15465002 DOI: 10.1016/J.Bbrc.2004.09.037 |
0.352 |
|
| 2004 |
Farboud B, Privalsky ML. Retinoic acid receptor-alpha is stabilized in a repressive state by its C-terminal, isotype-specific F domain. Molecular Endocrinology (Baltimore, Md.). 18: 2839-53. PMID 15331758 DOI: 10.1210/Me.2004-0236 |
0.52 |
|
| 2004 |
Hayakawa F, Towatari M, Ozawa Y, Tomita A, Privalsky ML, Saito H. Functional regulation of GATA-2 by acetylation. Journal of Leukocyte Biology. 75: 529-40. PMID 15001660 DOI: 10.1189/Jlb.0603389 |
0.387 |
|
| 2004 |
Privalsky ML. The role of corepressors in transcriptional regulation by nuclear hormone receptors. Annual Review of Physiology. 66: 315-60. PMID 14977406 DOI: 10.1146/Annurev.Physiol.66.032802.155556 |
0.604 |
|
| 2004 |
Jonas BA, Privalsky ML. 385 DIFFERENTIAL REGULATION OF NUCLEAR COREPRESSOR PROTEINS, SILENCING MEDIATOR OF RETIONIC ACID AND THYROID HORMONE RECEPTORS AND NUCLEAR HORMONE RECEPTOR COREPRESSOR. Journal of Investigative Medicine. 52: S146.3-S146. DOI: 10.1136/jim-52-suppl1-385 |
0.511 |
|
| 2003 |
Privalsky ML. Activation incarnate. Developmental Cell. 5: 1-2. PMID 12852843 DOI: 10.1016/S1534-5807(03)00196-5 |
0.388 |
|
| 2003 |
Farboud B, Hauksdottir H, Wu Y, Privalsky ML. Isotype-restricted corepressor recruitment: a constitutively closed helix 12 conformation in retinoic acid receptors beta and gamma interferes with corepressor recruitment and prevents transcriptional repression. Molecular and Cellular Biology. 23: 2844-58. PMID 12665583 DOI: 10.1128/Mcb.23.8.2844-2858.2003 |
0.787 |
|
| 2003 |
Hauksdottir H, Farboud B, Privalsky ML. Retinoic acid receptors beta and gamma do not repress, but instead activate target gene transcription in both the absence and presence of hormone ligand. Molecular Endocrinology (Baltimore, Md.). 17: 373-85. PMID 12554770 DOI: 10.1210/Me.2002-0340 |
0.821 |
|
| 2002 |
Yoh SM, Privalsky ML. Molecular analysis of human resistance to thyroid hormone syndrome. Methods in Molecular Biology (Clifton, N.J.). 202: 129-52. PMID 12094601 DOI: 10.1385/1-59259-174-4:129 |
0.34 |
|
| 2002 |
Ruse MD, Privalsky ML, Sladek FM. Competitive cofactor recruitment by orphan receptor hepatocyte nuclear factor 4alpha1: modulation by the F domain. Molecular and Cellular Biology. 22: 1626-38. PMID 11865043 DOI: 10.1128/Mcb.22.6.1626-1638.2002 |
0.447 |
|
| 2001 |
Hong SH, Yang Z, Privalsky ML. Arsenic trioxide is a potent inhibitor of the interaction of SMRT corepressor with Its transcription factor partners, including the PML-retinoic acid receptor alpha oncoprotein found in human acute promyelocytic leukemia. Molecular and Cellular Biology. 21: 7172-82. PMID 11585900 DOI: 10.1128/Mcb.21.21.7172-7182.2001 |
0.634 |
|
| 2001 |
Zhou Y, Gross W, Hong SH, Privalsky ML. The SMRT corepressor is a target of phosphorylation by protein kinase CK2 (casein kinase II) Molecular and Cellular Biochemistry. 220: 1-13. PMID 11451368 DOI: 10.1023/A:1011087910699 |
0.53 |
|
| 2001 |
Yang Z, Privalsky ML. Isoform-specific transcriptional regulation by thyroid hormone receptors: hormone-independent activation operates through a steroid receptor mode of co-activator interaction. Molecular Endocrinology (Baltimore, Md.). 15: 1170-85. PMID 11435616 DOI: 10.1210/Mend.15.7.0656 |
0.697 |
|
| 2001 |
Yoh SM, Privalsky ML. Transcriptional repression by thyroid hormone receptors. A role for receptor homodimers in the recruitment of SMRT corepressor Journal of Biological Chemistry. 276: 16857-16867. PMID 11278601 DOI: 10.1074/Jbc.M010022200 |
0.606 |
|
| 2001 |
Hauksdóttir H, Privalsky ML. DNA recognition by the aberrant retinoic acid receptors implicated in human acute promyelocytic leukemia. Cell Growth & Differentiation : the Molecular Biology Journal of the American Association For Cancer Research. 12: 85-98. PMID 11243468 |
0.383 |
|
| 2000 |
Privalsky ML. Regulation of SMRT and N-CoR corepressor function Current Topics in Microbiology and Immunology. 254: 117-136. PMID 11190570 |
0.496 |
|
| 2000 |
Hong SH, Privalsky ML. The SMRT corepressor is regulated by a MEK-1 kinase pathway: Inhibition of corepressor function is associated with SMRT phosphorylation and nuclear export Molecular and Cellular Biology. 20: 6612-6625. PMID 10938135 DOI: 10.1128/Mcb.20.17.6612-6625.2000 |
0.448 |
|
| 2000 |
Privalsky ML, Yoh SM. Resistance to thyroid hormone (RTH) syndrome reveals novel determinants regulating interaction of T3 receptor with corepressor Molecular and Cellular Endocrinology. 159: 109-124. PMID 10687857 DOI: 10.1016/S0303-7207(99)00201-4 |
0.557 |
|
| 2000 |
Kogan SC, Hong S, Shultz DB, Privalsky ML, Bishop JM. Leukemia initiated by PMLRARα : the PML domain plays a critical role while retinoic acid–mediated transactivation is dispensable Blood. 95: 1541-1550. DOI: 10.1182/Blood.V95.5.1541.005K28_1541_1550 |
0.348 |
|
| 2000 |
Privalsky ML, Yoh SM. Erratum to “Resistance to thyroid hormone (RTH) syndrome reveals novel determinants regulating interaction of T3 receptor with corepressor” Molecular and Cellular Endocrinology. 162: 235. DOI: 10.1016/S0303-7207(00)00214-8 |
0.518 |
|
| 1999 |
Yang Z, Hong SH, Privalsky ML. Transcriptional anti-repression. Thyroid hormone receptor beta-2 recruits SMRT corepressor but interferes with subsequent assembly of a functional corepressor complex. The Journal of Biological Chemistry. 274: 37131-8. PMID 10601274 DOI: 10.1074/Jbc.274.52.37131 |
0.654 |
|
| 1999 |
Hong SH, Privalsky ML. Retinoid isomers differ in the ability to induce release of SMRT corepressor from retinoic acid receptor-α Journal of Biological Chemistry. 274: 2885-2892. PMID 9915825 DOI: 10.1074/Jbc.274.5.2885 |
0.59 |
|
| 1998 |
Wong CW, Privalsky ML. Components of the SMRT corepressor complex exhibit distinctive interactions with the POZ domain oncoproteins PLZF, PLZF-RAR∅, and BCL-6 Journal of Biological Chemistry. 273: 27695-27702. PMID 9765306 DOI: 10.1074/Jbc.273.42.27695 |
0.493 |
|
| 1998 |
Wong CW, Privalsky ML. Transcriptional silencing is defined by isoform- and heterodimer- specific interactions between nuclear hormone receptors and corepressors Molecular and Cellular Biology. 18: 5724-5733. PMID 9742089 DOI: 10.1128/Mcb.18.10.5724 |
0.589 |
|
| 1998 |
Hong SH, Wong CW, Privalsky ML. Signaling by tyrosine kinases negatively regulates the interaction between transcription factors and SMRT (silencing mediator of retinoic acid and thyroid hormone receptor) corepressor Molecular Endocrinology. 12: 1161-1171. PMID 9717842 DOI: 10.1210/Mend.12.8.0160 |
0.62 |
|
| 1998 |
Wong CW, Privalsky ML. Transcriptional repression by the SMRT-mSin3 corepressor: Multiple interactions, multiple mechanisms, and a potential role for TFIIB Molecular and Cellular Biology. 18: 5500-5510. PMID 9710634 DOI: 10.1128/Mcb.18.9.5500 |
0.445 |
|
| 1998 |
Tzagarakis-Foster C, Privalsky ML. Phosphorylation of thyroid hormone receptors by protein kinase a regulates DNA recognition by specific inhibition of receptor monomer binding Journal of Biological Chemistry. 273: 10926-10932. PMID 9556570 DOI: 10.1074/Jbc.273.18.10926 |
0.453 |
|
| 1998 |
Privalsky ML. Depudecin makes a debut Proceedings of the National Academy of Sciences of the United States of America. 95: 3335-3337. PMID 9520362 DOI: 10.1073/Pnas.95.7.3335 |
0.424 |
|
| 1997 |
Lin BC, Hong SH, Krig S, Yoh SM, Privalsky ML. A conformational switch in nuclear hormone receptors is involved in coupling hormone binding to corepressor release. Molecular and Cellular Biology. 17: 6131-8. PMID 9315673 DOI: 10.1128/Mcb.18.12.7603 |
0.736 |
|
| 1997 |
Chen H, Lin RJ, Schiltz RL, Chakravarti D, Nash A, Nagy L, Privalsky ML, Nakatani Y, Evans RM. Nuclear receptor coactivator ACTR is a novel histone acetyltransferase and forms a multimeric activation complex with P/CAF and CBP/p300. Cell. 90: 569-80. PMID 9267036 DOI: 10.1016/S0092-8674(00)80516-4 |
0.49 |
|
| 1997 |
Hong SH, David G, Wong CW, Dejean A, Privalsky ML. SMRT corepressor interacts with PLZF and with the PML-retinoic acid receptor α (RARα) and PLZF-RARα oncoproteins associated with acute promyelocytic leukemia Proceedings of the National Academy of Sciences of the United States of America. 94: 9028-9033. PMID 9256429 DOI: 10.1073/Pnas.94.17.9028 |
0.559 |
|
| 1997 |
Chen HW, Privalsky ML. Retinoid X and retinoic acid receptors interact with transcription factor II-B by distinct mechanisms Molecular and Cellular Endocrinology. 129: 55-61. PMID 9175629 DOI: 10.1016/S0303-7207(97)04040-9 |
0.558 |
|
| 1997 |
Yoh SM, Chatterjee VKK, Privalsky ML. Thyroid hormone resistance syndrome manifests as an aberrant interaction between mutant T3 receptors and transcriptional corepressors Molecular Endocrinology. 11: 470-480. PMID 9092799 DOI: 10.1210/Mend.11.4.9914 |
0.599 |
|
| 1997 |
Lin BC, Wong CW, Chen HW, Privalsky ML. Plasticity of tetramer formation by retinoid X receptors. An alternative paradigm for DNA recognition. The Journal of Biological Chemistry. 272: 9860-7. PMID 9092522 DOI: 10.1074/Jbc.272.15.9860 |
0.669 |
|
| 1996 |
Sande S, Privalsky ML. Identification of TRACs (T3 receptor-associating cofactors), a family of cofactors that associate with, and modulate the activity of, nuclear hormone receptors Molecular Endocrinology. 10: 813-825. PMID 8813722 DOI: 10.1210/Mend.10.7.8813722 |
0.6 |
|
| 1996 |
Judelson C, Privalsky ML. DNA recognition by normal and oncogenic thyroid hormone receptors: Unexpected diversity in half-site specificity controlled by non-zinc-finger determinants Journal of Biological Chemistry. 271: 10800-10805. PMID 8631892 DOI: 10.1074/Jbc.271.18.10800 |
0.56 |
|
| 1995 |
Chen H, Privalsky ML. Cooperative formation of high-order oligomers by retinoid X receptors: An unexpected mode of DNA recognition Proceedings of the National Academy of Sciences of the United States of America. 92: 422-426. PMID 7831303 DOI: 10.1073/Pnas.92.2.422 |
0.539 |
|
| 1995 |
Wong CW, Privalsky ML. Role of the N terminus in DNA recognition by the v-erb A protein, an oncogenic derivative of a thyroid hormone receptor Molecular Endocrinology. 9: 551-562. PMID 7565803 DOI: 10.1210/Mend.9.5.7565803 |
0.539 |
|
| 1994 |
Smit-McBride Z, Privalsky ML. DNA sequence specificity of the v-erb A oncoprotein/thyroid hormone receptor: Role of the P-box and its interaction with more N-terminal determinants of DNA recognition Molecular Endocrinology. 8: 819-828. PMID 7984144 DOI: 10.1210/Mend.8.7.7984144 |
0.5 |
|
| 1994 |
Sande S, Privalsky ML. Reconstitution of thyroid hormone receptor and retinoic acid receptor function in the fission yeast Schizosaccharomyces pombe Molecular Endocrinology. 8: 1455-1464. PMID 7877615 DOI: 10.1210/Mend.8.11.7877615 |
0.59 |
|
| 1993 |
Hall BL, Smit-Mcbride Z, Privalsky ML. Reconstitution of retinoid X receptor function and combinatorial regulation of other nuclear hormone receptors in the yeast Saccharomyces cerevisiae Proceedings of the National Academy of Sciences of the United States of America. 90: 6929-6933. PMID 8394003 DOI: 10.1073/Pnas.90.15.6929 |
0.611 |
|
| 1993 |
Chen HW, Privalsky ML. The erbA oncogene represses the actions of both retinoid X and retinoid A receptors but does so by distinct mechanisms Molecular and Cellular Biology. 13: 5970-5980. PMID 8105369 DOI: 10.1128/Mcb.13.10.5970 |
0.592 |
|
| 1993 |
Smit-McBride Z, Privalsky ML. Functional domains of the v-erbA protein necessary for oncogenesis are required for transcriptional activation in Saccharomyces cerevisiae Oncogene. 8: 1465-1475. PMID 8099219 |
0.448 |
|
| 1993 |
Chen H, Smit-Mcbride Z, Lewis S, Sharif M, Privalsky ML. Nuclear hormone receptors involved in neoplasia: Erb A exhibits a novel DNA sequence specificity determined by amino acids outside of the zinc-finger domain Molecular and Cellular Biology. 13: 2366-2376. PMID 8096060 DOI: 10.1128/Mcb.13.4.2366 |
0.559 |
|
| 1993 |
Sande S, Sharif M, Chen H, Privalsky M. v-erbA acts on retinoic acid receptors in immature avian erythroid cells. Journal of Virology. 67: 1067-74. PMID 8093487 DOI: 10.1128/Jvi.67.2.1067-1074.1993 |
0.52 |
|
| 1992 |
Privalsky ML. v-erb A, nuclear hormone receptors, and oncogenesis Bba - Reviews On Cancer. 1114: 51-62. PMID 1356442 DOI: 10.1016/0304-419X(92)90006-K |
0.498 |
|
| 1992 |
Hall BL, Bonde BG, Judelson C, Privalsky ML. Functional interaction between the two zinc finger domains of the v-erb A oncoprotein Cell Growth &Amp; Differentiation : the Molecular Biology Journal of the American Association For Cancer Research. 3: 207-216. PMID 1355356 |
0.438 |
|
| 1992 |
Sharif M, Privalsky ML. V-erbA and c-erbA proteins enhance transcriptional activation by c-jun Oncogene. 7: 953-960. PMID 1349165 |
0.364 |
|
| 1992 |
Privalsky ML. Retinoid and thyroid hormone receptors: ligand-regulated transcription factors as proto-oncogenes Seminars in Cell Biology. 3: 99-106. PMID 1319230 DOI: 10.1016/S1043-4682(10)80019-4 |
0.612 |
|
| 1991 |
Sharif M, Privalsky ML. v-erbA Oncogene function in neoplasia correlates with its ability to repress retinoic acid receptor action Cell. 66: 885-893. PMID 1679679 DOI: 10.1016/0092-8674(91)90435-2 |
0.504 |
|
| 1991 |
Bonde BG, Sharif M, Privalsky ML. Ontogeny of the v-erbA oncoprotein from the thyroid hormone receptor: An alteration in the DNA binding domain plays a role crucial for v-erbA function Journal of Virology. 65: 2037-2046. PMID 1672166 DOI: 10.1128/Jvi.65.4.2037-2046.1991 |
0.46 |
|
| 1991 |
Privalsky ML. A subpopulation of the v-erb A oncogene protein, a derivative of a thyroid hormone receptor, associates with heat shock protein 90 Journal of Biological Chemistry. 266: 1456-1462. PMID 1671036 |
0.366 |
|
| 1990 |
Boucher P, Privalsky ML. Mapping of functional domains within the v-erb A oncogene protein: The remnants of the hormone binding domain play multiple, vital roles in protein action Oncogene. 5: 1303-1311. PMID 2170895 |
0.368 |
|
| 1990 |
Privalsky ML, Sharif M, Yamamoto KR. The viral erbA oncogene protein, a constitutive repressor in animal cells, is a hormone-regulated activator in yeast. Cell. 63: 1277-86. PMID 1979758 DOI: 10.1016/0092-8674(90)90423-C |
0.594 |
|
| 1990 |
Bonde BG, Privalsky ML. Sequence-specific DNA binding by the v-erbA oncogene protein of avian erythroblastosis virus Journal of Virology. 64: 1314-1320. PMID 1968105 DOI: 10.1128/Jvi.64.3.1314-1320.1990 |
0.561 |
|
| 1990 |
Privalsky ML. A subpopulation of the avian erythroblastosis virus v-erbA protein, a member of the nuclear hormone receptor family, is glycosylated Journal of Virology. 64: 463-466. PMID 1967151 DOI: 10.1128/Jvi.64.1.463-466.1990 |
0.469 |
|
| 1988 |
Privalsky ML, Boucher P, Koning A, Judelson C. Genetic dissection of functional domains within the avian erythroblastosis virus v-erbA oncogene Molecular and Cellular Biology. 8: 4510-4517. PMID 2847034 DOI: 10.1128/Mcb.8.10.4510 |
0.464 |
|
| 1988 |
Boucher P, Koning A, Privalsky ML. The avian erythroblastosis virus erbA oncogene encodes a DNA-binding protein exhibiting distinct nuclear and cytoplasmic subcellular localizations Journal of Virology. 62: 534-544. PMID 2826814 DOI: 10.1128/Jvi.62.2.534-544.1988 |
0.42 |
|
| 1987 |
Bassiri M, Privalsky ML. Transmembrane domain of the AEV erb B oncogene protein is not required for partial manifestation of the transformed phenotype Virology. 159: 20-30. PMID 3604059 DOI: 10.1016/0042-6822(87)90343-6 |
0.301 |
|
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