| Year |
Citation |
Score |
| 2016 |
Pastar I, Stojadinovic O, Sawaya AP, Stone RC, Lindley LE, Ojeh N, Vukelic S, Samuels HH, Tomic-Canic M. Skin Metabolite, Farnesyl Pyrophosphate, Regulates Epidermal Response to Inflammation, Oxidative Stress and Migration. Journal of Cellular Physiology. PMID 26916741 DOI: 10.1002/jcp.25357 |
0.305 |
|
| 2014 |
Das S, Yeung KT, Mahajan MA, Samuels HH. Fas Activated Serine-Threonine Kinase Domains 2 (FASTKD2) mediates apoptosis of breast and prostate cancer cells through its novel FAST2 domain. Bmc Cancer. 14: 852. PMID 25409762 DOI: 10.1186/1471-2407-14-852 |
0.673 |
|
| 2013 |
Tinnikov AA, Samuels HH. A novel cell lysis approach reveals that caspase-2 rapidly translocates from the nucleus to the cytoplasm in response to apoptotic stimuli. Plos One. 8: e61085. PMID 23596516 DOI: 10.1371/journal.pone.0061085 |
0.31 |
|
| 2011 |
Yeung KT, Das S, Zhang J, Lomniczi A, Ojeda SR, Xu CF, Neubert TA, Samuels HH. A novel transcription complex that selectively modulates apoptosis of breast cancer cells through regulation of FASTKD2. Molecular and Cellular Biology. 31: 2287-98. PMID 21444724 DOI: 10.1128/Mcb.01381-10 |
0.676 |
|
| 2010 |
Goyanka R, Das S, Samuels HH, Cardozo T. Nuclear receptor engineering based on novel structure activity relationships revealed by farnesyl pyrophosphate. Protein Engineering, Design & Selection : Peds. 23: 809-15. PMID 20817759 DOI: 10.1093/Protein/Gzq056 |
0.338 |
|
| 2009 |
Tinnikov AA, Yeung KT, Das S, Samuels HH. Identification of a novel pathway that selectively modulates apoptosis of breast cancer cells. Cancer Research. 69: 1375-82. PMID 19190336 DOI: 10.1158/0008-5472.Can-08-2896 |
0.657 |
|
| 2009 |
Garapaty S, Xu CF, Trojer P, Mahajan MA, Neubert TA, Samuels HH. Identification and characterization of a novel nuclear protein complex involved in nuclear hormone receptor-mediated gene regulation. The Journal of Biological Chemistry. 284: 7542-52. PMID 19131338 DOI: 10.1074/Jbc.M805872200 |
0.651 |
|
| 2008 |
Mahajan MA, Samuels HH. Nuclear receptor coactivator/coregulator NCoA6(NRC) is a pleiotropic coregulator involved in transcription, cell survival, growth and development. Nuclear Receptor Signaling. 6: e002. PMID 18301782 DOI: 10.1621/nrs.06002 |
0.493 |
|
| 2008 |
Garapaty S, Mahajan MA, Samuels HH. Components of the CCR4-NOT complex function as nuclear hormone receptor coactivators via association with the NRC-interacting Factor NIF-1. The Journal of Biological Chemistry. 283: 6806-16. PMID 18180299 DOI: 10.1074/Jbc.M706986200 |
0.649 |
|
| 2007 |
Das S, Schapira M, Tomic-Canic M, Goyanka R, Cardozo T, Samuels HH. Farnesyl pyrophosphate is a novel transcriptional activator for a subset of nuclear hormone receptors. Molecular Endocrinology (Baltimore, Md.). 21: 2672-86. PMID 17666588 DOI: 10.1210/Me.2007-0080 |
0.453 |
|
| 2007 |
Mahajan MA, Murray A, Levy D, Samuels HH. Nuclear receptor coregulator (NRC): mapping of the dimerization domain, activation of p53 and STAT-2, and identification of the activation domain AD2 necessary for nuclear receptor signaling. Molecular Endocrinology (Baltimore, Md.). 21: 1822-34. PMID 17536006 DOI: 10.1210/me.2005-0529 |
0.47 |
|
| 2007 |
Das S, Nwachukwu JC, Li D, Vulin AI, Martinez-Caballero S, Kinnally KW, Samuels HH. The nuclear receptor interacting factor-3 transcriptional coregulator mediates rapid apoptosis in breast cancer cells through direct and bystander-mediated events. Cancer Research. 67: 1775-82. PMID 17308120 DOI: 10.1158/0008-5472.Can-06-4034 |
0.448 |
|
| 2006 |
Flamant F, Baxter JD, Forrest D, Refetoff S, Samuels H, Scanlan TS, Vennström B, Samarut J. International union of pharmacology. LIX. The pharmacology and classification of the nuclear receptor superfamily: Thyroid hormone receptors Pharmacological Reviews. 58: 705-711. PMID 17132849 DOI: 10.1124/Pr.58.4.3 |
0.376 |
|
| 2006 |
Tian H, Mahajan MA, Wong CT, Habeos I, Samuels HH. The N-Terminal A/B domain of the thyroid hormone receptor-beta2 isoform influences ligand-dependent recruitment of coactivators to the ligand-binding domain. Molecular Endocrinology (Baltimore, Md.). 20: 2036-51. PMID 16645037 DOI: 10.1210/me.2005-0437 |
0.379 |
|
| 2005 |
Mahajan MA, Samuels HH. Nuclear hormone receptor coregulator: role in hormone action, metabolism, growth, and development. Endocrine Reviews. 26: 583-97. PMID 15561801 DOI: 10.1210/er.2004-0012 |
0.509 |
|
| 2005 |
Li D, Mahajan MA, Samuels HH. Functional consequences of interactions between thyroid hormone receptors and retinoid X receptor Current Opinion in Endocrinology and Diabetes. 12: 356-362. DOI: 10.1097/01.med.0000178270.24612.7d |
0.391 |
|
| 2004 |
Afonja O, Juste D, Das S, Matsuhashi S, Samuels HH. Induction of PDCD4 tumor suppressor gene expression by RAR agonists, antiestrogen and HER-2/neu antagonist in breast cancer cells. Evidence for a role in apoptosis. Oncogene. 23: 8135-45. PMID 15361828 DOI: 10.1038/sj.onc.1207983 |
0.446 |
|
| 2004 |
Li D, Das S, Yamada T, Samuels HH. The NRIF3 family of transcriptional coregulators induces rapid and profound apoptosis in breast cancer cells. Molecular and Cellular Biology. 24: 3838-48. PMID 15082778 |
0.37 |
|
| 2004 |
Li D, Yamada T, Wang F, Vulin AI, Samuels HH. Novel roles of retinoid X receptor (RXR) and RXR ligand in dynamically modulating the activity of the thyroid hormone receptor/RXR heterodimer. The Journal of Biological Chemistry. 279: 7427-37. PMID 14668324 DOI: 10.1074/jbc.M311596200 |
0.351 |
|
| 2002 |
Afonja O, Raaka BM, Huang A, Das S, Zhao X, Helmer E, Juste D, Samuels HH. RAR agonists stimulate SOX9 gene expression in breast cancer cell lines: evidence for a role in retinoid-mediated growth inhibition. Oncogene. 21: 7850-60. PMID 12420222 DOI: 10.1038/sj.onc.1205985 |
0.412 |
|
| 2002 |
Mahajan MA, Murray A, Samuels HH. NRC-interacting factor 1 is a novel cotransducer that interacts with and regulates the activity of the nuclear hormone receptor coactivator NRC. Molecular and Cellular Biology. 22: 6883-94. PMID 12215545 DOI: 10.1128/MCB.22.19.6883-6894.2002 |
0.51 |
|
| 2002 |
Li D, Li T, Wang F, Tian H, Samuels HH. Functional evidence for retinoid X receptor (RXR) as a nonsilent partner in the thyroid hormone receptor/RXR heterodimer. Molecular and Cellular Biology. 22: 5782-92. PMID 12138189 |
0.407 |
|
| 2001 |
Li D, Wang F, Samuels HH. Domain structure of the NRIF3 family of coregulators suggests potential dual roles in transcriptional regulation. Molecular and Cellular Biology. 21: 8371-84. PMID 11713274 DOI: 10.1128/MCB.21.24.8371-8384.2001 |
0.412 |
|
| 2001 |
Mathur M, Tucker PW, Samuels HH. PSF is a novel corepressor that mediates its effect through Sin3A and the DNA binding domain of nuclear hormone receptors. Molecular and Cellular Biology. 21: 2298-311. PMID 11259580 DOI: 10.1128/Mcb.21.7.2298-2311.2001 |
0.469 |
|
| 2000 |
Mahajan MA, Samuels HH. A new family of nuclear receptor coregulators that integrate nuclear receptor signaling through CREB-binding protein Molecular and Cellular Biology. 20: 5048-5063. PMID 10866662 DOI: 10.1128/MCB.20.14.5048-5063.2000 |
0.463 |
|
| 2000 |
Schapira M, Raaka BM, Samuels HH, Abagyan R. Rational discovery of novel nuclear hormone receptor antagonists. Proceedings of the National Academy of Sciences of the United States of America. 97: 1008-13. PMID 10655475 DOI: 10.1073/Pnas.97.3.1008 |
0.343 |
|
| 1999 |
Li D, Desai-Yajnik V, Lo E, Schapira M, Abagyan R, Samuels HH. NRIF3 is a novel coactivator mediating functional specificity of nuclear hormone receptors. Molecular and Cellular Biology. 19: 7191-202. PMID 10490654 DOI: 10.1128/Mcb.19.10.7191 |
0.476 |
|
| 1999 |
Qi JS, Yuan Y, Desai-Yajnik V, Samuels HH. Regulation of the mdm2 oncogene by thyroid hormone receptor. Molecular and Cellular Biology. 19: 864-72. PMID 9858609 DOI: 10.1128/MCB.19.1.864 |
0.375 |
|
| 1998 |
Selmi-Ruby S, Casanova J, Malhotra S, Roussett B, Raaka BM, Samuels HH. Role of the conserved C-terminal region of thyroid hormone receptor-alpha in ligand-dependent transcriptional activation. Molecular and Cellular Endocrinology. 138: 105-14. PMID 9685219 DOI: 10.1016/S0303-7207(98)00016-1 |
0.315 |
|
| 1998 |
Hadzic E, Habeos I, Raaka BM, Samuels HH. A novel multifunctional motif in the amino-terminal A/B domain of T3Ralpha modulates DNA binding and receptor dimerization. The Journal of Biological Chemistry. 273: 10270-8. PMID 9553079 DOI: 10.1074/jbc.273.17.10270 |
0.315 |
|
| 1998 |
Powers CA, Mathur M, Raaka BM, Ron D, Samuels HH. TLS (translocated-in-liposarcoma) is a high-affinity interactor for steroid, thyroid hormone, and retinoid receptors. Molecular Endocrinology (Baltimore, Md.). 12: 4-18. PMID 9440806 DOI: 10.1210/Mend.12.1.0043 |
0.426 |
|
| 1997 |
Qi JS, Desai-Yajnik V, Yuan Y, Samuels HH. Constitutive activation of gene expression by thyroid hormone receptor results from reversal of p53-mediated repression. Molecular and Cellular Biology. 17: 7195-207. PMID 9372952 DOI: 10.1128/MCB.17.12.7195 |
0.398 |
|
| 1996 |
Helmer EB, Raaka BM, Samuels HH. Hormone-dependent and -independent transcriptional activation by thyroid hormone receptors are mediated by different mechanisms Endocrinology. 137: 390-399. PMID 8593781 DOI: 10.1210/en.137.2.390 |
0.429 |
|
| 1996 |
Tomić-Canić M, Day D, Samuels HH, Freedberg IM, Blumenberg M. Novel regulation of keratin gene expression by thyroid hormone and retinoid receptors. The Journal of Biological Chemistry. 271: 1416-23. PMID 8576132 DOI: 10.1074/jbc.271.3.1416 |
0.418 |
|
| 1996 |
Hadzie E, Samuels HH. Differential transactivation potentials of the thyroid hormone receptor α and β isoforms Journal of Investigative Medicine. 44. |
0.368 |
|
| 1996 |
Pesai-Yajnik V, Samuels HH. Interactions of the thyroid hormone receptor with the human immunodeficiency virus type I (HIV-1) long terminal repeat and the HIV-1 tat trans activator Journal of Investigative Medicine. 44. |
0.313 |
|
| 1996 |
Qi JS, Desai-Yajnik V, Samuels HH. Molecular interactions of p53 with thyroid hormone nuclear receptors Journal of Investigative Medicine. 44. |
0.33 |
|
| 1995 |
Hao E, Menke JB, Smith AM, Jones C, Geffner ME, Hershman JM, Wuerth JP, Samuels HH, Ways DK, Usala SJ. Divergent dimerization properties of mutant beta 1 thyroid hormone receptors are associated with different dominant negative activities. Molecular Endocrinology (Baltimore, Md.). 8: 841-51. PMID 7984146 DOI: 10.1210/mend.8.7.7984146 |
0.383 |
|
| 1995 |
Qi JS, Desai-Yajnik V, Greene ME, Raaka BM, Samuels HH. The ligand-binding domains of the thyroid hormone/retinoid receptor gene subfamily function in vivo to mediate heterodimerization, gene silencing, and transactivation Molecular and Cellular Biology. 15: 1817-1825. PMID 7862171 DOI: 10.1128/MCB.15.3.1817 |
0.459 |
|
| 1995 |
Hadzic E, Desai-Yajnik V, Helmer E, Guo S, Wu S, Koudinova N, Casanova J, Raaka BM, Samuels HH. A 10-amino-acid sequence in the N-terminal A/B domain of thyroid hormone receptor alpha is essential for transcriptional activation and interaction with the general transcription factor TFIIB. Molecular and Cellular Biology. 15: 4507-17. PMID 7623841 DOI: 10.1128/MCB.15.8.4507 |
0.32 |
|
| 1994 |
Casanova J, Helmer E, Selmi-Ruby S, Qi JS, Au-Fliegner M, Desai-Yajnik V, Koudinova N, Yarm F, Raaka BM, Samuels HH. Functional evidence for ligand-dependent dissociation of thyroid hormone and retinoic acid receptors from an inhibitory cellular factor. Molecular and Cellular Biology. 14: 5756-65. PMID 8065310 DOI: 10.1128/MCB.14.9.5756 |
0.412 |
|
| 1993 |
Au-Fliegner M, Helmer E, Casanova J, Raaka BM, Samuels HH. The conserved ninth C-terminal heptad in thyroid hormone and retinoic acid receptors mediates diverse responses by affecting heterodimer but not homodimer formation. Molecular and Cellular Biology. 13: 5725-37. PMID 8395010 DOI: 10.1128/MCB.13.9.5725 |
0.393 |
|
| 1993 |
García-Villalba P, Au-Fliegner M, Samuels HH, Aranda A. Interaction of thyroid hormone and retinoic acid receptors on the regulation of the rat growth hormone gene promoter. Biochemical and Biophysical Research Communications. 191: 580-6. PMID 8384845 DOI: 10.1006/bbrc.1993.1257 |
0.317 |
|
| 1993 |
Desai-Yajnik V, Samuels HH. Regulation of the human immunodeficiency virus type 1 long terminal repeat: interactions of thyroid hormone receptor with retinoid-X receptor, nuclear factor kappa B, Sp1, and Tat Transactions of the Association of American Physicians. 106: 13-32. PMID 8036737 |
0.365 |
|
| 1992 |
Forman BM, Casanova J, Raaka BM, Ghysdael J, Samuels HH. Half-site spacing and orientation determines whether thyroid hormone and retinoic acid receptors and related factors bind to DNA response elements as monomers, homodimers, or heterodimers. Molecular Endocrinology (Baltimore, Md.). 6: 429-42. PMID 1316541 DOI: 10.1210/mend.6.3.1316541 |
0.336 |
|
| 1991 |
Tomic M, Jiang CK, Epstein HS, Freedberg IM, Samuels HH, Blumenberg M. Nuclear receptors for retinoic acid and thyroid hormone regulate transcription of keratin genes. Cell Regulation. 1: 965-73. PMID 1712634 DOI: 10.1091/mbc.1.12.965 |
0.398 |
|
| 1991 |
Selmi S, Samuels HH. Thyroid hormone receptor/and v-erbA: A single amino acid difference in the C-terminal region influences dominant negative activity and receptor dimer formation Journal of Biological Chemistry. 266: 11589-11593. PMID 1675637 |
0.326 |
|
| 1990 |
Forman BM, Yang CR, Au M, Casanova J, Ghysdael J, Samuels HH. A domain containing leucine-zipper-like motifs mediate novel in vivo interactions between the thyroid hormone and retinoic acid receptors. Molecular Endocrinology (Baltimore, Md.). 3: 1610-26. PMID 2558297 DOI: 10.1210/mend-3-10-1610 |
0.377 |
|
| 1990 |
Forman BM, Samuels HH. Interactions among a subfamily of nuclear hormone receptors: the regulatory zipper model Molecular Endocrinology. 4: 1293-1301. PMID 2172797 |
0.464 |
|
| 1990 |
Forman BM, Samuels HH. Dimerization among nuclear hormone receptors New Biologist. 2: 587-594. PMID 1964593 |
0.368 |
|
| 1989 |
Raaka BM, Finnerty M, Samuels HH. The glucocorticoid antagonist 17 alpha-methyltestosterone binds to the 10 S glucocorticoid receptor and blocks agonist-mediated dissociation of the 10 S oligomer to the 4 S deoxyribonucleic acid-binding subunit. Molecular Endocrinology (Baltimore, Md.). 3: 332-41. PMID 2710136 DOI: 10.1210/mend-3-2-332 |
0.371 |
|
| 1988 |
Aranda A, Pascual A, Copp R, Samuels H. Cholera toxin affects nuclear ADP-ribosylation in GH1 cells Biochemical and Biophysical Research Communications. 150: 323-328. PMID 2827673 DOI: 10.1016/0006-291X(88)90523-2 |
0.365 |
|
| 1987 |
Ye ZS, Samuels HH. Cell- and sequence-specific binding of nuclear proteins to 5'-flanking DNA of the rat growth hormone gene Journal of Biological Chemistry. 262: 6313-6317. PMID 3032962 |
0.322 |
|
| 1985 |
Raaka BM, Finnerty M, Sun E, Samuels HH. Effects of molybdate on steroid receptors in intact GH1 cells. Evidence for dissociation of an intracellular 10 S receptor oligomer prior to nuclear accumulation. The Journal of Biological Chemistry. 260: 14009-15. PMID 4055769 |
0.395 |
|
| 1985 |
McIntyre WR, Samuels HH. Triamcinolone acetonide regulates glucocorticoid-receptor levels by decreasing the half-life of the activated nuclear-receptor form Journal of Biological Chemistry. 260: 418-427. PMID 3965455 |
0.373 |
|
| 1985 |
Raaka BM, Finnerty M, Samuels HH. Molybdate inhibits nuclear accumulation and increases the half-life of the estrogen receptor in GH cells Federation Proceedings. 44. |
0.36 |
|
| 1984 |
Yaffe BM, Samuels HH. Hormonal regulation of the growth hormone gene. Relationship of the rate of transcription to the level of nuclear thyroid hormone-receptor complexes Journal of Biological Chemistry. 259: 6284-6291. PMID 6327674 |
0.32 |
|
| 1984 |
Aranda A, Samuels HH. Modulation of thyroid hormone nuclear receptors by cholera toxin in cultured GH1 cells Journal of Biological Chemistry. 259: 6110-6116. PMID 6327666 |
0.383 |
|
| 1983 |
Raaka BM, Samuels HH. The glucocorticoid receptor in GH1 cells. Evidence from dense amino acid labeling and whole cell studies for an equilibrium model explaining the influence of hormone on the intracellular distribution of receptor Journal of Biological Chemistry. 258: 417-425. PMID 6848510 |
0.361 |
|
| 1982 |
Perlman AJ, Stanley F, Samuels HH. Thyroid hormone nuclear receptor. Evidence for multimeric organization in chromatin. The Journal of Biological Chemistry. 257: 930-8. PMID 6274872 |
0.326 |
|
| 1982 |
Raaka BM, Samuels HH. An equilibrium model for hormone-mediated glucocorticoid receptor activation and translocation Clinical Research. 30. |
0.347 |
|
| 1981 |
Raaka BM, Samuels HH. Regulation of thyroid hormone nuclear receptor levels in GH1 cells by 3,5,3'-triiodo-L-thyronine Journal of Biological Chemistry. 256: 6883-6889. PMID 6263925 |
0.353 |
|
| 1980 |
Samuels HH, Stanley F, Casanova J, Shao TC. Thyroid hormone nuclear receptor levels are influenced by the acetylation of chromatin-associated proteins Journal of Biological Chemistry. 255: 2499-2508. PMID 6244282 |
0.355 |
|
| 1977 |
Samuels HH, Stanley F, Shapiro LE. Modulation of thyroid hormone nuclear receptor level by 3,5,3'-triiodo-L-thyronine in GH1 cells. Evidence for two functional components of nuclear-bound receptor and relationship to the induction of growth hormone synthesis Journal of Biological Chemistry. 252: 6052-6060. PMID 197080 |
0.379 |
|
| 1976 |
Samuels HH, Stanley F, Shapiro LE. Dose dependent depletion of nuclear receptors by L triiodothyronine: evidence for a role in induction of growth hormone synthesis in cultured GH1 cells Proceedings of the National Academy of Sciences of the United States of America. 73: 3877-3881. PMID 186776 |
0.308 |
|
| 1975 |
Samuels HH, Tsai JS. Nuclear poly(A) synthesis and the action of thyroid hormone: a clue to the biologic role of the nuclear receptor Clinical Research. 23. |
0.365 |
|
| 1973 |
Samuels HH, Tsai JR. Thyroid hormone action in cell culture: demonstration of nuclear receptors in intact cells and isolated nuclei Proceedings of the National Academy of Sciences of the United States of America. 70. PMID 4357872 |
0.365 |
|
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