| Year |
Citation |
Score |
| 2021 |
Li W, Hang S, Fang Y, Bae S, Zhang Y, Zhang M, Wang G, McCurry MD, Bae M, Paik D, Franzosa EA, Rastinejad F, Huttenhower C, Yao L, Devlin AS, et al. A bacterial bile acid metabolite modulates T activity through the nuclear hormone receptor NR4A1. Cell Host & Microbe. PMID 34416161 DOI: 10.1016/j.chom.2021.07.013 |
0.302 |
|
| 2020 |
Smith S, McHale K, Creech K, Rickard D, Jayawickreme C, Wu D, Rastinejad F, Rubenstein D. 595 Differential ligand binding distinguishes therapeutic from pathologic Aryl Hydrocarbon Receptor (AhR) modulating agents: Implications for inflammatory skin disease Journal of Investigative Dermatology. 140: S81. DOI: 10.1016/j.jid.2020.03.605 |
0.339 |
|
| 2018 |
Daniel B, Nagy G, Czimmerer Z, Horvath A, Hammers DW, Cuaranta-Monroy I, Poliska S, Tzerpos P, Kolostyak Z, Hays TT, Patsalos A, Houtman R, Sauer S, Francois-Deleuze J, Rastinejad F, et al. The Nuclear Receptor PPARγ Controls Progressive Macrophage Polarization as a Ligand-Insensitive Epigenomic Ratchet of Transcriptional Memory. Immunity. 49: 615-626.e6. PMID 30332629 DOI: 10.1016/J.Immuni.2018.09.005 |
0.338 |
|
| 2017 |
Chandra V, Wu D, Li S, Potluri N, Kim Y, Rastinejad F. The quaternary architecture of RARβ-RXRα heterodimer facilitates domain-domain signal transmission. Nature Communications. 8: 868. PMID 29021580 DOI: 10.1038/s41467-017-00981-y |
0.404 |
|
| 2016 |
Wu D, Su X, Potluri N, Kim Y, Rastinejad F. NPAS1-ARNT and NPAS3-ARNT crystal structures implicate the bHLH-PAS family as multi-ligand binding transcription factors. Elife. 5. PMID 27782878 DOI: 10.7554/eLife.18790 |
0.405 |
|
| 2016 |
Khorasanizadeh S, Rastinejad F. Visualizing the Architectures and Interactions of Nuclear Receptors. Endocrinology. en20161559. PMID 27704949 DOI: 10.1210/en.2016-1559 |
0.419 |
|
| 2015 |
Santori FR, Huang P, van de Pavert SA, Douglass EF, Leaver DJ, Haubrich BA, Keber R, Lorbek G, Konijn T, Rosales BN, Rozman D, Horvat S, Rahier A, Mebius RE, Rastinejad F, et al. Identification of natural RORγ ligands that regulate the development of lymphoid cells. Cell Metabolism. 21: 286-97. PMID 25651181 DOI: 10.1016/J.Cmet.2015.01.004 |
0.525 |
|
| 2015 |
Rastinejad F, Ollendorff V, Polikarpov I. Nuclear receptor full-length architectures: confronting myth and illusion with high resolution. Trends in Biochemical Sciences. 40: 16-24. PMID 25435400 DOI: 10.1016/j.tibs.2014.10.011 |
0.385 |
|
| 2014 |
Huang P, Chandra V, Rastinejad F. Retinoic acid actions through mammalian nuclear receptors. Chemical Reviews. 114: 233-54. PMID 24308533 DOI: 10.1021/cr400161b |
0.488 |
|
| 2013 |
Rastinejad F, Huang P, Chandra V, Khorasanizadeh S. Understanding nuclear receptor form and function using structural biology. Journal of Molecular Endocrinology. 51: T1-T21. PMID 24103914 DOI: 10.1530/JME-13-0173 |
0.599 |
|
| 2013 |
Huh JR, Englund EE, Wang H, Huang R, Huang P, Rastinejad F, Inglese J, Austin CP, Johnson RL, Huang W, Littman DR. Identification of Potent and Selective Diphenylpropanamide RORγ Inhibitors. Acs Medicinal Chemistry Letters. 4: 79-84. PMID 24040486 DOI: 10.1021/Ml300286H |
0.467 |
|
| 2013 |
Wu D, Potluri N, Kim Y, Rastinejad F. Structure and dimerization properties of the aryl hydrocarbon receptor PAS-A domain. Molecular and Cellular Biology. 33: 4346-56. PMID 24001774 DOI: 10.1128/MCB.00698-13 |
0.388 |
|
| 2013 |
Chandra V, Huang P, Potluri N, Wu D, Kim Y, Rastinejad F. Multidomain integration in the structure of the HNF-4α nuclear receptor complex. Nature. 495: 394-8. PMID 23485969 DOI: 10.1038/nature11966 |
0.542 |
|
| 2011 |
Huh JR, Leung MW, Huang P, Ryan DA, Krout MR, Malapaka RR, Chow J, Manel N, Ciofani M, Kim SV, Cuesta A, Santori FR, Lafaille JJ, Xu HE, Gin DY, ... Rastinejad F, et al. Digoxin and its derivatives suppress TH17 cell differentiation by antagonizing RORγt activity. Nature. 472: 486-90. PMID 21441909 DOI: 10.1038/Nature09978 |
0.425 |
|
| 2010 |
Kim D, Blus BJ, Chandra V, Huang P, Rastinejad F, Khorasanizadeh S. Corecognition of DNA and a methylated histone tail by the MSL3 chromodomain. Nature Structural & Molecular Biology. 17: 1027-9. PMID 20657587 DOI: 10.1038/Nsmb.1856 |
0.453 |
|
| 2010 |
Huang P, Chandra V, Rastinejad F. Structural overview of the nuclear receptor superfamily: insights into physiology and therapeutics. Annual Review of Physiology. 72: 247-72. PMID 20148675 DOI: 10.1146/Annurev-Physiol-021909-135917 |
0.567 |
|
| 2008 |
Chandra V, Huang P, Hamuro Y, Raghuram S, Wang Y, Burris TP, Rastinejad F. Structure of the intact PPAR-gamma-RXR- nuclear receptor complex on DNA. Nature. 456: 350-6. PMID 19043829 DOI: 10.1038/Nature07413 |
0.577 |
|
| 2007 |
Raghuram S, Stayrook KR, Huang P, Rogers PM, Nosie AK, McClure DB, Burris LL, Khorasanizadeh S, Burris TP, Rastinejad F. Identification of heme as the ligand for the orphan nuclear receptors REV-ERBalpha and REV-ERBbeta. Nature Structural & Molecular Biology. 14: 1207-13. PMID 18037887 DOI: 10.1038/Nsmb1344 |
0.58 |
|
| 2007 |
Flanagan JF, Blus BJ, Kim D, Clines KL, Rastinejad F, Khorasanizadeh S. Molecular implications of evolutionary differences in CHD double chromodomains. Journal of Molecular Biology. 369: 334-42. PMID 17433364 DOI: 10.1016/J.Jmb.2007.03.024 |
0.314 |
|
| 2004 |
Orlowski M, Szyszka M, Kowalska A, Grad I, Zoglowek A, Rymarczyk G, Dobryszycki P, Krowarsch D, Rastinejad F, Kochman M, Ozyhar A. Plasticity of the ecdysone receptor DNA binding domain. Molecular Endocrinology (Baltimore, Md.). 18: 2166-84. PMID 15192079 DOI: 10.1210/me.2004-0154 |
0.418 |
|
| 2003 |
Devarakonda S, Harp JM, Kim Y, Ozyhar A, Rastinejad F. Structure of the heterodimeric ecdysone receptor DNA-binding complex. The Embo Journal. 22: 5827-40. PMID 14592980 DOI: 10.1093/Emboj/Cdg569 |
0.451 |
|
| 2003 |
Mi LZ, Devarakonda S, Harp JM, Han Q, Pellicciari R, Willson TM, Khorasanizadeh S, Rastinejad F. Structural basis for bile acid binding and activation of the nuclear receptor FXR. Molecular Cell. 11: 1093-100. PMID 12718893 DOI: 10.1016/S1097-2765(03)00112-6 |
0.417 |
|
| 2001 |
Black BE, Holaska JM, Rastinejad F, Paschal BM. DNA binding domains in diverse nuclear receptors function as nuclear export signals. Current Biology : Cb. 11: 1749-58. PMID 11719216 DOI: 10.1016/S0960-9822(01)00537-1 |
0.446 |
|
| 2001 |
Chasse SA, Rastinejad F. Physical structure of nuclear receptor-DNA complexes. Methods in Molecular Biology (Clifton, N.J.). 176: 91-103. PMID 11554341 DOI: 10.1385/1-59259-115-9:91 |
0.351 |
|
| 2001 |
Mi LZ, Rastinejad F. Large scale production of nuclear receptor ligand-binding domains. Methods in Molecular Biology (Clifton, N.J.). 176: 81-90. PMID 11554340 DOI: 10.1385/1-59259-115-9:81 |
0.395 |
|
| 2001 |
Khorasanizadeh S, Rastinejad F. Nuclear-receptor interactions on DNA-response elements. Trends in Biochemical Sciences. 26: 384-90. PMID 11406412 DOI: 10.1016/S0968-0004(01)01800-X |
0.444 |
|
| 2001 |
Rastinejad F. Retinoid X receptor and its partners in the nuclear receptor family. Current Opinion in Structural Biology. 11: 33-8. PMID 11179889 DOI: 10.1016/S0959-440X(00)00165-2 |
0.396 |
|
| 2000 |
Rastinejad F, Wagner T, Zhao Q, Khorasanizadeh S. Structure of the RXR-RAR DNA-binding complex on the retinoic acid response element DR1. The Embo Journal. 19: 1045-54. PMID 10698945 DOI: 10.1093/Emboj/19.5.1045 |
0.442 |
|
| 2000 |
Zhao Q, Chasse SA, Devarakonda S, Sierk ML, Ahvazi B, Rastinejad F. Structural basis of RXR-DNA interactions. Journal of Molecular Biology. 296: 509-20. PMID 10669605 DOI: 10.1006/Jmbi.1999.3457 |
0.369 |
|
| 1998 |
Zhao Q, Khorasanizadeh S, Miyoshi Y, Lazar MA, Rastinejad F. Structural elements of an orphan nuclear receptor-DNA complex. Molecular Cell. 1: 849-61. PMID 9660968 DOI: 10.1016/S1097-2765(00)80084-2 |
0.443 |
|
| 1995 |
Rastinejad F, Perlmann T, Evans RM, Sigler PB. Structural determinants of nuclear receptor assembly on DNA direct repeats. Nature. 375: 203-11. PMID 7746322 DOI: 10.1038/375203A0 |
0.416 |
|
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