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Daniel T. Gewirth - Publications

Affiliations: 
Duke University, Durham, NC 
Area:
Biochemistry
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40 high-probability publications. We are testing a new system for linking publications to authors. You can help! If you notice any inaccuracies, please sign in and mark papers as correct or incorrect matches. If you identify any major omissions or other inaccuracies in the publication list, please let us know.

Year Citation  Score
2024 Amankwah YS, Fleifil Y, Unruh E, Collins P, Wang Y, Vitou K, Bates A, Obaseki I, Sugoor M, Alao JP, McCarrick RM, Gewirth DT, Sahu ID, Li Z, Lorigan GA, et al. Structural transitions modulate the chaperone activities of Grp94. Proceedings of the National Academy of Sciences of the United States of America. 121: e2309326121. PMID 38483986 DOI: 10.1073/pnas.2309326121  0.511
2023 Que NLS, Seidler PM, Aw WJ, Chiosis G, Gewirth DT. Selective inhibition of hsp90 paralogs: Structure and binding studies uncover the role of helix 1 in Grp94-selective ligand binding. Biorxiv : the Preprint Server For Biology. PMID 37577523 DOI: 10.1101/2023.07.31.551342  0.489
2020 Yan P, Patel HJ, Sharma S, Corben A, Wang T, Panchal P, Yang C, Sun W, Araujo TL, Rodina A, Joshi S, Robzyk K, Gandu S, White JR, de Stanchina E, ... ... Gewirth DT, et al. Molecular Stressors Engender Protein Connectivity Dysfunction through Aberrant N-Glycosylation of a Chaperone. Cell Reports. 31: 107840. PMID 32610141 DOI: 10.1016/J.Celrep.2020.107840  0.376
2019 Huck JD, Que NLS, Immormino RM, Shrestha L, Taldone T, Chiosis G, Gewirth DT. NECA derivatives exploit the paralog-specific properties of the Site 3 side pocket of Grp94, the ER Hsp90. The Journal of Biological Chemistry. PMID 31501246 DOI: 10.1074/Jbc.Ra119.009960  0.781
2019 Huck JD, Que NLS, Sharma S, Taldone T, Chiosis G, Gewirth DT. Structures of Hsp90α and Hsp90β bound to a purine-scaffold inhibitor reveal an exploitable residue for drug selectivity. Proteins. PMID 31141217 DOI: 10.1002/prot.25750  0.439
2019 Huck JD, Que NLS, Sharma S, Taldone T, Chiosis G, Gewirth DT. Structures of Hsp90 alpha and Hsp90 beta bound to a purine-scaffold inhibitor reveal an exploitable residue for drug selectivity. Proteins. 87: 869-877. DOI: 10.2210/Pdb6N8Y/Pdb  0.547
2018 Wang T, Rodina A, Dunphy MP, Corben A, Modi S, Guzman ML, Gewirth DT, Chiosis G. Chaperome heterogeneity and its implications for cancer study and treatment. The Journal of Biological Chemistry. PMID 30409908 DOI: 10.1074/Jbc.Rev118.002811  0.378
2018 Que NLS, Crowley VM, Duerfeldt AS, Zhao J, Kent CN, Blagg BSJ, Gewirth DT. Structure based design of a Grp94-selective inhibitor: Exploiting a key residue in Grp94 to optimize paralog-selective binding. Journal of Medicinal Chemistry. PMID 29528635 DOI: 10.1021/Acs.Jmedchem.7B01608  0.565
2017 Huck JD, Que NL, Hong F, Li Z, Gewirth DT. Structural and Functional Analysis of GRP94 in the Closed State Reveals an Essential Role for the Pre-N Domain and a Potential Client-Binding Site. Cell Reports. 20: 2800-2809. PMID 28930677 DOI: 10.1016/J.Celrep.2017.08.079  0.569
2017 Dalal K, Che M, Que NS, Sharma A, Yang R, Lallous N, Borgmann H, Ozistanbullu D, Tse R, Ban F, Li H, Tam KJ, Roshan-Moniri M, Leblanc E, Gleave ME, ... Gewirth DT, et al. Bypassing drug-resistance mechanisms of prostate cancer with small-molecules that target androgen receptor chromatin interactions. Molecular Cancer Therapeutics. PMID 28775145 DOI: 10.1158/1535-7163.Mct-17-0259  0.421
2016 Maharaj KA, Que NL, Hong F, Huck JD, Gill SK, Wu S, Li Z, Gewirth DT. Exploring the Functional Complementation between Grp94 and Hsp90. Plos One. 11: e0166271. PMID 27824935 DOI: 10.1371/Journal.Pone.0166271  0.502
2016 Gewirth DT. Paralog specific Hsp90 Inhibitors - a brief history and a bright future. Current Topics in Medicinal Chemistry. PMID 27072700 DOI: 10.2174/1568026616666160413141154  0.438
2016 Ansa-Addo EA, Thaxton J, Hong F, Wu BX, Zhang Y, Fugle CW, Metelli A, Riesenberg B, Williams K, Gewirth DT, Chiosis G, Liu B, Li Z. Clients and Oncogenic Roles of Molecular Chaperone gp96/grp94. Current Topics in Medicinal Chemistry. PMID 27072698 DOI: 10.2174/1568026616666160413141613  0.33
2015 Patel HJ, Patel PD, Ochiana SO, Yan P, Sun W, Patel MR, Shah SK, Tramentozzi E, Brooks J, Bolaender A, Shrestha L, Stephani R, Finotti P, Leifer C, Li Z, ... Gewirth DT, et al. Structure-activity relationship in a purine-scaffold compound series with selectivity for the endoplasmic reticulum Hsp90 paralog Grp94. Journal of Medicinal Chemistry. 58: 3922-43. PMID 25901531 DOI: 10.1021/Acs.Jmedchem.5B00197  0.428
2015 Yan P, Patel H, Patel P, Ochiana S, Sun W, Shah S, Finotti P, Leifer C, Li Z, Gewirth D, Taldone T, Chiosis G. Abstract 4716: Tumor-specific regulation of receptor tyrosine kinases by Grp94 Cancer Research. 75: 4716-4716. DOI: 10.1158/1538-7445.Am2015-4716  0.315
2015 Ochiana SO, Taldone T, Patel HJ, Patel P, Pengrong Y, Sun W, Rodina A, Shah S, Gewirth DT, Chiosis G. Abstract 2831: Development of selective GRP94 inhibitors for the treatment of cancer Cancer Research. 75: 2831-2831. DOI: 10.1158/1538-7445.Am2015-2831  0.443
2014 Seidler PM, Shinsky SA, Hong F, Li Z, Cosgrove MS, Gewirth DT. Characterization of the Grp94/OS-9 chaperone-lectin complex. Journal of Molecular Biology. 426: 3590-605. PMID 25193139 DOI: 10.1016/J.Jmb.2014.08.024  0.478
2013 Patel PD, Yan P, Seidler PM, Patel HJ, Sun W, Yang C, Que NS, Taldone T, Finotti P, Stephani RA, Gewirth DT, Chiosis G. Paralog-selective Hsp90 inhibitors define tumor-specific regulation of HER2. Nature Chemical Biology. 9: 677-84. PMID 23995768 DOI: 10.1038/Nchembio.1335  0.379
2013 Taldone T, Patel PD, Patel M, Patel HJ, Evans CE, Rodina A, Ochiana S, Shah SK, Uddin M, Gewirth D, Chiosis G. Experimental and structural testing module to analyze paralogue-specificity and affinity in the Hsp90 inhibitors series. Journal of Medicinal Chemistry. 56: 6803-18. PMID 23965125 DOI: 10.1021/Jm400619B  0.482
2013 Hong F, Liu B, Chiosis G, Gewirth DT, Li Z. α7 helix region of αI domain is crucial for integrin binding to endoplasmic reticulum chaperone gp96: a potential therapeutic target for cancer metastasis. The Journal of Biological Chemistry. 288: 18243-8. PMID 23671277 DOI: 10.1074/Jbc.M113.468850  0.42
2012 Wu S, Hong F, Gewirth D, Guo B, Liu B, Li Z. The molecular chaperone gp96/GRP94 interacts with Toll-like receptors and integrins via its C-terminal hydrophobic domain. The Journal of Biological Chemistry. 287: 6735-42. PMID 22223641 DOI: 10.1074/Jbc.M111.309526  0.505
2009 Immormino RM, Metzger LE, Reardon PN, Dollins DE, Blagg BS, Gewirth DT. Different poses for ligand and chaperone in inhibitor-bound Hsp90 and GRP94: implications for paralog-specific drug design. Journal of Molecular Biology. 388: 1033-42. PMID 19361515 DOI: 10.1016/J.Jmb.2009.03.071  0.764
2007 Dollins DE, Warren JJ, Immormino RM, Gewirth DT. Structures of GRP94-nucleotide complexes reveal mechanistic differences between the hsp90 chaperones. Molecular Cell. 28: 41-56. PMID 17936703 DOI: 10.1016/J.Molcel.2007.08.024  0.783
2007 Alam SM, McAdams M, Boren D, Rak M, Scearce RM, Gao F, Camacho ZT, Gewirth D, Kelsoe G, Chen P, Haynes BF. The role of antibody polyspecificity and lipid reactivity in binding of broadly neutralizing anti-HIV-1 envelope human monoclonal antibodies 2F5 and 4E10 to glycoprotein 41 membrane proximal envelope epitopes. Journal of Immunology (Baltimore, Md. : 1950). 178: 4424-35. PMID 17372000 DOI: 10.4049/Jimmunol.178.7.4424  0.307
2006 Immormino RM, Kang Y, Chiosis G, Gewirth DT. Structural and quantum chemical studies of 8-aryl-sulfanyl adenine class Hsp90 inhibitors. Journal of Medicinal Chemistry. 49: 4953-60. PMID 16884307 DOI: 10.1021/Jm060297X  0.76
2006 Williams AH, Immormino RM, Gewirth DT, Raetz CR. Structure of UDP-N-acetylglucosamine acyltransferase with a bound antibacterial pentadecapeptide. Proceedings of the National Academy of Sciences of the United States of America. 103: 10877-82. PMID 16835299 DOI: 10.1073/Pnas.0604465103  0.707
2006 He H, Zatorska D, Kim J, Aguirre J, Llauger L, She Y, Wu N, Immormino RM, Gewirth DT, Chiosis G. Identification of potent water soluble purine-scaffold inhibitors of the heat shock protein 90. Journal of Medicinal Chemistry. 49: 381-90. PMID 16392823 DOI: 10.1021/Jm0508078  0.723
2005 Dollins DE, Immormino RM, Gewirth DT. Structure of unliganded GRP94, the endoplasmic reticulum Hsp90. Basis for nucleotide-induced conformational change. The Journal of Biological Chemistry. 280: 30438-47. PMID 15951571 DOI: 10.1074/Jbc.M503761200  0.784
2005 Shaffer PL, McDonnell DP, Gewirth DT. Characterization of transcriptional activation and DNA-binding functions in the hinge region of the vitamin D receptor. Biochemistry. 44: 2678-85. PMID 15709781 DOI: 10.1021/Bi0477182  0.742
2004 Immormino RM, Dollins DE, Shaffer PL, Soldano KL, Walker MA, Gewirth DT. Ligand-induced conformational shift in the N-terminal domain of GRP94, an Hsp90 chaperone. The Journal of Biological Chemistry. 279: 46162-71. PMID 15292259 DOI: 10.1074/Jbc.M405253200  0.749
2004 Claessens F, Gewirth DT. DNA recognition by nuclear receptors. Essays in Biochemistry. 40: 59-72. PMID 15242339 DOI: 10.1042/Bse0400059  0.492
2004 Shaffer PL, Gewirth DT. Structural analysis of RXR-VDR interactions on DR3 DNA. The Journal of Steroid Biochemistry and Molecular Biology. 89: 215-9. PMID 15225774 DOI: 10.1016/J.Jsbmb.2004.03.084  0.745
2004 Shaffer PL, Gewirth DT. Vitamin D receptor-DNA interactions. Vitamins and Hormones. 68: 257-73. PMID 15193458 DOI: 10.1016/S0083-6729(04)68009-5  0.731
2004 Shaffer PL, Jivan A, Dollins DE, Claessens F, Gewirth DT. Structural basis of androgen receptor binding to selective androgen response elements. Proceedings of the National Academy of Sciences of the United States of America. 101: 4758-63. PMID 15037741 DOI: 10.1073/Pnas.0401123101  0.752
2003 Soldano KL, Jivan A, Nicchitta CV, Gewirth DT. Structure of the N-terminal domain of GRP94. Basis for ligand specificity and regulation. The Journal of Biological Chemistry. 278: 48330-8. PMID 12970348 DOI: 10.1074/Jbc.M308661200  0.57
2002 Shaffer PL, Gewirth DT. Structural basis of VDR-DNA interactions on direct repeat response elements. The Embo Journal. 21: 2242-52. PMID 11980721 DOI: 10.1093/Emboj/21.9.2242  0.741
2001 Wang SM, Kim GJ, Gewirth DT. Structural studies of a yeast quaternary transcription-initiation complex. Acta Crystallographica. Section D, Biological Crystallography. 57: 441-4. PMID 11223526 DOI: 10.1107/S0907444901000683  0.342
1995 Gewirth DT, Sigler PB. The basis for half-site specificity explored through a non-cognate steroid receptor-DNA complex. Nature Structural Biology. 2: 386-94. PMID 7664096 DOI: 10.1038/Nsb0595-386  0.441
1988 Gewirth DT, Moore PB. Exploration of the L18 binding site on 5S RNA by deletion mutagenesis Nucleic Acids Research. 16: 10717-10732. PMID 3060848 DOI: 10.1093/Nar/16.22.10717  0.339
1987 Gewirth DT, Abo SR, Leontis NB, Moore PB. Secondary structure of 5S RNA: NMR experiments on RNA molecules partially labeled with nitrogen-15 Biochemistry. 26: 5213-5220. PMID 2444255 DOI: 10.1021/Bi00390A047  0.303
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