Publications

Found 96 results
Filters: Author is Patel, Dinshaw J  [Clear All Filters]
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Saredi, G., Huang, H., Hammond, C. M., Alabert, C., Bekker-Jensen, S., Forne, I., Reverón-Gómez, N., Foster, B. M., Mlejnkova, L., Bartke, T., Cejka, P., Mailand, N., Imhof, A., Patel, D. J., and Groth, A. (2016) H4K20me0 marks post-replicative chromatin and recruits the TONSL–MMS22L DNA repair complex.. Nature. 534, 714-718
Wang, G. G., Song, J., Wang, Z., Dormann, H. L., Casadio, F., Li, H., Luo, J. - L., Patel, D. J., and C Allis, D. (2009) Haematopoietic malignancies caused by dysregulation of a chromatin-binding PHD finger. Nature. 459, 847-51
Zheng, L., Falschlunger, C., Huang, K., Mairhofer, E., Yuan, S., Wang, J., Patel, D. J., Micura, R., and Ren, A. (2019) Hatchet ribozyme structure and implications for cleavage mechanism. Proc Natl Acad Sci U S A. 10.1073/pnas.1902413116
Ruthenburg, A. J., Wang, W., Graybosch, D. M., Li, H., C Allis, D., Patel, D. J., and Verdine, G. L. (2006) Histone H3 recognition and presentation by the WDR5 module of the MLL1 complex. Nat Struct Mol Biol. 13, 704-12
Xie, W., Lama, L., Adura, C., Tomita, D., J Glickman, F., Tuschl, T., and Patel, D. J. (2019) Human cGAS catalytic domain has an additional DNA-binding interface that enhances enzymatic activity and liquid-phase condensation. Proc Natl Acad Sci U S A. 116, 11946-11955
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Rechkoblit, O., Malinina, L., Cheng, Y., Geacintov, N. E., Broyde, S., and Patel, D. J. (2009) Impact of conformational heterogeneity of OxoG lesions and their pairing partners on bypass fidelity by Y family polymerases. Structure. 17, 725-36
Rechkoblit, O., Delaney, J. C., Essigmann, J. M., and Patel, D. J. (2011) Implications for damage recognition during Dpo4-mediated mutagenic bypass of m1G and m3C lesions. Structure. 19, 821-32
Yang, H., and Patel, D. J. (2017) Inhibition Mechanism of an Anti-CRISPR Suppressor AcrIIA4 Targeting SpyCas9. Mol Cell. 10.1016/j.molcel.2017.05.024
Ren, A., Košutić, M., Rajashankar, K. R., Frener, M., Santner, T., Westhof, E., Micura, R., and Patel, D. J. (2014) In-line alignment and Mg²⁺ coordination at the cleavage site of the env22 twister ribozyme.. Nat Commun. 5, 5534
Weinberg, D. E., Nakanishi, K., Patel, D. J., and Bartel, D. P. (2011) The inside-out mechanism of Dicers from budding yeasts. Cell. 146, 262-76
Ausin, I., Greenberg, M. V. C., Simanshu, D. K., Hale, C. J., Vashisht, A. A., Simon, S. A., Lee, T. -fen, Feng, S., Española, S. D., Meyers, B. C., Wohlschlegel, J. A., Patel, D. J., and Jacobsen, S. E. (2012) INVOLVED IN DE NOVO 2-containing complex involved in RNA-directed DNA methylation in Arabidopsis. Proc Natl Acad Sci U S A. 109, 8374-81
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Huang, L., Ishibe-Murakami, S., Patel, D. J., and Serganov, A. (2011) Long-range pseudoknot interactions dictate the regulatory response in the tetrahydrofolate riboswitch. Proc Natl Acad Sci U S A. 108, 14801-6
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Du, J., Johnson, L. M., Groth, M., Feng, S., Hale, C. J., Li, S., Vashisht, A. A., Wohlschlegel, J. A., Patel, D. J., and Jacobsen, S. E. (2014) Mechanism of DNA methylation-directed histone methylation by KRYPTONITE. Mol Cell. 55, 495-504
Rechkoblit, O., Kolbanovskiy, A., Malinina, L., Geacintov, N. E., Broyde, S., and Patel, D. J. (2010) Mechanism of error-free and semitargeted mutagenic bypass of an aromatic amine lesion by Y-family polymerase Dpo4. Nat Struct Mol Biol. 17, 379-88
Košutić, M., Neuner, S., Ren, A., Flür, S., Wunderlich, C., Mairhofer, E., Vušurović, N., Seikowski, J., Breuker, K., Höbartner, C., Patel, D. J., Kreutz, C., and Micura, R. (2015) A Mini-Twister Variant and Impact of Residues/Cations on the Phosphodiester Cleavage of this Ribozyme Class. Angew Chem Int Ed Engl. 54, 15128-15133
Li, H., Ilin, S., Wang, W., Duncan, E. M., Wysocka, J., C Allis, D., and Patel, D. J. (2006) Molecular basis for site-specific read-out of histone H3K4me3 by the BPTF PHD finger of NURF. Nature. 442, 91-5
Zhong, X., Du, J., Hale, C. J., Gallego-Bartolome, J., Feng, S., Vashisht, A. A., Chory, J., Wohlschlegel, J. A., Patel, D. J., and Jacobsen, S. E. (2014) Molecular mechanism of action of plant DRM de novo DNA methyltransferases. Cell. 157, 1050-60
Xie, W., Wang, S., Wang, J., M de la Cruz, J., Xu, G., Scaltriti, M., and Patel, D. J. (2021) Molecular mechanisms of assembly and TRIP13-mediated remodeling of the human Shieldin complex. Proc Natl Acad Sci U S A. 10.1073/pnas.2024512118
Schnabl, J., Wang, J., Hohmann, U., Gehre, M., Batki, J., Andreev, V. I., Purkhauser, K., Fasching, N., Duchek, P., Novatchkova, M., Mechtler, K., Plaschka, C., Patel, D. J., and Brennecke, J. (2021) Molecular principles of Piwi-mediated cotranscriptional silencing through the dimeric SFiNX complex. Genes Dev. 35, 392-409
Cheng, Z., Cheung, P., Kuo, A. J., Yukl, E. T., Wilmot, C. M., Gozani, O., and Patel, D. J. (2014) A molecular threading mechanism underlies Jumonji lysine demethylase KDM2A regulation of methylated H3K36. Genes Dev. 28, 1758-71
Tian, Y., Simanshu, D. K., Ascano, M., Diaz-Avalos, R., Park, A. Young, Juranek, S. A., Rice, W. J., Yin, Q., Robinson, C. V., Tuschl, T., and Patel, D. J. (2011) Multimeric assembly and biochemical characterization of the Trax-translin endonuclease complex. Nat Struct Mol Biol. 18, 658-64
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Batki, J., Schnabl, J., Wang, J., Handler, D., Andreev, V. I., Stieger, C. E., Novatchkova, M., Lampersberger, L., Kauneckaite, K., Xie, W., Mechtler, K., Patel, D. J., and Brennecke, J. (2019) The nascent RNA binding complex SFiNX licenses piRNA-guided heterochromatin formation. Nat Struct Mol Biol. 26, 720-731
Simanshu, D. K., Kamlekar, R. Kanth, Wijesinghe, D. S., Zou, X., Zhai, X., Mishra, S. K., Molotkovsky, J. G., Malinina, L., Hinchcliffe, E. H., Chalfant, C. E., Brown, R. E., and Patel, D. J. (2013) Non-vesicular trafficking by a ceramide-1-phosphate transfer protein regulates eicosanoids. Nature. 500, 463-7
Wang, Y., Juranek, S., Li, H., Sheng, G., Wardle, G. S., Tuschl, T., and Patel, D. J. (2009) Nucleation, propagation and cleavage of target RNAs in Ago silencing complexes. Nature. 461, 754-61
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Yang, H., Gao, P., Rajashankar, K. R., and Patel, D. J. (2016) PAM-Dependent Target DNA Recognition and Cleavage by C2c1 CRISPR-Cas Endonuclease. Cell. 167, 1814-1828.e12

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