Scott Briggs
Affiliations: | Biochemistry | Purdue University, West Lafayette, IN, United States |
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Molecular Biology, GeneticsGoogle:
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Publications
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Saha D, Gregor JB, Hoda S, et al. (2024) maintains two ohnologs, and , for distinct roles in ergosterol gene regulation to mediate sterol homeostasis under azole and hypoxic conditions. Msphere. e0052424 |
Baker KM, Hoda S, Saha D, et al. (2022) The Set1 Histone H3K4 Methyltransferase Contributes to Azole Susceptibility in a Species-Specific Manner by Differentially Altering the Expression of Drug Efflux Pumps and the Ergosterol Gene Pathway. Antimicrobial Agents and Chemotherapy. e0225021 |
Strahl BD, Briggs SD. (2020) The SAGA continues: The rise of cis- and trans-histone crosstalk pathways. Biochimica Et Biophysica Acta. Gene Regulatory Mechanisms. 194600 |
Serratore ND, Baker KM, Macadlo LA, et al. (2017) A Novel Sterol-Signaling Pathway Governs Azole Antifungal Drug Resistance and Hypoxic Gene Repression in Saccharomyces cerevisiae. Genetics |
Li F, Zheng LD, Chen X, et al. (2017) Gcn5-mediated Rph1 acetylation regulates its autophagic degradation under DNA damage stress. Nucleic Acids Research |
Harmeyer KM, South PF, Bishop B, et al. (2015) Immediate chromatin immunoprecipitation and on-bead quantitative PCR analysis: a versatile and rapid ChIP procedure. Nucleic Acids Research. 43: e38 |
South PF, Harmeyer KM, Serratore ND, et al. (2013) H3K4 methyltransferase Set1 is involved in maintenance of ergosterol homeostasis and resistance to Brefeldin A. Proceedings of the National Academy of Sciences of the United States of America. 110: E1016-25 |
Mersman DP, Du HN, Fingerman IM, et al. (2012) Charge-based interaction conserved within histone H3 lysine 4 (H3K4) methyltransferase complexes is needed for protein stability, histone methylation, and gene expression. The Journal of Biological Chemistry. 287: 2652-65 |
South P, Briggs S. (2012) ASH2L (ash2 (absent, small, or homeotic)-like (Drosophila)) Atlas of Genetics and Cytogenetics in Oncology and Haematology |
Du HN, Briggs SD. (2010) A nucleosome surface formed by histone H4, H2A, and H3 residues is needed for proper histone H3 Lys36 methylation, histone acetylation, and repression of cryptic transcription. The Journal of Biological Chemistry. 285: 11704-13 |