Scott Briggs

Affiliations: 
Biochemistry Purdue University, West Lafayette, IN, United States 
Area:
Molecular Biology, Genetics
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"Scott Briggs"
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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
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