Myfanwy Adams
Affiliations: | 2018- | Molecular Medicine | Cornell University, Ithaca, NY, United States |
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Parents
Sign in to add mentorJoshua S. Chappie | grad student | 2017-2023 | Cornell | |
(Microbiology Graduate Program) | ||||
Dmitry Ghilarov | post-doc | 2023- | John Innes Centre |
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Publications
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Adams MC, Schiltz CJ, Sun J, et al. (2024) The crystal structure of bacteriophage λ RexA provides novel insights into the DNA binding properties of Rex-like phage exclusion proteins. Nucleic Acids Research |
Schiltz CJ, Wilson JR, Hosford CJ, et al. (2022) Polerovirus N-terminal readthrough domain structures reveal molecular strategies for mitigating virus transmission by aphids. Nature Communications. 13: 6368 |
Adams MC, Schiltz CJ, Heck ML, et al. (2021) Crystal structure of the potato leafroll virus coat protein and implications for viral assembly. Journal of Structural Biology. 214: 107811 |
Chowdhury R, Pavinski Bitar PD, Adams MC, et al. (2021) AraC-type regulators HilC and RtsA are directly controlled by an intestinal fatty acid to regulate Salmonella invasion Molecular Microbiology |
Thomason LC, Schiltz CJ, Court C, et al. (2021) Bacteriophage λ RexA and RexB Functions Assist the Transition from Lysogeny to Lytic Growth. Molecular Microbiology |
Hosford CJ, Adams MC, Niu Y, et al. (2020) The N-terminal domain of Staphylothermus marinus McrB shares structural homology with PUA-like RNA binding proteins Journal of Structural Biology |
Schiltz CJ, Adams MC, Chappie JS. (2020) The full-length structure of Thermus scotoductus OLD defines the ATP hydrolysis properties and catalytic mechanism of Class 1 OLD family nucleases. Nucleic Acids Research. 48: 2762-2776 |
Schiltz CJ, Adams MC, Chappie JS. (2020) The full-length structure of Thermus scotoductus OLD defines the ATP hydrolysis properties and catalytic mechanism of Class 1 OLD family nucleases. Nucleic Acids Research |
Murphy SG, Alvarez L, Adams MC, et al. (2019) Endopeptidase Regulation as a Novel Function of the Zur-Dependent Zinc Starvation Response. Mbio. 10 |