E
Ethan B. Butler
Researcher at University of South Alabama
Publications - 6
Citations - 1102
Ethan B. Butler is an academic researcher from University of South Alabama. The author has contributed to research in topics: Cell growth & Cancer cell. The author has an hindex of 4, co-authored 6 publications receiving 987 citations. Previous affiliations of Ethan B. Butler include Yale University.
Papers
More filters
Journal ArticleDOI
Targeting cellular metabolism to improve cancer therapeutics
TL;DR: The relationship between dysregulated cellular metabolism and cancer drug resistance is discussed and how targeting of metabolic enzymes can enhance the efficacy of common therapeutic agents or overcome resistance to chemotherapy or radiotherapy is discussed.
Journal ArticleDOI
Stalling the Engine of Resistance: Targeting Cancer Metabolism to Overcome Therapeutic Resistance
TL;DR: The specificity and efficacy of agents directed at the unique aspects of cancer metabolism are expected to be high; and may, when in used in combination with more traditional therapeutics, present a pathway to surmount resistance within tumors that no longer respond to current forms of treatment.
Journal ArticleDOI
Structural Basis of Cooperative Ligand Binding by the Glycine Riboswitch
TL;DR: The crystal structure of the tandem riboswitch from the glycine permease operon of Fusobacterium nucleatum reveals the glycines binding sites and an extensive network of interactions that serve to communicate ligand binding status between the aptamers.
Journal ArticleDOI
Regiospecificity of the peptidyl tRNA ester within the ribosomal P site.
TL;DR: Strong preferential binding to the O3' regioisomer indicates that the peptidyl transferase proceeds through a transition state with an O3'-linked peptide in the P-site.
Journal ArticleDOI
Exploiting multi-layered vector spaces for signal peptide detection
TL;DR: This work has developed a representation, entitled Multi-Layered Vector Spaces (MLVS), which is a simple mathematical model that maps sequences into a set of MLVS, and demonstrates the usefulness of the model by applying it to the problem of identifying signal peptides.