L
Leslie W. Glustrom
Researcher at University of Colorado Boulder
Publications - 6
Citations - 528
Leslie W. Glustrom is an academic researcher from University of Colorado Boulder. The author has contributed to research in topics: DNA & Viral structural protein. The author has an hindex of 4, co-authored 6 publications receiving 500 citations.
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Journal ArticleDOI
Full cost accounting for the life cycle of coal.
Paul R. Epstein,Jonathan J. Buonocore,Kevin Eckerle,Michael Hendryx,Benjamin M. Stout,Richard Heinberg,Richard W. Clapp,Beverly May,Nancy L. Reinhart,Melissa M. Ahern,Samir Doshi,Leslie W. Glustrom +11 more
TL;DR: This work estimates that the life cycle effects of coal and the waste stream generated are costing the U.S. public a third to over one‐half of a trillion dollars annually, and conservatively doubles to triples the price of electricity from coal per kWh generated, making wind, solar, and other forms of nonfossil fuel power generation, along with investments in efficiency and electricity conservation methods, economically competitive.
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Structural basis for telomeric single-stranded DNA recognition by yeast Cdc13.
Rachel M. Mitton-Fry,Emily M. Anderson,Douglas L. Theobald,Leslie W. Glustrom,Deborah S. Wuttke +4 more
TL;DR: The structure reported here provides a foundation for understanding the mechanism by which Cdc13 recognizes GT-rich heterogeneous sequences with both unusually strong affinity and high specificity, and indicates that molecular recognition of extended single-stranded nucleic acids may proceed via a folding-type mechanism rather than resulting from specific patterns of hydrogen bonds.
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Towards an understanding of the poliovirus replication complex: the solution structure of the soluble domain of the poliovirus 3A protein.
TL;DR: The structure of the soluble, N-terminal domain of 3A (3A-N) is determined using NMR spectroscopy, and it is shown that 3A- N exists as a symmetric dimer, and each monomer consists of an alpha-helical hairpin with unstructured, yet functional,N- and C termini.
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Re: 1,1-Dichloro-2,2-bis-(p-chlorophenyl)ethylene and polychlorinated biphenyls and breast cancer: combined analysis of five U.S. studies.
Journal ArticleDOI
Single-stranded telomere-binding protein employs a dual rheostat for binding affinity and specificity that drives function.
Leslie W. Glustrom,Kenneth Lyon,Margherita Paschini,Margherita Paschini,Cynthia M. Reyes,Cynthia M. Reyes,Nicholas V. Parsonnet,Tasha B. Toro,Victoria Lundblad,Victoria Lundblad,Deborah S. Wuttke +10 more
TL;DR: This study has found that a telomere-binding protein exhibits a degree of specificity for ssDNA that is finely tuned for its function, which includes specificity for G-rich sequences with some tolerance for substitution.