Lorena Sue Beese
· James B. Duke Distinguished Professor of BiochemistryDuke University · Biochemistry
Active 1980–2024
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About
Lorena Sue Beese is the James B. Duke Distinguished Professor of Biochemistry at Duke University and a Professor of Biochemistry. She is a member of the Duke Cancer Institute. Her primary affiliation is with the Duke Department of Biochemistry, where she is involved in research and teaching activities. Her work focuses on biochemistry, and she is part of the faculty contributing to the academic and research missions of Duke University.
Research topics
- Computer Science
- Biology
- Chemistry
- Programming language
- Genetics
- Microbiology
- Biochemistry
- Pharmacology
- Molecular biology
Selected publications
Journal of Biological Chemistry · 2012-05-31 · 69 citations
articleOpen accessSenior authorIn addition to discriminating against base pair mismatches, DNA polymerases exhibit a high degree of selectivity for deoxyribonucleotides over ribo- or dideoxynucleotides. It has been proposed that a single active site residue (steric gate) blocks productive binding of nucleotides containing 2'-hydroxyls. Although this steric gate plays a role in sugar moiety discrimination, its interactions do not account fully for the observed behavior of mutants. Here we present 10 high resolution crystal str…
Sensing and Processing of DNA Interstrand Crosslinks by the Mismatch Repair Pathway
Cell Reports · 2017-10-01 · 61 citations
articleOpen accessDNA interstrand crosslinks (ICLs) that are repaired in non-dividing cells must be recognized independently of replication-associated DNA unwinding. Using cell-free extracts from Xenopus eggs that support neither replication nor transcription, we establish that ICLs are recognized and processed by the mismatch repair (MMR) machinery. We find that ICL repair requires MutSα (MSH2-MSH6) and the mismatch recognition FXE motif in MSH6, strongly suggesting that MutSα functions as an ICL sensor. MutSα r…
Proceedings of the National Academy of Sciences · 2017-05-22 · 49 citations
articleOpen accessSenior authorHuman exonuclease 1 (hExo1) is a member of the RAD2/XPG structure-specific 5'-nuclease superfamily. Its dominant, processive 5'-3' exonuclease and secondary 5'-flap endonuclease activities participate in various DNA repair, recombination, and replication processes. A single active site processes both recessed ends and 5'-flap substrates. By initiating enzyme reactions in crystals, we have trapped hExo1 reaction intermediates that reveal structures of these substrates before and after their exo-…
The Closing Mechanism of DNA Polymerase I at Atomic Resolution
Structure · 2015-07-23 · 39 citations
articleOpen accessACS Chemical Biology · 2014-05-19 · 34 citations
articleOpen accessProtein farnesytransferase (PFTase) catalyzes the farnesylation of proteins with a carboxy-terminal tetrapeptide sequence denoted as a Ca1a2X box. To explore the specificity of this enzyme, an important therapeutic target, solid-phase peptide synthesis in concert with a peptide inversion strategy was used to prepare two libraries, each containing 380 peptides. The libraries were screened using an alkyne-containing isoprenoid analogue followed by click chemistry with biotin azide and subsequent v…
Recent grants
NIH · $647k · 2012
NIH · $3.5M · 2016
NIH · $1.8M · 2004
Frequent coauthors
- 57 shared
Homme W. Hellinga
Duke University Hospital
- 50 shared
Patrick J. Casey
Geological Survey of Sweden
- 30 shared
Michael A. Hast
- 25 shared
Stephen B. Long
Memorial Sloan Kettering Cancer Center
- 25 shared
Paul Modrich
Howard Hughes Medical Institute
- 21 shared
K.L. Terry
Duke University Hospital
- 21 shared
Anita Changela
National Institutes of Health
- 21 shared
Thomas A. Steitz
Yale University
Labs
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