Phoebe A. Rice

ORCID: 0000-0002-3467-341X
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About
Contact & Profiles
Research Areas
  • DNA and Nucleic Acid Chemistry
  • RNA and protein synthesis mechanisms
  • DNA Repair Mechanisms
  • Bacterial Genetics and Biotechnology
  • Bacteriophages and microbial interactions
  • Enzyme Structure and Function
  • Advanced biosensing and bioanalysis techniques
  • CRISPR and Genetic Engineering
  • Biochemical and Molecular Research
  • Protein Structure and Dynamics
  • RNA modifications and cancer
  • Cancer therapeutics and mechanisms
  • RNA Interference and Gene Delivery
  • Chromosomal and Genetic Variations
  • HIV/AIDS drug development and treatment
  • Genomics and Chromatin Dynamics
  • Gut microbiota and health
  • Clostridium difficile and Clostridium perfringens research
  • Antimicrobial Resistance in Staphylococcus
  • HIV Research and Treatment
  • Probiotics and Fermented Foods
  • Genomics and Phylogenetic Studies
  • Cytomegalovirus and herpesvirus research
  • Glycosylation and Glycoproteins Research
  • Photosynthetic Processes and Mechanisms

University of Chicago
2016-2025

University of Edinburgh
2021

Institute of Genetics and Cancer
2021

Western General Hospital
2021

Roslin Institute
2021

Johns Hopkins University
2008-2020

Howard Hughes Medical Institute
1989-2020

Yale University
1989-2020

Johns Hopkins Medicine
2020

University of Oxford
2017

Plasmids are extrachromosomal genetic elements that often encode fitness-enhancing features. However, many bacteria carry "cryptic" plasmids do not confer clear beneficial functions. We identified one such cryptic plasmid, pBI143, which is ubiquitous across industrialized gut microbiomes and 14 times as numerous crAssphage, currently established the most abundant element in human gut. The majority of mutations pBI143 accumulate specific positions thousands metagenomes, indicating strong...

10.1016/j.cell.2024.01.039 article EN cc-by Cell 2024-02-01

The dipyridodiazepinone Nevirapine is a potent and highly specific inhibitor of the reverse transcriptase (RT) from human immunodeficiency virus type 1 (HIV-1). It member an important class nonnucleoside drugs that appear to share part or all same binding site on enzyme but are susceptible variety spontaneous drug-resistance mutations. co-crystal-structure HIV-1 RT has been solved previously at 3.5-A resolution now partially refined against data extending 2.9-A spacing. drug bound in...

10.1073/pnas.91.9.3911 article EN Proceedings of the National Academy of Sciences 1994-04-26

The crystal structure of the catalytic domain site-specific recombination enzyme gamma delta resolvase has been determined at 2.7 A resolution. Its first 120 amino acids form a central five-stranded, beta-pleated sheet surrounded by five alpha helices. In one four dyad-related dimers, two active site Ser-10 residues are 19 apart, perhaps close enough to contact and become covalently linked DNA site. This dimer also forms only closely packed tetramer found in crystal. subunit interface second...

10.1016/0092-8674(90)90427-g article EN cc-by-nc-nd Cell 1990-12-01

To understand how a bacterium ultimately succeeds or fails in adapting to new host, it is essential assess the temporal dynamics of its fitness over course colonization. Here, we introduce human-derived commensal organism, Bacteroides thetaiotaomicron (Bt), into guts germ-free mice determine whether and genetic requirements for colonization shift time. Combining high-throughput functional genetics assay transcriptomics, find that gene usage changes drastically during first days colonization,...

10.1016/j.celrep.2023.113009 article EN cc-by-nc-nd Cell Reports 2023-08-01
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