Eric B. O’Neill

ORCID: 0000-0002-7622-4778
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About
Contact & Profiles
Research Areas
  • RNA and protein synthesis mechanisms
  • RNA modifications and cancer
  • Cellular Mechanics and Interactions
  • Genomics and Phylogenetic Studies
  • Fungal Infections and Studies
  • Plant Disease Resistance and Genetics
  • Pediatric health and respiratory diseases
  • Growth Hormone and Insulin-like Growth Factors
  • Pancreatic function and diabetes
  • DNA and Nucleic Acid Chemistry
  • Cancer, Hypoxia, and Metabolism
  • Cell Adhesion Molecules Research
  • Phytochemical compounds biological activities
  • Antifungal resistance and susceptibility
  • Hippo pathway signaling and YAP/TAZ
  • Tendon Structure and Treatment
  • Diabetes and associated disorders
  • Pituitary Gland Disorders and Treatments
  • Wnt/β-catenin signaling in development and cancer
  • Viral gastroenteritis research and epidemiology
  • RNA Research and Splicing
  • 3D Printing in Biomedical Research
  • RNA regulation and disease
  • Neuroendocrine Tumor Research Advances
  • Nail Diseases and Treatments

Georgia Institute of Technology
2012-2024

Georgia State University
1996-1998

Mg2+ shares a distinctive relationship with RNA, playing important and specific roles in the folding function of essentially all large RNAs. Here we use theory experiment to evaluate Fe2+ absence free oxygen as replacement for RNA catalysis. We describe both quantum mechanical calculations experiments that suggest can indeed be served by Fe2+. The results show geometry coordination phosphates is similar Mg2+. Chemical footprinting conformation Tetrahymena thermophila Group I intron P4–P6...

10.1371/journal.pone.0038024 article EN cc-by PLoS ONE 2012-05-31

Abstract How adhesive forces are transduced and integrated into biochemical signals at focal adhesions (FAs) is poorly understood. Using cells adhering to deformable micropillar arrays, we demonstrate that traction force FAK localization as well Y397-FAK phosphorylation linearly coupled individual FAs on stiff, but not soft, substrates. Similarly, increases with external applied using magnetic beads. This mechanosignaling coupling requires actomyosin contractility, talin-FAK binding,...

10.1038/s41467-021-22602-5 article EN cc-by Nature Communications 2021-04-21

Ancient components of the ribosome, inferred from a consensus previous work, were constructed in silico , vitro and vivo . The resulting model ancestral ribosome presented here incorporates ∼20% extant 23S rRNA fragments five ribosomal proteins. We test hypotheses that can: (i) assume canonical rRNA-like secondary structure, (ii) tertiary structure (iii) form native complexes with protein fragments. Footprinting experiments support formation predicted structure. Gel shift, spectroscopic...

10.1093/nar/gkt023 article EN cc-by-nc Nucleic Acids Research 2013-01-25

Abstract The domain architecture of a large RNA can help explain and/or predict folding, function, biogenesis and evolution. We offer formal general definition an use that to experimentally characterize the rRNA ribosomal small subunit. Here comprising is compact, with self-contained system molecular interactions. A given helix or stem-loop must be allocated uniquely single domain. Local changes such as mutations give domain-wide effects. Helices within have interdependent orientations,...

10.1038/srep20885 article EN cc-by Scientific Reports 2016-02-15

The three-dimensional structure of the ribosomal large subunit (LSU) reveals a single morphological element, although 23S rRNA is contained in six secondary domains. Based upon maps inter- and intra-domain interactions proposed evolutionary pathways development, we hypothesize that Domain III truly independent structural domain LSU. primarily stabilized by interactions, negligibly perturbed inter-domain not penetrated proteins or other rRNA. We have probed alone when within intact using...

10.1261/rna.030692.111 article EN RNA 2012-02-14

A method is described for the serotyping of Cryptococcus neoformans based on direct analysis culture supernatants major type-specific capsular antigen, glucuronoxylomannan. Factor sera prepared by absorption polyclonal rabbit antisera (Iatron Laboratories, Inc., Tokyo, Japan) or selected anti-C. monoclonal antibodies were used in a dot enzyme assay to detect presence antigen.

10.1128/jcm.34.2.466-470.1996 article EN Journal of Clinical Microbiology 1996-02-01

ABSTRACT Cryptococcus neoformans NIH 409 was cultured in a defined medium containing d -[1- 13 C]xylose (Xyl), C]mannose (Man), or C]mannitol as the sole carbon source. The distribution of C Man, Xyl, glucuronic acid (GlcA), and O-acetyl constituents native de-O-acetylated glucuronoxylomannan (GXM) determined by one-dimensional nuclear magnetic resonance spectroscopy. chain Man incorporated intact into GXM since observed only 1 GlcA, Xyl. mannitol carbons 6. This expected has an axis...

10.1128/iai.66.6.2996-2998.1998 article EN Infection and Immunity 1998-06-01

Abstract How adhesive forces are transduced and integrated into biochemical signals at focal adhesions (FAs) is poorly understood. Using cells adhering to deformable micropillar arrays, we demonstrate that traction force FAK localization as well Y397-FAK phosphorylation linearly coupled individual FAs on stiff, but not soft, substrates. Similarly, increases with external applied using magnetic beads. This mechanosignaling coupling requires actomyosin contractility, talin-FAK binding,...

10.21203/rs.3.rs-88495/v1 preprint EN cc-by Research Square (Research Square) 2020-10-22
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