Andrea A. Duina

Affiliation confirmed via AI analysis of OpenAlex, ORCID, and web sources.

Federal Grant PI

Professor of Biology

Hendrix College

Formerly Arkansas Affiliated with Hendrix College through 2024.

13 h-index 29 pubs 996 cited

Research Areas

Biomedical Subjects

Links

ORCID Lab Website

OverviewAI-generated summary

Andrea A. Duina's research focuses on understanding the molecular mechanisms governing gene expression and protein function, primarily utilizing the model organism *Saccharomyces cerevisiae* (budding yeast). Her work has investigated the roles of chaperone proteins, such as Hsp90 and cyclophilins, in signal transduction pathways and the regulation of cellular responses, including the heat shock response. Duina has also explored the intricate relationship between histone modifications, chromatin structure, and the process of transcriptional elongation, examining how factors like Spt6 and FACT interact with histones to facilitate or regulate gene transcription.

Her research has contributed to understanding how histone integrity influences the localization of elongation factors like Spt16 across transcribed genes. Additionally, Duina has analyzed mutant histones and their impact on chromatin-associated complexes, such as Swi/Snf. She has also received federal funding from the National Science Foundation (NSF) for a conference aimed at broadening research opportunities in South Central EPSCoR states. Duina has a publication record of 29 articles, with an h-index of 13 and a total of 996 citations, and actively collaborates with colleagues at Hendrix College.

Metrics

h-index: 13
Publications: 29
Citations: 996

Selected Publications

Trapping of yFACT at 3’ ends of genes is not a universal characteristic of yeast versions of Bryant-Li-Bhoj syndrome histone H3 mutants (2024)

PubMed 1 citation DOI OpenAlex
Assessing contributions of DNA sequences at the 3’ end of a yeast gene on yFACT, RNA polymerase II, and nucleosome occupancy (2024)

BMC Research Notes DOI OpenAlex
Dominant effects of the histone mutant H3-L61R on Spt16-gene interactions in budding yeast (2022)

Epigenetics 4 citations DOI OpenAlex
Evidence that dissociation of Spt16 from transcribed genes is partially dependent on RNA Polymerase II termination (2019)

Transcription 3 citations DOI OpenAlex
Targeted in Situ Mutagenesis of Histone Genes in Budding Yeast (2017)

Journal of Visualized Experiments 3 citations DOI OpenAlex
Charged residues on the side of the nucleosome contribute to normal Spt16-gene interactions in budding yeast (2017)

Epigenetics 16 citations DOI OpenAlex
Targeted in Situ Mutagenesis of Histone Genes in Budding Yeast (2017)

Journal of Visualized Experiments 5 citations DOI OpenAlex
A Systematic Mutational Analysis of a Histone H3 Residue in Budding Yeast Provides Insights into Chromatin Dynamics (2015)

G3 Genes Genomes Genetics 13 citations DOI OpenAlex
Budding Yeast for Budding Geneticists: A Primer on the Saccharomyces cerevisiae Model System (2014)

Genetics 238 citations DOI OpenAlex
A Nucleosomal Region Important for Ensuring Proper Interactions Between the Transcription Elongation Factor Spt16 and Transcribed Genes inSaccharomyces cerevisiae (2013)

G3 Genes Genomes Genetics 20 citations DOI OpenAlex
New Roles for Old Characters: An Educational Primer for Use with “Vps Factors Are Required for Efficient Transcription Elongation in Budding Yeast” (2013)

Genetics DOI OpenAlex
Identification of a nucleosomal region required for the proper distribution of the transcription elongation factor Spt16 across transcribed genes in Saccharomyces cerevisiae (2012)

The FASEB Journal DOI OpenAlex
Genetic evidence for an involvement of the TOR complex 1 in the process of transcription elongation in Saccharomyces cerevisiae (2012)

The FASEB Journal DOI OpenAlex
Histone Chaperones Spt6 and FACT: Similarities and Differences in Modes of Action at Transcribed Genes (2011)

Genetics Research International 51 citations DOI OpenAlex
Mutant Versions of the S. cerevisiae Transcription Elongation Factor Spt16 Define Regions of Spt16 That Functionally Interact with Histone H3 (2011)

PLoS ONE 29 citations DOI OpenAlex