Denise V. Greathouse
Affiliation confirmed via AI analysis of OpenAlex, ORCID, and web sources.
Research Assoc. Professor
Also affiliated: Centre National de la Recherche Scientifique (2000); University of Miami (2005); Utrecht University (1996–2003); Cornell University (1997–2003); Leipzig University (1998)
Faculty Researcher
Research Areas
Biomedical Subjects
Links
Biography and Research Information
OverviewAI-generated summary
Denise V. Greathouse is a Research Associate Professor at the University of Arkansas at Fayetteville. Her research focuses on the behavior and structure of lipid membranes and their interactions with peptides and proteins. Greathouse has published work investigating how specific amino acid residues, such as glutamic acid and tryptophan, influence membrane properties and protein structure within these environments. Her investigations often employ molecular modeling to understand these complex interactions. She has co-authored publications with researchers including Roger E. Koeppe from the University of Arkansas at Fayetteville and Jake R. Price from the University of Arkansas for Medical Sciences.
With a career marked by significant scholarly output, Greathouse has authored 149 publications, accumulating over 3,900 citations. Her work has been recognized with a designation as a highly cited researcher. Her recent publications in 2021 explored lipid-dependent titration at membrane interfaces and disorder induced by specific amino acids in transmembrane helices.
Metrics
- h-index: 33
- Publications: 149
- Citations: 3,979
Selected Publications
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Illuminating Disorder Induced by Glu in a Stable Arg-Anchored Transmembrane Helix (2021)
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Lipid-Dependent Titration of Glutamic Acid at a Bilayer Membrane Interface (2021)
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Examination of pH dependency and orientation differences of membrane spanning alpha helices carrying a single or pair of buried histidine residues (2020)
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Flanking aromatic residue competition influences transmembrane peptide helix dynamics (2020)
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Effect of pH and Lipid Composition on Membrane-Spanning Helices with Glutamic Acid Examined by Solid-State Nmr (2020)
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Effect of Charged Lipids on the Ionization Behavior of Glutamic Acid-Containing Transmembrane Helices (2020)
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Influence of interfacial tryptophan residues on an arginine-flanked transmembrane helix (2019)
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Lipid Optimization to Improve the Solid-State NMR Spectra from Membrane-Spanning Helices with Glutamic Acid (2019)
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Breaking the Backbone: Central Arginine Residues Induce Membrane Exit and Helix Distortions within a Dynamic Membrane Peptide (2019)
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Influence of Lipid Saturation, Hydrophobic Length and Cholesterol on Double‐Arginine‐Containing Helical Peptides in Bilayer Membranes (2019)
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Position Dependent Orientation Difference of Transmembrane Peptides Flanked by Single or Multiple Histidine Residues (2019)
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Novel F13,F15 Gramicidin Subunits Predicted to Cross Bilayer Membranes and form Ion Channels (2019)
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Characterization of Alpha-Helix Distortions at a Membrane Surface and a Partial 3(10)-Helix by Solid-State NMR (2019)
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Influence of Charged Lipids on Glutamic Acid Containing Transmembrane Helices (2019)
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Helix Fraying and Orientation of a Transmembrane Peptide having a Long Hydrophobic Core and Anchored by Interfacial Arginine Residues (2019)
Collaboration Network
Top Collaborators
- Lipid-Dependent Titration of Glutamic Acid at a Bilayer Membrane Interface
- Illuminating Disorder Induced by Glu in a Stable Arg-Anchored Transmembrane Helix
- Lipid-Dependent Titration of Glutamic Acid at a Bilayer Membrane Interface
- Illuminating Disorder Induced by Glu in a Stable Arg-Anchored Transmembrane Helix
- Lipid-Dependent Titration of Glutamic Acid at a Bilayer Membrane Interface
- Lipid-Dependent Titration of Glutamic Acid at a Bilayer Membrane Interface
- Illuminating Disorder Induced by Glu in a Stable Arg-Anchored Transmembrane Helix
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