Ashley N. Martfeld
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Also affiliated: Duke University (2019); Duke Medical Center (2017–2019)
Research Areas
Biomedical Subjects
Links
Biography and Research Information
OverviewAI-generated summary
Dr. Ashley N. Martfeld's research encompasses lipid membrane and protein structure, investigated through advanced NMR techniques. Her interests also extend to supramolecular self-assembly in materials and DNA/nucleic acid chemistry. Martfeld was most recently published in 2020.
Metrics
- h-index: 6
- Publications: 19
- Citations: 217
Selected Publications
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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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Influence of Lipid Saturation, Hydrophobic Length and Cholesterol on Double‐Arginine‐Containing Helical Peptides in Bilayer Membranes (2019)
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Control of Transmembrane Helix Dynamics by Interfacial Tryptophan Residues (2018)
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Influence of Saturation and Hydrophobic Length of Lipid Bilayers on Twin-Arginine Containing Helical Peptides (2018)
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Response of GWALP23 Transmembrane Peptides to Incorporation of Specific Pairs of Buried Charged Arginine Residues (2017)
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Interfacial Tryptophan Residues Govern Transmembrane Helix Dynamics (2017)
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Solid-State NMR Investigations of Transmembrane Helix Interactions (2017)
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Influence of High pH and Cholesterol on Single Arginine-Containing Transmembrane Peptide Helices (2016)
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Ionization Properties of Histidine Residues in the Lipid Bilayer Membrane Environment (2016)
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Use of Transmembrane Peptides to Understand Ionization Properties of Histidine Residues in Lipid Bilayers (2016)
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Cholesterol Influence on Arginine-Containing Transmembrane Peptides (2016)
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Monitoring the Consequences of Relocating the Tryptophan Anchors on Transmembrane Peptide Dynamics and Alignment (2016)
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Influence of a Potentially Destabilizing Central Tryptophan on Transmembrane Helix Domains (2015)
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Influence of Cholesterol on Single Arginine-Containing Transmembrane Helical Peptides (2015)
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Response of GWALP Transmembrane Peptides to Incorporation of Buried Histidine Residues (2015)
Collaboration Network
Top Collaborators
- Ionization Properties of Histidine Residues in the Lipid Bilayer Membrane Environment
- Dynamic regulation of lipid–protein interactions
- Control of Transmembrane Helix Dynamics by Interfacial Tryptophan Residues
- Influence of High pH and Cholesterol on Single Arginine-Containing Transmembrane Peptide Helices
- Influence of Lipid Saturation, Hydrophobic Length and Cholesterol on Double‐Arginine‐Containing Helical Peptides in Bilayer Membranes
Showing 5 of 18 shared publications
- Ionization Properties of Histidine Residues in the Lipid Bilayer Membrane Environment
- Dynamic regulation of lipid–protein interactions
- Control of Transmembrane Helix Dynamics by Interfacial Tryptophan Residues
- Influence of High pH and Cholesterol on Single Arginine-Containing Transmembrane Peptide Helices
- Influence of Lipid Saturation, Hydrophobic Length and Cholesterol on Double‐Arginine‐Containing Helical Peptides in Bilayer Membranes
Showing 5 of 18 shared publications
- Control of Transmembrane Helix Dynamics by Interfacial Tryptophan Residues
- Influence of Lipid Saturation, Hydrophobic Length and Cholesterol on Double‐Arginine‐Containing Helical Peptides in Bilayer Membranes
- Monitoring the Consequences of Relocating the Tryptophan Anchors on Transmembrane Peptide Dynamics and Alignment
- Interfacial Tryptophan Residues Govern Transmembrane Helix Dynamics
- Influence of High pH and Cholesterol on Single Arginine-Containing Transmembrane Peptide Helices
- Influence of Cholesterol on Single Arginine-Containing Transmembrane Helical Peptides
- Cholesterol Influence on Arginine-Containing Transmembrane Peptides
- Influence of Lipid Saturation, Hydrophobic Length and Cholesterol on Double‐Arginine‐Containing Helical Peptides in Bilayer Membranes
- Response of GWALP23 Transmembrane Peptides to Incorporation of Specific Pairs of Buried Charged Arginine Residues
- Influence of Saturation and Hydrophobic Length of Lipid Bilayers on Twin-Arginine Containing Helical Peptides
- Dynamic regulation of lipid–protein interactions
- Solid-State NMR Investigations of Transmembrane Helix Interactions
- Control of Transmembrane Helix Dynamics by Interfacial Tryptophan Residues
- Interfacial Tryptophan Residues Govern Transmembrane Helix Dynamics
- Control of Transmembrane Helix Dynamics by Interfacial Tryptophan Residues
- Interfacial Tryptophan Residues Govern Transmembrane Helix Dynamics
- Influence of Lipid Saturation, Hydrophobic Length and Cholesterol on Double‐Arginine‐Containing Helical Peptides in Bilayer Membranes
- Examination of pH dependency and orientation differences of membrane spanning alpha helices carrying a single or pair of buried histidine residues
- Influence of a Potentially Destabilizing Central Tryptophan on Transmembrane Helix Domains
- Solid-State NMR Investigations of Transmembrane Helix Interactions