Natalie Kegulian

Natalie Kegulian
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Natalie verified their affiliation via an institutional email.
Verified
Natalie verified their affiliation via an institutional email.
University of Southern California | USC · Center for Craniofacial Molecular Biology

PhD
Researching, communicating, and writing science every day with an emphasis on protein molecular structure

About

14
Publications
4,129
Reads
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278
Citations
Additional affiliations
October 2015 - June 2017
University of Southern California
Position
  • PostDoc Position
August 2017 - April 2018
University of Southern California
Position
  • PostDoc Position
November 2018 - November 2024
University of Southern California
Position
  • Research Associate

Publications

Publications (14)
Article
Full-text available
The enamel matrix protein Ameloblastin (Ambn) has critical physiological functions, including regulation of mineral formation, cell differentiation, and cell–matrix adhesion. We investigated localized structural changes in Ambn during its interactions with its targets. We performed biophysical assays and used liposomes as a cell membrane model. The...
Article
Full-text available
Objective: ApoC-III (apolipoprotein C-III) glycosylation can predict cardiovascular disease risk. Higher abundance of disialylated (apoC-III2) over monosialylated (apoC-III1) glycoforms is associated with lower plasma triglyceride levels. Yet, it remains unclear whether apoC-III glycosylation impacts TRL (triglyceride-rich lipoprotein) clearance a...
Article
Full-text available
Ameloblastin (Ambn), the most abundant non-amelogenin enamel protein, is intrinsically disordered and has the potential to interact with other enamel proteins and with cell membranes. Here, through multiple biophysical methods, we investigated the interactions between Ambn and large unilamellar vesicles (LUVs), whose lipid compositions mimicked cel...
Article
Full-text available
Expansion of the polyglutamine (polyQ) tract in exon 1 of the huntingtin protein (Httex1) leads to Huntington's disease resulting in fatal neurodegeneration. However, it remains poorly understood how polyQ expansions alter protein structure and cause toxicity. Using circular dichroism, electron paramagnetic resonance, and NMR spectroscopy, we found...
Article
Background: We previously reported an association between higher abundance of disialylated (apoC-III 2 ) over monosialylated (apoC-III 1 ) apoC-III and lower plasma triglyceride (TG) concentrations in three independent studies. Methods: The goal of this study was to get mechanistic insights in the metabolism of apoC-III 1 and apoC-III 2 . First, th...
Article
Full-text available
Expansion of the polyglutamine (polyQ) region in the first exon of huntingtin (htt) is the root of Huntington's disease (HD). Misfolding and aggregation have long been observed to a greater extent in polyQ-expanded htt, but studies have also uncovered many implications of polyQ expansion in alterations to the dynamics and intermolecular interaction...
Article
Full-text available
Islet amyloid polypeptide (IAPP) is a 37-amino-acid amyloid protein intimately associated with pancreatic islet β-cell dysfunction and death in type II diabetes. In this study, we combine spectroscopic methods and microscopy to investigate α-helical IAPP-membrane interactions. Using light scattering and fluorescence microscopy we observe that large...
Article
Full-text available
BACKGROUND In Huntington's disease, expansion of a CAG triplet repeat occurs in exon 1 of the huntingtin gene (HTT), resulting in a protein bearing>35 polyglutamine residues whose N-terminal fragments display a high propensity to misfold and aggregate. Recent data demonstrate that polyglutamine expansion results in conformational changes in the hun...
Article
Full-text available
Background: In Huntington's disease, expansion of a CAG triplet repeat occurs in exon 1 of the huntingtin gene (HTT), resulting in a protein bearing>35 polyglutamine residues whose N-terminal fragments display a high propensity to misfold and aggregate. Recent data demonstrate that polyglutamine expansion results in conformational changes in the h...
Article
Full-text available
α-Synuclein (αS) is a protein with multiple conformations and interactions. Natively unfolded in solution, αS accumulates as amyloid in neurological tissue in Parkinson disease and interacts with membranes under both physiological and pathological conditions. Here, we used cryoelectron microscopy in conjunction with electron paramagnetic resonance...

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