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Htet A. Khant

Researcher at Baylor College of Medicine

Publications -  30
Citations -  2384

Htet A. Khant is an academic researcher from Baylor College of Medicine. The author has contributed to research in topics: Zernike polynomials & Vesicle. The author has an hindex of 18, co-authored 25 publications receiving 2242 citations.

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Interbilayer-crosslinked multilamellar vesicles as synthetic vaccines for potent humoral and cellular immune responses

TL;DR: In this article, the authors describe interbilayer-crosslinked multilamellar vesicles formed by crosslinking headgroups of adjacent lipid bilayers within multilevel-vesicles, which can elicit endogenous T-cell and antibody responses comparable to those for the strongest vaccine vectors.
Journal Article

Interbilayer-crosslinked multilamellar vesicles as synthetic vaccines for potent humoral and cellular immune responses

TL;DR: It is found that interbilayer-crosslinked multilamellar vesicles (ICMVs) form an extremely potent whole-protein vaccine, eliciting endogenous T-cell and antibody responses comparable to the strongest vaccine vectors.
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Superparamagnetic gadonanotubes are high-performance MRI contrast agents

TL;DR: This work reports the nanoscale loading and confinement of aquated Gd3+n-ion clusters within ultra-short single-walled carbon nanotubes (US-tubes) that are linear superparamagnetic molecular magnets with Magnetic Resonance Imaging (MRI) efficacies 40 to 90 times larger than any Gd 3+-based contrast agent (CA) in current clinical use.
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Close membrane-membrane proximity induced by Ca(2+)-dependent multivalent binding of synaptotagmin-1 to phospholipids.

TL;DR: It is shown that Ca2+ induces high-affinity simultaneous binding of synaptotagmin to two membranes, bringing them into close proximity and accelerates membrane fusion through the highly positive electrostatic potential of its C2B domain.
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Interprotofilament interactions between Alzheimer's Aβ1–42 peptides in amyloid fibrils revealed by cryoEM

TL;DR: This model of mature Aβ1–42 fibrils is markedly different from previous cryoEM models of A β1–40 fibrILS, and the C terminus of Aβ forms the inside wall of the hollow core, which is supported by partial proteolysis analysis.