Publications by authors named "S A Landry"

Study Objectives: There is substantial night-to-night variability (NtNV) in obstructive sleep apnea (OSA) severity in some individuals, however predictors for this remain incompletely understood. This study aims to quantify the degree of NtNV in the apnea-hypopnea index (AHI), hypoxic burden, airflow limitation, and OSA endotypes; to determine if a relationship exists between the degree of NtNV in AHI and in endotype expression; to assess whether the degree of flow limited breathing is predictive of the degree of NtNV of the AHI.

Methods: 71 patients with OSA underwent two polysomnograms (PSGs).

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The synthetically evolved pHD family of peptides is known to self-assemble into macromolecule-sized nanopores of 2-10 nm diameter in synthetic lipid bilayers, but only when the pH is below ∼6. Here, we show that a representative family member, pHD108, has the same pH-responsive nanopore-forming activity in the endosomal membranes of living human cells, which is triggered by endosomal acidification. This enables the cytosolic delivery of endocytosed proteins and other macromolecules.

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Rapid Acceleration of Diagnostics-Underserved Populations (RADx-UP) Kansas worked with 10 Kansas counties from November 2020 through June 2022 to form local health equity action teams (LHEATs), develop COVID-19 testing strategies, foster communication about COVID-19, and share best practices through a learning collaborative. Participating counties documented 693 distinct COVID-19 testing and 178 communication activities. Although the intervention was not associated with changes in the proportion of positive COVID-19 tests, LHEATs in the learning collaborative implemented new testing strategies and responded to emerging COVID-19 challenges.

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Phosphorylation of proteins on tyrosine (Tyr) residues evolved in metazoan organisms as a mechanism of coordinating tissue growth. Multicellular eukaryotes typically have more than 50 distinct protein Tyr kinases that catalyse the phosphorylation of thousands of Tyr residues throughout the proteome. How a given Tyr kinase can phosphorylate a specific subset of proteins at unique Tyr sites is only partially understood.

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