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1.
J Grad Med Educ ; 14(4): 431-438, 2022 Aug.
Artículo en Inglés | MEDLINE | ID: mdl-35991103

RESUMEN

Background: The number of for-profit hospitals has increased in the United States, but their role in and outcomes for graduate medical education (GME) are unclear. Objectives: To describe for-profit involvement in internal medicine (IM), general surgery (GS), and pediatrics GME by quantifying change in for-profit affiliated residency programs and comparing for-profit and nonprofit affiliated program board certifying examination pass rates. Methods: We used Accreditation Council for Graduate Medical Education and Medicare data to quantify for-profit prevalence in IM, GS, and pediatrics GME from 2001 to 2021. We used public pass rate data from the American Board of Surgeons (2017-2019; n=242 programs; 6562 examinees), American Board of Internal Medicine (2018-2020; n=465 programs; 23 922 examinees), and American Board of Pediatrics (2018-2020; n=202 programs; 9819 examinees) to model the relationship between profit status and pass rate within each specialty and across specialties combined using linear regression. Results: The proportion of for-profit affiliated residency programs increased 400.0% in IM, 334.4% in GS, and 23.2% in pediatrics from 2001 to 2021. Bivariate linear regression revealed significantly lower pass rate in for-profit affiliated programs in IM ß =-7.73, P<.001), pediatrics (ß =-14.6, P<.001), and the 3 specialties combined (ß =-5.45, P<.001). Upon multiple regression with addition of program characteristic covariates, this relationship remained significant in pediatrics (ß =-10.04, P=.006). Conclusions: The proportion of for-profit affiliated residency programs has increased in IM, GS, and pediatrics from 2001 to 2021. After controlling for covariates, for-profit affiliated programs were associated with lower board examination pass rates in pediatrics with no association in IM, GS, or the combined measure.


Asunto(s)
Internado y Residencia , Acreditación , Anciano , Niño , Educación de Postgrado en Medicina , Humanos , Medicina Interna/educación , Medicare , Estados Unidos
2.
PLoS One ; 16(3): e0241738, 2021.
Artículo en Inglés | MEDLINE | ID: mdl-33760815

RESUMEN

Naegleria fowleri is a pathogenic, thermophilic, free-living amoeba which causes primary amebic meningoencephalitis (PAM). Penetrating the olfactory mucosa, the brain-eating amoeba travels along the olfactory nerves, burrowing through the cribriform plate to its destination: the brain's frontal lobes. The amoeba thrives in warm, freshwater environments, with peak infection rates in the summer months and has a mortality rate of approximately 97%. A major contributor to the pathogen's high mortality is the lack of sensitivity of N. fowleri to current drug therapies, even in the face of combination-drug therapy. To enable rational drug discovery and design efforts we have pursued protein production and crystallography-based structure determination efforts for likely drug targets from N. fowleri. The genes were selected if they had homology to drug targets listed in Drug Bank or were nominated by primary investigators engaged in N. fowleri research. In 2017, 178 N. fowleri protein targets were queued to the Seattle Structural Genomics Center of Infectious Disease (SSGCID) pipeline, and to date 89 soluble recombinant proteins and 19 unique target structures have been produced. Many of the new protein structures are potential drug targets and contain structural differences compared to their human homologs, which could allow for the development of pathogen-specific inhibitors. Five of the structures were analyzed in more detail, and four of five show promise that selective inhibitors of the active site could be found. The 19 solved crystal structures build a foundation for future work in combating this devastating disease by encouraging further investigation to stimulate drug discovery for this neglected pathogen.


Asunto(s)
Descubrimiento de Drogas , Naegleria fowleri/metabolismo , Proteínas Protozoarias/antagonistas & inhibidores , Adenosilhomocisteinasa/antagonistas & inhibidores , Adenosilhomocisteinasa/química , Adenosilhomocisteinasa/metabolismo , Sitios de Unión , Inhibidores Enzimáticos/química , Inhibidores Enzimáticos/metabolismo , Simulación de Dinámica Molecular , Naegleria fowleri/genética , Fosfoglicerato Mutasa/antagonistas & inhibidores , Fosfoglicerato Mutasa/química , Fosfoglicerato Mutasa/metabolismo , Estructura Cuaternaria de Proteína , Proteína-Arginina N-Metiltransferasas/antagonistas & inhibidores , Proteína-Arginina N-Metiltransferasas/química , Proteína-Arginina N-Metiltransferasas/metabolismo , Proteoma , Proteínas Protozoarias/química , Proteínas Protozoarias/metabolismo
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