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1.
Arch Intern Med ; 168(1): 40-6, 2008 Jan 14.
Artículo en Inglés | MEDLINE | ID: mdl-18195194

RESUMEN

BACKGROUND: Collecting data on medical errors is essential for improving patient safety, but factors affecting error reporting by physicians are poorly understood. METHODS: Survey of faculty and resident physicians in the midwest, mid-Atlantic, and northeast regions of the United States to investigate reporting of actual errors, likelihood of reporting hypothetical errors, attitudes toward reporting errors, and demographic factors. RESULTS: Responses were received from 338 participants (response rate, 74.0%). Most respondents agreed that reporting errors improves the quality of care for future patients (84.3%) and would likely report a hypothetical error resulting in minor (73%) or major (92%) harm to a patient. However, only 17.8% of respondents had reported an actual minor error (resulting in prolonged treatment or discomfort), and only 3.8% had reported an actual major error (resulting in disability or death). Moreover, 16.9% acknowledged not reporting an actual minor error, and 3.8% acknowledged not reporting an actual major error. Only 54.8% of respondents knew how to report errors, and only 39.5% knew what kind of errors to report. Multivariate analyses of answers to hypothetical vignettes showed that willingness to report was positively associated with believing that reporting improves the quality of care, knowing how to report errors, believing in forgiveness, and being a faculty physician (vs a resident). CONCLUSION: Most faculty and resident physicians are inclined to report harm-causing hypothetical errors, but only a minority have actually reported an error.


Asunto(s)
Errores Médicos , Calidad de la Atención de Salud , Gestión de Riesgos , Seguridad , Actitud del Personal de Salud , Docentes Médicos , Femenino , Encuestas de Atención de la Salud , Hospitales de Enseñanza , Humanos , Internado y Residencia , Masculino , Médicos , Encuestas y Cuestionarios , Revelación de la Verdad
2.
J Am Chem Soc ; 130(38): 12620-1, 2008 Sep 24.
Artículo en Inglés | MEDLINE | ID: mdl-18761447

RESUMEN

Combined magnetic and fluorescence cell sorting were used to select Fluorogen Activating Proteins (FAPs) from a yeast surface-displayed library for binding to the fluorogenic cyanine dye Dimethyl Indole Red (DIR). Several FAPs were selected that bind to the dye with low nanomolar Kd values and enhance fluorescence more than 100-fold. One of these FAPs also exhibits considerable promiscuity, binding with high affinity to several other fluorogenic cyanine dyes with emission wavelengths covering most of the visible and near-IR regions of the spectrum. This significantly expands the number and wavelength range of scFv-based fluoromodules.


Asunto(s)
Carbocianinas/química , Colorantes Fluorescentes/química , Fragmentos de Inmunoglobulinas/química , Región Variable de Inmunoglobulina/química , Carbocianinas/metabolismo , Colorantes/química , Colorantes/metabolismo , Citometría de Flujo/métodos , Colorantes Fluorescentes/metabolismo , Proteínas Fúngicas/química , Fragmentos de Inmunoglobulinas/metabolismo , Región Variable de Inmunoglobulina/metabolismo , Microscopía Fluorescente/métodos , Biblioteca de Péptidos , Unión Proteica , Espectrometría de Fluorescencia , Espectrofotometría Infrarroja , Levaduras/química
3.
J Gen Intern Med ; 22(7): 988-96, 2007 Jul.
Artículo en Inglés | MEDLINE | ID: mdl-17473944

RESUMEN

BACKGROUND: Disclosing errors to patients is an important part of patient care, but the prevalence of disclosure, and factors affecting it, are poorly understood. OBJECTIVE: To survey physicians and trainees about their practices and attitudes regarding error disclosure to patients. DESIGN AND PARTICIPANTS: Survey of faculty physicians, resident physicians, and medical students in Midwest, Mid-Atlantic, and Northeast regions of the United States. MEASUREMENTS: Actual error disclosure; hypothetical error disclosure; attitudes toward disclosure; demographic factors. RESULTS: Responses were received from 538 participants (response rate = 77%). Almost all faculty and residents responded that they would disclose a hypothetical error resulting in minor (97%) or major (93%) harm to a patient. However, only 41% of faculty and residents had disclosed an actual minor error (resulting in prolonged treatment or discomfort), and only 5% had disclosed an actual major error (resulting in disability or death). Moreover, 19% acknowledged not disclosing an actual minor error and 4% acknowledged not disclosing an actual major error. Experience with malpractice litigation was not associated with less actual or hypothetical error disclosure. Faculty were more likely than residents and students to disclose a hypothetical error and less concerned about possible negative consequences of disclosure. Several attitudes were associated with greater likelihood of hypothetical disclosure, including the belief that disclosure is right even if it comes at a significant personal cost. CONCLUSIONS: There appears to be a gap between physicians' attitudes and practices regarding error disclosure. Willingness to disclose errors was associated with higher training level and a variety of patient-centered attitudes, and it was not lessened by previous exposure to malpractice litigation.


Asunto(s)
Revelación/ética , Docentes Médicos , Internado y Residencia , Errores Médicos/psicología , Relaciones Médico-Paciente/ética , Práctica Profesional/ética , Estudiantes de Medicina , Competencia Clínica , Femenino , Encuestas de Atención de la Salud , Humanos , Masculino , Mala Praxis , Errores Médicos/ética , Estados Unidos
4.
Mol Biol Cell ; 15(6): 2593-605, 2004 Jun.
Artículo en Inglés | MEDLINE | ID: mdl-15047864

RESUMEN

The Sec1/Munc18 (SM) family of proteins is thought to impart compartmental specificity to vesicle fusion reactions. Here we report characterization of Vps33p, an SM family member previously thought to act exclusively at the vacuolar membrane with the vacuolar syntaxin Vam3p. Vacuolar morphology of vps33Delta cells resembles that of cells lacking both Vam3p and the endosomal syntaxin Pep12p, suggesting that Vps33p may function with these syntaxins at the vacuole and the endosome. Consistent with this, vps33 mutants secrete the Golgi precursor form of the vacuolar hydrolase CPY into the medium. We also demonstrate that Vps33p acts at other steps, for vps33 mutants show severe defects in endocytosis at the late endosome. At the endosome, Vps33p and other class C members exist as a complex with Vps8p, a protein previously known to act in transport between the late Golgi and the endosome. Vps33p also interacts with Pep12p, a known interactor of the SM protein Vps45p. High copy PEP7/VAC1 suppresses vacuolar morphology defects of vps33 mutants. These findings demonstrate that Vps33p functions at multiple trafficking steps and is not limited to action at the vacuolar membrane. This is the first report demonstrating the involvement of a single syntaxin with two SM proteins at the same organelle.


Asunto(s)
Endosomas/metabolismo , Proteínas del Tejido Nervioso/química , Proteínas de Saccharomyces cerevisiae/metabolismo , Saccharomyces cerevisiae/citología , Saccharomyces cerevisiae/metabolismo , Vacuolas/metabolismo , Proteínas de Transporte Vesicular/química , Proteínas de Transporte Vesicular/metabolismo , Proteínas Adaptadoras Transductoras de Señales , Catepsina A/metabolismo , Proteínas del Citoesqueleto/metabolismo , Endocitosis , Eliminación de Gen , Glicosilación , Aparato de Golgi/metabolismo , Factor de Apareamiento , Proteínas de la Membrana/deficiencia , Proteínas de la Membrana/genética , Proteínas de la Membrana/metabolismo , Complejos Multiproteicos , Proteínas Munc18 , Péptidos/metabolismo , Unión Proteica , Precursores de Proteínas/metabolismo , Proteínas Qa-SNARE , Saccharomyces cerevisiae/genética , Saccharomyces cerevisiae/ultraestructura , Proteínas de Saccharomyces cerevisiae/química , Proteínas de Saccharomyces cerevisiae/genética , Vacuolas/ultraestructura , Proteínas de Transporte Vesicular/deficiencia , Proteínas de Transporte Vesicular/genética
5.
J Gen Intern Med ; 21(9): 942-8, 2006 Sep.
Artículo en Inglés | MEDLINE | ID: mdl-16918739

RESUMEN

BACKGROUND: Physician disclosure of medical errors to institutions, patients, and colleagues is important for patient safety, patient care, and professional education. However, the variables that may facilitate or impede disclosure are diverse and lack conceptual organization. OBJECTIVE: To develop an empirically derived, comprehensive taxonomy of factors that affects voluntary disclosure of errors by physicians. DESIGN: A mixed-methods study using qualitative data collection (structured literature search and exploratory focus groups), quantitative data transformation (sorting and hierarchical cluster analysis), and validation procedures (confirmatory focus groups and expert review). RESULTS: Full-text review of 316 articles identified 91 impeding or facilitating factors affecting physicians' willingness to disclose errors. Exploratory focus groups identified an additional 27 factors. Sorting and hierarchical cluster analysis organized factors into 8 domains. Confirmatory focus groups and expert review relocated 6 factors, removed 2 factors, and modified 4 domain names. The final taxonomy contained 4 domains of facilitating factors (responsibility to patient, responsibility to self, responsibility to profession, responsibility to community), and 4 domains of impeding factors (attitudinal barriers, uncertainties, helplessness, fears and anxieties). CONCLUSIONS: A taxonomy of facilitating and impeding factors provides a conceptual framework for a complex field of variables that affects physicians' willingness to disclose errors to institutions, patients, and colleagues. This taxonomy can be used to guide the design of studies to measure the impact of different factors on disclosure, to assist in the design of error-reporting systems, and to inform educational interventions to promote the disclosure of errors to patients.


Asunto(s)
Actitud del Personal de Salud , Errores Médicos/psicología , Médicos/psicología , Revelación de la Verdad , Análisis por Conglomerados , Ética Médica , Grupos Focales , Humanos , Errores Médicos/ética , Investigación Cualitativa , Responsabilidad Social , Estados Unidos
6.
Jt Comm J Qual Patient Saf ; 32(4): 188-98, 2006 Apr.
Artículo en Inglés | MEDLINE | ID: mdl-16649649

RESUMEN

BACKGROUND: It is important for physicians to disclose medical errors to institutions (for patient safety), to colleagues (for professional learning), and to patients (as part of direct patient care), but no comprehensive review of factors that may facilitate or impede disclosure has been undertaken. METHODS: A MEDLINE search was conducted of English-language articles published from 1975-2004, with review of bibliographies. A total of 5,509 articles were reviewed by title, 881 articles were retrieved for full text review, and 475 articles satisfied the inclusion criteria. Article content was assessed by identifying factors that facilitate or impede disclosure and classifying each article's primary goal of disclosure. RESULTS: Thirty-five factors believed to facilitate disclosure were identified (for example, accountability, honesty, restitution), as were 41 factors believed to impede it (for example, professional repercussions, legal liability, blame). The three most common goals of disclosure were to improve patient safety, enhance learning, and inform patients. Facilitating factors were more commonly cited when the goal of disclosure was to inform patients. DISCUSSION: A wide range of factors are capable of facilitating or impeding the disclosure of medical errors. Innovations to enhance error disclosure should address both sides of the equation: impeding factors should be removed and facilitating factors should be promoted.


Asunto(s)
Errores Médicos , Médicos/psicología , Revelación de la Verdad , Barreras de Comunicación , Humanos , Estados Unidos
7.
Open Nutr J ; 10: 1-12, 2016.
Artículo en Inglés | MEDLINE | ID: mdl-28090221

RESUMEN

BACKGROUND: Research findings have suggested that exposure to environmental pollutants contributes to increased health risks, which may be modulated by certain nutrition and other protective health behaviors. Nutrition professionals play an important role in effectively disseminating this information and in devising specific community-based nutrition education programs for audiences located in areas with environmental health issues. OBJECTIVE: To assess awareness of environmental health problems and motivation to adopt protective health behaviors for use in planning nutrition education programs for communities exposed to environmental pollutants. METHOD: Data were collected from a modified, validated Environmental Health Engagement Profile (EHEP) survey instrument administered to adults (n=774) participating in community events in Kentucky based on location relative to hazardous waste sites. RESULTS: The modified EHEP survey instrument showed good internal consistency reliability, and demographic characteristics were evaluated. Correlation analyses revealed significant positive correlations in all groups, separately and combined, between awareness of environmental pollution in an individual's surroundings and the extent of concern that pollutants cause adverse health effects (P < 0.01) and between concern that pollutants cause adverse health effects and taking personal actions to protect against such environmental insults (P < 0.01). The groups having the highest level of awareness posed by pollution are those residing near federally designated hazardous waste sites. CONCLUSION: These results suggest that determining and expanding an audience's knowledge and perceptions of environmental health risks will enhance effective nutrition education program planning.

8.
Genetics ; 162(1): 29-43, 2002 Sep.
Artículo en Inglés | MEDLINE | ID: mdl-12242221

RESUMEN

INO1, encoding inositol 1-phosphate synthase, is the most highly regulated of a class of genes containing the repeated element, UAS(INO), in their promoters. Transcription of UAS(INO)-containing genes is modulated by the availability of exogenous inositol and by signals generated by alteration of phospholipid metabolism. The unfolded protein response (UPR) pathway also is involved in INO1 expression and the ire1Delta and hac1Delta mutants are inositol auxotrophs. We examined the role of the UPR in transmitting a signal generated in response to inositol deprivation and to alteration of phospholipid biosynthesis created in the sec14(ts) cki1Delta genetic background. We report that the UPR is required for sustained high-level INO1 expression in wild-type strains, but not for transient derepression in response to inositol deprivation. Moreover, the UPR is not required for expression or regulation of INO1 in response to the change in lipid metabolism that occurs in the sec14(ts) cki1Delta genetic background. Thus, the UPR signal transduction pathway is not involved directly in transcriptional regulation of INO1 and other UAS(INO)-containing genes. However, we discovered that inactivation of Sec14p leads to activation of the UPR, and that sec14 cki1 strains exhibit defective vacuolar morphology, suggesting that the mechanism by which the cki1Delta mutation suppresses the growth and secretory defect of sec14 does not fully restore wild-type morphology. Finally, synthetic lethality involving sec14 and UPR mutations suggests that the UPR plays an essential role in survival of sec14 cki1 strains.


Asunto(s)
Proteínas Portadoras/metabolismo , Proteínas de la Membrana/metabolismo , Proteínas de Saccharomyces cerevisiae , Saccharomyces cerevisiae/metabolismo , Proteínas Portadoras/genética , Genes Fúngicos , Genes Letales , Inositol/metabolismo , Proteínas de la Membrana/genética , Mutación , Proteínas de Transferencia de Fosfolípidos , Desnaturalización Proteica , Saccharomyces cerevisiae/genética , beta-Galactosidasa/genética
12.
Yeast ; 25(1): 41-6, 2008 Jan.
Artículo en Inglés | MEDLINE | ID: mdl-17924454

RESUMEN

5-Fluoroanthranilic acid (FAA)-resistant mutants were selected in homothallic diploids of three Saccharomyces species, taking care to isolate mutants of independent origin. Mutations were assigned to complementation groups by interspecific complementation with S. cerevisiae tester strains. In all three species, trp3, trp4 and trp5 mutants were recovered. trp1 mutants were also recovered if the selection was imposed on a haploid strain. Thus, FAA selection may be more generally applicable than was previously described.


Asunto(s)
Mutación , Saccharomyces/genética , Triptófano/genética , ortoaminobenzoatos/farmacología , Isomerasas Aldosa-Cetosa/genética , Isomerasas Aldosa-Cetosa/metabolismo , Antranilato Sintasa/genética , Antranilato Sintasa/metabolismo , Proteínas Fúngicas/genética , Prueba de Complementación Genética , Indol-3-Glicerolfosfato Sintasa/genética , Indol-3-Glicerolfosfato Sintasa/metabolismo , Saccharomyces/efectos de los fármacos , Saccharomyces/aislamiento & purificación , Saccharomyces/metabolismo , Triptófano/metabolismo , ortoaminobenzoatos/metabolismo
13.
Proc Natl Acad Sci U S A ; 103(4): 939-44, 2006 Jan 24.
Artículo en Inglés | MEDLINE | ID: mdl-16418276

RESUMEN

PBN1 was identified as a gene required for production of protease B (PrB) activity in Saccharomyces cerevisiae. PBN1 encodes an endoplasmic reticulum (ER)-localized, type I membrane glycoprotein and is essential for cell viability. To study the essential function(s) of Pbn1p, we constructed a strain with PBN1 under control of the GAL promoter. Depletion of Pbn1p in this strain abrogates processing of the ER precursor forms of PrB, Gas1p, and Pho8p. Depletion of Pbn1p does not affect exit of proprotease A or procarboxypeptidase Y from the ER, indicating that Pbn1p is not required for global exit from the ER. Depleting Pbn1p leads to a significant increase in the unfolded protein response pathway, accompanied by an expansion of bulk ER membrane, indicating that there is a defect in protein folding in the ER. pbn1-1, a nonlethal allele of PBN1, displays synthetic lethality with the ero1-1 allele (ERO1 is required for oxidation in the ER) and synthetic growth defects with the cne1Delta allele (CNE1 encodes calnexin). ER-associated degradation of a lumenal substrate, CPY*, is blocked in the absence of Pbn1p. These results suggest that Pbn1p is required for proper folding and/or the stability of a subset of proteins in the ER. Thus, Pbn1p is an essential chaperone-like protein in the ER of yeast.


Asunto(s)
Retículo Endoplásmico/metabolismo , Glicoproteínas de Membrana/fisiología , Proteínas de Saccharomyces cerevisiae/fisiología , Saccharomyces cerevisiae/metabolismo , Alelos , Calnexina , Catepsina A/metabolismo , Membrana Celular/metabolismo , Galactosa/farmacología , Genoma Fúngico , Glucosa/metabolismo , Glucosa/farmacología , Glicoproteínas/química , Glicoproteínas/metabolismo , Glicoproteínas de Membrana/metabolismo , Proteínas de la Membrana/metabolismo , Chaperonas Moleculares , Oxidorreductasas actuantes sobre Donantes de Grupos Sulfuro , Regiones Promotoras Genéticas , Desnaturalización Proteica , Proteínas de Saccharomyces cerevisiae/metabolismo , Serina Endopeptidasas/metabolismo , Factores de Tiempo
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