RESUMO
ABSTRACT: Institutions of higher learning offer flexible online master of science in nursing education (MSN NE) programs to increase the number of available nursing faculty. Such programs are a viable option to degree completion; however, online programs create challenges that impact student success. This qualitative pilot study describes challenges experienced by seven enrolled or recently graduated MSN NE students. Technology, scheduling, group behaviors, faculty, curricula, and personal barriers emerged as themes. The results underscore the need to create an effective community of inquiry that fosters an environment online to promote student success.
Assuntos
Educação a Distância , Estudantes de Enfermagem , Docentes de Enfermagem , Humanos , Projetos Piloto , Pesquisa QualitativaRESUMO
ABSTRACT: Nurse educators require information literacy (IL) to use evidence-based practices to design, develop, deliver, and evaluate education; to participate in research and scholarship of teaching and learning; and to disseminate new practices and evidence to the nursing education community. A needs assessment of students and faculty revealed knowledge deficits with IL for master of science in nursing-nurse educator students. A multidisciplinary team, guided by relevant theories, created an online applied learning and reflective tutorial to address the identified needs. Evaluation of students' participation indicated the tutorial served as an engaging resource and provided foundational knowledge of IL skills.
Assuntos
Educação a Distância , Educação em Enfermagem , Estudantes de Enfermagem , Docentes de Enfermagem , Humanos , Competência em InformaçãoRESUMO
Hypertrophic cardiomyopathy (HCM) and dilated cardiomyopathy (DCM) are the most common hereditary cardiac conditions. Both are frequent causes of sudden death and are often associated with an adverse disease course. Alpha-cardiac actin is one of the disease genes where different missense mutations have been found to cause either HCM or DCM. We have tested the hypothesis that the protein-folding pathway plays a role in disease development for two actin variants associated with DCM and six associated with HCM. Based on a cell-free coupled translation assay the actin variants could be graded by their tendency to associate with the chaperonin TCP-1 ring complex/chaperonin containing TCP-1 (TRiC/CCT) as well as their propensity to acquire their native conformation. Some variant proteins are completely stalled in a complex with TRiC and fail to fold into mature globular actin and some appear to fold as efficiently as the wild-type protein. A fraction of the translated polypeptide became ubiquitinated and detergent insoluble. Variant actin proteins overexpressed in mammalian cell lines fail to incorporate into actin filaments in a manner correlating with the degree of misfolding observed in the cell-free assay; ranging from incorporation comparable to wild-type actin to little or no incorporation. We propose that effects of mutations on folding and fiber assembly may play a role in the molecular disease mechanism.
Assuntos
Actinas/química , Actinas/metabolismo , Cardiomiopatia Dilatada/metabolismo , Cardiomiopatia Hipertrófica/metabolismo , Mutação/genética , Dobramento de Proteína , Citoesqueleto de Actina/química , Citoesqueleto de Actina/metabolismo , Actinas/genética , Animais , Cardiomiopatia Dilatada/genética , Cardiomiopatia Hipertrófica/genética , Linhagem Celular , Chaperoninas/química , Chaperoninas/metabolismo , Humanos , Cinética , Modelos Moleculares , Complexos Multiproteicos/química , Complexos Multiproteicos/metabolismo , Solubilidade , Ubiquitina/metabolismoRESUMO
The mechanisms by which molecular chaperones assist quality control of cytosolic proteins are poorly understood. Analysis of the chaperone requirements for degradation of misfolded variants of a cytosolic protein, the VHL tumor suppressor, reveals that distinct chaperone pathways mediate its folding and quality control. While both folding and degradation of VHL require Hsp70, the chaperonin TRiC is essential for folding but is dispensable for degradation. Conversely, the chaperone Hsp90 neither participates in VHL folding nor is required to maintain misfolded VHL solubility but is essential for its degradation. The cochaperone HOP/Sti1p also participates in VHL quality control and may direct the triage decision by bridging the Hsp70-Hsp90 interaction. Our finding that a distinct chaperone complex is uniquely required for quality control provides evidence for active and specific chaperone participation in triage decisions and suggests that a hierarchy of chaperone interactions can control the alternate fates of a cytosolic protein.