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1.
AEM Educ Train ; 5(4): e10698, 2021 Aug.
Artigo em Inglês | MEDLINE | ID: mdl-34859168

RESUMO

BACKGROUND: The Accreditation Council for Graduate Medical Education (ACGME) emphasizes constructive feedback as a critical component of residency training. Despite over a decade of using competency-based milestone evaluations, emergency medicine (EM) residency programs lack a standardized method for assessing the quality of feedback. We developed two novel EM-specific feedback surveys to assess the quality of feedback in the ER (FEED-ER) from both the resident and the faculty perspectives. This study aimed to evaluate the surveys' psychometric properties. METHODS: We developed FEED-ER using a Likert scale with faculty and resident versions based on the ACGME framework and a literature review. The preliminary survey consisted of 25 questions involving the feedback domains of timeliness, respect/communication, specificity, action plan, and feedback culture. We conducted two modified Delphi rounds involving 17 content experts to ensure respondent understanding of the items, item coherence to corresponding feedback domains, thematic saturation of domain content, and time duration. A multicenter study was conducted at five university-based EDs in the United States and one in Thailand in 2019. We evaluated the descriptive statistics of the frequency of responses, validity evidence, and reliability of FEED-ER. RESULTS: A total of 147 EM faculty and 126 EM residents completed the survey. Internal consistency was adequate (Cronbach's alpha > 0.70) and test-retest reliability showed adequate temporal stability (ICC > 0.80) for all dimensions. Content validity was deemed acceptable (CVC > 0.80) for all items. From the 25 items of FEED-ER, 23 loaded into the originally theorized dimensions (with factor loadings > 0.50). Additionally, the five feedback domains were found to be statistically distinct, with correlations between 0.40 and 0.60. The final survey has 23 items. CONCLUSIONS: This is the first study to develop and provide validity evidence for an EM-specific feedback tool that has strong psychometric properties, is reproducible and reliable, and provides an objective measure for assessing the quality of feedback in the ED.

2.
PLoS One ; 6(4): e18413, 2011 Apr 19.
Artigo em Inglês | MEDLINE | ID: mdl-21526164

RESUMO

BACKGROUND: Cyclic GMP-dependent protein kinases (PKGs) are central mediators of the NO-cGMP signaling pathway and phosphorylate downstream substrates that are crucial for regulating smooth muscle tone, platelet activation, nociception and memory formation. As one of the main receptors for cGMP, PKGs mediate most of the effects of cGMP elevating drugs, such as nitric oxide-releasing agents and phosphodiesterase inhibitors which are used for the treatment of angina pectoris and erectile dysfunction, respectively. METHODOLOGY/PRINCIPAL FINDINGS: We have investigated the mechanism of cyclic nucleotide binding to PKG by determining crystal structures of the amino-terminal cyclic nucleotide-binding domain (CNBD-A) of human PKG I bound to either cGMP or cAMP. We also determined the structure of CNBD-A in the absence of bound nucleotide. The crystal structures of CNBD-A with bound cAMP or cGMP reveal that cAMP binds in either syn or anti configurations whereas cGMP binds only in a syn configuration, with a conserved threonine residue anchoring both cyclic phosphate and guanine moieties. The structure of CNBD-A in the absence of bound cyclic nucleotide was similar to that of the cyclic nucleotide bound structures. Surprisingly, isothermal titration calorimetry experiments demonstrated that CNBD-A binds both cGMP and cAMP with a relatively high affinity, showing an approximately two-fold preference for cGMP. CONCLUSIONS/SIGNIFICANCE: Our findings suggest that CNBD-A binds cGMP in the syn conformation through its interaction with Thr193 and an unusual cis-peptide forming residues Leu172 and Cys173. Although these studies provide the first structural insights into cyclic nucleotide binding to PKG, our ITC results show only a two-fold preference for cGMP, indicating that other domains are required for the previously reported cyclic nucleotide selectivity.


Assuntos
AMP Cíclico/química , Proteínas Quinases Dependentes de GMP Cíclico/química , GMP Cíclico/química , Modelos Moleculares , Sequência de Aminoácidos , Apoproteínas/química , Sítios de Ligação , Calorimetria , Cristalografia por Raios X , Subunidade RIalfa da Proteína Quinase Dependente de AMP Cíclico/química , Proteína Quinase Dependente de GMP Cíclico Tipo I , Humanos , Ligantes , Dados de Sequência Molecular , Ligação Proteica , Estrutura Secundária de Proteína , Estrutura Terciária de Proteína , Homologia Estrutural de Proteína
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