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1.
J Nurs Meas ; 30(3): 508-517, 2022 09 01.
Artigo em Inglês | MEDLINE | ID: mdl-36127151

RESUMO

Background and Purpose: To psychometrically evaluate a new investigator-developed 14-item Addiction Self-Efficacy Scale (ASES). Methods: One hundred seventy-one subjects (114 male and 57 female) were recruited from an in-house rehabilitation program. Subjects were given the 14-item ASES between days 25 and 30 of the treatment program. Results: The item means ranged from 7.19 to 9.34. There was a ceiling effect on all 14 items. The ASES was found to be multidimensional with two factors accounting for 64% of the total variance explained. Reliability of subscale 1 with nine items was .92 whereas, subscale 2 with five items had a reliability of .86. Conclusions: The ASES has evidence of reliability, face validity, and content validity.


Assuntos
Autoeficácia , Feminino , Humanos , Masculino , Psicometria , Reprodutibilidade dos Testes
2.
J Pediatr Health Care ; 36(2): 170-173, 2022.
Artigo em Inglês | MEDLINE | ID: mdl-34961629

RESUMO

Abdominal pain in the context of fever, tachypnea, or cough is a known presentation of pneumonia in preschool-aged children. We describe a 4-year-old male who presented to a pediatric emergency department with abdominal pain and decreased appetite. During his abdominal pain workup, he was found to have pneumonia complicated by pleural effusion and pneumothorax. It is critical for pediatric providers to be aware of age-based differentials.


Assuntos
Derrame Pleural , Pneumonia , Dor Abdominal/etiologia , Criança , Pré-Escolar , Serviço Hospitalar de Emergência , Febre/etiologia , Humanos , Masculino , Derrame Pleural/diagnóstico , Derrame Pleural/etiologia , Pneumonia/complicações , Pneumonia/diagnóstico
3.
Hosp Top ; 99(1): 44-47, 2021.
Artigo em Inglês | MEDLINE | ID: mdl-33357127

RESUMO

Pediatric Hospital Medicine (PHM) is a growing subspecialty with a broad scope. The Covid-19 pandemic demands flexible staffing models. Advanced practice providers (APPs) can be a valuable addition to hospital medicine teams, although there is no established training program for APPs within PHM. The authors' purpose is to describe how one institution rapidly established a PHM APP team by collaborating with experienced APPs working in other areas of the hospital. This APP team cared for 16% of the average daily census during the pilot period with no significant difference in length of stay compared to traditional teams.


Assuntos
Prática Avançada de Enfermagem/estatística & dados numéricos , Hospitais Pediátricos/tendências , Prática Avançada de Enfermagem/tendências , COVID-19/enfermagem , Hospitais Pediátricos/organização & administração , Hospitais Pediátricos/estatística & dados numéricos , Humanos , Pandemias/prevenção & controle , Pandemias/estatística & dados numéricos , Equipe de Assistência ao Paciente , Projetos Piloto , Capacidade de Resposta ante Emergências/normas , Capacidade de Resposta ante Emergências/estatística & dados numéricos
4.
Mol Biol Cell ; 29(3): 285-294, 2018 02 01.
Artigo em Inglês | MEDLINE | ID: mdl-29187574

RESUMO

XMAP215/Dis1 family proteins are potent microtubule polymerases, critical for mitotic spindle structure and dynamics. While microtubule polymerase activity is driven by an N-terminal tumor overexpressed gene (TOG) domain array, proper cellular localization is a requisite for full activity and is mediated by a C-terminal domain. Structural insight into the C-terminal domain's architecture and localization mechanism remain outstanding. We present the crystal structure of the Saccharomyces cerevisiae Stu2 C-terminal domain, revealing a 15-nm parallel homodimeric coiled coil. The parallel architecture of the coiled coil has mechanistic implications for the arrangement of the homodimer's N-terminal TOG domains during microtubule polymerization. The coiled coil has two spatially distinct conserved regions: CRI and CRII. Mutations in CRI and CRII perturb the distribution and localization of Stu2 along the mitotic spindle and yield defects in spindle morphology including increased frequencies of mispositioned and fragmented spindles. Collectively, these data highlight roles for the Stu2 dimerization domain as a scaffold for factor binding that optimally positions Stu2 on the mitotic spindle to promote proper spindle structure and dynamics.


Assuntos
Cinetocoros/fisiologia , Proteínas Associadas aos Microtúbulos/metabolismo , Proteínas Associadas aos Microtúbulos/fisiologia , Proteínas de Saccharomyces cerevisiae/metabolismo , Proteínas de Saccharomyces cerevisiae/fisiologia , Cinetocoros/metabolismo , Microtúbulos/metabolismo , Ligação Proteica , Domínios Proteicos/fisiologia , Elementos Estruturais de Proteínas/fisiologia , Saccharomyces cerevisiae/metabolismo , Fuso Acromático/metabolismo , Fuso Acromático/fisiologia , Tubulina (Proteína)/metabolismo
5.
J Biol Chem ; 290(16): 10149-62, 2015 Apr 17.
Artigo em Inglês | MEDLINE | ID: mdl-25720490

RESUMO

Microtubule-associated proteins regulate microtubule (MT) dynamics spatially and temporally, which is essential for proper formation of the bipolar mitotic spindle. The XMAP215 family is comprised of conserved microtubule-associated proteins that use an array of tubulin-binding tumor overexpressed gene (TOG) domains, consisting of six (A-F) Huntingtin, elongation factor 3, protein phosphatase 2A, target of rapamycin (HEAT) repeats, to robustly increase MT plus-end polymerization rates. Recent work showed that TOG domains have differentially conserved architectures across the array, with implications for position-dependent TOG domain tubulin binding activities and function within the XMAP215 MT polymerization mechanism. Although TOG domains 1, 2, and 4 are well described, structural and mechanistic information characterizing TOG domains 3 and 5 is outstanding. Here, we present the structure and characterization of Drosophila melanogaster Mini spindles (Msps) TOG3. Msps TOG3 has two unique features as follows: the first is a C-terminal tail that stabilizes the ultimate four HEAT repeats (HRs), and the second is a unique architecture in HR B. Structural alignments of TOG3 with other TOG domain structures show that the architecture of TOG3 is most similar to TOG domains 1 and 2 and diverges from TOG4. Docking TOG3 onto recently solved Stu2 TOG1· and TOG2·tubulin complex structures suggests that TOG3 uses similarly conserved tubulin-binding intra-HEAT loop residues to engage α- and ß-tubulin. This indicates that TOG3 has maintained a TOG1- and TOG2-like TOG-tubulin binding mode despite structural divergence. The similarity of TOG domains 1-3 and the divergence of TOG4 suggest that a TOG domain array with polarized structural diversity may play a key mechanistic role in XMAP215-dependent MT polymerization activity.


Assuntos
Proteínas de Drosophila/química , Drosophila melanogaster/metabolismo , Proteínas Associadas aos Microtúbulos/química , Microtúbulos/química , Fuso Acromático/química , Tubulina (Proteína)/química , Sequência de Aminoácidos , Animais , Cristalografia por Raios X , Proteínas de Drosophila/genética , Proteínas de Drosophila/metabolismo , Drosophila melanogaster/genética , Expressão Gênica , Proteínas Associadas aos Microtúbulos/genética , Proteínas Associadas aos Microtúbulos/metabolismo , Microtúbulos/metabolismo , Mitose , Modelos Moleculares , Dados de Sequência Molecular , Polimerização , Ligação Proteica , Isoformas de Proteínas/química , Isoformas de Proteínas/genética , Isoformas de Proteínas/metabolismo , Estabilidade Proteica , Estrutura Secundária de Proteína , Estrutura Terciária de Proteína , Alinhamento de Sequência , Fuso Acromático/metabolismo , Tubulina (Proteína)/genética , Tubulina (Proteína)/metabolismo
6.
Mol Biol Cell ; 25(16): 2375-92, 2014 Aug 15.
Artigo em Inglês | MEDLINE | ID: mdl-24966168

RESUMO

XMAP215 family members are potent microtubule (MT) polymerases, with mutants displaying reduced MT growth rates and aberrant spindle morphologies. XMAP215 proteins contain arrayed tumor overexpressed gene (TOG) domains that bind tubulin. Whether these TOG domains are architecturally equivalent is unknown. Here we present crystal structures of TOG4 from Drosophila Msps and human ch-TOG. These TOG4 structures architecturally depart from the structures of TOG domains 1 and 2, revealing a conserved domain bend that predicts a novel engagement with α-tubulin. In vitro assays show differential tubulin-binding affinities across the TOG array, as well as differential effects on MT polymerization. We used Drosophila S2 cells depleted of endogenous Msps to assess the importance of individual TOG domains. Whereas a TOG1-4 array largely rescues MT polymerization rates, mutating tubulin-binding determinants in any single TOG domain dramatically reduces rescue activity. Our work highlights the structurally diverse yet positionally conserved TOG array that drives MT polymerization.


Assuntos
Proteínas de Drosophila/metabolismo , Proteínas Associadas aos Microtúbulos/metabolismo , Microtúbulos/metabolismo , Multimerização Proteica , Tubulina (Proteína)/metabolismo , Sequência de Aminoácidos , Animais , Cristalografia por Raios X , Drosophila , Proteínas de Drosophila/genética , Humanos , Proteínas Associadas aos Microtúbulos/genética , Modelos Moleculares , Dados de Sequência Molecular , Ligação Proteica , Estrutura Terciária de Proteína , Fuso Acromático , Tubulina (Proteína)/genética , Xenopus , Proteínas de Xenopus/genética , Proteínas de Xenopus/metabolismo
7.
Appl Nurs Res ; 18(1): 13-21, 2005 Feb.
Artigo em Inglês | MEDLINE | ID: mdl-15812731

RESUMO

The rising tide of obesity erodes the health of youths and many times results in adult obesity. The purpose of this investigation was to examine the effectiveness of an eight-session health promotion/transtheoretical model Internet/video-delivered intervention to increase physical activity and reduce dietary fat among low-income, culturally diverse, seventh-grade students. Those who completed more than half the sessions increased exercise, t (103) = -1.99, p = .05, and decreased the percentage of dietary fat, t (87) = 2.73, p = .008. Responses to the intervention by stage of change, race, and income are examined.


Assuntos
Instrução por Computador/métodos , Exercício Físico , Comportamento Alimentar , Educação em Saúde/métodos , Obesidade/prevenção & controle , Adolescente , Criança , Gorduras na Dieta , Feminino , Humanos , Internet , Modelos Lineares , Masculino , Meio-Oeste dos Estados Unidos , Gravação de Videoteipe
8.
J Nurs Scholarsh ; 35(2): 171-6, 2003.
Artigo em Inglês | MEDLINE | ID: mdl-12854299

RESUMO

PURPOSE: Natural Family Planning (NFP) requires periodic abstinence and partner cooperation to prevent pregnancy. The aim of this study was to learn about the effects of modern NFP methods on marital relationships. DESIGN: Descriptive survey. METHODS: Questionnaires were mailed to 1,400 randomly selected couples known to use NFP and residing in the United States of America; 334 couples (24%) responded. Content analysis was used to identify meanings and themes. Numeric analyses were used to determine frequencies. FINDINGS: Nearly two-thirds of the qualitative comments were positive. Four themes were identified in the positive responses: relationship enhancements, knowledge improvements, spirituality enrichments, and method successes. Three negative themes were identified: strained sexual interactions, worsened relationships, and method problems. Although about one-fourth of the comments indicated that NFP presented challenges, the majority (74%) found it beneficial, often resulting in stronger bonds, better communication, and improved knowledge. CONCLUSIONS: NFP had more positive than negative effects and its use warrants further consideration.


Assuntos
Atitude Frente a Saúde , Serviços de Planejamento Familiar , Casamento/psicologia , Métodos Naturais de Planejamento Familiar , Cônjuges/psicologia , Adulto , Comunicação , Serviços de Planejamento Familiar/métodos , Feminino , Conhecimentos, Atitudes e Prática em Saúde , Humanos , Masculino , Pesquisa Metodológica em Enfermagem , Apego ao Objeto , Pesquisa Qualitativa , Inquéritos e Questionários , Estados Unidos
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