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1.
Creat Nurs ; 25(1): 17-24, 2019 Feb 01.
Artigo em Inglês | MEDLINE | ID: mdl-30808781

RESUMO

In response to the merger of our 248-bed community hospital with a new health system, a multidisciplinary team began a journey of holistic transformation via the evolution of a new rounding process called Leadership, Ownership, Transformation, Unity, and Sustainability (LOTUS) in the 20-bed ICU. Morphing from a hierarchical practice structure with limited engagement of multidisciplinary members, the LOTUS initiative (named for the blossom whose petals surround its core, the patient) afforded each discipline (petal) an equal voice and allowed a once-fragmented team to work cohesively, collaboratively, and at the highest level of the scope of practice for each discipline, thus affording expert guidance during care planning while providing a method to collect quality metrics. LOTUS allows us to view our patients in a new way as we refocused goal determination on patients and their families. The restructuring and evolution into a high-functioning team was targeted with the goal of enhancing quality critical care for patients, which, in the literature, has correlated with improved patient safety and decreased mortality and ICU length of stay.


Assuntos
Unidades de Terapia Intensiva/organização & administração , Assistência Centrada no Paciente/organização & administração , Instituições Associadas de Saúde , Hospitais Comunitários , Humanos , New Jersey , Qualidade da Assistência à Saúde
2.
PLoS One ; 8(5): e63352, 2013.
Artigo em Inglês | MEDLINE | ID: mdl-23691031

RESUMO

G protein-coupled receptors (GPCRs) constitute the largest family of membrane proteins in the human genome. Their signaling is regulated by scaffold proteins containing PDZ domains, but although these interactions are important for GPCR function, they are still poorly understood. We here present a quantitative characterization of the kinetics and affinity of interactions between GPCRs and one of the best characterized PDZ scaffold proteins, postsynaptic density protein 95 (PSD-95), using fluorescence polarization (FP) and surface plasmon resonance (SPR). By comparing these in vitro findings with colocalization of the full-length proteins in cells and with previous studies, we suggest that the range of relevant interactions might extend to interactions with K i = 450 µM in the in vitro assays. Within this range, we identify novel PSD-95 interactions with the chemokine receptor CXCR2, the neuropeptide Y receptor Y2, and four of the somatostatin receptors (SSTRs). The interaction with SSTR1 was further investigated in mouse hippocampal neurons, where we found a clear colocalization between the endogenously expressed proteins, indicating a potential for further investigation of the role of this interaction. The approach can easily be transferred to other receptors and scaffold proteins and this could help accelerate the discovery and quantitative characterization of GPCR-PDZ interactions.


Assuntos
Peptídeos e Proteínas de Sinalização Intracelular/metabolismo , Proteínas de Membrana/metabolismo , Domínios PDZ , Receptores Acoplados a Proteínas G/química , Receptores Acoplados a Proteínas G/metabolismo , Sequência de Aminoácidos , Animais , Proteína 4 Homóloga a Disks-Large , Células HEK293 , Hipocampo/citologia , Humanos , Cinética , Camundongos , Neurônios/metabolismo , Peptidomiméticos/síntese química , Peptidomiméticos/metabolismo , Ligação Proteica , Transporte Proteico , Especificidade por Substrato
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