Night-time communication at Stanford University Hospital: perceptions, reality and solutions
BMJ QUALITY & SAFETY
2018; 27 (2): 156–62
Improving and sustaining a reduction in iatrogenic pneumothorax through a multifaceted quality-improvement approach
JOURNAL OF HOSPITAL MEDICINE
2015; 10 (9): 599-607
Improving and sustaining a reduction in iatrogenic pneumothorax through a multifaceted quality-improvement approach.
Journal of hospital medicine
2015; 10 (9): 599-607
Resident work hour restrictions have led to the creation of the 'night float' to care for the patients of multiple primary teams after hours. These residents are often inundated with acute issues in the numerous patients they cover and are less able to address non-urgent issues that arise at night. Further, non-urgent pages may contribute to physician alarm fatigue and negatively impact patient outcomes.To delineate the burden of non-urgent paging at night and propose solutions.We performed a resident review and categorisation of 1820 pages to night floats between September 2014 and December 2014. Both attending and nursing review of 10% of pages was done and compared.Of reviewed pages, 62.1% were urgent and 27.7% were non-urgent. Attending review of random page samples correlated well with resident review. Common reasons for non-urgent pages were non-urgent patient status updates, low-priority order requests and non-critical lab values.A significant number of non-urgent pages are sent at night. These pages likely distract from acute issues that arise at night and place an unnecessary burden on night floats. Both behavioural and systemic adjustments are needed to address this issue. Possible interventions include integrating low-priority messaging into the electronic health record system and use of charge nurses to help determine urgency of issues and batch non-urgent pages.
View details for DOI 10.1136/bmjqs-2017-006727
View details for Web of Science ID 000423231600011
View details for PubMedID 29055898
Structural protein 4.1R is integrally involved in nuclear envelope protein localization, centrosome-nucleus association and transcriptional signaling
JOURNAL OF CELL SCIENCE
2011; 124 (9): 1433-1444
The Agency for Healthcare Research and Quality has adopted iatrogenic pneumothorax (IAP) as a Patient Safety Indicator. In 2006, in response to a low performance ranking for IAP rate from the University Healthsystem Consortium (UHC), the authors established a multidisciplinary team to reduce our institution's IAP rate. Root-cause analysis found that subclavian insertion of central venous catheterization (CVC) was the most common procedure associated with IAP OBJECTIVE: Our short-term goal was a 50% reduction of both CVC-associated and all-cause IAP rates within 18 months, with long-term goals of sustained reduction.Observational study.Academic tertiary care hospital.Consecutive inpatients from 2006 to 2014.Our multifaceted intervention included: (1) clinical and documentation standards based on evidence, (2) cognitive aids, (3) simulation training, (4) purchase and deployment of ultrasound equipment, and (5) feedback to clinical services.CVC-associated IAP, all-cause IAP rate.We achieved both a short-term (years 2006 to 2008) and long-term (years 2006 to 2008-2014) reduction in our CVC-associated and all-cause IAP rates. Our short-term reduction in our CVC-associated IAP was 53% (P = 0.088), and our long-term reduction was 85% (P < 0.0001). Our short-term reduction in the all-cause IAP rate was 26% (P < 0.0001), and our long-term reduction was 61% (P < 0.0001).A multidisciplinary team, focused on evidence, patient safety, and standardization, can use a set of multifaceted interventions to sustainably improve patient outcomes for several years after implementation. Our hospital was in the highest performance UHC quartile for all-cause IAP in 2012 to 2014. Journal of Hospital Medicine 2015. © 2015 Society of Hospital Medicine.
View details for DOI 10.1002/jhm.2388
View details for PubMedID 26041246
Downregulation of protein 4.1R, a mature centriole protein, disrupts centrosomes, alters cell cycle progression, and perturbs mitotic spindles and anaphase
MOLECULAR AND CELLULAR BIOLOGY
2008; 28 (7): 2283-2294
The multifunctional structural protein 4.1R is required for assembly and maintenance of functional nuclei but its nuclear roles are unidentified. 4.1R localizes within nuclei, at the nuclear envelope, and in cytoplasm. Here we show that 4.1R, the nuclear envelope protein emerin and the intermediate filament protein lamin A/C co-immunoprecipitate, and that 4.1R-specific depletion in human cells by RNA interference produces nuclear dysmorphology and selective mislocalization of proteins from several nuclear subcompartments. Such 4.1R-deficiency causes emerin to partially redistribute into the cytoplasm, whereas lamin A/C is disorganized at nuclear rims and displaced from nucleoplasmic foci. The nuclear envelope protein MAN1, nuclear pore proteins Tpr and Nup62, and nucleoplasmic proteins NuMA and LAP2α also have aberrant distributions, but lamin B and LAP2β have normal localizations. 4.1R-deficient mouse embryonic fibroblasts show a similar phenotype. We determined the functional effects of 4.1R-deficiency that reflect disruption of the association of 4.1R with emerin and A-type lamin: increased nucleus-centrosome distances, increased β-catenin signaling, and relocalization of β-catenin from the plasma membrane to the nucleus. Furthermore, emerin- and lamin-A/C-null cells have decreased nuclear 4.1R. Our data provide evidence that 4.1R has important functional interactions with emerin and A-type lamin that impact upon nuclear architecture, centrosome-nuclear envelope association and the regulation of β-catenin transcriptional co-activator activity that is dependent on β-catenin nuclear export.
View details for DOI 10.1242/jcs.077883
View details for Web of Science ID 000289621300009
View details for PubMedID 21486941
Centrosomes nucleate and organize interphase microtubules and are instrumental in mitotic bipolar spindle assembly, ensuring orderly cell cycle progression with accurate chromosome segregation. We report that the multifunctional structural protein 4.1R localizes at centrosomes to distal/subdistal regions of mature centrioles in a cell cycle-dependent pattern. Significantly, 4.1R-specific depletion mediated by RNA interference perturbs subdistal appendage proteins ninein and outer dense fiber 2/cenexin at mature centrosomes and concomitantly reduces interphase microtubule anchoring and organization. 4.1R depletion causes G(1) accumulation in p53-proficient cells, similar to depletion of many other proteins that compromise centrosome integrity. In p53-deficient cells, 4.1R depletion delays S phase, but aberrant ninein distribution is not dependent on the S-phase delay. In 4.1R-depleted mitotic cells, efficient centrosome separation is reduced, resulting in monopolar spindle formation. Multipolar spindles and bipolar spindles with misaligned chromatin are also induced by 4.1R depletion. Notably, all types of defective spindles have mislocalized NuMA (nuclear mitotic apparatus protein), a 4.1R binding partner essential for spindle pole focusing. These disruptions contribute to lagging chromosomes and aberrant microtubule bridges during anaphase/telophase. Our data provide functional evidence that 4.1R makes crucial contributions to the structural integrity of centrosomes and mitotic spindles which normally enable mitosis and anaphase to proceed with the coordinated precision required to avoid pathological events.
View details for DOI 10.1128/MCB.02021-07
View details for Web of Science ID 000254181400015
View details for PubMedID 18212055