Implementation fidelity of a nurse-led falls prevention program in acute hospitals during the 6-PACK trial

Background: When tested in a randomized controlled trial (RCT) of 31,411 patients, the nurse-led 6-PACK falls prevention program did not reduce falls. Poor implementation fidelity (i.e., program not implemented as intended) may explain this result. Despite repeated calls for the examination of implementation fidelity as an essential component of evaluating interventions designed to improve the delivery of care, it has been neglected in prior falls prevention studies. This study examined implementation fidelity of the 6-PACK program during a large multi-site RCT. Methods: Based on the 6-PACK implementation framework and intervention description, implementation fidelity was examined by quantifying adherence to program components and organizational support. Adherence indicators were: 1) falls-risk tool completion; and for patients classified as high-risk, provision of 2) a ‘Falls alert’ sign; and 3) at least one additional 6-PACK intervention. Organizational support indicators were: 1) provision of resources (executive sponsorship, site clinical leaders and equipment); 2) implementation activities (modification of patient care plans; training; implementation tailoring; audits, reminders and feedback; and provision of data); and 3) program acceptability. Data were collected from daily bedside observation, medical records, resource utilization diaries and nurse surveys. Results: All seven intervention components were delivered on the 12 intervention wards. Program adherence data were collected from 103,398 observations and medical record audits. The falls-risk tool was completed each day for 75% of patients. Of the 38% of patients classified as high-risk, 79% had a ‘Falls alert’ sign and 63% were provided with at least one additional 6-PACK intervention, as recommended. All hospitals provided the recommended resources and undertook the nine outlined program implementation activities. Most of the nurses surveyed considered program components important for falls prevention. Conclusions: While implementation fidelity was variable across wards, overall it was found to be acceptable during the RCT. Implementation failure is unlikely to be a key factor for the observed lack of program effectiveness in the 6-PACK trial. Trial registration: The 6-PACK cluster RCT is registered with the Australian New Zealand Clinical Trials Registry, number ACTRN12611000332921 (29 March 2011)

Computer model documentation guide /

Item 247.S/N 003-003-02282-9."Issued January 1981" -t.p.Includes bibliographical references (p. 48-49).Mode of access: Internet

Crystal structure of L-Trp/Indoleamine 2,3-dioxygenagse 1 (hIDO1) complex with the JK-loop refined in the closed conformation

Protein dynamics governs most of the fundamental processes in the human body. Particularly, the dynamics of loops located near an active site can be involved in the positioning of the substrate and the reaction mechanism. The understanding of the functioning of dynamic loops is therefore a challenge, and often requires the use of a multi-disciplinary approach mixing, for example, crystallographic experiments and molecular dynamics simulations. In the present work, the dynamic behavior of the JK-loop of the human indoleamine 2,3-dioxygenase 1 hemoprotein, a target for immunotherapy, is investigated. To overcome the lack of knowledge on this dynamism, the study reported here is based on 3 crystal structures presenting different conformations of the loop, completed with molecular dynamics trajectories and MM-GBSA analyses, in order to trace the reaction pathway of the enzyme. In addition, the crystal structures identify an exo site in the small unit of the enzyme, that is populated redundantly by the substrate or the product of the reaction. The role of this newer reported exo site still needs to be investigated

Structure of human indoleamine-2,3-dioxygenase 1 (hIDO1) with a complete JK loop

Indoleamine 2,3-dioxygenase 1 has sparked interest as an immunotherapeutic target in cancer research. Its structure includes a loop, named the JK-loop, that controls the orientation of the substrate or inhibitor within the active site. However, little has been reported about the crystal structure of this loop. In the present work, the conformation of the JK-loop is determined for the first time in the presence of the heme cofactor in the active site through X-ray diffraction experiments (2.44 Å resolution). Molecular-dynamics trajectories were also obtained to provide dynamic information about the loop according to the presence of cofactor. This new structural and dynamic information highlights the importance of the JK-loop in confining the labile heme cofactor to the active site

MOESM1 of Intensive, personalized multimodal rehabilitation in patients with primary or revision total knee arthroplasty: a retrospective cohort study

Additional file 1. TIDieR-checklist

MOESM3 of Intensive, personalized multimodal rehabilitation in patients with primary or revision total knee arthroplasty: a retrospective cohort study

Additional file 3. Table S4 illustrating a secondary analysis

MOESM4 of Intensive, personalized multimodal rehabilitation in patients with primary or revision total knee arthroplasty: a retrospective cohort study

Additional file 4. Table S5 illustrating a secondary analysis

MOESM2 of Intensive, personalized multimodal rehabilitation in patients with primary or revision total knee arthroplasty: a retrospective cohort study

Additional file 2. Rehabilitation protocol

Intensive, personalized multimodal rehabilitation in patients with primary or revision total knee arthroplasty: a retrospective cohort study

Abstract Background Recent evidence has shown that many patients suffer from persistent pain and impaired function after primary or revision total knee arthroplasty (TKA). Post-surgical complications may in addition decrease physical performances and lead to more pain and impacted quality of life. The purpose of the study was to assess the changes in pain intensity and functional capacity among patients with post-surgical complications after TKA three weeks of intensive, personalized multimodal rehabilitation. Methods A retrospective cohort study consisting of 217 patient of which 166 had primary TKA and 51 had revision TKA was conducted. On average, primary TKA patients and revision TKA patients were 3.7 and 2.7 months post-surgical, respectively. All patients have had post-surgical complications and were referred to an inpatient rehabilitation department, where they received a personalized three-week intensive, multimodal rehabilitation protocol. The rehabilitation consisted of sessions targeting neuromuscular function, postural control, and flexibility, sessions focusing on improving muscle strength and cardiovascular function and sessions with focus on gait retraining. The frequency of training was 2–4 sessions/day. The primary outcome was the Knee injury and Osteoarthritis Outcome Score (KOOS) and secondary outcomes were pain intensities measured using numerical rating scale, 6 min. walking test, stair-climbing test and range of motion for knee flexion and extension. Outcome measures were assessed at baseline upon referral and at follow-up before discharge. Results All outcomes, except pain at rest in the revision group, improved significantly. KOOS subscales, improved 8.5 to 14.2 in the primary TKA group (

Crystal structure of L-Trp/Indoleamine 2,3-dioxygenase (hIDO1) complex with the JK-loop refined in the intermediate conformation

Protein dynamics governs most of the fundamental processes in the human body. Particularly, the dynamics of loops located near an active site can be involved in the positioning of the substrate and the reaction mechanism. The understanding of the functioning of dynamic loops is therefore a challenge, and often requires the use of a multi-disciplinary approach mixing, for example, crystallographic experiments and molecular dynamics simulations. In the present work, the dynamic behavior of the JK-loop of the human indoleamine 2,3-dioxygenase 1 hemoprotein, a target for immunotherapy, is investigated. To overcome the lack of knowledge on this dynamism, the study reported here is based on 3 crystal structures presenting different conformations of the loop, completed with molecular dynamics trajectories and MM-GBSA analyses, in order to trace the reaction pathway of the enzyme. In addition, the crystal structures identify an exo site in the small unit of the enzyme, that is populated redundantly by the substrate or the product of the reaction. The role of this newer reported exo site still needs to be investigated