Patients' perceptions of individualized care: evaluating psychometric properties and results of the individualized care scale.

Health-care organizations aim to provide patient-centred care, yet measurement of this aspect of care quality remains a challenge.This cross-sectional study investigated the reliability and validity of the bipartite Individualized Care Scale (ICSA, ICS-B) in a Canadian hip and knee arthroplasty population. Internal consistency of the ICS-A and ICS-B was high; however, factorial validity was not fully supported. Twenty-five percent of participants provided additional open-ended comments to describe individual perceptions, needs, and suggestions, noting that the Likert-scale approach required them to aggregate their feedback about rather than share their perceptions of individual nurses.The findings indicate that it is important to patients to be able to share their individual stories when evaluating nursing care. Future qualitative studies should examine the nurse perspective on the provision of patient-centred care, including investigation of systems and process-related features that foster or hinder more individualized care.

Kaposi's sarcoma-associated herpesvirus viral interferon regulatory factor 4 (vIRF4/K10) is a novel interaction partner of CSL/CBF1, the major downstream effector of Notch signaling.

In cells infected with the Kaposi's sarcoma-associated herpesvirus (KSHV), CSL/CBF1 signaling is essential for viral replication and promotes the survival of KSHV-infected cells. CSL/CBF1 is a DNA adaptor molecule which recruits coactivator and corepressor complexes to regulate viral and cellular gene transcription and which is a major downstream effector molecule of activated Notch. The interaction of KSHV RTA and LANA with CSL/CBF1 has been shown to balance the lytic and latent viral life cycle. Here we report that a third KSHV protein, viral interferon regulatory factor 4 (vIRF4/K10), but none of the three other KSHV-encoded vIRFs, interacts with CSL/CBF1. Two regions of vIRF4 with dissimilar affinities contribute to CSL/CBF1 binding. Similar to Notch, vIRF4 targets the hydrophobic pocket in the beta trefoil domain of CSL/CBF1 through a short peptide motif which closely resembles a motif found in Notch but does not strictly follow the ΦWΦP consensus conserved in human and mouse Notch proteins. Our results suggest that vIRF4 might compete with Notch for CSL/CBF1 binding and signaling.