An Immunocytochemistry Method to Investigate the Translationally Active HIV Reservoir.

Despite the success of combination antiretroviral therapy (cART) to suppress HIV replication, HIV persists in a long-lived reservoir that can give rise to rebounding viremia upon cART cessation. The translationally active reservoir consists of HIV-infected cells that continue to produce viral proteins even in the presence of cART. These active reservoir cells are implicated in the resultant viremia upon cART cessation and likely contribute to chronic immune activation in people living with HIV (PLWH) on cART.

Improving access to services in neuro-developmental disability: proceedings of a national meeting to advance community capacity.

As part of a participatory project to advance navigational service delivery systems for children with neurodevelopmental disability (NDD) and their families, this paper addresses proceedings from a capacity-building conference in Vancouver, Canada. A total of 29 invited key stakeholders attended the meeting with the following aims: knowledge sharing amongst provincial/territorial regions advancing NDD navigation capacity; sustainable action-oriented knowledge exchange; and operationalizing next steps to build navigation resources across Canadian regions. Regional representation included multiple and inter-sectoral partners (e.

Impact of Non-Hepatectomy Opioid Reduction Efforts on Post-Hepatectomy Opioid Prescriptions: Analysis of 2,005 Patients.

Introduction: Pathway-driven, post-pancreatectomy opioid reduction interventions have proven effective and sustainable and may have a "halo effect" on other major abdominal cancer operations. This study's aim was to analyze the sequential effects of expanding opioid reduction efforts from pancreatectomy on opioids prescribed after hepatectomy.

Methods: This is a retrospective cohort study utilizing data from the electronic health record and a prospective quality improvement database for consecutive hepatectomy patients (09/2016-02/2024).

FUT10 and FUT11 are protein O-fucosyltransferases that modify protein EMI domains.

O-Fucosylation plays crucial roles in various essential biological events. Alongside the well-established O-fucosylation of epidermal growth factor-like repeats by protein O-fucosyltransferase 1 (POFUT1) and thrombospondin type 1 repeats by POFUT2, we recently identified a type of O-fucosylation on the elastin microfibril interface (EMI) domain of Multimerin-1 (MMRN1). Here, using AlphaFold2 screens, co-immunoprecipitation, enzymatic assays combined with mass spectrometric analysis and CRISPR-Cas9 knockouts, we demonstrate that FUT10 and FUT11, originally annotated in UniProt as α1,3-fucosyltransferases, are actually POFUTs responsible for modifying EMI domains; thus, we renamed them as POFUT3 and POFUT4, respectively.