Erratum: Visualization of endogenous p27 and Ki67 reveals the importance of a c-Myc-driven metabolic switch in promoting survival of quiescent cancer cells: Erratum.

[This corrects the article DOI: 10.7150/thno.63763.

Decrease of Prolylcarboxypeptidase Dose of Aqueous Humor is Involved in the Pathogenesis of Primary Open-Angle Glaucoma via Finetuning of the Local Ocular Renin-Angiotensin System.

Objective: In this study, we investigated the cause of the AngII dose elevation in aqueous humor of primary open-angle glaucoma (POAG) patients.

Methods: Enzyme-linked immunosorbent assay (ELISA), western blotting were used to detect concentration of Angiotensin Converting Enzyme 2 (ACE2) and Prolylcarboxypeptidase (PRCP). AngII and AngII + Recombinant PRCP were injected into anterior chamber of mouse eye.

A first determination of the strong coupling at approximate LO order in a global PDF fit.

We present the first determination of the value of the strong coupling via a simultaneous global fit of the proton parton distribution functions (PDFs) at approximate LO (a LO) order in QCD. This makes use of the MSHT global PDF fitting framework, and in particular the recent theoretical advances t l;;mhat allow a PDF fit to now be performed at this order. The value of the strong coupling is found to be .

Real-World Prescription Data for Intrathecal Drug Delivery: A Retrospective Analysis in 32,784 Patients.

Objectives: Currently, there are three monotherapy drugs approved by the United States Food and Drug Administration (FDA) for use in intrathecal drug delivery systems (IDDS): morphine, ziconotide, and baclofen. In practice, use includes alternate drugs, drug combinations, and drug concentrations. There is a paucity of real-world data examining prescription patterns for IDDS.

A structural perspective on the temperature-dependent activity of enzymes.

Enzymes are biomolecular catalysts whose activity varies with temperature. Unlike for small-molecule catalysts, the structural ensembles of enzymes can vary substantially with temperature, and it is in general unclear how this modulates the temperature dependence of activity. Here multi-temperature X-ray crystallography was used to record structural changes from -20°C to 40°C for a mesophilic enzyme in complex with inhibitors mimicking substrate-, intermediate-, and product-bound states, representative of major complexes underlying the kinetic constant .