Correcting sponge names: nomenclatural update of lower taxa level Porifera.

The online World Porifera Database (WPD), the Porifera part of the World Register of Marine Species (WoRMS), lists virtually all published scientific names of sponges. The names of the WPD (as indeed all names in WoRMS) are guided by the Code of the International Comnission on Zoological Nomenclature (ICZN). The WPD names include all currently accepted as well as original combinations, and a majority of non-accepted non-original combinations.

A side-specific nomogram for extraprostatic extension may reduce the positive surgical margin rate in radical prostatectomy.

Purpose: Nomograms predicting side-specific extraprostatic extension (EPE) may be applied to reduce positive surgical margin (PSM) rates in patients planned for radical prostatectomy (RP). This study evaluates the impact of implementing an externally validated nomogram for side-specific EPE on PSM rate and degree of nerve-sparing.

Methods: In patients planned for RP, the side-specific nomogram predictions (based on MRI, ISUP grade group, and PSA density), with an advised threshold of 20% for safe nerve-sparing, were presented preoperatively to the urological surgeon.

The terminology of sponge spicules.

Sponges (Porifera) are a diverse and globally distributed clade of benthic organisms, with an evolutionary history reaching at least the Ediacaran-Cambrian (541 Ma) boundary interval. Throughout their research history, sponges have been subjects of intense studies in many fields, including paleontology, evolutionary biology, and even bioengineering and pharmacology. The skeletons of sponges are mostly characterized by the presence of mineral elements termed spicules, which structurally support the sponge bodies, though they also minimize the metabolic cost of water exchange and deter predators.

An antibody-free platform for multiplexed, sensitive quantification of protein biomarkers in complex biomatrices.

Sensitive, multiplexed protein quantification remains challenging despite recent advancements in LC-MS assays for targeted protein biomarker quantification. High-sensitivity protein biomarker measurements usually require immuno-affinity enrichment of target protein; a process which is highly dependent on capture reagent and limited in capability to measure multiple analytes. Herein, we report a novel antibody-free platform, which measures multiple biomarkers from complex matrices employing a strategically optimized solid-phase extraction cleanup and orthogonal multidimensional LC-MS.