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Drug Development.
Alzheimers Dement
December 2024
Indiana University School of Medicine, Indianapolis, IN, USA.
Background: SHIP1 is a phosphatidyl inositol phosphatase encoded by INPP5D, which has been identified as a risk gene for Alzheimer's disease (AD). SHIP1 is expressed in microglia, the resident macrophage in brain. It is a complex, multidomain protein that acts as a negative regulator downstream from TREM2.
View Article and Find Full Text PDFThymidine Phosphodiester Chemiluminescent Probe for Sensitive and Selective Detection of Ectonucleotide Pyrophosphatase 1.
Bioconjug Chem
January 2025
School of Chemistry, Raymond and Beverly Sackler Faculty of Exact Sciences, Tel-Aviv University, Tel Aviv 69978, Israel.
ENPP-1 is a transmembrane enzyme involved in nucleotide metabolism, and its overexpression is associated with various cancers, making it a potential therapeutic target and biomarker for early tumor diagnosis. Current detection methods for ENPP-1 utilize a colorimetric probe, , which has significant limitations in sensitivity. Here, we present probe , the first nucleic acid-based chemiluminescent probe designed for rapid and highly sensitive detection of ENPP-1 activity.
View Article and Find Full Text PDFEvaluation of a point-of-care test for quantitative determination of total thyroxine in feline serum.
J Feline Med Surg
January 2025
Department of Veterinary Medicine and Animal Sciences (DIVAS), University of Milan, Lodi (LO), Italy.
Objectives: Total thyroxine (TT4) evaluation is the most commonly used first-line test for the diagnosis and monitoring of cats with hyperthyroidism. Vcheck T4 is a point-of-care immunoassay that measures TT4 using a Vcheck V200 analyser. This study aimed to evaluate the analytic performance of the Vcheck T4 assay in feline sera and the agreement in the classification of normal, high and low TT4 concentrations of Vcheck T4 with those measured by an enzyme immunoassay (EIA).
View Article and Find Full Text PDFRecent Developments and Challenges in the Enzymatic Formation of Nitrogen-Nitrogen Bonds.
ACS Catal
January 2025
Department of Chemical and Pharmaceutical Biology, Groningen Research Institute of Pharmacy, University of Groningen, Antonius Deusinglaan 1, Groningen 9713AV, The Netherlands.
The biological formation of nitrogen-nitrogen (N-N) bonds represents intriguing reactions that have attracted much attention in the past decade. This interest has led to an increasing number of N-N bond-containing natural products (NPs) and related enzymes that catalyze their formation (referred to in this review as NNzymes) being elucidated and studied in greater detail. While more detailed information on the biosynthesis of N-N bond-containing NPs, which has only become available in recent years, provides an unprecedented source of biosynthetic enzymes, their potential for biocatalytic applications has been minimally explored.
View Article and Find Full Text PDF[This corrects the article DOI: 10.1002/ece3.70751.
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