Results 121 to 130 of about 41,379 (247)

Impact of Dupilumab Therapy on Skin Barrier Function in Patients With Moderate‐to‐Severe Atopic Dermatitis: A Phase IV, Non‐Randomized, Open‐Label, Parallel‐Group Clinical Study

open access: yesMedComm, Volume 7, Issue 11, November 2026.
This 16‑week study assessed impact of dupilumab on skin barrier function in patients with moderate‑to‑severe atopic dermatitis (AD). Tape‑stripped stratum corneum samples for multi‑omic profiling, alongside transepidermal water loss measurements, were collected from lesional/non‑lesional AD skin and healthy controls at seven time points.
Taoming Liu   +21 more
wiley   +1 more source

N-ACETYLALANINE AMINOPEPTIDASE, A NEW ENZYME FROM HUMAN-ERYTHROCYTES

open access: yes, 1981
SCHONBERGER OL, Tschesche H. N-ACETYLALANINE AMINOPEPTIDASE, A NEW ENZYME FROM HUMAN-ERYTHROCYTES. HOPPE-SEYLERS ZEITSCHRIFT FUR PHYSIOLOGISCHE CHEMIE.
Tschesche, Harald   +3 more
core   +1 more source

Targeted Protein Degradation: From Molecular Mechanisms to Emerging Therapeutic Strategies

open access: yesMedComm, Volume 7, Issue 11, November 2026.
Graphical overview of targeted protein degradation: mechanisms, molecular determinants, delivery strategies, and therapeutic development. This graphical abstract summarizes the major degradation pathways involved in targeted protein degradation, including the ubiquitin–proteasome system, endocytosis–lysosome pathway, and autophagy‐dependent degradation.
Huaijuan Guo   +8 more
wiley   +1 more source

Substrate‐Dependent Crosslinking by the Cytochrome P450 From Aminopyruvatide Biosynthesis

open access: yesAngewandte Chemie, Volume 138, Issue 44, 26 October 2026.
Substitutions in the aminopyruvatide precursor peptide altered the C─C linkage formed from a YLY motif by the P450 ApyO to a N─C linkage in a WLY motif. Moreover, constitutional isomers crosslinked by C─C and C─O linkages were formed from YYY or YWY motifs. ABSTRACT Cytochrome P450s catalyze an array of reactions including crosslinking of aromatic side
Chandrashekhar Padhi   +6 more
wiley   +2 more sources

Plasmepsins as Antimalarial Drug Targets—Then, Now, and the Future

open access: yesMedicinal Research Reviews, Volume 46, Issue 6, Page 1574-1602, November 2026.
ABSTRACT Malaria is a devastating disease caused by Plasmodium parasites. Plasmodium parasites express ten cathepsin D‐like aspartyl proteases, called plasmepsins (PMs). These PMs have diverse roles fulfill diverse functions throughout the parasite's lifecycle, though several exhibit functional redundancies. Among them, PMV, PMIV, and PMX are essential
Brad E. Sleebs
wiley   +1 more source

Purification and characterization of aminopeptidase yspI from Schizosaccharomyces pombe

open access: yes, 1993
Aminopeptidase yspI was purified to apparent homogeneity from the fission yeast Schizosaccharomyces pombe. The molecular mass of the native enzyme was estimated to be 184 kDa by gel filtration chromatography. A value of 92 kDa was calculated after sodium
Arbesú, María José   +2 more
core   +1 more source

Characterizing gas diffusivity, air permeability, and extracellular enzyme activity in an early‐stage comparison of conventional and regenerative pasture

open access: yesSoil Science Society of America Journal, Volume 90, Issue 6, November/December 2026.
Abstract Regenerative pasture is an emerging agricultural framework characterized by high forage diversity, adaptive grazing, and reduced external inputs. However, early‐stage soil structural transitions and associated microbial activities remain unclear, particularly given the higher spatial variability expected in these systems.
Chamindu Deepagoda T.K.K.   +10 more
wiley   +1 more source

Characterization of a glutamyl aminopeptidase from Bacillus licheniformis NS115

open access: yes, 1998
An extracellular glutamyl aminopeptidase (EC 3.4.11.7) producing bacterium was isolated from soil and identified as Bacillus licheniformis based on its morphological and physiological characteristics.
Jong Woo Kim   +4 more
core  

Chromogenic Substrates for Aminopeptidase.

open access: yesExperimental Biology and Medicine, 1954
SummaryChromogenic aminopeptides have been synthesized which are readily hydrolyzed by extracts of human tissues and human serum, duodenal juice and urine. It is possible to localize enzymatic activity histochemically by the use of these substrates.
openaire   +2 more sources

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