Results 51 to 60 of about 98,151 (252)

Modeling and structural analysis of PA clan serine proteases

open access: yesBMC Research Notes, 2012
Background Serine proteases account for over a third of all known proteolytic enzymes; they are involved in a variety of physiological processes and are classified into clans sharing structural homology. The PA clan of endopeptidases is the most abundant
Laskar Aparna   +3 more
doaj   +1 more source

Viral SERPINS—A Family of Highly Potent Immune-Modulating Therapeutic Proteins

open access: yesBiomolecules, 2023
Serine protease inhibitors, SERPINS, are a highly conserved family of proteins that regulate serine proteases in the central coagulation and immune pathways, representing 2–10% of circulating proteins in the blood.
Kyle Varkoly   +5 more
doaj   +1 more source

Membrane composition and thermodynamic identity as boundaries of life for synthetic cell research

open access: yesFEBS Letters, EarlyView.
What makes a cell a cell? The boundary of a living cell is not just a wall. Read as a Markov blanket, the membrane separates internal from external states, generating identity and non‐equilibrium order. Can this identity be rebuilt from scratch in a synthetic cell?
Caterina Presutti, Bert Poolman
wiley   +1 more source

Pharmacological Inhibition of Serine Proteases to Reduce Cardiac Inflammation and Fibrosis in Atrial Fibrillation

open access: yesFrontiers in Pharmacology, 2019
Systemic inflammation correlates with an increased risk of atrial fibrillation (AF) and thrombogenesis. Systemic inflammation alters vessel permeability, allowing inflammatory and immune cell migration toward target organs, including the heart.
Raffaele Coppini   +5 more
doaj   +1 more source

The HtrA family of serine proteases [PDF]

open access: yesMolecular Microbiology, 1997
HtrA, also known as DegP and probably identical to the Do protease, is a heat shock‐induced serine protease that is active in the periplasm of Escherichia coli. Homologues of HtrA have been described in a wide range of bacteria and in eukaryotes. Its chief role is to degrade misfolded proteins in the periplasm.
M J, Pallen, B W, Wren
openaire   +2 more sources

Inhibition of dipeptidyl peptidase 7 impairs lysophagy in LLOMe‐treated HepG2 cells

open access: yesFEBS Letters, EarlyView.
DPP7 inhibition delays ubiquitin‐dependent lysophagy by attenuating ubiquitin accumulation and the recruitment of SQSTM1 and LC3 to damaged lysosomes, resulting in delayed clearance of damaged lysosomes and impaired restoration of lysosomal homeostasis. Created using FigureLabs (Certificate ID: FL‐PUB‐20260922‐Z99XNX).
Na Yeon Park   +8 more
wiley   +1 more source

Tumour–host interactions in Drosophila: mechanisms in the tumour micro‐ and macroenvironment

open access: yesMolecular Oncology, EarlyView.
This review examines how tumour–host crosstalk takes place at multiple levels of biological organisation, from local cell competition and immune crosstalk to organism‐wide metabolic and physiological collapse. Here, we integrate findings from Drosophila melanogaster studies that reveal conserved mechanisms through which tumours hijack host systems to ...
José Teles‐Reis, Tor Erik Rusten
wiley   +1 more source

KDM7A and KDM1A inhibition suppresses tumour promoting pathways in prostate cancer

open access: yesMolecular Oncology, EarlyView.
Treatment resistance is a major challenge for patients with advanced prostate cancer. This study examined an alternative approach to target the major prostate cancer‐promoting pathway by targeting epigenetic factors, whose levels are higher in tumours.
Jennie N Jeyapalan   +16 more
wiley   +1 more source

Effect of hyperhomocysteinemia on proteolytic activity in the spleen

open access: yesBiomedical and Biotechnology Research Journal, 2023
Background: The aim of the study was to investigate the effect of hyperhomocysteinemia (HC) on proteolytic activity in the spleen of rats. Methods: Albino nonlinear male rats of different ages (young, adults, and old) were involved in the study.
Nataliia Raksha   +9 more
doaj   +1 more source

The epidermolytic toxins are serine proteases [PDF]

open access: yesFEBS Letters, 1990
Certain strains of Staphylococcus aureus usually belonging to phage group II produce epidermolytic toxins (ETA and ETB) which cause intraepidermal splitting in mice, neonates and occasionally adults. Amino acid sequences of ETA and ETB have been reported but the mechanism of epidermolysis remains unknown.
Dancer, Stephanie J.   +4 more
openaire   +2 more sources

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