Results 31 to 40 of about 14,423 (252)
Genetic Diversity of Serine Protease Inhibitors in Myxozoan (Cnidaria, Myxozoa) Fish Parasites
We studied the genetic variability of serine protease inhibitors (serpins) of Myxozoa, microscopic endoparasites of fish. Myxozoans affect the health of both farmed and wild fish populations, causing diseases and mortalities. Despite their global impact,
Edit Eszterbauer+6 more
doaj +1 more source
Granule Leakage Induces Cell-Intrinsic, Granzyme B-Mediated Apoptosis in Mast Cells
Mast cells are multifunctional immune cells scattered in tissues near blood vessels and mucosal surfaces where they mediate important reactions against parasites and contribute to the pathogenesis of allergic reactions.
Sabrina Sofia Burgener+14 more
doaj +1 more source
RNAi-mediated knockdown of serine protease inhibitor genes increases the mortality of Plutella xylostella challenged by destruxin A. [PDF]
Destruxin A is a mycotoxin that is secreted by entomopathogenic fungi which has a broad-spectrum insecticidal effect. Previous transcript and protein profiling analysis showed that destruxin A has significant effects on the expression of serine protease ...
Pengfei Han+6 more
doaj +1 more source
Structural and functional characterization of cleavage and inactivation of human serine protease inhibitors by the bacterial SPATE protease EspPα from enterohemorrhagic E. coli. [PDF]
EspPα and EspI are serine protease autotransporters found in enterohemorrhagic Escherichia coli. They both belong to the SPATE autotransporter family and are believed to contribute to pathogenicity via proteolytic cleavage and inactivation of different ...
André Weiss+2 more
doaj +1 more source
The moment a very old bacterial pathogen met a young virus from the 80’s defined the beginning of a tragic syndemic for humanity. Such is the case for the causative agent of tuberculosis and the human immunodeficiency virus (HIV).
Elsa Anes+2 more
doaj +1 more source
Interaction of subtilisins with serpins [PDF]
AbstractSerpins are well‐characterized inhibitors of the chymotrypsin family serine proteinases. We have investigated the interaction of two serpins with members of the subtilisin family, proteinases that possess a similar catalytic mechanism to the chymotrypsins, but a totally different scaffold.
Philip A. Pemberton+4 more
openaire +3 more sources
Thrombin inhibition by the serpins [PDF]
Thrombin is the central protease in the blood coagulation network. It has multiple substrates and cofactors, and it appears that four serpins are responsible for inhibiting the thrombin produced in haemostasis and thrombosis. Structural studies conducted over the last 10 years have resolved how thrombin recognises these serpins with the aid of ...
James A. Huntington
semanticscholar +4 more sources
Serpins Are Getting Hotter [PDF]
AbstractProtease inhibitors of the serpin family require thermodynamic instability for their mechanism of inhibition, and a recent paper from Irving and colleagues demonstrates the structural basis for how a serpin from a bacterial thermophile deals with life at elevated temperature.
Guy S. Salvesen, Fiona L. Scott
openaire +2 more sources
Serpins in thrombosis, hemostasis and fibrinolysis [PDF]
Hemostasis and fibrinolysis, the biological processes that maintain proper blood flow, are the consequence of a complex series of cascading enzymatic reactions. Serine proteases involved in these processes are regulated by feedback loops, local cofactor molecules, and serine protease inhibitors (serpins).
J. C. Rau+3 more
semanticscholar +4 more sources
Alpha-1 antitrypsin (AAT, also known as alpha-1 proteinase inhibitor or SERPINA1) is the most abundant member of the serpin superfamily found in human plasma.
Mostafa Hamada+4 more
doaj +1 more source