The role of proteases in pathologies of the synovial joint [PDF]
Synovial (diarthrodial) joints are employed within the body to provide skeletal mobility and have a characteristic structure adapted to provide a smooth almost frictionless surface for articulation.
Buttle, D, Jones, GC, Riley, GP
core +1 more source
By dawn or dusk—how circadian timing rewrites bacterial infection outcomes
The circadian clock shapes immune function, yet its influence on infection outcomes is only beginning to be understood. This review highlights how circadian timing alters host responses to the bacterial pathogens Salmonella enterica, Listeria monocytogenes, and Streptococcus pneumoniae revealing that the effectiveness of immune defense depends not only
Devons Mo +2 more
wiley +1 more source
Pretreatment with serine protease inhibitors impairs Leishmania amazonensis survival on macrophages
Background Leishmaniases are neglected tropical diseases with great clinical and epidemiological importance. The current chemotherapy available for the treatment of leishmaniasis presents several problems, such as adverse effects, toxicity, long ...
Patrícia de Almeida Machado +3 more
doaj +1 more source
Modeling and structural analysis of PA clan serine proteases
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
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
Type II Transmembrane Serine Proteases [PDF]
Analysis of genome and expressed sequence tag data bases at the turn of the millennium unveiled a new protease family named the type II transmembrane serine proteases (TTSPs) in a Journal of Biological Chemistry minireview (Hooper, J. D., Clements, J. A., Quigley, J. P., and Antalis, T. M. (2001) J. Biol. Chem. 276, 857-860).
Thomas H, Bugge +2 more
openaire +2 more sources
Engineering novel complement activity into a pulmonary surfactant protein [PDF]
Complement neutralizes invading pathogens, stimulates inflammatory and adaptive immune responses, and targets non- or altered-self structures for clearance.
Anthony H. Keeble +38 more
core +2 more sources
The Caenorhabditis elegans DPF‐3 and human DPP4 have tripeptidyl peptidase activity
The dipeptidyl peptidase IV (DPPIV) family comprises serine proteases classically defined by their ability to remove dipeptides from the N‐termini of substrates, a feature that gave the family its name. Here, we report the discovery of a previously unrecognized tripeptidyl peptidase activity in DPPIV family members from two different species.
Aditya Trivedi, Rajani Kanth Gudipati
wiley +1 more source
Site-directed mutagenesis of the proposed catalytic amino acids of the Sindbis virus capsid protein autoprotease [PDF]
The structural proteins of Sindbis virus are translated as a polyprotein precursor that is cleaved upon translation. The capsid protein is postulated to be a serine protease that releases itself from the N terminus of the nascent polyprotein by ...
Hahn, Chang S., Strauss, James H.
core
Production and characterization of monoclonal antibodies raised against recombinant human granzymes A and B and showing cross reactions with the natural proteins [PDF]
The human serine proteases granzymes A and B are expressed in cytotoplasmic granules of activated cytotoxic T lymphocytes and natural killer cells. Recombinant granzyme A and granzyme B proteins were produced in bacteria, purified and then used to raise ...
Borst, Jannie +9 more
core +4 more sources

