Gene expression patterns following unilateral traumatic brain injury reveals a local pro-inflammatory and remote anti-inflammatory response. [PDF]
, 2013 BackgroundTraumatic brain injury (TBI) results in irreversible damage at the site of impact and initiates cellular and molecular processes that lead to secondary neural injury in the surrounding tissue.
Ford, Byron D +5 more
core +2 more sources
A new family of diverse skin peptides from the microhylid frog genus phrynomantis [PDF]
, 2020 A wide range of frogs produce skin poisons composed of bioactive peptides for defence against pathogens, parasites and predators. While several frog families have been thoroughly screened for skin-secreted peptides, others, like the Microhylidae, have ...
Ballet, Steven +7 more
core +1 more source
Binding and sequestration of poison frog alkaloids by a plasma globulin
eLife, 2023 Alkaloids are important bioactive molecules throughout the natural world, and in many animals they serve as a source of chemical defense against predation.
Aurora Alvarez-Buylla +9 more
doaj +1 more source
Serpin functions in host-pathogen interactions
PeerJ, 2018 Serpins are a broadly distributed superfamily of protease inhibitors that are present in all kingdoms of life. The acronym, serpin, is derived from their function as potent serine proteases inhibitors.
J. Bao +5 more
semanticscholar +1 more source
Serpins in Hemostasis as Therapeutic Targets for Bleeding or Thrombotic Disorders
Frontiers in Cardiovascular Medicine, 2021 Bleeding and thrombotic disorders result from imbalances in coagulation or fibrinolysis, respectively. Inhibitors from the serine protease inhibitor (serpin) family have a key role in regulating these physiological events, and thus stand out as potential
Elsa P. Bianchini +6 more
doaj +1 more source
Plant serpin protease inhibitors: specificity and duality of function.
Journal of Experimental Botany, 2019 The serpins are a family of structurally conserved protease inhibitors found in all animal and plant kingdoms. After interaction with their cognate substrate(s), their native energetically stressed state is relaxed by hydrolysis, resulting in a semi ...
Maja Cohen, Olga Davydov, R. Fluhr
semanticscholar +1 more source
All-atom simulations reveal how single point mutations promote serpin misfolding
, 2018 Protein misfolding is implicated in many diseases, including the serpinopathies. For the canonical inhibitory serpin {\alpha}1-antitrypsin (A1AT), mutations can result in protein deficiencies leading to lung disease, and misfolded mutants can accumulate ...
Beccara, Silvio a +7 more
core +1 more source
Deciphering the phylogenetic history of neuroserpin orthologs across metazoans by analysis of synteny and rare genomic characters [PDF]
, 2008 The superfamily of serine proteinase inhibitors (serpins) is involved in wide arrays of fundamental biological processes such as blood coagulation, complement activation, fibrinolysis, angiogenesis, inflammation and tumor suppression. The average protein
Abhishek Kumar, Hermann Ragg
core +2 more sources
PLoS Neglected Tropical Diseases, 2019 Ticks successfully feed and transmit pathogens by injecting pharmacological compounds in saliva to thwart host defenses. We have previously used LC-MS/MS to identify proteins that are present in saliva of unfed Amblyomma americanum ticks that were ...
Lucas Tirloni +5 more
semanticscholar +1 more source
Vaspin inhibits kallikrein 7 by serpin mechanism [PDF]
, 2013 The molecular target of the adipokine vaspin (visceral adipose tissue-derived serpin; serpinA12) and its mode of action are unknown. Here, we provide the vaspin crystal structure and identify human kallikrein 7 (hK7) as a first protease target of vaspin ...
Annette G. Beck-Sickinger +9 more
core +1 more source