Results 31 to 40 of about 754,866 (196)
Proteinase inhibitors in Brazilian leguminosae
Memorias do Instituto Oswaldo Cruz, 1991 Serine proteinase inhitors, in the seeds of several Leguminosae from the Pantanal region (West Brazil), were studied using bovine trypsin, a digestive enzyme, Factor XIIa and human plasma Kallikrein, two blood clotting factors.
C. A. M. Sampaio +3 more
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Dietary regulation of serine proteinases that are resistant to serine proteinase inhibitors
Journal of Insect Physiology, 1997 Ingestion of Kunitz soybean trypsin inhibitor (STI) by larval Helicoverpa zea, Agrotis ipsilon, and Trichoplusia ni extended the retention time of food in the digestive tract and increased the level of activity of proteolytic enzymes that were not susceptible to inhibition by STI.
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The effects of serine proteinase inhibitors on bone resorption in vitro [PDF]
Journal of Endocrinology, 2003 Abstract The aims of this study were to identify the role and sites of action of serine proteinases (SPs) in bone resorption, a process which involves a cascade of events, the central step of which is the removal of bone matrix by osteoclasts (OCs).
Tumber, A +5 more
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TMPRSS2 as a Key Player in Viral Pathogenesis: Influenza and Coronaviruses
BiomoleculesTMPRSS2, a human transmembrane protease enzyme, plays a crucial role in the spread of certain viruses, including influenza and coronaviruses. This enzyme promotes viral infection by cleaving viral glycoproteins, which helps viruses like SARS-CoV-2 and ...
Gilmara Barros de Lima +5 more
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Virology Journal, 2005 Through the use of transient expression assays and directed genetics, the vaccinia virus (VV) I7L gene product has been implicated as the major maturational proteinase required for viral core protein cleavage to occur during virion assembly.
Hruby Dennis E, Byrd Chelsea M
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Toxins, 2016 Kazal-type serine proteinase inhibitors are found in a large number of living organisms and play crucial roles in various biological and physiological processes.
Yanmei Lai +8 more
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Serine proteinases and their inhibitors in Phycomyces blakesleeanus.
Journal of Biological Chemistry, 1979 Three serine proteinases of Phycomyces blakesleeanus were isolated and characterized. The molecular weights were determined to be 18,000, 22,000, and 60,000. The proteinases were solubilized by detergent or salt treatment. Two soluble proteins that specifically inhibit these proteinases were also isolated and characterized. Both these proteins formed 1:
E P, Fischer, K S, Thomson
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Toxins, 2021 A global strategy, under the coordination of the World Health Organization, is being unfolded to reduce the impact of snakebite envenoming. One of the pillars of this strategy is to ensure safe and effective treatments.
José María Gutiérrez +6 more
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Squash inhibitor family of serine proteinases.
Acta Biochimica Polonica, 1996 Squash inhibitors of serine proteinases form an uniform family of small proteins. They are built of 27-33 amino-acid residues and cross-linked with three disulfide bridges. The reactive site peptide bond (P1-P1') is between residue 5 (Lys, Arg or Leu) and 6 (always Ile). High resolution X-ray structures are available for two squash inhibitors complexed
J, Otlewski, D, Krowarsch
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The effects of a plant proteinase inhibitor from Enterolobium contortisiliquum on human tumor cell lines [PDF]
, 2011 Supplementary to the efficient inhibition of trypsin, chymotrypsin, plasma kallikrein, and plasmin already described by the EcTI inhibitor from Enterolobium contortisiliquum, it also blocks human neutrophil elastase (K(iapp)=4.3 nM) and prevents phorbol ...
Sampaio, Misako U. [UNIFESP] +21 more
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