Results 31 to 40 of about 1,749,266 (388)

Beyond Inhibition: A Novel Strategy of Targeting HIV-1 Protease to Eliminate Viral Reservoirs

open access: yesViruses, 2022
HIV-1 protease (PR) is a viral enzyme that cleaves the Gag and Gag-Pol polyprotein precursors to convert them into their functional forms, a process which is essential to generate infectious viral particles.
Josh G. Kim, Liang Shan
doaj   +1 more source

Cryptococcal Protease(s) and the Activation of SARS-CoV-2 Spike (S) Protein

open access: yesCells, 2022
In this contribution, we report on the possibility that cryptococcal protease(s) could activate the SARS-CoV-2 spike (S) protein. The S protein is documented to have a unique four-amino-acid sequence (underlined, SPRRAR↓S) at the interface between the S1
Nozethu Mjokane   +7 more
doaj   +1 more source

Molecular Characterization of Protease Activity in Serratia sp. Strain SCBI and Its Importance in Cytotoxicity and Virulence [PDF]

open access: yes, 2014
A newly recognized Serratia species, termed South African Caenorhabditis briggsae isolate (SCBI), is both a mutualist of the nematode Caenorhabditis briggsae KT0001 and a pathogen of lepidopteran insects. Serratia sp.
Petersen, Lauren M., Tisa, Louis S.
core   +2 more sources

Statistical Optimization of the Production of NaCl-Tolerant Proteases by a Moderate Halophile, Virgibacillus sp. SK37

open access: yesFood Technology and Biotechnology, 2015
The objectives of this study are to optimize the conditions for providing high yield of NaCl-tolerant extracellular protease from Virgibacillus sp. SK37 based on a fi sh-based medium and to investigate the eff ects of the key factors (mass per volume ...
Sornchai Sinsuwan   +4 more
doaj   +1 more source

Shotgun Proteomics Revealed Preferential Degradation of Misfolded In Vivo Obligate GroE Substrates by Lon Protease in Escherichia coli

open access: yesMolecules, 2022
The Escherichia coli chaperonin GroEL/ES (GroE) is one of the most extensively studied molecular chaperones. So far, ~80 proteins in E. coli are identified as GroE substrates that obligately require GroE for folding in vivo. In GroE-depleted cells, these
Tatsuya Niwa   +2 more
doaj   +1 more source

Serine proteases [PDF]

open access: yesIUBMB Life, 2009
AbstractOver one third of all known proteolytic enzymes are serine proteases. Among these, the trypsins underwent the most predominant genetic expansion yielding the enzymes responsible for digestion, blood coagulation, fibrinolysis, development, fertilization, apoptosis, and immunity.
openaire   +3 more sources

Plant Proteases [PDF]

open access: yes, 2020
Plant proteases are involved in most aspects of plant physiology and development, playing key roles in the generation of signaling molecules and as regulators of essential cellular processes such as cell division and metabolism. They take part in important pathways like protein turnover by the degradation of misfolded proteins and the ubiquitin ...
Diaz-Mendoza, M   +2 more
openaire   +3 more sources

Screening and Selection of Media Components for Protease Production by Bacillus sp. EBTA6 Using Plackett–Burman Design

open access: yesTurkish Journal of Agriculture: Food Science and Technology, 2020
In this study, effects of medium components and inoculum size on the protease production by Bacillus sp. EBTA6 that was isolated from a home-made Tarhana sample were investigated. The cell-free supernatant of bacterium cultured on a shaking incubator for
Fikriye Alev Akçay, Ayşe Avcı
doaj   +1 more source

In vitro and in vivo studies of the trypanocidal properties of WRR-483 against Trypanosoma cruzi. [PDF]

open access: yes, 2010
BackgroundCruzain, the major cysteine protease of Trypanosoma cruzi, is an essential enzyme for the parasite life cycle and has been validated as a viable target to treat Chagas' disease.
Brinen, Linda S   +6 more
core   +3 more sources

Peptide synthesis by recombinant Fasciola hepatica cathepsin L1 [PDF]

open access: yes, 2006
Synthesis of the tripeptide Z-Phe-Arg-SerNH2 has been accomplished by a recombinant cysteine protease, cathepsin L1 from liver fluke (Fasciola hepatica), using Z-Phe-Arg-OMe as acyl acceptor and SerNH2 as nucleophile in 0.1 M ammonium acetate pH 9.0–12.5%
Ciarán Ó'Fágáin   +16 more
core   +1 more source

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