Cardiotoxicity of Iron and Zinc and Their Association with the Mitochondrial Unfolded Protein Response in Humans. [PDF]
Mirosevic V +12 more
europepmc +1 more source
Exploration of isolated actives from Coleus amboinicus leaves as anticancer agents: in vitro testing, network pharmacology studies, and molecular docking. [PDF]
Gurning K +5 more
europepmc +1 more source
Circular RNA profiling uncovers regulators of early body color transition in juvenile leopard coral grouper (Plectropomus leopardus). [PDF]
Deng X +9 more
europepmc +1 more source
Proteomic Differences Reveal Early Development of Contrasting Energetic Strategies Between Divergent Migratory Ecotypes in Three-Spined Stickleback. [PDF]
Barnes M +3 more
europepmc +1 more source
Ovary Transcriptome Profiling in Broody and Egg-laying Chahua Chickens. [PDF]
Du Y +7 more
europepmc +1 more source
X-linked Hypophosphatemic Rickets Revealed by Exome Sequencing: A Pediatric Case Report of a PHEX Pathogenic Variant. [PDF]
Larbi Ouassou K, Amale H, Abilkassem R.
europepmc +1 more source
The novel ADAMs-like microbial metalloendopeptidase [PDF]
Heterologous gene expression of extracellular minor metalloendopeptidase of Bacillus pumilus 3-19 in protease-deficient B. subtilis strain has been studied. The fraction of enzyme in total pool of B. pumilus 3-19 secreted proteases composes less than 8%.
Balaban N. +4 more
exaly +6 more sources
Features of gene expression of Bacillus pumilus metalloendopeptidase [PDF]
Features of gene expression of the secreted Bacillus pumilus metalloendopeptidase belonging to the adamalysin/reprolysin family were investigated. In the regulatory region of the gene, we identified hypothetical binding sites for transcription factors CcpA and TnrA.
Rudakova N. +4 more
exaly +6 more sources
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Extracellular metalloendopeptidase of Streptomyces rimosus
Archives of Microbiology, 2006Metalloendopeptidase was isolated from Streptomyces rimosus culture filtrates in a homogeneous form. It was determined to be a 15 kDa basic protein, most active around pH 7.5, and susceptible to inhibition by chelating agents, N-bromosuccinimide, thiorphan, and 10(-4) M zinc. The enzyme was highly specific for phenylalanine at the N-side of endopeptide
Igor Krizaj, Ljubinka Vitale
exaly +4 more sources

