نتایج جستجو برای: aspartyl proteinase

تعداد نتایج: 13130  

Journal: :The Journal of Experimental Medicine 1996
H Herwald M Collin W Müller-Esterl L Björck

Previous work has indicated a crucial role for the extracellular cysteine proteinase of Streptococcus pyogenes in the pathogenicity and virulence of this important human pathogen. Here we find that the purified streptococcal cysteine proteinase releases biologically active kinins from their purified precursor protein, H-kininogen, in vitro, and from kininogens present in the human plasma, ex vi...

Journal: :The Biochemical journal 1988
L Serrano F Wandosell J de la Torre J Avila

The capacity for self-polymerization and shape of the tubulin polymers assembled after digestion with trypsin, Pronase, chymotrypsin, subtilisin, Staphylococcus aureus proteinase V8 and proteinase K were investigated. Digestion with trypsin, Pronase or chymotrypsin resulted in a decrease in the ability of tubulin for self-assembly, whereas limited proteolysis with subtilisin, S. aureus proteina...

Journal: :Journal of cell science 2003
Weiming Xia Michael S Wolfe

Regulated intramembrane proteolysis is a novel mechanism involving proteases that hydrolyze their substrates in a hydrophobic environment. Presenilin (PS) 1 and PS 2 are required for intramembrane cleavage of an increasing number of type I membrane proteins, including the amyloid precursor protein of Alzheimer's disease and the Notch receptor, which signals during differentiation and developmen...

Journal: :Journal of cell science 1990
K Murakami K Tanabe S Takada

A cation-transporting ATPase gene of Plasmodium yoelii was cloned from the parasite genomic library using an oligonucleotide probe derived from a conserved amino acid sequence of the phosphorylation domain of the aspartyl phosphate family of ATPases. The complete nucleotide sequence was determined and it predicts a 126,717 Mr encoded protein composed of 1115 amino acids. Northern blot analysis ...

Journal: :The Journal of biological chemistry 1975
P Sepulveda J Marciniszyn D Liu J Tang

The complete amino acid sequence of porcine pepsin (EC 3.4.4.1) was constructed from the sequence of five cyanogen bromide fragments. The sequence of one of these fragments, CB2A, is reported here. The sequences of 4 other fragments are known from previous work. Porcine pepsin contains 327 residues with three structural variants. The active center aspartyl residue, which reacts with 1,2-epoxy-3...

Journal: :Molecular medicine 2016
Erik J M Toonen Andreea-Manuela Mirea Cees J Tack Rinke Stienstra Dov B Ballak Janna A van Diepen Anneke Hijmans Triantafyllos Chavakis Wim H Dokter Christine T N Pham Mihai G Netea Charles A Dinarello Leo A B Joosten

Activation of inflammatory pathways is known to accompany development of obesity-induced non-alcoholic fatty liver disease (NAFLD), insulin resistance and type 2 diabetes. In addition to caspase-1, the neutrophil serine proteases proteinase 3, neutrophil elastase and cathepsin G are able to process the inactive pro-inflammatory mediators IL-1β and IL-18 to their bioactive forms, thereby regulat...

Journal: :Nature 1971

Journal: :Proceedings of the National Academy of Sciences 1989

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