Results 121 to 130 of about 4,088 (165)
Some of the next articles are maybe not open access.
Membrane Metalloendopeptidases in Immune Function and Disease
1997The enzymes that compose the ‘Metallopeptidases’ are a diverse group1. Forty-seven distinct evolutionary families of metallopeptidases have been identified in the last eight years; more than for any other protease classes, i.e., the serine/threonine, cysteine, or aspartic classes of proteases (see the Peptidase World Wide Web sites:http://www.qmw.ac.uk/
J S, Bond, W, Jiang
openaire +2 more sources
Substrate-related potent inhibitors of brain metalloendopeptidase
Biochemistry, 1988Rat brain metalloendopeptidase (EC 3.4.24.15) generates Leu- and Met-enkephalin from several larger opioid peptides and is capable of degrading a number of neuropeptides. Substrate-related N-(1-carboxy-3-phenylpropyl) peptide derivatives were synthesized and tested for enzyme inhibition.
M, Orlowski, C, Michaud, C J, Molineaux
openaire +2 more sources
Metalloendopeptidase EC 3.4.24.15 in Neurodegeneration
2002The metalloendopeptidases represent a fascinating class of enzymes involved in neurodegenerative diseases. Many metalloendopeptidases are integrally involved in brain processes. This family boasts enkephalinase (24.11), neurolysin (24.16), and others.
Carmela R. Abraham, Franchot Slot
openaire +1 more source
Degradation of bradykinin by a metalloendopeptidase from Streptococcus pyogenes
Journal of Oral Biosciences, 2016Streptococcus pyogenes secretes streptococcal pyrogenic exotoxin B (SpeB), which cleaves kininogen to liberate bradykinin. In addition, this bacterium also has cell-associated bradykinin-degrading activity. Here, we characterized the bradykinin-degrading enzyme produced by S.
Yoichi, Miyamoto +11 more
openaire +2 more sources
Structural aspects of the metzincin clan of metalloendopeptidases
Molecular Biotechnology, 2003Metalloendopeptidases are present across all kingdoms of living organisms; they are ubiquitous and widely involved in metabolism regulation through their ability either to extensively degrade proteins or to selectively hydrolyze specific peptide bonds. They must be subjected to exquisite spatial and temporal control to prevent this vast potential from ...
openaire +2 more sources
Mammalian metalloendopeptidases
International Journal of Biochemistry, 1985J S, Bond, R J, Beynon
openaire +2 more sources
Peptidyl-Asp metalloendopeptidase.
Methods in enzymology, 1995M L, Hagmann +3 more
openaire +3 more sources
Metalloendopeptidase activity in urine of rodents.
Biomedica biochimica acta, 1992The brush border membrane of mice and rats contains a phosphoramidon-insensitive metalloproteinase, meprin (neutral endopeptidase-2; NEP-2). The role of meprin is unknown, but we have shown that urine from these species contains insulin B chain degrading activity that is due to a phosphoramidon-insensitive metalloendopeptidase.
R J, Beynon, A V, Flannery, G C, Macadam
openaire +1 more source
Evaluation of Antidiabetic Activities of Casein Hydrolysates by a Bacillus Metalloendopeptidase
International Journal of Peptide Research and Therapeutics, 2020Zhennai Yang, , Xiao Zhao
exaly