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Modeling ETBF-Mediated Colorectal Tumorigenesis Using AOM/DSS in Wild-Type Mice. [PDF]
Int J Mol SciHwang S, Lee Y, Rhee KJ.
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Clinical Outcomes and Molecular Characteristics of Bacteroides fragilis Infections. [PDF]
Ann Lab MedKim B, Kim M, Lee K, Lee Y.
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Membrane Metalloendopeptidases in Immune Function and Disease
Advances in Experimental Medicine and Biology, 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, Jiang Weiping, Judith S Bond
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Mammalian metalloendopeptidases
International Journal of Biochemistry & Cell Biology, 1985Robert Beynon, J S Bond
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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
Vitale, Ljubinka +2 more
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ADAM10, myelin-associated metalloendopeptidase
2004The subject of this chapter is ADAM10, myelin-associated metalloendopeptidase. ADAM10 is a zinc-dependent metallo-endopeptidase with a C-terminal distintegrin domain. It is a homolog of adamalysin. As an α-secretase, it is protective against Alzheimer’s disease, cleaving the Aβ protein so that the damaging β-secretase cleavage is reduced.
Postina, Rolf, Fahrenholz, Falk
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The novel ADAMs-like microbial metalloendopeptidase
Russian Journal of Bioorganic Chemistry, 2012Heterologous 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
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New metalloendopeptidase of Morganella morganii ZM
Russian Journal of Bioorganic Chemistry, 2014Proteolytic activity which is inhibited in the presence of o-phenanthroline was found in M. morganii ZM. Intracellular proteases of M. morganii ZM unlimited split musculoskeletal actin in contrast to grimelysin. Several proteolitic proteins of M. morganii ZM cells were identified by zymography with gelatin. Metalloproteinase of M.
Zamaliutdinova N. +3 more
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Inhibition of metalloendopeptidases by 2‐mercaptoacetyl‐dipeptides
European Journal of Biochemistry, 1983A series of 2‐mercaptoacetyl‐dipeptides, a potential group of metalloendopeptidase inhibitors, has been synthesized by coupling the N‐hydroxysuccinimide ester of S‐acetyl‐2‐mercaptoacetic acid with hydrophobic dipeptide methyl ester hydrochlorides, followed by hydrolysis with NaOH in aqueous methanol and acidification with HCl.
S, Blumberg, Z, Tauber
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