Results 201 to 210 of about 7,597 (252)
Some of the next articles are maybe not open access.

Structural aspects of the metzincin clan of metalloendopeptidases

Molecular Biotechnology, 2003
Metalloendopeptidases 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

Metalloendopeptidase EC 3.4.24.15 in Neurodegeneration

2002
The 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

Mammalian metalloendopeptidases

International Journal of Biochemistry, 1985
J S, Bond, R J, Beynon
openaire   +2 more sources

Peptidyl-Asp metalloendopeptidase.

Methods in enzymology, 1995
M L, Hagmann   +3 more
openaire   +3 more sources

Metalloendopeptidase activity in urine of rodents.

Biomedica biochimica acta, 1992
The 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

Peptidyl-Asp Metalloendopeptidase

2013
Shujia Dai   +3 more
openaire   +1 more source

Structural basis of substrate recognition and conformational gating in the bacteriophage M15 metalloendopeptidase LysPH

bioRxiv
Dhruv Pahwa   +13 more
semanticscholar   +1 more source

Home - About - Disclaimer - Privacy