Results 171 to 180 of about 5,484 (240)

Exploring the role of ADAMTSL2 across multiple cancer types: A pan-cancer analysis and validated in colorectal cancer. [PDF]

Discov Oncol
Yu QX, Wu RC, Wang J, Tuo ZT, Yang J, Zhang YP, Jin J, Yuan Q, Wang CN, Feng DC, Li DX.   +10 more
europepmc   +1 more source

Astacin metalloproteases in human-parasitic nematodes. [PDF]

Adv Parasitol
Moser MS, Hallem EA.
europepmc   +1 more source

The secreted proteases <i>aur, scpA, sspA and sspB</i> suppress the virulence of <i>Staphylococcus aureus</i> USA300 by shaping the extracellular proteome. [PDF]

Virulence
Li X, Maaß S, Ferrero-Bordera B, Zhang Z, Wang M, Sietsema E, Liu L, Divinagracia M, van Dijl JM, Buist G.   +9 more
europepmc   +1 more source

Hemodynamic regulation of metalloendopeptidases EC3.4; 24.15 and EC3.4; 24.16: expression and function in the vascular endothelium

, 2005
Eoin J. Cotter
openalex   +1 more source

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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 ...
F. Gomis-Rüth
openaire   +3 more sources

Inhibition of metalloendopeptidases by 2‐mercaptoacetyl‐dipeptides

European Journal of Biochemistry, 1983
A 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
openaire   +3 more sources

Mammalian metalloendopeptidases

International Journal of Biochemistry, 1985
J S, Bond, R J, Beynon
openaire   +3 more sources

[50] Thermolysin and other neutral metalloendopeptidases

1974
Publisher Summary Thermolysin from Bacillus thermoproteolyticus and the neutral proteases of Bacillus subtilis are neutral metalloendopeptidases having similar size, metal content, amino acid composition, and substrate specificity. Recent evidence indicates that their amino acid sequences have regions of identity, suggesting that these enzymes ...
K.A. Walsh, Y. Burstein, M.K. Pangburn
openaire   +2 more sources

StcE Peptidase and the StcE-Like Metalloendopeptidases

2013
Rose L. Szabady, Rodney A. Welch
openaire   +2 more sources