P A Roche et al.
Biochemistry, 28(19), 7629-7636 (1989-09-19)
Treatment of the human plasma proteinase inhibitor alpha 2-macroglobulin (alpha 2M) with proteinase results in conformational changes in the inhibitor and subsequent activation and cleavage of the internal thiolester bonds of alpha 2M. Previous studies from this laboratory have shown...
H Ishibashi et al.
Methods in enzymology, 163, 485-495 (1988-01-01)
Paul Dent et al.
Journal of cellular physiology, 235(10), 6862-6874 (2020-01-28)
We have extended our analyses of (curcumin+sildenafil) biology. The drug combination caused vascularization and degradation of mutant K-RAS that correlated with reduced phosphorylation of ERK1/2, AKT T308, mTORC1, mTORC2, ULK1 S757, STAT3, STAT5, and NFκB and increased phosphorylation of eIF2α...
Yonathan Uriel et al.
Insect science, 27(2), 256-265 (2018-07-27)
We tested the recent hypothesis that the "fly factor" phenomenon (food currently or previously fed on by flies attracts more flies than the same type of food kept inaccessible to flies) is mediated by bacterial symbionts deposited with feces or...
J J Feige et al.
Hormone research, 45(3-5), 227-232 (1996-01-01)
alpha 2-Macroglobulin (alpha 2M) is a large plasma glycoprotein that has long been known as an irreversible inhibitor of a variety of proteinases. More recently, it has been reported that numerous growth factors, cytokines and hormones bind to alpha 2M...