𝔖 Bobbio Scriptorium
✦   LIBER   ✦

Processing of yeast exoglucanase (β-glucosidase) in a KEX2-dependent manner

✍ Scribed by Ricardo D. Basco; Guillermo Giménez-Gallego; Germán Larriba


Book ID
115923789
Publisher
Elsevier Science
Year
1990
Tongue
English
Weight
489 KB
Volume
268
Category
Article
ISSN
0014-5793

No coin nor oath required. For personal study only.


📜 SIMILAR VOLUMES


Rap1 controls activation of the αMβ2 int
✍ Jenson Lim; Aurélien G. Dupuy; David R. Critchley; Emmanuelle Caron 📂 Article 📅 2010 🏛 John Wiley and Sons 🌐 English ⚖ 386 KB

The small GTPase Rap1 and the cytoskeletal protein talin regulate binding of C3bi-opsonised red blood cells (RBC) to integrin a M b 2 in phagocytic cells, although the mechanism has not been investigated. Using COS-7 cells transfected with a M b 2 , we show that Rap1 acts on the b 2 and not the a M

S100B(ββ) inhibits the protein kinase C-
✍ Paul T. Wilder; Richard R. Rustandi; Alexander C. Drohat; David J. Weber 📂 Article 📅 1998 🏛 Cold Spring Harbor Laboratory Press 🌐 English ⚖ 509 KB

## Abstract S100B(ββ) is a dimeric Ca^2+^‐binding protein that is known to inhibit the protein kinase C (PKC)‐dependent phosphorylation of several proteins. To further characterize this inhibition, we synthesized peptides based on the PKC phosphorylation domains of p53 (residues 367‐388), neuromodu

The inhibition of β-D-glucosidase (Asper
✍ Jonathan Woodward; James M. Lee; Glenna S. Zachry 📂 Article 📅 1983 🏛 Springer Netherlands 🌐 English ⚖ 361 KB

An inhibitor of $-D-glucosidase (E.C. 3.2.1.21) was found to be present in commercial yeast extract. The inhibitor was shown to be heat-labile, of low molecular weight, and unstable at acid pH. Inhibition was noncompetitive and apparently was not caused by proteinaceous material. Fractionation of th