𝔖 Bobbio Scriptorium
✦   LIBER   ✦

Denervation increases protein tyrosine kinase and protein tyrosine phosphatase activities in fast and slow skeletal muscle

✍ Scribed by Hanne R. Augestad; F. Hoover


Publisher
Springer
Year
2001
Tongue
English
Weight
243 KB
Volume
204
Category
Article
ISSN
0340-2061

No coin nor oath required. For personal study only.


📜 SIMILAR VOLUMES


Automated nonisotopic assay for protein-
✍ John Babcook; Julian Watts; Ruedi Aebersold; Hermann J. Ziltener 📂 Article 📅 1991 🏛 Elsevier Science 🌐 English ⚖ 848 KB

A sensitive, automated, and nonisotopic assay for protein-tyrosine kinases and phosphatases has been developed. The assay uses commercially available antiphosphotyrosine monoclonal antibodies and the recently developed particle concentration immunofluorescence immunoassay technology. The assay is sp

Protein phosphorylation in fast and slow
✍ X. Wang; J.A.P. Rostas 📂 Article 📅 1998 🏛 John Wiley and Sons 🌐 English ⚖ 620 KB

We have identified proteins in adult chicken skeletal muscle whose phosphorylation can be used as markers for the mature fast and slow muscle phenotype. These include phosphorylase, phosphorylase kinase, and a cyclic adenosine 3Ј,5Ј-monophosphate (cAMP)-stimulated, calmodulin-inhibited 28-kDa band (

On the cross-regulation of protein tyros
✍ Jason M. Haugh; Ian C. Schneider; Jodee M. Lewis 📂 Article 📅 2004 🏛 Elsevier Science 🌐 English ⚖ 587 KB

Intracellular signaling proteins are very often regulated by site-specific phosphorylation. For example, growth factor receptors in eukaryotic cells contain intrinsic tyrosine kinase activity and use inter- and intra-molecular interactions to recruit and orient potential protein substrates for phosp

Activation of Src kinase by protein–tyro
✍ Meenakshi A. Chellaiah; Michael D. Schaller 📂 Article 📅 2009 🏛 John Wiley and Sons 🌐 English ⚖ 403 KB 👁 2 views

## Abstract PTP–PEST is involved in the regulation of sealing ring formation in osteoclasts. In this article, we have shown a regulatory role for PTP–PEST on dephosphorylation of c‐Src at Y527 and phosphorylation at Y418 in the catalytic site. Activation of Src in osteoclasts by over‐expression of