✦ LIBER ✦

Regulation of the Ca2+/CaM-Responsive Pool of CaMKII by Scaffold-Dependent Autophosphorylation

✍ Scribed by Cecilia S. Lu; James J.L. Hodge; Jennifer Mehren; Xiu Xia Sun; Leslie C. Griffith

Book ID: 117608853
Publisher: Elsevier Science
Year: 2003
Tongue: English
Weight: 548 KB
Volume: 40
Category: Article
ISSN: 0896-6273
DOI: 10.1016/s0896-6273(03)00786-4

No coin nor oath required. For personal study only.

📜 SIMILAR VOLUMES

Regulation of alpha CaMKII activation by

Regulation of alpha CaMKII activation by its autophosphorylation and change in Ca2+ level in living cells

✍ Kenichi Katou; Taku Iwamoto; Satoshi Kida 📂 Article 📅 2007 🏛 Elsevier Science 🌐 English ⚖ 79 KB

The modulation of the excitability of pr

The modulation of the excitability of primary sensory neurons by Ca2+–CaM–CaMKII pathway

✍ Renjie Liang, Xianli Liu, Limin Wei, Wei Wang, Ping Zheng, Xisheng Yan, Yilin Zh 📂 Article 📅 2011 🏛 Springer Milan 🌐 English ⚖ 604 KB

Alternative splicing modulates the frequ

Alternative splicing modulates the frequency-dependent response of CaMKII to Ca2+ oscillations

✍ Bayer, K.U. 📂 Article 📅 2002 🏛 Nature Publishing Group 🌐 English ⚖ 304 KB

Autophosphorylation and ADP Regulate the

Autophosphorylation and ADP Regulate the Ca 2+ -Dependent Interaction of Recoverin with Rhodopsin Kinase †

✍ Satpaev, Daulet K.; Chen, Ching-Kang; Scotti, Anthony; Simon, Melvin I.; Hurley, 📂 Article 📅 1998 🏛 American Chemical Society 🌐 English ⚖ 87 KB

CaMKIIα enhances the desensitization of

CaMKIIα enhances the desensitization of NR2B-containing NMDA receptors by an autophosphorylation-dependent mechanism

✍ Suzanne Sessoms-Sikes; Yumiko Honse; David M. Lovinger; Roger J. Colbran 📂 Article 📅 2005 🏛 Elsevier Science 🌐 English ⚖ 474 KB

Protein phosphatase 2A–negative regulati

Protein phosphatase 2A–negative regulation of the protective signaling pathway of Ca2+/CaM-dependent ERK activation in cerebral ischemia

✍ Jie Zhao; Hui-wen Wu; Yun-jiao Chen; He-ping Tian; Li-xin Li; Xiao Han; Jun Guo 📂 Article 📅 2008 🏛 John Wiley and Sons 🌐 English ⚖ 600 KB

## Abstract Extracellular‐signal‐regulated kinase (ERK) undergoes rapid inactivation following the intense activation evoked by cerebral ischemia and reperfusion. However, the precise mechanism of this inactivation has not been elucidated. To investigate how phosphatases regulate the ERK cascade fo