✦ LIBER ✦

Translocation of PDK-1 to the plasma membrane is important in allowing PDK-1 to activate protein kinase B

✍ Scribed by Karen E. Anderson; John Coadwell; Len R. Stephens; Phillip T. Hawkins

Book ID: 118606719
Publisher: Elsevier Science
Year: 1998
Tongue: English
Weight: 306 KB
Volume: 8
Category: Article
ISSN: 0960-9822
DOI: 10.1016/s0960-9822(98)70274-x

No coin nor oath required. For personal study only.

📜 SIMILAR VOLUMES

Insulin-Induced Translocation of Protein

Insulin-Induced Translocation of Protein Kinase B to the Plasma Membrane in Rat Adipocytes

✍ Olga Göransson; Jonny Wijkander; Vincent Manganiello; Eva Degerman 📂 Article 📅 1998 🏛 Elsevier Science 🌐 English ⚖ 312 KB

Rational Drug Design || Use of a Fluores

Rational Drug Design || Use of a Fluorescent ATP Analog to Probe the Allosteric Conformational Change in the Active Site of the Protein Kinase PDK1

✍ Zheng, Yi 📂 Article 📅 2012 🏛 Humana Press ⚖ 308 KB

Impaired phosphorylation and insulin-sti

Impaired phosphorylation and insulin-stimulated translocation to the plasma membrane of protein kinase B/Akt in adipocytes from Type II diabetic subjects

✍ E. Carvalho; B. Eliasson; C. Wesslau; U. Smith 📂 Article 📅 2000 🏛 Springer 🌐 English ⚖ 236 KB

The C2 domain of protein kinase Cα is di

The C2 domain of protein kinase Cα is directly involved in the diacylglycerol-dependent binding of the C1 domain to the membrane

✍ Pablo Conesa-Zamora; Juan C Gómez-Fernández; Senena Corbalán-Garcı́a 📂 Article 📅 2000 🏛 Elsevier Science 🌐 English ⚖ 454 KB

Vitamin D receptor is not required for t

Vitamin D receptor is not required for the rapid actions of 1,25-dihydroxyvitamin D3 to increase intracellular calcium and activate protein kinase C in mouse osteoblasts

✍ Ramesh K. Wali; Juan Kong; Michael D. Sitrin; Marc Bissonnette; Yan Chun Li 📂 Article 📅 2003 🏛 John Wiley and Sons 🌐 English ⚖ 190 KB

## Abstract The rapid, non‐genomic actions of 1,25‐dihydroxyvitamin D~3~ [1,25(OH)~2~D~3~] have been well described, however, the role of the nuclear vitamin D receptor (VDR) in this pathway remains unclear. To address this question, we used VDR(+/+) and VDR(−/−) osteoblasts isolated from wild‐type

Basic region of residues 228–231 of prot

Basic region of residues 228–231 of protein kinase CK1α is involved in its interaction with axin: Binding to axin does not affect the kinase activity

✍ Pablo Sobrado; Ana Jedlicki; Victor H. Bustos; Catherine C. Allende; Jorge E. Al 📂 Article 📅 2005 🏛 John Wiley and Sons 🌐 English ⚖ 148 KB 👁 1 views

Protein kinase CK1, also known as casein kinase 1, participates in the phosphorylation of b-catenin, which regulates the functioning of the Wnt signaling cascade involved in embryogenesis and carcinogenesis. b-catenin phosphorylation occurs in a multiprotein complex assembled on the scaffold protein