✦ LIBER ✦

Phosphorylation-induced changes in backbone dynamics of the dematin headpiece C-terminal domain

✍ Scribed by Liliya Vugmeyster; C. James McKnight

Publisher: Springer Netherlands
Year: 2008
Tongue: English
Weight: 595 KB
Volume: 43
Category: Article
ISSN: 0925-2738
DOI: 10.1007/s10858-008-9289-4

No coin nor oath required. For personal study only.

📜 SIMILAR VOLUMES

Comparison of fast backbone dynamics at

Comparison of fast backbone dynamics at amide nitrogen and carbonyl sites in dematin headpiece C-terminal domain and its S74E mutant

✍ Liliya Vugmeyster; Dmitry Ostrovsky; Ying Li 📂 Article 📅 2010 🏛 Springer Netherlands 🌐 English ⚖ 481 KB

Analysis of Lanthanide-Induced Conformat

Analysis of Lanthanide-Induced Conformational Change of the C-Terminal Domain on Centrin

✍ Ya-Qin Zhao; Jun Yan; Li Song; Ya-Nan Feng; Ai-Hua Liang; Bin-Sheng Yang 📂 Article 📅 2011 🏛 Springer 🌐 English ⚖ 476 KB

Role of C-terminal domain phosphorylatio

Role of C-terminal domain phosphorylation in RNA polymerase II transcription through the nucleosome

✍ Y. V. Liu; D. J. Clark; V. Tchernajenko; M. E. Dahmus; V. M. Studitsky 📂 Article 📅 2003 🏛 Wiley (John Wiley & Sons) 🌐 English ⚖ 406 KB 👁 1 views

Phosphorylation-Induced Structural Chang

Phosphorylation-Induced Structural Changes in the C-Terminus of c-Fos Detected by CD and NMR

✍ Ting-Ting Hu; Shi-Zhong Luo 📂 Article 📅 2011 🏛 Springer Netherlands 🌐 English ⚖ 420 KB

Phosphorylation of c-Jun N-terminal Kina

Phosphorylation of c-Jun N-terminal Kinases (JNKs) is involved in the preventive effect of xanthorrhizol on cisplatin-induced hepatotoxicity

✍ Kyoung Ok Hong; Jae Kwan Hwang; Kwang-Kyun Park; Seong Hwan Kim 📂 Article 📅 2004 🏛 Springer-Verlag 🌐 English ⚖ 339 KB

Target-peptide-induced changes in the st

Target-peptide-induced changes in the structure and dynamics of calmodulin as probed by frequency domain fluorimetry of bound Tb(III)

✍ Patricia B. O'Hara; Mohammad A. Rahman; Anastasia Rowland; A.John Turjoman 📂 Article 📅 1995 🏛 Elsevier Science 🌐 English ⚖ 640 KB

Tb(III) luminescence is used to probe the conformational change induced in the calcium regulatory protein calmodulin upon binding to a target peptide. The luminescence lifetime for Tb(III) measured by frequency domain fluorimetry increases from 1278 microseconds for the calmodulin complex to 1496 mi