CONFORMATION AND STABILITY OF THE HELIX-LOOP-HELIX DOMAIN OF THE ID PROTEIN FAMILY

被引：0
作者：
Kiewitzl, S. [1 ,2 ]
Kiso, Y. [2 ]
Cabrelel, C. [3 ]
机构：
[1] Univ Regensburg, Fac Chem & Pharm, D-93053 Regensburg, Germany
[2] Kyoto Pharmaceut Univ, Dept Med Chem, Ctr Frontier Res Med Sci, Yamashina Ku, Kyoto 6078412, Japan
[3] Ruhr Univ Bochum, Fac Chem & Biochem, D-44780 Bochum, Germany
来源：
BIOPOLYMERS | 2009年 / 92卷 / 04期
关键词：
FRAGMENTS;
D O I：
暂无
中图分类号：
Q5 [生物化学]; Q7 [分子生物学];
学科分类号：
071010 ; 081704 ;
摘要：
引用
收藏
页码：334 / 334
页数：1
相关论文
共 4 条
[1]   Synthesis and conformational analysis of Id2 protein fragments: impact of chain length and point mutations on the structural HLH motif [J].
Colombo, Noemi ;
Cabrele, Chiara .
JOURNAL OF PEPTIDE SCIENCE, 2006, 12 (08) :550-558
[2]   Synthesis and conformational properties of protein fragments based on the Id family of DNA-binding and cell-differentiation inhibitors [J].
Kiewitz, SD ;
Cabrele, C .
BIOPOLYMERS, 2005, 80 (06) :762-774
[3]   Switching from the unfolded to the folded state of the helix-loop-helix domain of the Id proteins based on the O-acyl isopeptide method [J].
Kiewitz, Sebastian D. ;
Kakizawa, Taeko ;
Kiso, Yoshiaki ;
Cabrele, Chiara .
JOURNAL OF PEPTIDE SCIENCE, 2008, 14 (11) :1209-1215
[4]   ID family of helix-loop-helix proteins in cancer [J].
Perk, J ;
Iavarone, A ;
Benezra, R .
NATURE REVIEWS CANCER, 2005, 5 (08) :603-614
1