Preferential domain orientation of HMGB2 determined by the weak intramolecular interactions mediated by the interdomain linker-Reference-Cited by-同舟云学术

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Preferential domain orientation of HMGB2 determined by the weak intramolecular interactions mediated by the interdomain linker

Published:2013-06 Issue: Volume:419 Page:212-223
ISSN:0301-0104
Container-title:Chemical Physics
language:en
Short-container-title:Chemical Physics

Author:

Uewaki Jun-ichi,Kamikubo Hironari,Kurita Jun-ichi,Hiroguchi Noriteru,Moriuchi Hiroshi,Yoshida Michiteru,Kataoka Mikio,Utsunomiya-Tate Naoko,Tate Shin-ichi

Funder

Japan Society for the Promotion of Science (JSPS)

JST-PRESTO

Grant-in-Aid of the Creative Scientific Research Program

JSPS

Publisher

Elsevier BV

Subject

Physical and Theoretical Chemistry,General Physics and Astronomy

Reference46 articles.

1. The unfoldomics decade: an update on intrinsically disordered proteins

2. Model of a Six Immunoglobulin-Like Domain Fragment of Filamin A (16–21) Built Using Residual Dipolar Couplings

3. Domain Orientation and Dynamics in Multidomain Proteins from Residual Dipolar Couplings

4. Complementary Use of NMR to X-ray Crystallography for the Analysis of Protein Morphological Change in Solution;Tate,2011

5. Anisotropic Nuclear Spin Interactions for the Morphology Analysis of Proteins in Solution by NMR Spectroscopy

Cited by 1 articles. 订阅此论文施引文献订阅此论文施引文献，注册后可以免费订阅5篇论文的施引文献，订阅后可以查看论文全部施引文献

1. Redox-sensitive structural change in the A-domain of HMGB1 and its implication for the binding to cisplatin modified DNA;Biochemical and Biophysical Research Communications;2013-11

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