Preferred side-chain conformation of arginine residues in a triple-helical structure-Reference-Cited by-同舟云学术

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Preferred side-chain conformation of arginine residues in a triple-helical structure

Published:2014-07-23 Issue:10 Volume:101 Page:1000-1009
ISSN:0006-3525
Container-title:Biopolymers
language:en
Short-container-title:Biopolymers

Author:

Okuyama Kenji¹,Haga Mitsuru²,Noguchi Keiichi²,Tanaka Toshiki³

Affiliation:

1. Department of Macromolecular Science; Graduate School of Science; Osaka University; Toyonaka Osaka 560-0043 Japan

2. Graduate School of Technology; Tokyo University of Agriculture and Technology; Koganei Tokyo 184-8588 Japan

3. Department of Materials Sciences; Graduate School of Engineering; Nagoya Institute of Technology; Gokiso-chou Nagoya 466-8555 Japan

Publisher

Wiley

Subject

Organic Chemistry,Biomaterials,Biochemistry,General Medicine,Biophysics

Reference37 articles.

1. Primary Structure

2. Structure of Collagen

3. Revisiting the Molecular Structure of Collagen

4. The Structure of Collagen

5. The molecular structure of collagen

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1. The coordinated activities of collagen VI and XII in maintenance of tissue structure, function and repair: evidence for a physical interaction;Frontiers in Molecular Biosciences;2024-03-28

2. Arginine (315) is required for the PLIN2-CGI-58 interface and plays a functional role in regulating nascent LDs formation in bovine adipocytes;Genomics;2024-03

3. Terminal repeats impact collagen triple-helix stability through hydrogen bonding;Chemical Science;2022

4. The structure of collagen;Biophysical and Chemical Properties of Collagen Biophysical Applications;2019-11

5. Variation in the Yaa position of collagen peptides containing azaGlycine;Chemical Communications;2018

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