Solution structure, dynamics and function investigation of Kringle domain of human receptor tyrosine kinase-like orphan receptor 1-Reference-Cited by-同舟云学术

Solution structure, dynamics and function investigation of Kringle domain of human receptor tyrosine kinase-like orphan receptor 1

Published:2019-07-09 Issue:8 Volume:38 Page:2229-2239
ISSN:0739-1102
Container-title:Journal of Biomolecular Structure and Dynamics
language:en
Short-container-title:Journal of Biomolecular Structure and Dynamics

Author:

Ma Xiaofang¹²,Liu Bin¹²,Yang Jiahui³^ORCID,Hu Kaifeng¹⁴^ORCID

Affiliation:

1. State Key Laboratory of Phytochemistry and Plant Resources in West China, Kunming Institute of Botany, Chinese Academy of Science, Kunming, People’s Republic of China;

2. University of the Chinese Academy of Sciences, Beijing, People’s Republic of China;

3. School of Basic Medicine, Chengdu University of Traditional Chinese Medicine, Chengdu, People’s Republic of China;

4. Innovative Institute of Chinese Medicine and Pharmacy, Chengdu University of Traditional Chinese Medicine, Chengdu, People’s Republic of China

Funder

National Key Research and Development Program of China

National Natural Science Foundation of China

Yunnan Provincial Science and Technology Department

Publisher

Informa UK Limited

Subject

Molecular Biology,General Medicine,Structural Biology

Link

https://www.tandfonline.com/doi/pdf/10.1080/07391102.2019.1635914

Reference59 articles.

1. Solution structure of the kringle 4 domain from human plasminogen by 1H nuclear magnetic resonance spectroscopy and distance geometry

2. Solution Structure and Functional Characterization of Human Plasminogen Kringle 5,

3. Kringle Structures and Antiangiogenesis

4. Nuclear Magnetic Resonance (NMR) Solution Structure, Dynamics, and Binding Properties of the Kringle IV Type 8 Module of Apolipoprotein(a),

5. Prediction of Tight Turns and Their Types in Proteins

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