N-terminal truncations on L1 proteins of human papillomaviruses promote their soluble expression in Escherichia coli and self-assembly in vitro-Reference-Cited by-同舟云学术

N-terminal truncations on L1 proteins of human papillomaviruses promote their soluble expression in Escherichia coli and self-assembly in vitro

Published:2018-09-26 Issue:1 Volume:7 Page:1-12
ISSN:2222-1751
Container-title:Emerging Microbes & Infections
language:en
Short-container-title:Emerging Microbes & Infections

Author:

Wei Minxi¹,Wang Daning²,Li Zhihai¹,Song Shuo¹,Kong Xianglin¹,Mo Xiaobing¹,Yang Yurou¹,He Maozhou²,Li Zhongyi³,Huang Bo³,Lin Zhijie³,Pan Huirong³,Zheng Qingbing²,Yu Hai²,Gu Ying¹²,Zhang Jun²,Li Shaowei¹²^ORCID,Xia Ningshao¹²

Affiliation:

1. State Key Laboratory of Molecular Vaccinology and Molecular Diagnostics, School of Life SciencesXiamen University 361102 Xiamen China

2. National Institute of Diagnostics and Vaccine Development in Infectious Disease, School of Public HealthXiamen University 361102 Xiamen China

3. Xiamen Innovax Biotech Company, Ltd 361022 Xiamen China

Funder

National Natural Science Foundation of China (National Science Foundation of China)

Natural Science Foundation of Fujian Province (Fujian Provincial Natural Science Foundation)

Publisher

Informa UK Limited

Subject

Virology,Infectious Diseases,Drug Discovery,General Medicine,Immunology,Microbiology,Parasitology,Epidemiology

Link

http://www.nature.com/articles/s41426-018-0158-2.pdf

Reference59 articles.

1. Diseases associated with human papillomavirus infection

2. Evaluation of tributyltin toxicity in Chinese rare minnow larvae by abnormal behavior, energy metabolism and endoplasmic reticulum stress

3. Cross-roads in the classification of papillomaviruses

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