Specification of binding modes between a transmembrane peptide mimic of ATP6V0C and polytopic E5 of human papillomavirus-16
Author:
Affiliation:
1. Institute of Biophotonics, School of Biomedical Science and Engineering, National Yang-Ming University, 155, Li-Nong St., Sec. 2, Taipei 112, Taiwan
Funder
Ministry of Science and Technology, Taiwan
Publisher
Informa UK Limited
Subject
Molecular Biology,General Medicine,Structural Biology
Link
https://www.tandfonline.com/doi/pdf/10.1080/07391102.2017.1364671
Reference52 articles.
1. Vacuolar H+-ATPase Mutants Transform Cells and Define a Binding Site for the Papillomavirus E5 Oncoprotein
2. Membrane physical properties influence transmembrane helix formation
3. Genomic Cloning and Characterization of the Nonoccupied Allele Corresponding to the Integration Site of Human Papillomavirus Type 16 DNA in the Cervical Cancer Cell Line SiHa
4. DNA sequence of the HPV-16 E5 ORF and the structural conservation of its encoded protein
5. Enhanced recognition of protein transmembrane domains with prediction-based structural profiles
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1. Molecular dynamics simulation perception study of the binding affinity performance for main protease of SARS-CoV-2;Journal of Biomolecular Structure and Dynamics;2020-11-23
2. Hallmarks of HPV carcinogenesis: The role of E6, E7 and E5 oncoproteins in cellular malignancy;Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanisms;2019-02
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