Conserved methionine 165 of matrix protein contributes to the nuclear import and is essential for influenza A virus replication
出版年份 2018 全文链接
标题
Conserved methionine 165 of matrix protein contributes to the nuclear import and is essential for influenza A virus replication
作者
关键词
Influenza a virus, M1 protein, NP protein, CLUH, Reverse genetic
出版物
Virology Journal
Volume 15, Issue 1, Pages -
出版商
Springer Nature
发表日期
2018-12-03
DOI
10.1186/s12985-018-1056-x
参考文献
相关参考文献
注意:仅列出部分参考文献,下载原文获取全部文献信息。- Selective incorporation of vRNP into influenza A virions determined by its specific interaction with M1 protein
- (2017) Chutikarn Chaimayo et al. VIROLOGY
- Mutations in matrix protein 1 and nucleoprotein caused human-specific defects in nuclear exportation and viral assembly of an avian influenza H7N1 virus
- (2017) Khwansiri Ninpan et al. VIRUS RESEARCH
- Differential nucleocytoplasmic shuttling of the nucleoprotein of influenza a viruses and association with host tropism
- (2016) Jing Li et al. CELLULAR MICROBIOLOGY
- Involvement of an Arginine Triplet in M1 Matrix Protein Interaction with Membranes and in M1 Recruitment into Virus-Like Particles of the Influenza A(H1N1)pdm09 Virus
- (2016) Adeline Kerviel et al. PLoS One
- The host protein CLUH participates in the subnuclear transport of influenza virus ribonucleoprotein complexes
- (2016) Tomomi Ando et al. Nature Microbiology
- Two polar residues within C-terminal domain of M1 are critical for the formation of influenza A Virions
- (2015) Ke Zhang et al. CELLULAR MICROBIOLOGY
- Nucleocytoplasmic Shuttling of Influenza A Virus Proteins
- (2015) Jing Li et al. Viruses-Basel
- Characteristics of Nucleocytoplasmic Transport of H1N1 Influenza A Virus Nuclear Export Protein
- (2014) S. Gao et al. JOURNAL OF VIROLOGY
- The Methionine-aromatic Motif Plays a Unique Role in Stabilizing Protein Structure
- (2012) Christopher C. Valley et al. JOURNAL OF BIOLOGICAL CHEMISTRY
- Identification and Characterization of Three Novel Nuclear Export Signals in the Influenza A Virus Nucleoprotein
- (2012) M. Yu et al. JOURNAL OF VIROLOGY
- The Compensatory G88R Change Is Essential in Restoring the Normal Functions of Influenza A/WSN/33 Virus Matrix Protein 1 with a Disrupted Nuclear Localization Signal
- (2012) H. Xie et al. JOURNAL OF VIROLOGY
- Dissection of Influenza A Virus M1 Protein: pH-Dependent Oligomerization of N-Terminal Domain and Dimerization of C-Terminal Domain
- (2012) Ke Zhang et al. PLoS One
- An Overlapping Protein-Coding Region in Influenza A Virus Segment 3 Modulates the Host Response
- (2012) B. W. Jagger et al. SCIENCE
- Identification of a Novel Splice Variant Form of the Influenza A Virus M2 Ion Channel with an Antigenically Distinct Ectodomain
- (2012) Helen M. Wise et al. PLoS Pathogens
- Overlapping signals for translational regulation and packaging of influenza A virus segment 2
- (2011) H. M. Wise et al. NUCLEIC ACIDS RESEARCH
- Influenza virus assembly and budding
- (2011) Jeremy S. Rossman et al. VIROLOGY
- Influenza A virus replication is inhibited in IFN-λ2 and IFN-λ3 transfected or stimulated cells
- (2010) Darina Svetlikova et al. ANTIVIRAL RESEARCH
- The Lack of an Inherent Membrane Targeting Signal Is Responsible for the Failure of the Matrix (M1) Protein of Influenza A Virus To Bud into Virus-Like Particles
- (2010) D. Wang et al. JOURNAL OF VIROLOGY
- A Complicated Message: Identification of a Novel PB1-Related Protein Translated from Influenza A Virus Segment 2 mRNA
- (2009) H. M. Wise et al. JOURNAL OF VIROLOGY
- The In Situ Structural Characterization of the Influenza A Virus Matrix M1 Protein within a Virion
- (2009) Alexander Shishkov et al. PROTEIN AND PEPTIDE LETTERS
- Interaction of Polymerase Subunit PB2 and NP with Importin α1 Is a Determinant of Host Range of Influenza A Virus
- (2008) Gülsah Gabriel et al. PLoS Pathogens
Find Funding. Review Successful Grants.
Explore over 25,000 new funding opportunities and over 6,000,000 successful grants.
ExploreFind the ideal target journal for your manuscript
Explore over 38,000 international journals covering a vast array of academic fields.
Search