- Home
- Publications
- Publication Search
- Publication Details
Title
Host ANP32A mediates the assembly of the influenza virus replicase
Authors
Keywords
-
Journal
NATURE
Volume 587, Issue 7835, Pages 638-643
Publisher
Springer Science and Business Media LLC
Online
2020-11-19
DOI
10.1038/s41586-020-2927-z
References
Ask authors/readers for more resources
Related references
Note: Only part of the references are listed.- A Structure-Based Model for the Complete Transcription Cycle of Influenza Polymerase
- (2020) Joanna M. Wandzik et al. CELL
- Structure and Function of Influenza Polymerase
- (2020) Joanna M. Wandzik et al. Cold Spring Harbor Perspectives in Medicine
- Interplay between Influenza Virus and the Host RNA Polymerase II Transcriptional Machinery
- (2019) Alexander P. Walker et al. TRENDS IN MICROBIOLOGY
- ANP32 proteins are essential for influenza virus replication in human cells
- (2019) Ecco Staller et al. JOURNAL OF VIROLOGY
- Host Determinants of Influenza RNA Synthesis
- (2019) Thomas P. Peacock et al. Annual Review of Virology
- Structural insight into RNA synthesis by influenza D polymerase
- (2019) Qi Peng et al. Nature Microbiology
- Structures of influenza A virus RNA polymerase offer insight into viral genome replication
- (2019) Haitian Fan et al. NATURE
- Structure of the human metapneumovirus polymerase phosphoprotein complex
- (2019) Junhua Pan et al. NATURE
- Structure and Function of the Influenza Virus Transcription and Replication Machinery
- (2019) Ervin Fodor et al. Cold Spring Harbor Perspectives in Medicine
- A Mechanism for the Activation of the Influenza Virus Transcriptase
- (2018) Itziar Serna Martin et al. MOLECULAR CELL
- SWISS-MODEL: homology modelling of protein structures and complexes
- (2018) Andrew Waterhouse et al. NUCLEIC ACIDS RESEARCH
- Influenza
- (2018) Florian Krammer et al. Nature Reviews Disease Primers
- Differential Splicing of ANP32A in Birds Alters Its Ability to Stimulate RNA Synthesis by Restricted Influenza Polymerase
- (2018) Steven F. Baker et al. Cell Reports
- MotionCor2: anisotropic correction of beam-induced motion for improved cryo-electron microscopy
- (2017) Shawn Q Zheng et al. NATURE METHODS
- cryoSPARC: algorithms for rapid unsupervised cryo-EM structure determination
- (2017) Ali Punjani et al. NATURE METHODS
- Addressing preferred specimen orientation in single-particle cryo-EM through tilting
- (2017) Yong Zi Tan et al. NATURE METHODS
- Measuring the effects of particle orientation to improve the efficiency of electron cryomicroscopy
- (2017) Katerina Naydenova et al. Nature Communications
- Functional Insights into ANP32A-Dependent Influenza A Virus Polymerase Host Restriction
- (2017) Patricia Domingues et al. Cell Reports
- Model-based local density sharpening of cryo-EM maps
- (2017) Arjen J Jakobi et al. eLife
- Introducing the Proceedings of the CCP-EM Spring Symposium
- (2017) Tom Burnley Acta Crystallographica Section D-Structural Biology
- Gctf: Real-time CTF determination and correction
- (2016) Kai Zhang JOURNAL OF STRUCTURAL BIOLOGY
- Influenza Polymerase Can Adopt an Alternative Configuration Involving a Radical Repacking of PB2 Domains
- (2016) Eric Thierry et al. MOLECULAR CELL
- Species difference in ANP32A underlies influenza A virus polymerase host restriction
- (2016) Jason S. Long et al. NATURE
- Structural basis of an essential interaction between influenza polymerase and Pol II CTD
- (2016) Maria Lukarska et al. NATURE
- Cryo-EM Structure of Influenza Virus RNA Polymerase Complex at 4.3 Å Resolution
- (2015) Shenghai Chang et al. MOLECULAR CELL
- Crystal structure of the RNA-dependent RNA polymerase from influenza C virus
- (2015) Narin Hengrung et al. NATURE
- Influenza virus activation of the interferon system
- (2015) Marian J. Killip et al. VIRUS RESEARCH
- pp32 and APRIL are host cell-derived regulators of influenza virus RNA synthesis from cRNA
- (2015) Kenji Sugiyama et al. eLife
- Structure of influenza A polymerase bound to the viral RNA promoter
- (2014) Alexander Pflug et al. NATURE
- Deciphering key features in protein structures with the new ENDscript server
- (2014) Xavier Robert et al. NUCLEIC ACIDS RESEARCH
- Influenza A viruses with different amino acid residues at PB2-627 display distinct replication properties in vitro and in vivo : Revealing the sequence plasticity of PB2-627 position
- (2014) Alex W.H. Chin et al. VIROLOGY
- Host Restriction of Influenza Virus Polymerase Activity by PB2 627E Is Diminished on Short Viral Templates in a Nucleoprotein-Independent Manner
- (2013) D. Paterson et al. JOURNAL OF VIROLOGY
- RELION: Implementation of a Bayesian approach to cryo-EM structure determination
- (2012) Sjors H.W. Scheres JOURNAL OF STRUCTURAL BIOLOGY
- NIH Image to ImageJ: 25 years of image analysis
- (2012) Caroline A Schneider et al. NATURE METHODS
- Adaptive mutations in NEP compensate for defective H5N1 RNA replication in cultured human cells
- (2012) Benjamin Mänz et al. Nature Communications
- MultiBac: expanding the research toolbox for multiprotein complexes
- (2011) Christoph Bieniossek et al. TRENDS IN BIOCHEMICAL SCIENCES
- Features and development ofCoot
- (2010) P. Emsley et al. ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY
- PHENIX: a comprehensive Python-based system for macromolecular structure solution
- (2010) Paul D. Adams et al. ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY
- Biological and Structural Characterization of a Host-Adapting Amino Acid in Influenza Virus
- (2010) Shinya Yamada et al. PLoS Pathogens
- NS2/NEP protein regulates transcription and replication of the influenza virus RNA genome
- (2009) Nicole C. Robb et al. JOURNAL OF GENERAL VIROLOGY
- Adaptive strategies of the influenza virus polymerase for replication in humans
- (2009) Andrew Mehle et al. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
Discover Peeref hubs
Discuss science. Find collaborators. Network.
Join a conversationBecome a Peeref-certified reviewer
The Peeref Institute provides free reviewer training that teaches the core competencies of the academic peer review process.
Get Started