Structural basis for reversible amyloids of hnRNPA1 elucidates their role in stress granule assembly
出版年份 2019 全文链接
标题
Structural basis for reversible amyloids of hnRNPA1 elucidates their role in stress granule assembly
作者
关键词
-
出版物
Nature Communications
Volume 10, Issue 1, Pages -
出版商
Springer Science and Business Media LLC
发表日期
2019-05-01
DOI
10.1038/s41467-019-09902-7
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注意:仅列出部分参考文献,下载原文获取全部文献信息。- A Solid-State Conceptualization of Information Transfer from Gene to Message to Protein
- (2018) Masato Kato et al. Annual Review of Biochemistry
- Relationship of Sequence and Phase Separation in Protein Low-Complexity Regions
- (2018) Erik W. Martin et al. BIOCHEMISTRY
- Atomic structures of TDP-43 LCD segments and insights into reversible or pathogenic aggregation
- (2018) Elizabeth L. Guenther et al. NATURE STRUCTURAL & MOLECULAR BIOLOGY
- Atomic structures of FUS LC domain segments reveal bases for reversible amyloid fibril formation
- (2018) Feng Luo et al. NATURE STRUCTURAL & MOLECULAR BIOLOGY
- Atomic structures of low-complexity protein segments reveal kinked β sheets that assemble networks
- (2018) Michael P. Hughes et al. SCIENCE
- Atomic structures of TDP-43 LCD segments and insights into reversible or pathogenic aggregation
- (2018) Elizabeth L. Guenther et al. NATURE STRUCTURAL & MOLECULAR BIOLOGY
- Atomic structures of FUS LC domain segments reveal bases for reversible amyloid fibril formation
- (2018) Feng Luo et al. NATURE STRUCTURAL & MOLECULAR BIOLOGY
- Structural characterization of the D290V mutation site in hnRNPA2 low-complexity–domain polymers
- (2018) Dylan T. Murray et al. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
- Structural variation in amyloid-β fibrils from Alzheimer's disease clinical subtypes
- (2017) Wei Qiang et al. NATURE
- Biomolecular condensates: organizers of cellular biochemistry
- (2017) Salman F. Banani et al. NATURE REVIEWS MOLECULAR CELL BIOLOGY
- The Structure and Dynamics of Higher-Order Assemblies: Amyloids, Signalosomes, and Granules
- (2016) Hao Wu et al. CELL
- ATPase-Modulated Stress Granules Contain a Diverse Proteome and Substructure
- (2016) Saumya Jain et al. CELL
- The hnRNP family: insights into their role in health and disease
- (2016) Thomas Geuens et al. HUMAN GENETICS
- Structural, super-resolution microscopy analysis of paraspeckle nuclear body organization
- (2016) Jason A. West et al. JOURNAL OF CELL BIOLOGY
- Sequence Determinants of Intracellular Phase Separation by Complex Coacervation of a Disordered Protein
- (2016) Chi W. Pak et al. MOLECULAR CELL
- The activities of amyloids from a structural perspective
- (2016) Roland Riek et al. NATURE
- Solid-state NMR structure of a pathogenic fibril of full-length human α-synuclein
- (2016) Marcus D Tuttle et al. NATURE STRUCTURAL & MOLECULAR BIOLOGY
- Phase Separation: Linking Cellular Compartmentalization to Disease
- (2016) Adriano Aguzzi et al. TRENDS IN CELL BIOLOGY
- Principles and Properties of Stress Granules
- (2016) David S.W. Protter et al. TRENDS IN CELL BIOLOGY
- Hypo- and Hyper-Assembly Diseases of RNA–Protein Complexes
- (2016) Siddharth Shukla et al. TRENDS IN MOLECULAR MEDICINE
- Cross-β Polymerization of Low Complexity Sequence Domains
- (2016) Masato Kato et al. Cold Spring Harbor Perspectives in Biology
- Solid-state NMR structure of a pathogenic fibril of full-length human α-synuclein
- (2016) Marcus D Tuttle et al. NATURE STRUCTURAL & MOLECULAR BIOLOGY
- Distinct stages in stress granule assembly and disassembly
- (2016) Joshua R Wheeler et al. eLife
- Phase Separation by Low Complexity Domains Promotes Stress Granule Assembly and Drives Pathological Fibrillization
- (2015) Amandine Molliex et al. CELL
- A Liquid-to-Solid Phase Transition of the ALS Protein FUS Accelerated by Disease Mutation
- (2015) Avinash Patel et al. CELL
- Formation and Maturation of Phase-Separated Liquid Droplets by RNA-Binding Proteins
- (2015) Yuan Lin et al. MOLECULAR CELL
- Residue-by-Residue View of In Vitro FUS Granules that Bind the C-Terminal Domain of RNA Polymerase II
- (2015) Kathleen A. Burke et al. MOLECULAR CELL
- Phase Transition of a Disordered Nuage Protein Generates Environmentally Responsive Membraneless Organelles
- (2015) Timothy J. Nott et al. MOLECULAR CELL
- Structure of the toxic core of α-synuclein from invisible crystals
- (2015) Jose A. Rodriguez et al. NATURE
- Tunable assembly of amyloid-forming peptides into nanosheets as a retrovirus carrier
- (2015) Bin Dai et al. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
- SHELXT– Integrated space-group and crystal-structure determination
- (2015) George M. Sheldrick Acta Crystallographica A-Foundation and Advances
- Crystal structure refinement withSHELXL
- (2015) George M. Sheldrick Acta Crystallographica Section C-Structural Chemistry
- Structure-Based Design of Functional Amyloid Materials
- (2014) Dan Li et al. JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
- The amyloid state and its association with protein misfolding diseases
- (2014) Tuomas P. J. Knowles et al. NATURE REVIEWS MOLECULAR CELL BIOLOGY
- Presynaptic Localization of Smn and hnRNP R in Axon Terminals of Embryonic and Postnatal Mouse Motoneurons
- (2014) Benjamin Dombert et al. PLoS One
- Phosphorylation-Regulated Binding of RNA Polymerase II to Fibrous Polymers of Low-Complexity Domains
- (2013) Ilmin Kwon et al. CELL
- Altered Ribostasis: RNA-Protein Granules in Degenerative Disorders
- (2013) Mani Ramaswami et al. CELL
- Stress granules as crucibles of ALS pathogenesis
- (2013) Yun R. Li et al. JOURNAL OF CELL BIOLOGY
- Mutations in prion-like domains in hnRNPA2B1 and hnRNPA1 cause multisystem proteinopathy and ALS
- (2013) Hong Joo Kim et al. NATURE
- Hexanucleotide Repeats in ALS/FTD Form Length-Dependent RNA Foci, Sequester RNA Binding Proteins, and Are Neurotoxic
- (2013) Youn-Bok Lee et al. Cell Reports
- Towards automated crystallographic structure refinement withphenix.refine
- (2012) Pavel V. Afonine et al. ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY
- The tip of the iceberg: RNA-binding proteins with prion-like domains in neurodegenerative disease
- (2012) Oliver D. King et al. BRAIN RESEARCH
- Cell-free Formation of RNA Granules: Low Complexity Sequence Domains Form Dynamic Fibers within Hydrogels
- (2012) Masato Kato et al. CELL
- The RIP1/RIP3 Necrosome Forms a Functional Amyloid Signaling Complex Required for Programmed Necrosis
- (2012) Jixi Li et al. CELL
- Cell-free Formation of RNA Granules: Bound RNAs Identify Features and Components of Cellular Assemblies
- (2012) Tina W. Han et al. CELL
- The Amyloid State of Proteins in Human Diseases
- (2012) David Eisenberg et al. CELL
- Requirements for Stress Granule Recruitment of Fused in Sarcoma (FUS) and TAR DNA-binding Protein of 43 kDa (TDP-43)
- (2012) Eva Bentmann et al. JOURNAL OF BIOLOGICAL CHEMISTRY
- Phase transitions in the assembly of multivalent signalling proteins
- (2012) Pilong Li et al. NATURE
- Toxic fibrillar oligomers of amyloid- have cross- structure
- (2012) J. C. Stroud et al. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
- Out-of-register -sheets suggest a pathway to toxic amyloid aggregates
- (2012) C. Liu et al. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
- Atomic View of a Toxic Amyloid Small Oligomer
- (2012) Arthur Laganowsky et al. SCIENCE
- Molecular Determinants and Genetic Modifiers of Aggregation and Toxicity for the ALS Disease Protein FUS/TLS
- (2011) Zhihui Sun et al. PLOS BIOLOGY
- XDS
- (2010) Wolfgang Kabsch ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY
- Features and development ofCoot
- (2010) P. Emsley et al. ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY
- hnRNP K interacts with RNA binding motif protein 42 and functions in the maintenance of cellular ATP level during stress conditions
- (2009) Toshiyuki Fukuda et al. GENES TO CELLS
- TDP-43 Is Intrinsically Aggregation-prone, and Amyotrophic Lateral Sclerosis-linked Mutations Accelerate Aggregation and Increase Toxicity
- (2009) Brian S. Johnson et al. JOURNAL OF BIOLOGICAL CHEMISTRY
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