Bioinformatic identification of previously unrecognized amyloidogenic proteins
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M. P. Hughes | D. Eisenberg | L. Salwínski | R. Abskharon | K. Murray | Gregory M. Rosenberg | M. Hughes
[1] M. P. Hughes,et al. Identifying amyloid-related diseases by mapping mutations in low-complexity protein domains to pathologies , 2022, Nature Structural & Molecular Biology.
[2] M. P. Hughes,et al. Extended β-Strands Contribute to Reversible Amyloid Formation. , 2022, ACS nano.
[3] S. McKnight,et al. How do protein domains of low sequence complexity work? , 2021, RNA.
[4] D. Eisenberg,et al. The expanding amyloid family: Structure, stability, function, and pathogenesis , 2021, Cell.
[5] Peter B. McGarvey,et al. UniProt: the universal protein knowledgebase in 2021 , 2020, Nucleic Acids Res..
[6] R. Tycko,et al. Transiently structured head domains control intermediate filament assembly , 2020, Proceedings of the National Academy of Sciences.
[7] S. McKnight,et al. Dynamic structural order of a low-complexity domain facilitates assembly of intermediate filaments , 2020, Proceedings of the National Academy of Sciences.
[8] E. Rogaeva,et al. Neuropathologic description of CHCHD10 mutated amyotrophic lateral sclerosis , 2020, Neurology: Genetics.
[9] D. Eisenberg,et al. Structure-based inhibitors halt prion-like seeding by Alzheimer's disease–and tauopathy–derived brain tissue samples , 2019, The Journal of Biological Chemistry.
[10] M. Batchelor,et al. Desmin forms toxic, seeding-competent amyloid aggregates that persist in muscle fibers , 2019, Proceedings of the National Academy of Sciences.
[11] B. Reif,et al. Cysteine oxidation triggers amyloid fibril formation of the tumor suppressor p16INK4A , 2019, bioRxiv.
[12] Alan F. Scott,et al. OMIM.org: leveraging knowledge across phenotype–gene relationships , 2018, Nucleic Acids Res..
[13] D. Eisenberg,et al. Identification of two principal amyloid-driving segments in variable domains of Ig light chains in systemic light-chain amyloidosis , 2018, The Journal of Biological Chemistry.
[14] R. Tycko,et al. Structural characterization of the D290V mutation site in hnRNPA2 low-complexity–domain polymers , 2018, Proceedings of the National Academy of Sciences.
[15] R. Pappu,et al. A Molecular Grammar Governing the Driving Forces for Phase Separation of Prion-like RNA Binding Proteins , 2018, Cell.
[16] S. Alberti,et al. Prion-like low-complexity sequences: Key regulators of protein solubility and phase behavior , 2018, The Journal of Biological Chemistry.
[17] E. L. Guenther,et al. Atomic Structures of Segments from TDP-43 LCD and insight into Reversible and Pathogenic Aggregation , 2018, Nature Structural & Molecular Biology.
[18] M. P. Hughes,et al. Atomic structures of low-complexity protein segments reveal kinked β sheets that assemble networks , 2018, Science.
[19] Nicolas L. Fawzi,et al. Mechanistic View of hnRNPA2 Low-Complexity Domain Structure, Interactions, and Phase Separation Altered by Mutation and Arginine Methylation. , 2018, Molecular cell.
[20] Chunlei Liu,et al. ClinVar: improving access to variant interpretations and supporting evidence , 2017, Nucleic Acids Res..
[21] K. Talbot,et al. Pathogenesis of FUS-associated ALS and FTD: insights from rodent models , 2016, Acta Neuropathologica Communications.
[22] C. Brangwynne,et al. The disordered P granule protein LAF-1 drives phase separation into droplets with tunable viscosity and dynamics , 2015, Proceedings of the National Academy of Sciences.
[23] S. Stagg,et al. TFG clusters COPII‐coated transport carriers and promotes early secretory pathway organization , 2015, The EMBO journal.
[24] Timothy D. Craggs,et al. Phase Transition of a Disordered Nuage Protein Generates Environmentally Responsive Membraneless Organelles , 2015, Molecular cell.
[25] P. Tsai,et al. A novel TFG mutation causes Charcot-Marie-Tooth disease type 2 and impairs TFG function , 2014, Neurology.
[26] N. Nukina,et al. Intranuclear Aggregation of Mutant FUS/TLS as a Molecular Pathomechanism of Amyotrophic Lateral Sclerosis* , 2013, The Journal of Biological Chemistry.
[27] Kun Huang,et al. Disulfide bonds in amyloidogenesis diseases related proteins , 2013, Proteins.
[28] Michael Benatar,et al. Prion-like domain mutations in hnRNPs cause multisystem proteinopathy and ALS , 2013, Nature.
[29] Stavros J. Hamodrakas,et al. A Consensus Method for the Prediction of ‘Aggregation-Prone’ Peptides in Globular Proteins , 2013, PloS one.
[30] S. Tsuji,et al. The TRK-fused gene is mutated in hereditary motor and sensory neuropathy with proximal dominant involvement. , 2012, American journal of human genetics.
[31] Jimin Pei,et al. Cell-free Formation of RNA Granules: Low Complexity Sequence Domains Form Dynamic Fibers within Hydrogels , 2012, Cell.
[32] J. Haines,et al. Mutations in UBQLN2 cause dominant X-linked juvenile and adult onset ALS and ALS/dementia , 2011, Nature.
[33] D. Seldin,et al. Amyloidosis: pathogenesis and new therapeutic options. , 2011, Journal of clinical oncology : official journal of the American Society of Clinical Oncology.
[34] Juliet A. Ellis,et al. Novel LMNA mutations in patients with Emery‐Dreifuss muscular dystrophy and functional characterization of four LMNA mutations , 2011, Human mutation.
[35] David Eisenberg,et al. Identifying the amylome, proteins capable of forming amyloid-like fibrils , 2010, Proceedings of the National Academy of Sciences.
[36] John Q Trojanowski,et al. Mutations in TDP-43 link glycine-rich domain functions to amyotrophic lateral sclerosis. , 2009, Human molecular genetics.
[37] L. Serpell,et al. Amyloid fibrils , 2008, Prion.
[38] Christina Zeitz,et al. Night blindness–associated mutations in the ligand‐binding, cysteine‐rich, and intracellular domains of the metabotropic glutamate receptor 6 abolish protein trafficking , 2007, Human mutation.
[39] A. Wills,et al. Oculopharyngeal muscular dystrophy: a point mutation which mimics the effect of the PABPN1 gene triplet repeat expansion mutation , 2005, Journal of Medical Genetics.
[40] M. R. Nilsson. Techniques to study amyloid fibril formation in vitro. , 2004, Methods.
[41] R. Rudolph,et al. Trinucleotide expansions leading to an extended poly‐l‐alanine segment in the poly (A) binding protein PABPN1 cause fibril formation , 2003, Protein science : a publication of the Protein Society.
[42] H. Levine. Quantification of beta-sheet amyloid fibril structures with thioflavin T. , 1999, Methods in enzymology.
[43] C. Deber,et al. Alpha-helical, but not beta-sheet, propensity of proline is determined by peptide environment. , 1996, Proceedings of the National Academy of Sciences of the United States of America.
[44] John C. Wootton,et al. Statistics of Local Complexity in Amino Acid Sequences and Sequence Databases , 1993, Comput. Chem..
[45] M. Levitt. Conformational preferences of amino acids in globular proteins. , 1978, Biochemistry.