Amyloid conformation-dependent disaggregation revealed by a reconstituted yeast prion system
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H. Taguchi | Y. Sako | M. Shirouzu | S. Uchiyama | Elena Krayukhina | T. Yokoyama | Tatsuya Niwa | Y. Nakagawa | Motomasa Tanaka | Y. Tomabechi | K. Okamoto | M. Inaba | Shinju Sugiyama | Howard C.-H. Shen
[1] H. Schätzl,et al. From Seeds to Fibrils and Back: Fragmentation as an Overlooked Step in the Propagation of Prions and Prion-Like Proteins , 2020, Biomolecules.
[2] Y. Sugita,et al. Short disordered protein segment regulates cross-species transmission of a yeast prion , 2020, Nature Chemical Biology.
[3] Nadinath B. Nillegoda,et al. The Hsp70 chaperone network , 2019, Nature Reviews Molecular Cell Biology.
[4] M. Diamond,et al. Propagation of Protein Aggregation in Neurodegenerative Diseases. , 2019, Annual review of biochemistry.
[5] Y. Sako,et al. Single-Molecule Förster Resonance Energy Transfer Measurement Reveals the Dynamic Partially Ordered Structure of the Epidermal Growth Factor Receptor C-Tail Domain. , 2019, The journal of physical chemistry. B.
[6] A. Aguzzi,et al. Prions, prionoids and protein misfolding disorders , 2018, Nature Reviews Genetics.
[7] S. Uchiyama,et al. Sedimentation velocity analytical ultracentrifugation for characterization of therapeutic antibodies , 2018, Biophysical Reviews.
[8] Y. Yamaguchi,et al. Molecular basis for diversification of yeast prion strain conformation , 2018, Proceedings of the National Academy of Sciences.
[9] C. Dobson,et al. Protein Misfolding, Amyloid Formation, and Human Disease: A Summary of Progress Over the Last Decade. , 2017, Annual review of biochemistry.
[10] J. Shorter. Designer protein disaggregases to counter neurodegenerative disease. , 2017, Current opinion in genetics & development.
[11] J. Hoskins,et al. Substrate Discrimination by ClpB and Hsp104 , 2017, Front. Mol. Biosci..
[12] Nadinath B. Nillegoda,et al. Human Hsp70 Disaggregase Reverses Parkinson's-Linked α-Synuclein Amyloid Fibrils. , 2015, Molecular cell.
[13] N. Taniguchi,et al. Defining the Interaction of Human Soluble Lectin ZG16p and Mycobacterial Phosphatidylinositol Mannosides , 2015, Chembiochem : a European journal of chemical biology.
[14] Yusuke Komi,et al. Layers of structure and function in protein aggregation. , 2015, Nature chemical biology.
[15] B. Bukau,et al. Cooperation of Hsp70 and Hsp100 chaperone machines in protein disaggregation , 2015, Front. Mol. Biosci..
[16] H. Taguchi,et al. Single-molecule Analyses of the Dynamics of Heat Shock Protein 104 (Hsp104) and Protein Aggregates* , 2015, The Journal of Biological Chemistry.
[17] R. Wickner,et al. Yeast Prions: Structure, Biology, and Prion-Handling Systems , 2015, Microbiology and Molecular Reviews.
[18] S. Lindquist,et al. Distinct prion strains are defined by amyloid core structure and chaperone binding site dynamics. , 2014, Chemistry & biology.
[19] M. Mayer,et al. Hsp70 chaperone dynamics and molecular mechanism. , 2013, Trends in biochemical sciences.
[20] K. Caldwell,et al. Potentiated Hsp104 Variants Antagonize Diverse Proteotoxic Misfolding Events , 2013, Cell.
[21] J. Shorter,et al. Hsp104 drives "protein-only" positive selection of Sup35 prion strains encoding strong [PSI(+)]. , 2012, Chemistry & biology.
[22] J. Shorter,et al. Operational Plasticity Enables Hsp104 to Disaggregate Diverse Amyloid and Nonamyloid Clients , 2012, Cell.
[23] B. Bukau,et al. Hsp70 targets Hsp100 chaperones to substrates for protein disaggregation and prion fragmentation , 2012, The Journal of cell biology.
[24] Y. Chernoff,et al. Prions in Yeast , 2012, Genetics.
[25] Mathias Jucker,et al. The Amyloid State of Proteins in Human Diseases , 2012, Cell.
[26] M. Ter‐Avanesyan,et al. Amyloid-Mediated Sequestration of Essential Proteins Contributes to Mutant Huntingtin Toxicity in Yeast , 2012, PloS one.
[27] J. Shorter,et al. Purification of hsp104, a protein disaggregase. , 2011, Journal of visualized experiments : JoVE.
[28] Manuel Théry,et al. A new micropatterning method of soft substrates reveals that different tumorigenic signals can promote or reduce cell contraction levels. , 2011, Lab on a chip.
[29] Mick F. Tuite,et al. The prion hypothesis: from biological anomaly to basic regulatory mechanism , 2010, Nature Reviews Molecular Cell Biology.
[30] J. Weissman,et al. Differences in prion strain conformations result from non-native interactions in a nucleus. , 2010, Nature chemical biology.
[31] J. Weissman,et al. In vivo monitoring of the prion replication cycle reveals a critical role for Sis1 in delivering substrates to Hsp104. , 2008, Molecular cell.
[32] E. Craig,et al. Specificity of the J-protein Sis1 in the propagation of 3 yeast prions , 2008, Proceedings of the National Academy of Sciences.
[33] S. Lindquist,et al. Hsp104, Hsp70 and Hsp40 interplay regulates formation, growth and elimination of Sup35 prions , 2008, The EMBO journal.
[34] J. Richmond,et al. Variant-specific [PSI+] infection is transmitted by Sup35 polymers within [PSI+] aggregates with heterogeneous protein composition. , 2008, Molecular biology of the cell.
[35] B. Bukau,et al. Substrate threading through the central pore of the Hsp104 chaperone as a common mechanism for protein disaggregation and prion propagation , 2008, Molecular microbiology.
[36] Jonathan S. Weissman,et al. The structural basis of yeast prion strain variants , 2007, Nature.
[37] Jonathan S. Weissman,et al. The physical basis of how prion conformations determine strain phenotypes , 2006, Nature.
[38] Paolo De Los Rios,et al. Hsp70 chaperones accelerate protein translocation and the unfolding of stable protein aggregates by entropic pulling. , 2006, Proceedings of the National Academy of Sciences of the United States of America.
[39] R. Melki,et al. Molecular chaperones and the assembly of the prion Sup35p, an in vitro study , 2006, The EMBO journal.
[40] S. Walter,et al. Substrate Binding to the Molecular Chaperone Hsp104 and Its Regulation by Nucleotides* , 2005, Journal of Biological Chemistry.
[41] S. Müller,et al. Hsp70 Chaperones as Modulators of Prion Life Cycle , 2005, Genetics.
[42] A. Kishimoto,et al. Hsp104 Binds to Yeast Sup35 Prion Fiber but Needs Other Factor(s) to Sever It* , 2004, Journal of Biological Chemistry.
[43] S. Lindquist,et al. Hsp104 Catalyzes Formation and Elimination of Self-Replicating Sup35 Prion Conformers , 2004, Science.
[44] Roger Cooke,et al. Conformational variations in an infectious protein determine prion strain differences , 2004, Nature.
[45] D. Kryndushkin,et al. Yeast [PSI+] Prion Aggregates Are Formed by Small Sup35 Polymers Fragmented by Hsp104* , 2003, Journal of Biological Chemistry.
[46] D. Masison,et al. Saccharomyces cerevisiae Hsp70 mutations affect [PSI+] prion propagation and cell growth differently and implicate Hsp40 and tetratricopeptide repeat cochaperones in impairment of [PSI+]. , 2003, Genetics.
[47] D. E. Anderson,et al. Tobacco etch virus protease: mechanism of autolysis and rational design of stable mutants with wild-type catalytic proficiency. , 2001, Protein engineering.
[48] D. Masison,et al. A role for cytosolic hsp70 in yeast [PSI(+)] prion propagation and [PSI(+)] as a cellular stress. , 2000, Genetics.
[49] P. Schuck,et al. Size-distribution analysis of macromolecules by sedimentation velocity ultracentrifugation and lamm equation modeling. , 2000, Biophysical journal.
[50] S. Lindquist,et al. Self-Seeded Fibers Formed by Sup35, the Protein Determinant of [PSI +], a Heritable Prion-like Factor of S. cerevisiae , 1997, Cell.
[51] M. Nakai,et al. Binding of Mitochondrial Presequences to Yeast Cytosolic Heat Shock Protein 70 Depends on the Amphiphilicity of the Presequence (*) , 1996, The Journal of Biological Chemistry.
[52] S W Liebman,et al. Role of the chaperone protein Hsp104 in propagation of the yeast prion-like factor [psi+]. , 1995, Science.
[53] Susan Lindquist,et al. Protein disaggregation mediated by heat-shock protein Hspl04 , 1994, Nature.
[54] S. Lindquist,et al. Saccharomyces cerevisiae Hsp104 protein. Purification and characterization of ATP-induced structural changes. , 1994, The Journal of biological chemistry.
[55] S. Wickner,et al. Hsp104 and ClpB: protein disaggregating machines. , 2009, Trends in biochemical sciences.