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Research Paper

Protein Aggregation and Polyasparagine-Mediated Cellular Toxicity in Saccharomyces cerevisiae

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Pages 144-153 | Received 23 May 2007, Accepted 26 Jun 2007, Published online: 11 Jul 2007

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Stephanie Valtierra, Zhiqiang Du & Liming Li. (2017) Analysis of Small Critical Regions of Swi1 Conferring Prion Formation, Maintenance, and Transmission. Molecular and Cellular Biology 37:20.
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Anton A. Nizhnikov, Kirill S. Antonets, Stanislav A. Bondarev, Sergey G. Inge-Vechtomov & Irina L. Derkatch. (2016) Prions, amyloids, and RNA: Pieces of a puzzle. Prion 10:3, pages 182-206.
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Alexander I. Alexandrov & Michael D. Ter-Avanesyan. (2013) Could yeast prion domains originate from polyQ/N tracts?. Prion 7:3, pages 209-214.
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Emily T. Crow, Zhiqiang Du & Liming Li. (2011) A Small, Glutamine-Free Domain Propagates the [SWI+] Prion in Budding Yeast. Molecular and Cellular Biology 31:16, pages 3436-3444.
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James A. Toombs, Blake R. McCarty & Eric D. Ross. (2010) Compositional Determinants of Prion Formation in Yeast. Molecular and Cellular Biology 30:1, pages 319-332.
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Articles from other publishers (14)

Taylor Stewart, Benjamin E. Wolfe & Stephen M. Fuchs. (2021) Defining the role of the polyasparagine repeat domain of the S. cerevisiae transcription factor Azf1p. PLOS ONE 16:5, pages e0247285.
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Viet Hoang Man, Yuan Zhang, Christopher Roland & Celeste Sagui. 2018. Biomolecular Simulations in Structure-Based Drug Discovery. Biomolecular Simulations in Structure-Based Drug Discovery 301 324 .
Karl N. Blodgett, Joshua L. Fischer, Jaeyeon Lee, Soo Hyuk Choi & Timothy S. Zwier. (2018) Conformation-Specific Spectroscopy of Asparagine-Containing Peptides: Influence of Single and Adjacent Asn Residues on Inherent Conformational Preferences. The Journal of Physical Chemistry A 122:44, pages 8762-8775.
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Kobi Simpson-Lavy, Tianchang Xu, Mark Johnston & Martin Kupiec. (2017) The Std1 Activator of the Snf1/AMPK Kinase Controls Glucose Response in Yeast by a Regulated Protein Aggregation. Molecular Cell 68:6, pages 1120-1133.e3.
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Heledd M. Davies, Stephanie D. Nofal, Emilia J. McLaughlin & Andrew R. Osborne. (2017) Repetitive sequences in malaria parasite proteins. FEMS Microbiology Reviews 41:6, pages 923-940.
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Yuan Zhang, Viet Hoang Man, Christopher Roland & Celeste Sagui. (2016) Amyloid Properties of Asparagine and Glutamine in Prion-like Proteins. ACS Chemical Neuroscience 7:5, pages 576-587.
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K. S. Antonets, H. M. Sargsyan & A. A. Nizhnikov. (2016) A glutamine/asparagine-rich fragment of Gln3, but not the full-length protein, aggregates in Saccharomyces cerevisiae. Biochemistry (Moscow) 81:4, pages 407-413.
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Xiaomeng Lu & Regina M. Murphy. (2015) Asparagine Repeat Peptides: Aggregation Kinetics and Comparison with Glutamine Repeats. Biochemistry 54:31, pages 4784-4794.
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Vasant Muralidharan, Anna Oksman, Priya Pal, Susan Lindquist & Daniel E. Goldberg. (2012) Plasmodium falciparum heat shock protein 110 stabilizes the asparagine repeat-rich parasite proteome during malarial fevers. Nature Communications 3:1.
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Choonkyun Jung, Yeon-Ki Kim, Nam Iee Oh, Jae Sung Shim, Jun Sung Seo, Yang Do Choi, Baek Hie Nahm & Jong-Joo Cheong. (2012) Quadruple 9-mer-based protein binding microarray analysis confirms AACnG as the consensus nucleotide sequence sufficient for the specific binding of AtMYB44. Molecules and Cells 34:6, pages 531-537.
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Bea Unterer, Cord-Michael Becker & Carmen Villmann. (2012) The Importance of TM3-4 Loop Subdomains for Functional Reconstitution of Glycine Receptors by Independent Domains. Journal of Biological Chemistry 287:46, pages 39205-39215.
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Natalia V. Kochneva-Pervukhova, Alexander I. Alexandrov & Michael D. Ter-Avanesyan. (2012) Amyloid-Mediated Sequestration of Essential Proteins Contributes to Mutant Huntingtin Toxicity in Yeast. PLoS ONE 7:1, pages e29832.
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Emily T. Crow & Liming Li. (2011) Newly identified prions in budding yeast, and their possible functions. Seminars in Cell & Developmental Biology 22:5, pages 452-459.
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Kazuo Fushimi, Charles Long, Neha Jayaram, Xiaoping Chen, Liming Li & Jane Y. Wu. (2011) Expression of human FUS/TLS in yeast leads to protein aggregation and cytotoxicity, recapitulating key features of FUS proteinopathy. Protein & Cell 2:2, pages 141-149.
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