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  • Author: Hess S
  • References

Author: Hess S


References 16 references


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  • Yahya G, et al. (2021) Profiling the physiological pitfalls of anti-hepatitis C direct-acting agents in budding yeast. Microb Biotechnol 14(5):2199-2213 PMID:34378349
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  • Zimmermann J, et al. (2020) One cysteine is enough: A monothiol Grx can functionally replace all cytosolic Trx and dithiol Grx. Redox Biol 36:101598 PMID:32521506
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  • Backes S, et al. (2018) Tom70 enhances mitochondrial preprotein import efficiency by binding to internal targeting sequences. J Cell Biol 217(4):1369-1382 PMID:29382700
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  • Liu JM, et al. (2016) Improved 6-Plex Tandem Mass Tags Quantification Throughput Using a Linear Ion Trap-High-Energy Collision Induced Dissociation MS(3) Scan. Anal Chem 88(15):7471-5 PMID:27377715
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  • Sung MK, et al. (2016) A conserved quality-control pathway that mediates degradation of unassembled ribosomal proteins. Elife 5 PMID:27552055
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  • Sung MK, et al. (2016) Ribosomal proteins produced in excess are degraded by the ubiquitin-proteasome system. Mol Biol Cell 27(17):2642-52 PMID:27385339
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  • Gristick HB, et al. (2015) Mechanism of Assembly of a Substrate Transfer Complex during Tail-anchored Protein Targeting. J Biol Chem 290(50):30006-17 PMID:26451041
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  • Kolawa N, et al. (2013) Perturbations to the ubiquitin conjugate proteome in yeast δubx mutants identify Ubx2 as a regulator of membrane lipid composition. Mol Cell Proteomics 12(10):2791-803 PMID:23793018
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  • Kalli A and Hess S (2012) Effect of mass spectrometric parameters on peptide and protein identification rates for shotgun proteomic experiments on an LTQ-orbitrap mass analyzer. Proteomics 12(1):21-31 PMID:22065615
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  • Sohn CH, et al. (2012) Designer reagents for mass spectrometry-based proteomics: clickable cross-linkers for elucidation of protein structures and interactions. Anal Chem 84(6):2662-9 PMID:22339618
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  • Sweredoski MJ, et al. (2011) LogViewer: a software tool to visualize quality control parameters to optimize proteomics experiments using Orbitrap and LTQ-FT mass spectrometers. J Biomol Tech 22(4):122-6 PMID:22131886
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  • Suhre MH, et al. (2009) Influence of divalent copper, manganese and zinc ions on fibril nucleation and elongation of the amyloid-like yeast prion determinant Sup35p-NM. J Inorg Biochem 103(12):1711-20 PMID:19853305
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  • Krammer C, et al. (2008) Prion protein/protein interactions: fusion with yeast Sup35p-NM modulates cytosolic PrP aggregation in mammalian cells. FASEB J 22(3):762-73 PMID:17928365
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  • Hess S, et al. (2007) Alternative assembly pathways of the amyloidogenic yeast prion determinant Sup35-NM. EMBO Rep 8(12):1196-201 PMID:17975557
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  • Slotta U, et al. (2007) Spider silk and amyloid fibrils: a structural comparison. Macromol Biosci 7(2):183-8 PMID:17295405
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  • Li YF, et al. (2001) In vivo mechanism-based inactivation of S-adenosylmethionine decarboxylases from Escherichia coli, Salmonella typhimurium, and Saccharomyces cerevisiae. Proc Natl Acad Sci U S A 98(19):10578-83 PMID:11526206
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