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Title:	Rpn1 provides adjacent receptor sites for substrate binding and deubiquitination by the proteasome
Source:	Science [0036-8075] Shi, Y yr:2016

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description	1.	Matouschek, A. "An assay for 26S proteasome activity based on fluorescence anisotropy measurements of dye-labeled protein substrates." Analytical biochemistry 509 (2016): 50-59.
description	2.	Schweitzer, A. "Structure of the human 26S proteasome at a resolution of 3.9 Å." Proceedings of the National Academy of Sciences of the United States of America 113.28 (2016): 7816-7821.
description	3.	Elsasser, S. "Proteasome subunit Rpn1 binds ubiquitin-like protein domains." Nature cell biology 4.9 (2002): 725-30.
description	4.	Chen, S. "Structural basis for dynamic regulation of the human 26S proteasome." Proceedings of the National Academy of Sciences of the United States of America 113.46 (2016): 12991-12996.
description	5.	Singharoy, A. "Molecular dynamics-based refinement and validation for sub-5 Å cryo-electron microscopy maps." eLife 5 (2016).
description	6.	Lee, B. "USP14 deubiquitinates proteasome-bound substrates that are ubiquitinated at multiple sites." Nature 532.7599 (2016): 398-401.
description	7.	Finley, D. "Gates, Channels, and Switches: Elements of the Proteasome Machine." Trends in biochemical sciences 41.1 (2016): 77-93.
description	8.	Schmidt, M. "Regulation of proteasome activity in health and disease." Biochimica et biophysica acta. Molecular cell research 1843.1: 13-25.
description	9.	Zhou, M. "Mass Spectrometry of Intact V-Type ATPases Reveals Bound Lipids and the Effects of Nucleotide Binding." Science 334.6054 (2011): 380-385.
description	10.	Verma, Raymond J. "Role of Rpn11 metalloprotease in deubiquitination and degradation by the 26S proteasome." Science 298.5593 (2002): 611-5.
description	11.	Lupas, A. "Predicting Coiled Coils from Protein Sequences." Science 252.5009 (1991): 1162-1164.
description	12.	Elsasser, S. "Rad23 and Rpn10 serve as alternative ubiquitin receptors for the proteasome." The Journal of biological chemistry 279.26 (2004): 26817-26822.
description	13.	Pugnaloni, Luis A. "Competitive adsorption of proteins and low-molecular-weight surfactants: computer simulation and microscopic imaging." Advances in colloid and interface science 107.1 (2004): 27-49.
description	14.	Ouvry-Patat, S. "Characterization of antimicrobial histone sequences and posttranslational modifications by mass spectrometry." Journal of mass spectrometry 42.5 (2007): 664-674.
description	15.	Mueller, Thomas D D. "Structural determinants for the binding of ubiquitin-like domains to the proteasome." The EMBO journal 22.18 (2003): 4634-4645.
description	16.	Lupas, A. "Coiled coils: new structures and new functions." Trends in biochemical sciences 21.10 (1996): 375-82.
description	17.	Lupas, A. "Predicting coiled-coil regions in proteins." Current opinion in structural biology 7.3 (1997): 388-93.
description	18.	Huang, X. "An atomic structure of the human 26S proteasome." Nature Structural & Molecular Biology 23.9 (2016): 778-785.
description	19.	Hanna, J. "Deubiquitinating enzyme Ubp6 functions noncatalytically to delay proteasomal degradation." Cell 127.1 (2006): 99-111.
description	20.	Pugnaloni, LA. "Growth and aggregation of surfactant islands during the displacement of an adsorbed protein monolayer: a Brownian dynamics simulation study." Colloids and surfaces. B, Biointerfaces 31.1-4 (2003): 149-157.