Co-Authors
This is a "connection" page, showing publications co-authored by FRANCIS TSAI and SUKYEONG LEE.
Connection Strength
3.515
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Cryo-EM Structures of the Hsp104 Protein Disaggregase Captured in the ATP Conformation. Cell Rep. 2019 01 02; 26(1):29-36.e3.
Score: 0.620
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Electron cryomicroscopy structure of a membrane-anchored mitochondrial AAA protease. J Biol Chem. 2011 Feb 11; 286(6):4404-11.
Score: 0.355
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CryoEM structure of Hsp104 and its mechanistic implication for protein disaggregation. Proc Natl Acad Sci U S A. 2010 May 04; 107(18):8135-40.
Score: 0.339
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Crystallization and preliminary X-ray crystallographic analysis of a 40 kDa N-terminal fragment of the yeast prion-remodeling factor Hsp104. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2007 Sep 01; 63(Pt 9):784-6.
Score: 0.283
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Visualizing the ATPase cycle in a protein disaggregating machine: structural basis for substrate binding by ClpB. Mol Cell. 2007 Jan 26; 25(2):261-71.
Score: 0.271
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Molecular chaperones in protein quality control. J Biochem Mol Biol. 2005 May 31; 38(3):259-65.
Score: 0.242
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Crystallization and preliminary X-ray crystallographic analysis of the Hsp100 chaperone ClpB from Thermus thermophilus. Acta Crystallogr D Biol Crystallogr. 2003 Dec; 59(Pt 12):2334-6.
Score: 0.218
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The structure of ClpB: a molecular chaperone that rescues proteins from an aggregated state. Cell. 2003 Oct 17; 115(2):229-40.
Score: 0.216
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Crystal Structure of the YcjX Stress Protein Reveals a Ras-Like GTP-Binding Protein. J Mol Biol. 2019 08 09; 431(17):3179-3190.
Score: 0.160
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Structural determinants for protein unfolding and translocation by the Hsp104 protein disaggregase. Biosci Rep. 2017 12 22; 37(6).
Score: 0.144
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Overlapping and Specific Functions of the Hsp104 N Domain Define Its Role in Protein Disaggregation. Sci Rep. 2017 09 11; 7(1):11184.
Score: 0.142
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Mitochondrial Hsp90 is a ligand-activated molecular chaperone coupling ATP binding to dimer closure through a coiled-coil intermediate. Proc Natl Acad Sci U S A. 2016 Mar 15; 113(11):2952-7.
Score: 0.127
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Heat shock protein (Hsp) 70 is an activator of the Hsp104 motor. Proc Natl Acad Sci U S A. 2013 May 21; 110(21):8513-8.
Score: 0.105
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Structural basis for intersubunit signaling in a protein disaggregating machine. Proc Natl Acad Sci U S A. 2012 Jul 31; 109(31):12515-20.
Score: 0.099
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Functional analysis of conserved cis- and trans-elements in the Hsp104 protein disaggregating machine. J Struct Biol. 2012 Aug; 179(2):172-80.
Score: 0.098
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The E3 ubiquitin ligase CHIP binds the androgen receptor in a phosphorylation-dependent manner. Biochim Biophys Acta. 2006 Jun; 1764(6):1073-9.
Score: 0.064
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M domains couple the ClpB threading motor with the DnaK chaperone activity. Mol Cell. 2007 Jan 26; 25(2):247-60.
Score: 0.017
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Thermotolerance requires refolding of aggregated proteins by substrate translocation through the central pore of ClpB. Cell. 2004 Nov 24; 119(5):653-65.
Score: 0.015