FRANCIS TSAI to Heat-Shock Proteins
This is a "connection" page, showing publications FRANCIS TSAI has written about Heat-Shock Proteins.
Connection Strength
4.711
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Atomic structure of the Leishmania spp. Hsp100 N-domain. Proteins. 2022 06; 90(6):1242-1246.
Score: 0.679
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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: 0.564
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Structural determinants for protein unfolding and translocation by the Hsp104 protein disaggregase. Biosci Rep. 2017 12 22; 37(6).
Score: 0.509
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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: 0.500
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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: 0.369
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The M-domain controls Hsp104 protein remodeling activity in an Hsp70/Hsp40-dependent manner. J Mol Biol. 2010 Sep 10; 402(1):30-7.
Score: 0.304
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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: 0.299
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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: 0.249
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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: 0.239
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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: 0.192
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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: 0.191
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Structural basis of impaired disaggregase function in the oxidation-sensitive SKD3 mutant causing 3-methylglutaconic aciduria. Nat Commun. 2023 04 11; 14(1):2028.
Score: 0.184
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Deciphering the mechanism and function of Hsp100 unfoldases from protein structure. Biochem Soc Trans. 2022 12 16; 50(6):1725-1736.
Score: 0.180
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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: 0.086
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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: 0.060
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Molecular chaperones in protein quality control. J Biochem Mol Biol. 2005 May 31; 38(3):259-65.
Score: 0.053
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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: 0.051