FRANCIS TSAI to Molecular Chaperones
This is a "connection" page, showing publications FRANCIS TSAI has written about Molecular Chaperones.
Connection Strength
2.796
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Structural determinants for protein unfolding and translocation by the Hsp104 protein disaggregase. Biosci Rep. 2017 12 22; 37(6).
Score: 0.568
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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: 0.557
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Molecular chaperones in protein quality control. J Biochem Mol Biol. 2005 May 31; 38(3):259-65.
Score: 0.238
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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: 0.214
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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: 0.213
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Second Virtual International Symposium on Cellular and Organismal Stress Responses, September 8-9, 2022. Cell Stress Chaperones. 2023 01; 28(1):1-9.
Score: 0.201
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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: 0.201
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Atomic structure of the Leishmania spp. Hsp100 N-domain. Proteins. 2022 06; 90(6):1242-1246.
Score: 0.190
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Functional cooperativity between the trigger factor chaperone and the ClpXP proteolytic complex. Nat Commun. 2021 01 12; 12(1):281.
Score: 0.176
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The mitochondrial HSP90 paralog TRAP1 forms an OXPHOS-regulated tetramer and is involved in mitochondrial metabolic homeostasis. BMC Biol. 2020 01 27; 18(1):10.
Score: 0.164
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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: 0.057
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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