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Sukyeong Lee

Showing results (21-30 of 47) with videos related to

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Cell Reports|January 4, 2019
Cryo-EM Structures of the Hsp104 Protein Disaggregase Captured in the ATP ConformationSukyeong Lee, Soung Hun Roh, Jungsoon Lee, et al.
Acta Crystallographica. Section D, Structural Biology|August 5, 2016
2.4 Å resolution crystal structure of human TRAP1NM, the Hsp90 paralog in the mitochondrial matrixNuri Sung, Jungsoon Lee, Ji Hyun Kim, et al.
Proceedings of the National Academy of Sciences of the United States of America|May 8, 2013
Heat shock protein (Hsp) 70 is an activator of the Hsp104 motorJungsoon Lee, Ji-Hyun Kim, Amadeo B Biter, et al.
Molecular Cell|January 25, 2007
M domains couple the ClpB threading motor with the DnaK chaperone activityTobias Haslberger, Jimena Weibezahn, Regina Zahn, et al.
Proteins|February 5, 2022
Atomic structure of the Leishmania spp. Hsp100 N-domainJonathan M Mercado, Sukyeong Lee, Changsoo Chang, et al.
Proceedings of the National Academy of Sciences of the United States of America|March 2, 2016
Mitochondrial Hsp90 is a ligand-activated molecular chaperone coupling ATP binding to dimer closure through a coiled-coil intermediateNuri Sung, Jungsoon Lee, Ji-Hyun Kim, et al.
Nucleic Acids Research|September 24, 2023
Coordination between aminoacylation and editing to protect against proteotoxicityHong Zhang, Parker Murphy, Jason Yu, et al.
Scientific Reports|September 13, 2017
Overlapping and Specific Functions of the Hsp104 N Domain Define Its Role in Protein DisaggregationJungsoon Lee, Nuri Sung, Jonathan M Mercado, et al.
Journal of Inherited Metabolic Disease|May 9, 2020
A biallelic pathogenic variant in the OGDH gene results in a neurological disorder with features of a mitochondrial diseaseZheng Yie Yap, Klaudia Strucinska, Satoshi Matsuzaki, et al.
Cell|October 22, 2003
The structure of ClpB: a molecular chaperone that rescues proteins from an aggregated stateSukyeong Lee, Mathew E Sowa, Yo-hei Watanabe, et al.
Pageof 5

Showing results (21-30 of 47) with videos related to

Sort By:
Pageof 5
Cell Reports|January 4, 2019
Cryo-EM Structures of the Hsp104 Protein Disaggregase Captured in the ATP ConformationSukyeong Lee, Soung Hun Roh, Jungsoon Lee, et al.
Acta Crystallographica. Section D, Structural Biology|August 5, 2016
2.4 Å resolution crystal structure of human TRAP1NM, the Hsp90 paralog in the mitochondrial matrixNuri Sung, Jungsoon Lee, Ji Hyun Kim, et al.
Proceedings of the National Academy of Sciences of the United States of America|May 8, 2013
Heat shock protein (Hsp) 70 is an activator of the Hsp104 motorJungsoon Lee, Ji-Hyun Kim, Amadeo B Biter, et al.
Molecular Cell|January 25, 2007
M domains couple the ClpB threading motor with the DnaK chaperone activityTobias Haslberger, Jimena Weibezahn, Regina Zahn, et al.
Proteins|February 5, 2022
Atomic structure of the Leishmania spp. Hsp100 N-domainJonathan M Mercado, Sukyeong Lee, Changsoo Chang, et al.
Proceedings of the National Academy of Sciences of the United States of America|March 2, 2016
Mitochondrial Hsp90 is a ligand-activated molecular chaperone coupling ATP binding to dimer closure through a coiled-coil intermediateNuri Sung, Jungsoon Lee, Ji-Hyun Kim, et al.
Nucleic Acids Research|September 24, 2023
Coordination between aminoacylation and editing to protect against proteotoxicityHong Zhang, Parker Murphy, Jason Yu, et al.
Scientific Reports|September 13, 2017
Overlapping and Specific Functions of the Hsp104 N Domain Define Its Role in Protein DisaggregationJungsoon Lee, Nuri Sung, Jonathan M Mercado, et al.
Journal of Inherited Metabolic Disease|May 9, 2020
A biallelic pathogenic variant in the OGDH gene results in a neurological disorder with features of a mitochondrial diseaseZheng Yie Yap, Klaudia Strucinska, Satoshi Matsuzaki, et al.
Cell|October 22, 2003
The structure of ClpB: a molecular chaperone that rescues proteins from an aggregated stateSukyeong Lee, Mathew E Sowa, Yo-hei Watanabe, et al.
Pageof 5