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Items: 19

1.

2.4 Å resolution crystal structure of human TRAP1NM, the Hsp90 paralog in the mitochondrial matrix.

Sung N, Lee J, Kim JH, Chang C, Tsai FT, Lee S.

Acta Crystallogr D Struct Biol. 2016 Aug;72(Pt 8):904-11. doi: 10.1107/S2059798316009906. Epub 2016 Jul 13.

PMID:
27487821
2.

Mitochondrial Hsp90 is a ligand-activated molecular chaperone coupling ATP binding to dimer closure through a coiled-coil intermediate.

Sung N, Lee J, Kim JH, Chang C, Joachimiak A, Lee S, Tsai FT.

Proc Natl Acad Sci U S A. 2016 Mar 15;113(11):2952-7. doi: 10.1073/pnas.1516167113. Epub 2016 Feb 29.

3.

Molecular chaperones: guardians of the proteome in normal and disease states.

Jeng W, Lee S, Sung N, Lee J, Tsai FT.

F1000Res. 2015 Dec 15;4. pii: F1000 Faculty Rev-1448. doi: 10.12688/f1000research.7214.1. eCollection 2015. Review.

4.

Pharmacogenetic characterization of naturally occurring germline NT5C1A variants to chemotherapeutic nucleoside analogs.

Saliba J, Zabriskie R, Ghosh R, Powell BC, Hicks S, Kimmel M, Meng Q, Ritter DI, Wheeler DA, Gibbs RA, Tsai FT, Plon SE.

Pharmacogenet Genomics. 2016 Jun;26(6):271-9. doi: 10.1097/FPC.0000000000000208.

5.

Heat shock protein (Hsp) 70 is an activator of the Hsp104 motor.

Lee J, Kim JH, Biter AB, Sielaff B, Lee S, Tsai FT.

Proc Natl Acad Sci U S A. 2013 May 21;110(21):8513-8. doi: 10.1073/pnas.1217988110. Epub 2013 May 6.

6.

Structural basis for intersubunit signaling in a protein disaggregating machine.

Biter AB, Lee S, Sung N, Tsai FT.

Proc Natl Acad Sci U S A. 2012 Jul 31;109(31):12515-20. doi: 10.1073/pnas.1207040109. Epub 2012 Jul 16.

7.

Functional analysis of conserved cis- and trans-elements in the Hsp104 protein disaggregating machine.

Biter AB, Lee J, Sung N, Tsai FT, Lee S.

J Struct Biol. 2012 Aug;179(2):172-80. doi: 10.1016/j.jsb.2012.05.007. Epub 2012 May 24.

8.

Electron cryomicroscopy structure of a membrane-anchored mitochondrial AAA protease.

Lee S, Augustin S, Tatsuta T, Gerdes F, Langer T, Tsai FT.

J Biol Chem. 2011 Feb 11;286(6):4404-11. doi: 10.1074/jbc.M110.158741. Epub 2010 Dec 8.

9.

Structural and functional conservation of Mycobacterium tuberculosis GroEL paralogs suggests that GroEL1 Is a chaperonin.

Sielaff B, Lee KS, Tsai FT.

J Mol Biol. 2011 Jan 21;405(3):831-9. doi: 10.1016/j.jmb.2010.11.021. Epub 2010 Nov 19.

10.

The M-domain controls Hsp104 protein remodeling activity in an Hsp70/Hsp40-dependent manner.

Sielaff B, Tsai FT.

J Mol Biol. 2010 Sep 10;402(1):30-7. doi: 10.1016/j.jmb.2010.07.030. Epub 2010 Jul 21.

11.

CryoEM structure of Hsp104 and its mechanistic implication for protein disaggregation.

Lee S, Sielaff B, Lee J, Tsai FT.

Proc Natl Acad Sci U S A. 2010 May 4;107(18):8135-40. doi: 10.1073/pnas.1003572107. Epub 2010 Apr 19.

12.

Crystallization and preliminary X-ray crystallographic analysis of a GroEL1 fragment from Mycobacterium tuberculosis H37Rv.

Sielaff B, Lee KS, Tsai FT.

Acta Crystallogr Sect F Struct Biol Cryst Commun. 2010 Apr 1;66(Pt 4):418-20. doi: 10.1107/S1744309110004409. Epub 2010 Mar 31.

13.

Crystallization and preliminary X-ray crystallographic analysis of a 40 kDa N-terminal fragment of the yeast prion-remodeling factor Hsp104.

Lee S, Tsai FT.

Acta Crystallogr Sect F Struct Biol Cryst Commun. 2007 Sep 1;63(Pt 9):784-6. Epub 2007 Aug 31.

14.
15.

The E3 ubiquitin ligase CHIP binds the androgen receptor in a phosphorylation-dependent manner.

Rees I, Lee S, Kim H, Tsai FT.

Biochim Biophys Acta. 2006 Jun;1764(6):1073-9. Epub 2006 Apr 4.

PMID:
16725394
16.

Molecular chaperones in protein quality control.

Lee S, Tsai FT.

J Biochem Mol Biol. 2005 May 31;38(3):259-65. Review.

PMID:
15943899
17.

The ClpB/Hsp104 molecular chaperone-a protein disaggregating machine.

Lee S, Sowa ME, Choi JM, Tsai FT.

J Struct Biol. 2004 Apr-May;146(1-2):99-105. Review.

PMID:
15037241
18.

Crystallization and preliminary X-ray crystallographic analysis of the Hsp100 chaperone ClpB from Thermus thermophilus.

Lee S, Hisayoshi M, Yoshida M, Tsai FT.

Acta Crystallogr D Biol Crystallogr. 2003 Dec;59(Pt 12):2334-6. Epub 2003 Nov 27.

PMID:
14646112
19.

The structure of ClpB: a molecular chaperone that rescues proteins from an aggregated state.

Lee S, Sowa ME, Watanabe YH, Sigler PB, Chiu W, Yoshida M, Tsai FT.

Cell. 2003 Oct 17;115(2):229-40.

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