Hsu SD - Search Results

1

Elucidation of the folding pathway of a circular permutant of topologically knotted YbeA by tryptophan substitutions.

Puri S, Liu CY, Hu IC, Lai CH, Hsu SD, Lyu PC. Puri S, et al. Among authors: hsu sd. Biochem Biophys Res Commun. 2023 Sep 10;672:81-88. doi: 10.1016/j.bbrc.2023.06.021. Epub 2023 Jun 14. Biochem Biophys Res Commun. 2023. PMID: 37343318

2

Comparative folding analyses of unknotted versus trefoil-knotted ornithine transcarbamylases suggest stabilizing effects of protein knots.

Sriramoju MK, Yang TJ, Hsu SD. Sriramoju MK, et al. Among authors: hsu sd. Biochem Biophys Res Commun. 2018 Sep 5;503(2):822-829. doi: 10.1016/j.bbrc.2018.06.082. Epub 2018 Jun 21. Biochem Biophys Res Commun. 2018. PMID: 29920242

3

Untying a Protein Knot by Circular Permutation.

Chuang YC, Hu IC, Lyu PC, Hsu SD. Chuang YC, et al. Among authors: hsu sd. J Mol Biol. 2019 Feb 15;431(4):857-863. doi: 10.1016/j.jmb.2019.01.005. Epub 2019 Jan 9. J Mol Biol. 2019. PMID: 30639189

4

Untying a Knotted SPOUT RNA Methyltransferase by Circular Permutation Results in a Domain-Swapped Dimer.

Ko KT, Hu IC, Huang KF, Lyu PC, Hsu SD. Ko KT, et al. Among authors: hsu sd. Structure. 2019 Aug 6;27(8):1224-1233.e4. doi: 10.1016/j.str.2019.04.004. Epub 2019 May 16. Structure. 2019. PMID: 31104814 Free article.

5

Cross-over Loop Cysteine C152 Acts as an Antioxidant to Maintain the Folding Stability and Deubiquitinase Activity of UCH-L1 Under Oxidative Stress.

Puri S, Hsu SD. Puri S, et al. Among authors: hsu sd. J Mol Biol. 2021 Apr 16;433(8):166879. doi: 10.1016/j.jmb.2021.166879. Epub 2021 Feb 19. J Mol Biol. 2021. PMID: 33617897

6

Converging experimental and computational views of the knotting mechanism of a small knotted protein.

Paissoni C, Puri S, Wang I, Chen SY, Camilloni C, Hsu SD. Paissoni C, et al. Among authors: hsu sd. Biophys J. 2021 Jun 1;120(11):2276-2286. doi: 10.1016/j.bpj.2021.03.032. Epub 2021 Apr 1. Biophys J. 2021. PMID: 33812848 Free PMC article.

7

Oxidation of catalytic cysteine of human deubiquitinase BAP1 triggers misfolding and aggregation in addition to functional loss.

Puri S, Hsu SD. Puri S, et al. Among authors: hsu sd. Biochem Biophys Res Commun. 2022 Apr 9;599:57-62. doi: 10.1016/j.bbrc.2022.02.029. Epub 2022 Feb 10. Biochem Biophys Res Commun. 2022. PMID: 35176625

8

Impacts of Cancer-associated Mutations on the Structure-Activity Relationship of BAP1.

Puri S, Chen SN, Chiu YH, Draczkowski P, Ko KT, Yang TJ, Wang YS, Uchiyama S, Hsu SD. Puri S, et al. Among authors: hsu sd. J Mol Biol. 2022 May 15;434(9):167553. doi: 10.1016/j.jmb.2022.167553. Epub 2022 Mar 19. J Mol Biol. 2022. PMID: 35317997

9

Elucidation of folding pathways of knotted proteins.

Puri S, Hsu SD. Puri S, et al. Among authors: hsu sd. Methods Enzymol. 2022;675:275-297. doi: 10.1016/bs.mie.2022.07.012. Epub 2022 Aug 19. Methods Enzymol. 2022. PMID: 36220273 Review.

10

Folding and functions of knotted proteins.

Hsu SD. Hsu SD. Curr Opin Struct Biol. 2023 Dec;83:102709. doi: 10.1016/j.sbi.2023.102709. Epub 2023 Sep 29. Curr Opin Struct Biol. 2023. PMID: 37778185 Free article. Review.

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