Zitzewitz JA - Search Results

1

A Hydrophobic Core Stabilizes the Residual Structure in the RRM2 Intermediate State of the ALS-linked Protein TDP-43.

Mackness BC, Morgan BR, Deveau LM, Kathuria SV, Zitzewitz JA, Massi F. Mackness BC, et al. Among authors: zitzewitz ja. J Mol Biol. 2024 Nov 15;436(22):168823. doi: 10.1016/j.jmb.2024.168823. Epub 2024 Oct 18. J Mol Biol. 2024. PMID: 39426615

2

Structural Rearrangement upon Fragmentation of the Stability Core of the ALS-Linked Protein TDP-43.

Morgan BR, Zitzewitz JA, Massi F. Morgan BR, et al. Among authors: zitzewitz ja. Biophys J. 2017 Aug 8;113(3):540-549. doi: 10.1016/j.bpj.2017.06.049. Biophys J. 2017. PMID: 28793209 Free PMC article.

3

Folding of the RNA recognition motif (RRM) domains of the amyotrophic lateral sclerosis (ALS)-linked protein TDP-43 reveals an intermediate state.

Mackness BC, Tran MT, McClain SP, Matthews CR, Zitzewitz JA. Mackness BC, et al. Among authors: zitzewitz ja. J Biol Chem. 2014 Mar 21;289(12):8264-76. doi: 10.1074/jbc.M113.542779. Epub 2014 Feb 4. J Biol Chem. 2014. PMID: 24497641 Free PMC article.

4

Characterization of TDP-43 RRM2 Partially Folded States and Their Significance to ALS Pathogenesis.

Tavella D, Zitzewitz JA, Massi F. Tavella D, et al. Among authors: zitzewitz ja. Biophys J. 2018 Nov 6;115(9):1673-1680. doi: 10.1016/j.bpj.2018.09.011. Epub 2018 Sep 21. Biophys J. 2018. PMID: 30309612 Free PMC article.

5

Trifluoroethanol Partially Unfolds G93A SOD1 Leading to Protein Aggregation: A Study by Native Mass Spectrometry and FPOP Protein Footprinting.

Niu B, Mackness BC, Zitzewitz JA, Matthews CR, Gross ML. Niu B, et al. Among authors: zitzewitz ja. Biochemistry. 2020 Oct 6;59(39):3650-3659. doi: 10.1021/acs.biochem.0c00425. Epub 2020 Sep 21. Biochemistry. 2020. PMID: 32924445 Free PMC article.

6

Incorporation of a Reporter Peptide in FPOP Compensates for Adventitious Scavengers and Permits Time-Dependent Measurements.

Niu B, Mackness BC, Rempel DL, Zhang H, Cui W, Matthews CR, Zitzewitz JA, Gross ML. Niu B, et al. Among authors: zitzewitz ja. J Am Soc Mass Spectrom. 2017 Feb;28(2):389-392. doi: 10.1007/s13361-016-1552-4. Epub 2016 Dec 6. J Am Soc Mass Spectrom. 2017. PMID: 27924496 Free PMC article.

7

Disulfide-reduced ALS variants of Cu, Zn superoxide dismutase exhibit increased populations of unfolded species.

Kayatekin C, Zitzewitz JA, Matthews CR. Kayatekin C, et al. Among authors: zitzewitz ja. J Mol Biol. 2010 Apr 30;398(2):320-31. doi: 10.1016/j.jmb.2010.02.034. Epub 2010 Feb 23. J Mol Biol. 2010. PMID: 20184893 Free PMC article.

8

Mapping the folding free energy surface for metal-free human Cu,Zn superoxide dismutase.

Svensson AK, Bilsel O, Kondrashkina E, Zitzewitz JA, Matthews CR. Svensson AK, et al. Among authors: zitzewitz ja. J Mol Biol. 2006 Dec 15;364(5):1084-102. doi: 10.1016/j.jmb.2006.09.005. Epub 2006 Sep 7. J Mol Biol. 2006. PMID: 17046019

9

Mapping the structure of folding cores in TIM barrel proteins by hydrogen exchange mass spectrometry: the roles of motif and sequence for the indole-3-glycerol phosphate synthase from Sulfolobus solfataricus.

Gu Z, Zitzewitz JA, Matthews CR. Gu Z, et al. Among authors: zitzewitz ja. J Mol Biol. 2007 Apr 27;368(2):582-94. doi: 10.1016/j.jmb.2007.02.027. Epub 2007 Feb 20. J Mol Biol. 2007. PMID: 17359995 Free PMC article.

10

Zinc binding modulates the entire folding free energy surface of human Cu,Zn superoxide dismutase.

Kayatekin C, Zitzewitz JA, Matthews CR. Kayatekin C, et al. Among authors: zitzewitz ja. J Mol Biol. 2008 Dec 12;384(2):540-55. doi: 10.1016/j.jmb.2008.09.045. Epub 2008 Sep 26. J Mol Biol. 2008. PMID: 18840448 Free PMC article.

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