Jill Zitzewitz to DNA-Binding Proteins
This is a "connection" page, showing publications Jill Zitzewitz has written about DNA-Binding Proteins.
Connection Strength
0.777
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Mackness BC, Tran MT, McClain SP, Matthews CR, Zitzewitz JA. Folding of the RNA recognition motif (RRM) domains of the amyotrophic lateral sclerosis (ALS)-linked protein TDP-43 reveals an intermediate state. J Biol Chem. 2014 Mar 21; 289(12):8264-76.
Score: 0.277
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Mackness BC, Morgan BR, Deveau LM, Kathuria SV, Zitzewitz JA, Massi F. A Hydrophobic Core Stabilizes the Residual Structure in the RRM2 Intermediate State of the ALS-linked Protein TDP-43. J Mol Biol. 2024 Nov 15; 436(22):168823.
Score: 0.145
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Zitzewitz JA, Ibarra-Molero B, Fishel DR, Terry KL, Matthews CR. Preformed secondary structure drives the association reaction of GCN4-p1, a model coiled-coil system. J Mol Biol. 2000 Mar 03; 296(4):1105-16.
Score: 0.105
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Tavella D, Zitzewitz JA, Massi F. Characterization of TDP-43 RRM2 Partially Folded States and Their Significance to ALS Pathogenesis. Biophys J. 2018 11 06; 115(9):1673-1680.
Score: 0.095
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Morgan BR, Zitzewitz JA, Massi F. Structural Rearrangement upon Fragmentation of the Stability Core of the ALS-Linked Protein TDP-43. Biophys J. 2017 Aug 08; 113(3):540-549.
Score: 0.088
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Ibarra-Molero B, Zitzewitz JA, Matthews CR. Salt-bridges can stabilize but do not accelerate the folding of the homodimeric coiled-coil peptide GCN4-p1. J Mol Biol. 2004 Mar 05; 336(5):989-96.
Score: 0.035
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Knappenberger JA, Smith JE, Thorpe SH, Zitzewitz JA, Matthews CR. A buried polar residue in the hydrophobic interface of the coiled-coil peptide, GCN4-p1, plays a thermodynamic, not a kinetic role in folding. J Mol Biol. 2002 Aug 02; 321(1):1-6.
Score: 0.031