Jill Zitzewitz to Mutation
This is a "connection" page, showing publications Jill Zitzewitz has written about Mutation.
Connection Strength
0.280
-
Boopathy S, Silvas TV, Tischbein M, Jansen S, Shandilya SM, Zitzewitz JA, Landers JE, Goode BL, Schiffer CA, Bosco DA. Structural basis for mutation-induced destabilization of profilin 1 in ALS. Proc Natl Acad Sci U S A. 2015 Jun 30; 112(26):7984-9.
Score: 0.068
-
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: 0.062
-
Wu CH, Fallini C, Ticozzi N, Keagle PJ, Sapp PC, Piotrowska K, Lowe P, Koppers M, McKenna-Yasek D, Baron DM, Kost JE, Gonzalez-Perez P, Fox AD, Adams J, Taroni F, Tiloca C, Leclerc AL, Chafe SC, Mangroo D, Moore MJ, Zitzewitz JA, Xu ZS, van den Berg LH, Glass JD, Siciliano G, Cirulli ET, Goldstein DB, Salachas F, Meininger V, Rossoll W, Ratti A, Gellera C, Bosco DA, Bassell GJ, Silani V, Drory VE, Brown RH, Landers JE. Mutations in the profilin 1 gene cause familial amyotrophic lateral sclerosis. Nature. 2012 Aug 23; 488(7412):499-503.
Score: 0.056
-
Cohen NR, Kayatekin C, Zitzewitz JA, Bilsel O, Matthews CR. Friction-Limited Folding of Disulfide-Reduced Monomeric SOD1. Biophys J. 2020 04 21; 118(8):1992-2000.
Score: 0.024
-
Cohen NR, Zitzewitz JA, Bilsel O, Matthews CR. Nonnative structure in a peptide model of the unfolded state of superoxide dismutase 1 (SOD1): Implications for ALS-linked aggregation. J Biol Chem. 2019 09 13; 294(37):13708-13717.
Score: 0.023
-
Niu B, Mackness BC, Rempel DL, Zhang H, Cui W, Matthews CR, Zitzewitz JA, Gross ML. Incorporation of a Reporter Peptide in FPOP Compensates for Adventitious Scavengers and Permits Time-Dependent Measurements. J Am Soc Mass Spectrom. 2017 02; 28(2):389-392.
Score: 0.019
-
Kayatekin C, Zitzewitz JA, Matthews CR. Disulfide-reduced ALS variants of Cu, Zn superoxide dismutase exhibit increased populations of unfolded species. J Mol Biol. 2010 Apr 30; 398(2):320-31.
Score: 0.012
-
Noel AF, Bilsel O, Kundu A, Wu Y, Zitzewitz JA, Matthews CR. The folding free-energy surface of HIV-1 protease: insights into the thermodynamic basis for resistance to inhibitors. J Mol Biol. 2009 Apr 10; 387(4):1002-16.
Score: 0.011
-
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: 0.007