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Connection

Jill Zitzewitz to Thermodynamics

This is a "connection" page, showing publications Jill Zitzewitz has written about Thermodynamics.
Connection Strength

0.407
  1. 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.
    View in: PubMed
    Score: 0.137
  2. Svensson AK, Bilsel O, Kondrashkina E, Zitzewitz JA, Matthews CR. Mapping the folding free energy surface for metal-free human Cu,Zn superoxide dismutase. J Mol Biol. 2006 Dec 15; 364(5):1084-102.
    View in: PubMed
    Score: 0.082
  3. Zitzewitz JA, Bilsel O, Luo J, Jones BE, Matthews CR. Probing the folding mechanism of a leucine zipper peptide by stopped-flow circular dichroism spectroscopy. Biochemistry. 1995 Oct 3; 34(39):12812-9.
    View in: PubMed
    Score: 0.038
  4. Svensson AK, Bilsel O, Kayatekin C, Adefusika JA, Zitzewitz JA, Matthews CR. Metal-free ALS variants of dimeric human Cu,Zn-superoxide dismutase have enhanced populations of monomeric species. PLoS One. 2010 Apr 09; 5(4):e10064.
    View in: PubMed
    Score: 0.026
  5. 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.
    View in: PubMed
    Score: 0.024
  6. Kayatekin C, Zitzewitz JA, Matthews CR. Zinc binding modulates the entire folding free energy surface of human Cu,Zn superoxide dismutase. J Mol Biol. 2008 Dec 12; 384(2):540-55.
    View in: PubMed
    Score: 0.024
  7. Svensson AK, Zitzewitz JA, Matthews CR, Smith VF. The relationship between chain connectivity and domain stability in the equilibrium and kinetic folding mechanisms of dihydrofolate reductase from E.coli. Protein Eng Des Sel. 2006 Apr; 19(4):175-85.
    View in: PubMed
    Score: 0.020
  8. 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 5; 336(5):989-96.
    View in: PubMed
    Score: 0.017
  9. 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 2; 321(1):1-6.
    View in: PubMed
    Score: 0.015
  10. Gualfetti PJ, Iwakura M, Lee JC, Kihara H, Bilsel O, Zitzewitz JA, Matthews CR. Apparent radii of the native, stable intermediates and unfolded conformers of the alpha-subunit of tryptophan synthase from E. coli, a TIM barrel protein. Biochemistry. 1999 Oct 5; 38(40):13367-78.
    View in: PubMed
    Score: 0.013
  11. Bilsel O, Zitzewitz JA, Bowers KE, Matthews CR. Folding mechanism of the alpha-subunit of tryptophan synthase, an alpha/beta barrel protein: global analysis highlights the interconversion of multiple native, intermediate, and unfolded forms through parallel channels. Biochemistry. 1999 Jan 19; 38(3):1018-29.
    View in: PubMed
    Score: 0.012
Connection Strength

The connection strength for concepts is the sum of the scores for each matching publication.

Publication scores are based on many factors, including how long ago they were written and whether the person is a first or senior author.