J. Zitzewitz

发表

Molecular dissection of the folding mechanism of the alpha subunit of tryptophan synthase: an amino-terminal autonomous folding unit controls several rate-limiting steps in the folding of a single domain protein.

C. Matthews, J. Zitzewitz, 1999, Biochemistry.

Time-resolved fluorescence anisotropy study of the refolding reaction of the alpha-subunit of tryptophan synthase reveals nonmonotonic behavior of the rotational correlation time.

J. Beechem, C. Matthews, O. Bilsel, 1999, Biochemistry.

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.

C. Matthews, J. Zitzewitz, Z. Gu, 2007, Journal of molecular biology.

Folding of the RNA Recognition Motif (RRM) Domains of the Amyotrophic Lateral Sclerosis (ALS)-linked Protein TDP-43 Reveals an Intermediate State*

C. Matthews, J. Zitzewitz, Brian C Mackness, 2014, The Journal of Biological Chemistry.

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

J. Zitzewitz, F. Massi, D. Tavella, 2018, Biophysical journal.

Structural basis for mutation-induced destabilization of profilin 1 in ALS

D. A. Bosco, C. Schiffer, J. Landers, 2015, Proceedings of the National Academy of Sciences.

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

M. Gross, C. Matthews, J. Zitzewitz, 2017, Journal of The American Society for Mass Spectrometry.

Apparent radii of the native, stable intermediates and unfolded conformers of the alpha-subunit of tryptophan synthase from E. coli, a TIM barrel protein.

J. Lee, C. Matthews, O. Bilsel, 1999, Biochemistry.

The relationship between chain connectivity and domain stability in the equilibrium and kinetic folding mechanisms of dihydrofolate reductase from E.coli

C. Matthews, J. Zitzewitz, Anna-Karin E. Svensson, 2006, Protein engineering, design & selection : PEDS.

Mutations in the Profilin 1 Gene Cause Familial Amyotrophic Lateral Sclerosis

S. C. Chafe, D. Goldstein, Robert H. Brown, 2012, Nature.

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

M. Gross, C. Matthews, J. Zitzewitz, 2020, Biochemistry.

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

C. Matthews, Can Kayatekin, J. Zitzewitz, 2010, Journal of molecular biology.

Metal-Free ALS Variants of Dimeric Human Cu,Zn-Superoxide Dismutase Have Enhanced Populations of Monomeric Species

C. Matthews, O. Bilsel, Can Kayatekin, 2010, PloS one.

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

Can Kayatekin, C. Matthews, Can Kayatekin, 2008, Journal of molecular biology.

Protein engineering strategies in examining protein folding intermediates: Current opinion in Structural Biology 1993, 3:594–600

C. Matthews, J. Zitzewitz, 1993 .

Nonnative structure in a peptide model of the unfolded state of superoxide dismutase 1 (SOD1): Implications for ALS-linked aggregation

C. Matthews, O. Bilsel, J. Zitzewitz, 2019, The Journal of Biological Chemistry.

A buried polar residue in the hydrophobic interface of the coiled-coil peptide, GCN4-p1, plays a thermodynamic, not a kinetic role in folding.

C. Matthews, J. Zitzewitz, J. Smith, 2002, Journal of molecular biology.

Probing the folding mechanism of a leucine zipper peptide by stopped-flow circular dichroism spectroscopy.

C. Matthews, O. Bilsel, J. Zitzewitz, 1995, Biochemistry.

The folding free-energy surface of HIV-1 protease: insights into the thermodynamic basis for resistance to inhibitors.

C. Matthews, O. Bilsel, Ying Wu, 2009, Journal of molecular biology.

Preformed secondary structure drives the association reaction of GCN4-p1, a model coiled-coil system.

C. Matthews, J. Zitzewitz, B. Ibarra-Molero, 2000, Journal of molecular biology.

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

E. Kondrashkina, C. Matthews, O. Bilsel, 2006, Journal of molecular biology.

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

J. Zitzewitz, F. Massi, Brittany R. Morgan, 2017, Biophysical journal.

Folding Mechanism of the α-Subunit of Tryptophan Synthase, an α/β Barrel Protein: Global Analysis Highlights the Interconversion of Multiple Native, Intermediate, and Unfolded Forms through Parallel Channels†

O. Bilsel, J. Zitzewitz, Matthews Cr, 1999 .

Friction-Limited Folding of Disulfide-Reduced Monomeric SOD1.

C. Matthews, O. Bilsel, Can Kayatekin, 2020, Biophysical journal.

Mutations in the Profilin 1 Gene Cause Familial Amyotrophic Lateral Sclerosis

S. C. Chafe, D. Goldstein, M. Moore, 2012, Nature.

Structural basis for mutation-induced destabilization of profilin 1 in ALS

D. A. Bosco, C. Schiffer, J. Landers, 2015, Proceedings of the National Academy of Sciences.

Identifying the structural boundaries of independent folding domains in the a subunit of tryptophan synthase, a β/α barrel protein

C. Matthews, J. Zitzewitz, J A Zitzewitz, 1999, Protein science : a publication of the Protein Society.

A hydrophobic core stabilizes the residual structure in the RRM2 intermediate state of the ALS-linked protein TDP-43

J. Zitzewitz, Sagar V. Kathuria, F. Massi, 2024, bioRxiv.