Search Results - "ZITZEWITZ, JILL A."

Structural basis for mutation-induced destabilization of profilin 1 in ALS by Boopathy, Sivakumar, Tania V. Silvas, Maeve Tischbein, Silvia Jansen, Shivender M. Shandilya, Jill A. Zitzewitz, John E. Landers, Bruce L. Goode, Celia A. Schiffer, Daryl A. Bosco

“…Mutations in profilin 1 (PFN1) are associated with amyotrophic lateral sclerosis (ALS); however, the pathological mechanism of PFN1 in this fatal disease is…”
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Folding of the RNA Recognition Motif (RRM) Domains of the Amyotrophic Lateral Sclerosis (ALS)-linked Protein TDP-43 Reveals an Intermediate State by Mackness, Brian C., Tran, Meme T., McClain, Shannan P., Matthews, C. Robert, Zitzewitz, Jill A.

“…Pathological alteration of TDP-43 (TAR DNA-binding protein-43), a protein involved in various RNA-mediated processes, is a hallmark feature of the…”
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Disulfide-Reduced ALS Variants of Cu, Zn Superoxide Dismutase Exhibit Increased Populations of Unfolded Species by Kayatekin, Can, Zitzewitz, Jill A., Matthews, C. Robert

“…Cu,Zn superoxide dismutase (SOD1) is a dimeric metal-binding enzyme responsible for the dismutation of toxic superoxide to hydrogen peroxide and oxygen in…”
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Metal-free ALS variants of dimeric human Cu,Zn-superoxide dismutase have enhanced populations of monomeric species by Svensson, Anna-Karin E, Bilsel, Osman, Kayatekin, Can, Adefusika, Jessica A, Zitzewitz, Jill A, Matthews, C Robert

“…Amino acid replacements at dozens of positions in the dimeric protein human, Cu,Zn superoxide dismutase (SOD1) can cause amyotrophic lateral sclerosis (ALS)…”
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Characterization of TDP-43 RRM2 Partially Folded States and Their Significance to ALS Pathogenesis by Tavella, Davide, Zitzewitz, Jill A., Massi, Francesca

“…The human protein TDP-43 is a major component of the cellular aggregates found in amyotrophic lateral sclerosis and other neurodegenerative diseases. Insoluble…”
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Mapping the Folding Free Energy Surface for Metal-free Human Cu,Zn Superoxide Dismutase by Svensson, Anna-Karin E., Bilsel, Osman, Kondrashkina, Elena, Zitzewitz, Jill A., Matthews, C. Robert

“…Mutations at many different sites in the gene encoding human Cu,Zn superoxide dismutase (SOD) are known to be causative agents in amyotrophic lateral sclerosis…”
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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 by Gu, Zhenyu, Zitzewitz, Jill A., Matthews, C. Robert

“…To test the roles of motif and amino acid sequence in the folding mechanisms of TIM barrel proteins, hydrogen-deuterium exchange was used to explore the…”
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A Hydrophobic Core Stabilizes the Residual Structure in the RRM2 Intermediate State of the ALS-linked Protein TDP-43 by Mackness, Brian C., Morgan, Brittany R., Deveau, Laura M., Kathuria, Sagar V., Zitzewitz, Jill A., Massi, Francesca

“…[Display omitted] •Folding intermediates can mediate misfolding and aggregation in human diseases.•We identified the core structure for a folding intermediate…”
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Structural Rearrangement upon Fragmentation of the Stability Core of the ALS-Linked Protein TDP-43 by Morgan, Brittany R., Zitzewitz, Jill A., Massi, Francesca

“…Amyotrophic lateral sclerosis (ALS) is the most common adult degenerative motor neuron disease. Experimental evidence indicates a direct role of…”
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Trifluoroethanol Partially Unfolds G93A SOD1 Leading to Protein Aggregation: A Study by Native Mass Spectrometry and FPOP Protein Footprinting by Niu, Ben, Mackness, Brian C, Zitzewitz, Jill A, Matthews, C. Robert, Gross, Michael L

“…Misfolding of Cu, Zn superoxide dismutase (SOD1) variants may lead to protein aggregation and ultimately amyotrophic lateral sclerosis (ALS). The mechanism and…”
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Nonnative structure in a peptide model of the unfolded state of superoxide dismutase 1 (SOD1): Implications for ALS-linked aggregation by Cohen, Noah R., Zitzewitz, Jill A., Bilsel, Osman, Matthews, C. Robert

“…Dozens of mutations throughout the sequence of the gene encoding superoxide dismutase 1 (SOD1) have been linked to toxic protein aggregation in the…”
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Friction-Limited Folding of Disulfide-Reduced Monomeric SOD1 by Cohen, Noah R., Kayatekin, Can, Zitzewitz, Jill A., Bilsel, Osman, Matthews, C.R.

“…The folding reaction of a stable monomeric variant of Cu/Zn superoxide dismutase (mSOD1), an enzyme responsible for the conversion of superoxide free radicals…”
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Preformed secondary structure drives the association reaction of GCN4-p1, a model coiled-coil system by Zitzewitz, J A, Ibarra-Molero, B, Fishel, D R, Terry, K L, Matthews, C R

“…The structure of the transition state for the rate-limiting step in the folding and association of the homodimeric coiled-coil peptide GCN4-p1, was probed by…”
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Incorporation of a Reporter Peptide in FPOP Compensates for Adventitious Scavengers and Permits Time-Dependent Measurements by Niu, Ben, Mackness, Brian C., Rempel, Don. L., Zhang, Hao, Cui, Weidong, Matthews, C. Robert, Zitzewitz, Jill A., Gross, Michael L.

“…Incorporation of a reporter peptide in solutions submitted to fast photochemical oxidation of proteins (FPOP) allows for the correction of adventitious…”
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Zinc Binding Modulates the Entire Folding Free Energy Surface of Human Cu,Zn Superoxide Dismutase by Kayatekin, Can, Zitzewitz, Jill A., Matthews, C. Robert

“…Over 100 amino acid replacements in human Cu,Zn superoxide dismutase (SOD) are known to cause amyotrophic lateral sclerosis, a gain-of-function…”
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The relationship between chain connectivity and domain stability in the equilibrium and kinetic folding mechanisms of dihydrofolate reductase from E.coli by Svensson, Anna-Karin E., Zitzewitz, Jill A., Matthews, C.Robert, Smith, Virginia F.

“…The role of domains in defining the equilibrium and kinetic folding properties of dihydrofolate reductase (DHFR) from Escherichia coli was probed by examining…”
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The Folding Free-Energy Surface of HIV-1 Protease: Insights into the Thermodynamic Basis for Resistance to Inhibitors by Noel, Amanda F., Bilsel, Osman, Kundu, Agnita, Wu, Ying, Zitzewitz, Jill A., Matthews, C. Robert

“…Spontaneous mutations at numerous sites distant from the active site of human immunodeficiency virus type 1 protease enable resistance to inhibitors while…”
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Salt-bridges can Stabilize but do not Accelerate the Folding of the Homodimeric Coiled-coil Peptide GCN4-p1 by Ibarra-Molero, Beatriz, Zitzewitz, Jill A., Matthews, C.Robert

“…Double mutant cycle analysis was employed to ascertain the role of intra- and interchain salt-bridges in the folding and stability of the dimeric coiled-coil…”
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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 by Bilsel, Osman, Zitzewitz, Jill A, Bowers, Katherine E, Matthews, C. Robert

“…A variety of techniques have been used to investigate the urea-induced kinetic folding mechanism of the α-subunit of tryptophan synthase from Escherichia coli…”
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Probing the Folding Mechanism of a Leucine Zipper Peptide by Stopped-Flow Circular Dichroism Spectroscopy by Zitzewitz, Jill A, Bilsel, Osman, Luo, Jiabin, Jones, Bryan E, Matthews, C. Robert

“…Leucine zipper peptides provide simple model systems for studying both the intramolecular and intermolecular interactions that govern protein folding. The…”
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