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Unfolded and intermediate states of PrP play a key role in the mechanism of action of an antiprion chaperone

Proceedings of the National Academy of Sciences - PNAS, 2021-03, Vol.118 (9)

2021

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Direct observation of prion-like propagation of protein misfolding templated by pathogenic mutants

Nature chemical biology, 2024-09, Vol.20 (9), p.1220-1226

2024

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Early stages of aggregation of engineered α-synuclein monomers and oligomers in solution

Scientific reports, 2019-02, Vol.9 (1), p.1734, Article 1734

2019

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Partially native intermediates mediate misfolding of SOD1 in single-molecule folding trajectories

Nature communications, 2017-12, Vol.8 (1), p.1881-11, Article 1881

2017

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Structural characteristics and membrane interactions of tandem α-synuclein oligomers

Scientific reports, 2018-04, Vol.8 (1), p.6755-11, Article 6755

2018

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Characterizing the inhibition of α‐synuclein oligomerization by a pharmacological chaperone that prevents prion formation by the protein PrP

Protein science, 2019-09, Vol.28 (9), p.1690-1702

2019

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Probing the origin of prion protein misfolding via reconstruction of ancestral proteins

Protein science, 2022-12, Vol.31 (12), p.e4477-n/a

2022

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Integration of light scattering with machine learning for label free cell detection

Biomedical optics express, 2021-06, Vol.12 (6), p.3512-3529

2021

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The Structures of Thermoplasma volcanium Phosphoribosyl Pyrophosphate Synthetase Bound to Ribose-5-Phosphate and ATP Analogs

Journal of molecular biology, 2011-11, Vol.413 (4), p.844-856

2011

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The Molecular Structure of Ornithine Acetyltransferase from Mycobacterium tuberculosis Bound to Ornithine, a Competitive Inhibitor

Journal of molecular biology, 2010-04, Vol.397 (4), p.979-990

2010

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The Structure of the Arginine Repressor from Mycobacterium tuberculosis Bound with its DNA Operator and Co-repressor, L-Arginine

Journal of molecular biology, 2009-04, Vol.388 (1), p.85-97

2009

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X-ray crystal structure of Mycobacterium tuberculosis haloalkane dehalogenase Rv2579

Biochimica et biophysica acta, 2008-02, Vol.1784 (2), p.351-362

2008

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Mutations protective against prion disease redirect the folding pathway of PrP in single-molecule trajectories

Biophysical journal, 2022-02, Vol.121 (3), p.326a-326a

2022

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Crystal Structure of the Intermediate Complex of the Arginine Repressor from Mycobacterium tuberculosis Bound with Its DNA Operator Reveals Detailed Mechanism of Arginine Repression

Journal of molecular biology, 2010-06, Vol.399 (2), p.240-254

2010

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Crystal Structure of the Arginine Repressor Protein in Complex with the DNA Operator from Mycobacterium tuberculosis

Journal of molecular biology, 2008-12, Vol.384 (5), p.1330-1340

2008

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Probing the Single Molecule Folding Dynamics of Mammalian Prion Proteins from Species with Different Disease Susceptibility

Biophysical journal, 2018-02, Vol.114 (3), p.355a-355a

2018

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Crystal structure of Mycobacterium tuberculosis Rv0760c at 1.50 A resolution, a structural homolog of Delta(5)-3-ketosteroid isomerase

Biochimica et biophysica acta, 2008-11, Vol.1784 (11), p.1625

2008

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The Crystal Structures of Ornithine Carbamoyltransferase from Mycobacterium tuberculosis and Its Ternary Complex with Carbamoyl Phosphate and l-Norvaline Reveal the Enzyme's Catalytic Mechanism

Journal of molecular biology, 2008-01, Vol.375 (4), p.1052-1063

2008

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Direct observation of prion-like propagation of misfolding in single protein molecules

Biophysical journal, 2022-02, Vol.121 (3), p.417a-417a

2022

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Crystal Structure of N-acetyl-γ-glutamyl-phosphate Reductase from Mycobacterium tuberculosis in Complex with NADP

Journal of molecular biology, 2007-04, Vol.367 (5), p.1357-1369

2007

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The significance and symbolism of the number three in traditional cultural events of the Yugur ethnic minority of China

SN Social Sciences, 2022-08, Vol.2 (8), Article 155

2022

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Structure of the C-terminal domain of the arginine repressor protein from Mycobacterium tuberculosis

Acta crystallographica. Section D, Biological crystallography., 2008-09, Vol.64 (9), p.950-956

2008

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Single-Molecule Force Spectroscopy Shows that the Anti-Prion Compound Pentosan Polysulfate Binds Heterogeneously to Folded and Unfolded Prion Protein

Biophysical journal, 2019-02, Vol.116 (3), p.193a-193a

2019

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Role of Dimer Interface on the Cooperativity and Misfolding in SOD1 Studied by Single Molecule Force Spectroscopy

Biophysical journal, 2018-02, Vol.114 (3), p.356a-356a

2018

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Crystal structure of Mycobacterium tuberculosis Rv0760c at 1.50 Å resolution, a structural homolog of Δ5-3-ketosteroid isomerase

Biochimica et biophysica acta. Proteins and proteomics, 2008-11, Vol.1784 (11), p.1625-1632

2008

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Unfolded and intermediate states of PrP play a key role in the mechanism of action of an antiprion chaperone

Direct observation of prion-like propagation of protein misfolding templated by pathogenic mutants

Early stages of aggregation of engineered α-synuclein monomers and oligomers in solution

Partially native intermediates mediate misfolding of SOD1 in single-molecule folding trajectories

Structural characteristics and membrane interactions of tandem α-synuclein oligomers

Characterizing the inhibition of α‐synuclein oligomerization by a pharmacological chaperone that prevents prion formation by the protein PrP

Probing the origin of prion protein misfolding via reconstruction of ancestral proteins

Integration of light scattering with machine learning for label free cell detection

The Structures of Thermoplasma volcanium Phosphoribosyl Pyrophosphate Synthetase Bound to Ribose-5-Phosphate and ATP Analogs

The Molecular Structure of Ornithine Acetyltransferase from Mycobacterium tuberculosis Bound to Ornithine, a Competitive Inhibitor

The Structure of the Arginine Repressor from Mycobacterium tuberculosis Bound with its DNA Operator and Co-repressor, L-Arginine

X-ray crystal structure of Mycobacterium tuberculosis haloalkane dehalogenase Rv2579

Mutations protective against prion disease redirect the folding pathway of PrP in single-molecule trajectories

Crystal Structure of the Intermediate Complex of the Arginine Repressor from Mycobacterium tuberculosis Bound with Its DNA Operator Reveals Detailed Mechanism of Arginine Repression

Crystal Structure of the Arginine Repressor Protein in Complex with the DNA Operator from Mycobacterium tuberculosis

Probing the Single Molecule Folding Dynamics of Mammalian Prion Proteins from Species with Different Disease Susceptibility

Crystal structure of Mycobacterium tuberculosis Rv0760c at 1.50 A resolution, a structural homolog of Delta(5)-3-ketosteroid isomerase

The Crystal Structures of Ornithine Carbamoyltransferase from Mycobacterium tuberculosis and Its Ternary Complex with Carbamoyl Phosphate and l-Norvaline Reveal the Enzyme's Catalytic Mechanism

Direct observation of prion-like propagation of misfolding in single protein molecules

Crystal Structure of N-acetyl-γ-glutamyl-phosphate Reductase from Mycobacterium tuberculosis in Complex with NADP

The significance and symbolism of the number three in traditional cultural events of the Yugur ethnic minority of China

Structure of the C-terminal domain of the arginine repressor protein from Mycobacterium tuberculosis

Single-Molecule Force Spectroscopy Shows that the Anti-Prion Compound Pentosan Polysulfate Binds Heterogeneously to Folded and Unfolded Prion Protein

Role of Dimer Interface on the Cooperativity and Misfolding in SOD1 Studied by Single Molecule Force Spectroscopy

Crystal structure of Mycobacterium tuberculosis Rv0760c at 1.50 Å resolution, a structural homolog of Δ5-3-ketosteroid isomerase

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