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Fast Protein Motions Are Coupled to Enzyme H‑Transfer Reactions

Journal of the American Chemical Society, 2013-02, Vol.135 (7), p.2512-2517

2013

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Allomorphy as a mechanism of post-translational control of enzyme activity

Nature communications, 2020-11, Vol.11 (1), p.5538-12, Article 5538

2020

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α-Fluorophosphonates reveal how a phosphomutase conserves transition state conformation over hexose recognition in its two-step reaction

Proceedings of the National Academy of Sciences - PNAS, 2014-08, Vol.111 (34), p.12384-12389

2014

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Measurement of energy landscape roughness of folded and unfolded proteins

Proceedings of the National Academy of Sciences - PNAS, 2012-11, Vol.109 (48), p.19563-19568

2012

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Peri active site catalysis of proline isomerisation is the molecular basis of allomorphy in β-phosphoglucomutase

Communications biology, 2024-07, Vol.7 (1), p.909-14, Article 909

2024

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Pharmacological chaperone for the structured domain of human prion protein

Proceedings of the National Academy of Sciences - PNAS, 2010-10, Vol.107 (41), p.17610-17615

2010

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Near attack conformers dominate β-phosphoglucomutase complexes where geometry and charge distribution reflect those of substrate

Proceedings of the National Academy of Sciences - PNAS, 2012-05, Vol.109 (18), p.6910-6915

2012

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Multiple forms of copper (II) co-ordination occur throughout the disordered N-terminal region of the prion protein at pH 7.4

Biochemical journal, 2006-12, Vol.400 (3), p.501-510

2006

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A reassessment of copper(II) binding in the full-length prion protein

Biochemical journal, 2006-11, Vol.399 (3), p.435-444

2006

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Anionic Charge Is Prioritized over Geometry in Aluminum and Magnesium Fluoride Transition State Analogs of Phosphoryl Transfer Enzymes

Journal of the American Chemical Society, 2008-03, Vol.130 (12), p.3952-3958

2008

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N-terminal Domain of Prion Protein Directs Its Oligomeric Association

The Journal of biological chemistry, 2014-09, Vol.289 (37), p.25497-25508

2014

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Essential Role of Proline Isomerization in Stefin B Tetramer Formation

Journal of molecular biology, 2007-03, Vol.366 (5), p.1569-1579

2007

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Folding kinetics of the human prion protein probed by temperature jump

Proceedings of the National Academy of Sciences - PNAS, 2009-04, Vol.106 (14), p.5651-5656

2009

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Metal Fluorides as Analogues for Studies on Phosphoryl Transfer Enzymes

Angewandte Chemie International Edition, 2017-04, Vol.56 (15), p.4110-4128

International ed. in English, 2017

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Metal fluorides—multi-functional tools for the study of phosphoryl transfer enzymes, a practical guide

Structure (London), 2024-08

2024

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Simultaneously Enhancing Spectral Resolution and Sensitivity in Heteronuclear Correlation NMR Spectroscopy

Angewandte Chemie (International ed.), 2013-10, Vol.52 (44), p.11616-11619

International ed. in English, 2013

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Loss of Residues 119–136, Including the First β-strand of Human Prion Protein, Generates an Aggregation-competent Partially “Open” Form

Journal of molecular biology, 2023-08, Vol.435 (15), p.168158-168158, Article 168158

2023

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A Trojan horse transition state analogue generated by MgF3− formation in an enzyme active site

Proceedings of the National Academy of Sciences - PNAS, 2006-10, Vol.103 (40), p.14732-14737

2006

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Cryogenic and Laser Photoexcitation Studies Identify Multiple Roles for Active Site Residues in the Light-driven Enzyme Protochlorophyllide Oxidoreductase

The Journal of biological chemistry, 2009-07, Vol.284 (27), p.18160-18166

2009

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The Relationship between Enzyme Conformational Change, Proton Transfer, and Phosphoryl Transfer in β‑Phosphoglucomutase

ACS catalysis, 2021-11, Vol.11 (21), p.12840-12849

2021

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Why did Nature select phosphate for its dominant roles in biology?

New journal of chemistry, 2010, Vol.34 (5), p.784

2010

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Arginine Kinase Activates Arginine for Phosphorylation by Pyramidalization and Polarization

ACS catalysis, 2024-05, Vol.14 (9), p.6650-6658

2024

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Enzymatic production of β-glucose 1,6-bisphosphate through manipulation of catalytic magnesium coordination

Green chemistry : an international journal and green chemistry resource : GC, 2021-02, Vol.23 (2), p.752-762

2021

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Cystatin forms a Tetramer through Structural Rearrangement of Domain-swapped Dimers prior to Amyloidogenesis

Journal of molecular biology, 2004-02, Vol.336 (1), p.165-178

2004

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Mapping Hidden Residual Structure within the Myc bHLH-LZ Domain Using Chemical Denaturant Titration

Structure (London), 2019-10, Vol.27 (10), p.1537-1546.e4

2019

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Fast Protein Motions Are Coupled to Enzyme H‑Transfer Reactions

Allomorphy as a mechanism of post-translational control of enzyme activity

α-Fluorophosphonates reveal how a phosphomutase conserves transition state conformation over hexose recognition in its two-step reaction

Measurement of energy landscape roughness of folded and unfolded proteins

Peri active site catalysis of proline isomerisation is the molecular basis of allomorphy in β-phosphoglucomutase

Pharmacological chaperone for the structured domain of human prion protein

Near attack conformers dominate β-phosphoglucomutase complexes where geometry and charge distribution reflect those of substrate

Multiple forms of copper (II) co-ordination occur throughout the disordered N-terminal region of the prion protein at pH 7.4

A reassessment of copper(II) binding in the full-length prion protein

Anionic Charge Is Prioritized over Geometry in Aluminum and Magnesium Fluoride Transition State Analogs of Phosphoryl Transfer Enzymes

N-terminal Domain of Prion Protein Directs Its Oligomeric Association

Essential Role of Proline Isomerization in Stefin B Tetramer Formation

Folding kinetics of the human prion protein probed by temperature jump

Metal Fluorides as Analogues for Studies on Phosphoryl Transfer Enzymes

Metal fluorides—multi-functional tools for the study of phosphoryl transfer enzymes, a practical guide

Simultaneously Enhancing Spectral Resolution and Sensitivity in Heteronuclear Correlation NMR Spectroscopy

Loss of Residues 119–136, Including the First β-strand of Human Prion Protein, Generates an Aggregation-competent Partially “Open” Form

A Trojan horse transition state analogue generated by MgF3− formation in an enzyme active site

Cryogenic and Laser Photoexcitation Studies Identify Multiple Roles for Active Site Residues in the Light-driven Enzyme Protochlorophyllide Oxidoreductase

The Relationship between Enzyme Conformational Change, Proton Transfer, and Phosphoryl Transfer in β‑Phosphoglucomutase

Why did Nature select phosphate for its dominant roles in biology?

Arginine Kinase Activates Arginine for Phosphorylation by Pyramidalization and Polarization

Enzymatic production of β-glucose 1,6-bisphosphate through manipulation of catalytic magnesium coordination

Cystatin forms a Tetramer through Structural Rearrangement of Domain-swapped Dimers prior to Amyloidogenesis

Mapping Hidden Residual Structure within the Myc bHLH-LZ Domain Using Chemical Denaturant Titration

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