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Heme–Cu Bound Aβ Peptides: Spectroscopic Characterization, Reactivity, and Relevance to Alzheimer’s Disease

Journal of the American Chemical Society, 2011-10, Vol.133 (39), p.15545-15552

2011

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Alzheimer’s Disease: A Heme–Aβ Perspective

Accounts of chemical research, 2015-09, Vol.48 (9), p.2556-2564

2015

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Ligand-Field and Ligand-Binding Analysis of the Active Site of Copper-Bound Aβ Associated with Alzheimer’s Disease

Inorganic chemistry, 2013-02, Vol.52 (3), p.1318-1327

2013

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Peroxidase to Cytochrome b Type Transition in the Active Site of Heme-Bound Amyloid β Peptides Relevant to Alzheimer’s Disease

Inorganic chemistry, 2016-02, Vol.55 (4), p.1748-1757

2016

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Interaction of amyloid β peptides with redox active heme cofactor: Relevance to Alzheimer's disease

Coordination chemistry reviews, 2013-01, Vol.257 (1), p.81-92

2013

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Copper induced spin state change of heme-Aβ associated with Alzheimer's disease

Dalton transactions : an international journal of inorganic chemistry, 2017-10, Vol.46 (39), p.13171-13175

2017

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Formation of compound I in heme bound Aβ-peptides relevant to Alzheimer's disease

Chemical science (Cambridge), 2019-09, Vol.1 (36), p.845-841

2019

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Direct electron transfer between Cyt c and heme-Aβ relevant to Alzheimer's disease

Chemical communications (Cambridge, England), 2013-06, Vol.49 (51), p.5754

2013

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Copper induced spin state change of heme-Aβ associated with Alzheimer's diseaseElectronic supplementary information (ESI) available. See DOI: 10.1039/c7dt01700f

2017-10

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Nitrite reductase activity of heme and copper bound Aβ peptides

Dalton transactions : an international journal of inorganic chemistry, 2019-05, Vol.48 (21), p.7451-7461

2019

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Formation of compound I in heme bound Aβ-peptides relevant to Alzheimer's disease† †Electronic supplementary information (ESI) available. See DOI: 10.1039/c9sc01679a

Chemical science (Cambridge), 2019-07, Vol.10 (36), p.8405-8410

2019

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Direct electron transfer between Cyt c and heme-A relevant to Alzheimer's diseaseElectronic Supplementary Information (ESI) available: Experimental details, absorption, EPR and rR data. See DOI: 10.1039/c3cc42700e

2013-05

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Cytochrome c peroxidase activity of heme bound amyloid β peptides

Journal of biological inorganic chemistry, 2016-09, Vol.21 (5-6), p.683-690

2016

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Interaction of NO with Cu and Heme-Bound Aβ Peptides Associated with Alzheimer’s Disease

Inorganic chemistry, 2013-01, Vol.52 (1), p.362-368

2013

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Heme Proteins – Structure and Function

Fundamentals of Porphyrin Chemistry, 2022

2022

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Heme–Cu Bound Aβ Peptides: Spectroscopic Characterization, Reactivity, and Relevance to Alzheimer’s Disease

Alzheimer’s Disease: A Heme–Aβ Perspective

Ligand-Field and Ligand-Binding Analysis of the Active Site of Copper-Bound Aβ Associated with Alzheimer’s Disease

Peroxidase to Cytochrome b Type Transition in the Active Site of Heme-Bound Amyloid β Peptides Relevant to Alzheimer’s Disease

Interaction of amyloid β peptides with redox active heme cofactor: Relevance to Alzheimer's disease

Copper induced spin state change of heme-Aβ associated with Alzheimer's disease

Formation of compound I in heme bound Aβ-peptides relevant to Alzheimer's disease

Direct electron transfer between Cyt c and heme-Aβ relevant to Alzheimer's disease

Copper induced spin state change of heme-Aβ associated with Alzheimer's diseaseElectronic supplementary information (ESI) available. See DOI: 10.1039/c7dt01700f

Nitrite reductase activity of heme and copper bound Aβ peptides

Formation of compound I in heme bound Aβ-peptides relevant to Alzheimer's disease† †Electronic supplementary information (ESI) available. See DOI: 10.1039/c9sc01679a

Direct electron transfer between Cyt c and heme-A relevant to Alzheimer's diseaseElectronic Supplementary Information (ESI) available: Experimental details, absorption, EPR and rR data. See DOI: 10.1039/c3cc42700e

Cytochrome c peroxidase activity of heme bound amyloid β peptides

Interaction of NO with Cu and Heme-Bound Aβ Peptides Associated with Alzheimer’s Disease

Heme Proteins – Structure and Function

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