P. Faller

发表

Metal ions and intrinsically disordered proteins and peptides: from Cu/Zn amyloid-β to general principles.

P. Faller, C. Hureau, G. La Penna, 2014, Accounts of chemical research.

Amyloid β Protein and Alzheimer's Disease: When Computer Simulations Complement Experimental Studies.

N. Buchete, J. H. Viles, S. Melchionna, 2015, Chemical reviews.

Impact of Cu(II) Binding on Structures and Dynamics of Aβ42 Monomer and Dimer: Molecular Dynamics Study.

M. Li, Q. Vuong, P. Faller, 2016, ACS chemical neuroscience.

Amyloid‐Beta Peptide Forms Monomeric Complexes With CuII and ZnII Prior to Aggregation

P. Faller, H. Mazarguil, Y. Coppel, 2007 .

Photosystem II: evolutionary perspectives.

P. Faller, A. Rutherford, 2003, Philosophical transactions of the Royal Society of London. Series B, Biological sciences.

Reversible turn-on fluorescent Cu(ii) sensors: rather dream than reality?

G. Ulrich, P. Faller, L. Raibaut, 2019, Dalton transactions.

Bioinorganic Chemistry of Copper and Zinc Ions Coordinated to Amyloid‐β Peptide

P. Faller, C. Hureau, 2009 .

Inhibition of Cu-amyloid-β by using bifunctional peptides with β-sheet breaker and chelator moieties.

O. Cuvillier, J. Østergaard, P. Faller, 2012, Chemistry.

X-ray and solution structures of Cu(II) GHK and Cu(II) DAHK complexes: influence on their redox properties.

S. Sayen, E. Guillon, P. Faller, 2011, Chemistry.

Intense Raman bands and low luminescence of thin films of heme proteins on silica

W. Bacsa, P. Faller, V. Sonois, 2009 .

Reevaluation of copper(I) affinity for amyloid-β peptides by competition with ferrozine--an unusual copper(I) indicator.

P. Faller, C. Hureau, Bruno Aliès, 2012, Chemistry.

Copper in Alzheimer disease: too much, too little, or misplaced?

P. Faller, 2012, Free radical biology & medicine.

Metal-Binding to Amyloid-β Peptide: Coordination, Aggregation, and Reactive Oxygen Species Production

V. Borghesani, P. Faller, C. Hureau, 2017 .

Metal-catalyzed oxidation of Aβ and the resulting reorganization of Cu binding sites promote ROS production

D. Testemale, P. Faller, C. Hureau, 2016, Metallomics : integrated biometal science.

Free Superoxide is an Intermediate in the Production of H2O2 by Copper(I)-Aβ Peptide and O2.

João V. Rodrigues, C. Gomes, P. Faller, 2016, Angewandte Chemie.

How Zn can impede Cu detoxification by chelating agents in Alzheimer's disease: a proof-of-concept study

P. Faller, C. Hureau, A. Conte-Daban, 2016, Dalton transactions.

Iron(II) binding to amyloid-β, the Alzheimer's peptide.

P. Faller, C. Hureau, Y. Coppel, 2011, Inorganic chemistry.

Redox Chemistry of Copper–Amyloid‐β: The Generation of Hydroxyl Radical in the Presence of Ascorbate is Linked to Redox‐Potentials and Aggregation State

P. Faller, H. Mazarguil, Luc Guilloreau, 2007, Chembiochem : a European journal of chemical biology.

Resolving intermediates in biological proton-coupled electron transfer: A tyrosyl radical prior to proton movement

A. Rutherford, P. Faller, S. Un, 2003, Proceedings of the National Academy of Sciences of the United States of America.

Dynamics of Zn(II) binding as a key feature in the formation of amyloid fibrils by Aβ11-28.

P. Faller, C. Hureau, Bruno Aliès, 2012, Inorganic chemistry.

Isolation, primary structures and metal binding properties of neuronal growth inhibitory factor (GIF) from bovine and equine brain

P. Hunziker, P. Faller, D. Pountney, 1994, FEBS letters.

Redox Silencing of Copper in Metal-linked Neurodegenerative Disorders

Gabriele Meloni, P. Faller, M. Vašák, 2007, Journal of Biological Chemistry.

Copper-Catalyzed Glutathione Oxidation is Accelerated by the Anticancer Thiosemicarbazone Dp44mT and Further Boosted at Lower pH

P. Heffeter, P. Hellwig, P. Faller, 2022, Journal of the American Chemical Society.

Carotenoid oxidation in photosystem II.

A. Rutherford, Y. Deligiannakis, P. Faller, 1999, Biochemistry.

Side-Path Electron Donors: Cytochrome b559, Chlorophyll Z and β-Carotene

A. Rutherford, P. Faller, C. Fufezan, 2005 .

Rapid formation of the stable tyrosyl radical in photosystem II

A. Rutherford, R. Debus, M. Sugiura, 2001, Proceedings of the National Academy of Sciences of the United States of America.

The stable tyrosyl radical in photosystem II: why D?

A. Boussac, P. Faller, A. Rutherford, 2004, Biochimica et biophysica acta.

Cysteine and glutathione trigger the Cu-Zn swap between Cu(ii)-amyloid-β4-16 peptide and Zn7-metallothionein-3.

W. Bal, P. Faller, M. Vašák, 2017, Chemical communications.

Copper-binding motifs Xxx-His or Xxx-Zzz-His (ATCUN) linked to an antimicrobial peptide: Cu-binding, antimicrobial activity and ROS production.

C. Aisenbrey, B. Bechinger, P. Faller, 2020, Journal of inorganic biochemistry.

Concept for simultaneous and specific in situ monitoring of amyloid oligomers and fibrils via Förster resonance energy transfer.

P. Faller, C. Hureau, E. Essassi, 2014, Analytical chemistry.

The role of metal ions in amyloid formation: general principles from model peptides.

P. Faller, C. Hureau, Bruno Aliès, 2013, Metallomics : integrated biometal science.

The Na+/K+-ATPase and the amyloid-beta peptide aβ1-40 control the cellular distribution, abundance and activity of TRPC6 channels.

M. Jadot, Sylvain Chauvet, Marielle Boonen, 2015, Biochimica et biophysica acta.

Neurodegenerative diseases and exposure to the environmental metals Mn, Pb, and Hg

P. Baveye, L. Charlet, P. Faller, 2012 .

Metal ions in neurodegenerative diseases

P. Faller, C. Hureau, 2012 .

Chlorophyll and carotenoid radicals in photosystem II studied by pulsed ENDOR.

A. Rutherford, P. Faller, T. Maly, 2001, Biochemistry.

Copper(I/II), α/β‐Synuclein and Amyloid‐β: Menage à Trois?

L. Casella, P. Faller, C. Hureau, 2015, Chembiochem : a European journal of chemical biology.

Amyloid Oligomers: A Joint Experimental/Computational Perspective on Alzheimer's Disease, Parkinson's Disease, Type II Diabetes, and Amyotrophic Lateral Sclerosis.

Son Tung Ngo, Bikash R. Sahoo, R. Nussinov, 2021, Chemical reviews.

Zinc binding to amyloid-beta: isothermal titration calorimetry and Zn competition experiments with Zn sensors.

P. Faller, Christine Talmard, Ana C S Bouzan, 2007, Biochemistry.

Pulse EPR spectroscopy reveals the coordination sphere of copper(II) ions in the 1-16 amyloid-beta peptide: a key role of the first two N-terminus residues.

P. Faller, C. Hureau, S. Gambarelli, 2009, Angewandte Chemie.

Copper(I) targeting in the Alzheimer's disease context: a first example using the biocompatible PTA ligand.

D. Testemale, P. Faller, C. Hureau, 2015, Metallomics : integrated biometal science.

Interference of a new cyclometallated Pt compound with Cu binding to amyloid-β peptide.

P. Faller, C. Hureau, S. Ladeira, 2012, Dalton transactions.

New insights into the coordination of Cu(II) by the amyloid-B 16 peptide from Fourier transform IR spectroscopy and isotopic labeling.

P. Hellwig, P. Faller, Youssef El Khoury, 2011, The journal of physical chemistry. B.

Aggregation‐Prone Amyloid‐β⋅CuII Species Formed on the Millisecond Timescale under Mildly Acidic Conditions

L. Hemmingsen, K. Teilum, T. Knowles, 2015, Chembiochem : a European journal of chemical biology.

Metal Binding to Aβ Peptides Inhibits Interaction with Cytochrome c: Insights from Abiological Constructs

A. Dey, A. Sarkar, P. Faller, 2018, ACS omega.

The glutathione/metallothionein system challenges the design of efficient O2-activating Cu-complexes.

A. Krężel, Gabriele Meloni, P. Faller, 2020, Angewandte Chemie.

A terbium(iii) luminescent ATCUN-based peptide sensor for selective and reversible detection of copper(ii) in biological media.

P. Faller, L. Raibaut, O. Sénèque, 2020, Chemical communications.

Cu(II) Binding to the N-Terminal Model Peptide of the Human Ctr2 Transporter at Lysosomal and Extracellular pH.

P. Faller, N. E. Wezynfeld, B. Vileno, 2019, Inorganic chemistry.

Cu(II) Binding to the Peptide Ala-His-His, a Chimera of the Canonical Cu(II)-Binding Motifs Xxx-His and Xxx-Zzz-His.

W. Bal, P. Hellwig, P. Faller, 2017, Inorganic chemistry.

Remote His50 Acts as a Coordination Switch in the High-Affinity N-Terminal Centered Copper(II) Site of α-Synuclein.

L. Casella, P. Faller, C. Hureau, 2015, Inorganic chemistry.

Why the Ala-His-His Peptide Is an Appropriate Scaffold to Remove and Redox Silence Copper Ions from the Alzheimer’s-Related Aβ Peptide

P. Faller, C. Hureau, Emilie Mathieu, 2022, Biomolecules.

Use of a new water-soluble Zn sensor to determine Zn affinity for the amyloid-β peptide and relevant mutants.

S. Sayen, E. Guillon, P. Faller, 2014, Metallomics : integrated biometal science.

Is ascorbate Dr Jekyll or Mr Hyde in the Cu(Aβ) mediated oxidative stress linked to Alzheimer’s disease?†

P. Faller, C. Hureau, F. Collin, 2016, Dalton transactions.

Cu transfer from amyloid-β4-16 to metallothionein-3: the role of the neurotransmitter glutamate and metallothionein-3 Zn(ii)-load states.

A. Krężel, Adam Pomorski, W. Bal, 2018, Chemical communications.

Copper(II) coordination to amyloid β: murine versus human peptide.

P. Faller, C. Hureau, Hélène Eury, 2011, Angewandte Chemie.

Mechanism of Cd2+ toxicity: Cd2+ inhibits photoactivation of Photosystem II by competitive binding to the essential Ca2+ site.

A. Krieger-Liszkay, P. Faller, K. Kienzler, 2005, Biochimica et biophysica acta.

How trimerization of CTR1 N-terminal model peptides tunes Cu-binding and redox-chemistry.

P. Faller, N. E. Wezynfeld, L. Raibaut, 2020, Chemical communications.

Copper and heme-mediated Abeta toxicity: redox chemistry, Abeta oxidations and anti-ROS compounds.

P. Faller, C. Hureau, P. Dorlet, 2013, Current topics in medicinal chemistry.

Isolation and characterization of a novel monomeric zinc‐ and heme‐containing protein from bovine brain

P. Gehrig, P. Faller, D. Pountney, 1996, FEBS letters.

Amyloid fibrils: modulation of formation and structure by copper(II)

P. Faller, V. Pradines, Alina Jurca Stroia, 2008 .

Metals and Alzheimer's Disease

C. Atwood, P. Faller, Anthony R. White, 2011, International journal of Alzheimer's disease.

Binding of transition metal ions to albumin: sites, affinities and rates.

W. Bal, P. Faller, E. Kurowska, 2013, Biochimica et biophysica acta.

pH-Dependent Cu(II) coordination to amyloid-β peptide: impact of sequence alterations, including the H6R and D7N familial mutations.

P. Faller, C. Hureau, Bruno Aliès, 2011, Inorganic chemistry.

Structural and thermodynamical properties of CuII amyloid-β16/28 complexes associated with Alzheimer’s disease

M. Winterhalter, P. Faller, H. Mazarguil, 2006, JBIC Journal of Biological Inorganic Chemistry.

Coordination complexes and biomolecules: A wise wedding for catalysis upgrade

P. Faller, C. Hureau, M. Hoarau, 2016 .

Thioflavin Derivatives as Markers for Amyloid‐β Fibrils: Insights into Structural Features Important for High‐Affinity Binding

S. Mazères, P. Faller, E. Gras, 2008, ChemMedChem.

Why Is Research on Amyloid-β Failing to Give New Drugs for Alzheimer's Disease?

A. Doig, P. Derreumaux, N. Hooper, 2017, ACS chemical neuroscience.

Copper coordination to native N-terminally modified versus full-length amyloid-β: second-sphere effects determine the species present at physiological pH.

S. Sayen, E. Guillon, P. Faller, 2012, Inorganic chemistry.

P. Hellwig, P. Faller, Youssef El Khoury, 2017, JBIC Journal of Biological Inorganic Chemistry.

Thermodynamic study of Cu2+ binding to the DAHK and GHK peptides by isothermal titration calorimetry (ITC) with the weaker competitor glycine

Mathias Winterhalter, Peter Faller, M. Winterhalter, 2011, JBIC Journal of Biological Inorganic Chemistry.

Copper-Targeting Approaches in Alzheimer's Disease: How To Improve the Fallouts Obtained from in Vitro Studies.

P. Faller, C. Hureau, C. Esmieu, 2019, Inorganic chemistry.

Cu and Zn coordination to amyloid peptides: From fascinating chemistry to debated pathological relevance.

P. Faller, C. Hureau, Bruno Aliès, 2018, Coordination chemistry reviews.

Cu(II) affinity for the Alzheimer's peptide: tyrosine fluorescence studies revisited.

W. Bal, P. Faller, C. Hureau, 2013, Analytical chemistry.

Deprotonation of the Asp1-Ala2 peptide bond induces modification of the dynamic copper(II) environment in the amyloid-beta peptide near physiological pH.

S. Sayen, E. Guillon, P. Faller, 2009, Angewandte Chemie.

A bioinorganic view of Alzheimer's disease: when misplaced metal ions (re)direct the electrons to the wrong target.

P. Faller, C. Hureau, 2012, Chemistry.

Zinc(II) binds to the neuroprotective peptide humanin.

P. Faller, H. Mazarguil, V. Sonois, 2006, Journal of inorganic biochemistry.

Characterization of the ZnII Binding to the Peptide Amyloid‐β1–16 linked to Alzheimer's Disease

P. Faller, H. Mazarguil, Y. Coppel, 2005, Chembiochem : a European journal of chemical biology.

Metal-binding properties of the peptide APP170-188: a model of the ZnII-binding site of amyloid precursor protein (APP).

P. Faller, Y. Mekmouche, Eliza-Diana Ciuculescu, 2005, Chemistry.

Extracellular Cu2+ pools and their detection: From current knowledge to next-generation probes

N. Vitale, P. Faller, L. Raibaut, 2021 .

The heart of photosynthesis in glorious 3D.

P. Faller, A. Rutherford, 2001, Trends in biochemical sciences.

Development of Cu(ii)-specific peptide shuttles capable of preventing Cu–amyloid beta toxicity and importing bioavailable Cu into cells

S. Chasserot-Golaz, N. Vitale, S. Gasman, 2022, Chemical science.

Reactivity of Cu(ii)-, Zn(ii)- and Fe(ii)-thiosemicarbazone complexes with glutathione and metallothionein: from stability to dissociation to transmetallation.

A. Krężel, P. Faller, M. D. Peris-Díaz, 2019, Metallomics : integrated biometal science.

Activity of Metal-Responsive Transcription Factor 1 by Toxic Heavy Metals and H2O2 In Vitro Is Modulated by Metallothionein

Bo Zhang, Michael Hagmann, Walter Schaffner, 2003, Molecular and Cellular Biology.

Oxidative stress and the amyloid beta peptide in Alzheimer’s disease

M. Tomás, D. Bonnefont-Rousselot, P. Faller, 2017, Redox biology.

Copper Induces Protein Aggregation, a Toxic Process Compensated by Molecular Chaperones

D. Reichmann, U. Jakob, P. Genevaux, 2022, mBio.

Rapid exchange of metal between Zn(7)-metallothionein-3 and amyloid-β peptide promotes amyloid-related structural changes.

L. Hemmingsen, J. Østergaard, N. Heegaard, 2012, Biochemistry.

Identification of key structural features of the elusive Cu–Aβ complex that generates ROS in Alzheimer’s disease

P. Faller, C. Hureau, I. Kieffer, 2017, Chemical science.

Abeta-mediated ROS production by Cu ions: structural insights, mechanisms and relevance to Alzheimer's disease.

P. Faller, C. Hureau, 2009, Biochimie.

Beta-carotene redox reactions in photosystem II: electron transfer pathway.

A. Rutherford, P. Faller, A. Pascal, 2001, Biochemistry.

Growth inhibitory factor and zinc affect neural cell cultures in a tissue specific manner.

P. Faller, A. Bruinink, C. Sidler, 1998, Chemico-biological interactions.

The catalytically active copper-amyloid-Beta state: coordination site responsible for reactive oxygen species production.

F. Nepveu, P. Faller, C. Hureau, 2013, Angewandte Chemie.

Amyloid-beta peptide forms monomeric complexes with Cu(II) and Zn(II) prior to aggregation.

P. Faller, H. Mazarguil, Y. Coppel, 2007, Chembiochem : a European journal of chemical biology.

Switching on Endogenous Metal Binding Proteins in Parkinson’s Disease

M. Goulding, P. Faller, R. Chung, 2019, Cells.

N-Terminal Cu-Binding Motifs (Xxx-Zzz-His, Xxx-His) and Their Derivatives: Chemistry, Biology and Medicinal Applications.

W. Bal, P. Faller, C. Hureau, 2018, Chemistry.

Role of metal ions in the self-assembly of the Alzheimer's amyloid-β peptide.

P. Faller, C. Hureau, O. Berthoumieu, 2013, Inorganic chemistry.

Zinc release of Zn₇-metallothionein-3 induces fibrillar type amyloid-β aggregates.

Gabriele Meloni, P. Faller, Christine Talmard, 2010, Metallomics : integrated biometal science.

Bioinorganic chemistry of copper and zinc ions coordinated to amyloid-beta peptide.

P. Faller, C. Hureau, 2009, Dalton transactions.

Coordination of Metal Ions to β-Amyloid Peptide: Impact on Alzheimer’s Disease

G. Penna, S. Furlan, P. Faller, 2011 .

Evidence that the principal CoII-binding site in human serum albumin is not at the N-terminus: implication on the albumin cobalt binding test for detecting myocardial ischemia.

P. Faller, Emmanuelle Mothes, 2007, Biochemistry.

Low catalytic activity of the Cu(ii)-binding motif (Xxx-Zzz-His; ATCUN) in reactive oxygen species production and inhibition by the Cu(i)-chelator BCS.

P. Faller, L. Raibaut, B. Vileno, 2018, Chemical communications.

In Vitro Is Modulated by Metallothionein 2 O 2 Factor 1 by Toxic Heavy Metals and H Activity of Metal-Responsive Transcription

M. Hagmann, Çağatay, P. Faller, 2003 .

Methods and techniques to study the bioinorganic chemistry of metal–peptide complexes linked to neurodegenerative diseases

P. Hellwig, P. Faller, C. Hureau, 2012 .

Metallothionein, Copper and Alpha-Synuclein in Alpha-Synucleinopathies

M. Goulding, P. Faller, R. Chung, 2017, Front. Neurosci..

Importance of dynamical processes in the coordination chemistry and redox conversion of copper amyloid-β complexes

E. Fonda, P. Faller, C. Hureau, 2009, JBIC Journal of Biological Inorganic Chemistry.

Copper Imbalance in Alzheimer's Disease and Its Link with the Amyloid Hypothesis: Towards a Combined Clinical, Chemical, and Genetic Etiology.

R. Squitti, K. P. Kepp, P. Faller, 2021, Journal of Alzheimer's disease : JAD.

Copper and Zinc Binding to Amyloid‐β: Coordination, Dynamics, Aggregation, Reactivity and Metal‐Ion Transfer

Peter Faller, P. Faller, 2009, Chembiochem : a European journal of chemical biology.

A thienoquinoxaline and a styryl-quinoxaline as new fluorescent probes for amyloid-β fibrils

H. Benzeid, P. Faller, E. Essassi, 2012 .

Metal swap between Zn7-metallothionein-3 and amyloid-beta-Cu protects against amyloid-beta toxicity.

J. Teissié, Gabriele Meloni, P. Faller, 2008, Nature chemical biology.

Tyrosine D oxidation at cryogenic temperature in photosystem II.

A. Rutherford, R. Debus, P. Faller, 2002, Biochemistry.

High-Field EPR Study of Carotenoid•+ and the Angular Orientation of Chlorophyll z•+ in Photosystem II

P. Faller, S. Un, Rutherford Aw, 2000 .

Copper Transfer from Cu–Aβ to Human Serum Albumin Inhibits Aggregation, Radical Production and Reduces Aβ Toxicity

M. Maddelein, M. Miquel, P. Faller, 2009, Chembiochem : a European journal of chemical biology.

(Bio)Chemical strategies to modulate amyloid-β self-assembly.

P. Genevaux, P. Faller, C. Hureau, 2019, ACS chemical neuroscience.

Zinc(II) Binding Site to the Amyloid-β Peptide: Insights from Spectroscopic Studies with a Wide Series of Modified Peptides

S. Sayen, E. Guillon, P. Faller, 2016, Inorganic chemistry.

Folding of the prion peptide GGGTHSQW around the copper(II) ion: identifying the oxygen donor ligand at neutral pH and probing the proximity of the tryptophan residue to the copper ion

T. Mattioli, P. Faller, C. Hureau, 2008, JBIC Journal of Biological Inorganic Chemistry.

Evidence for Cu(I) clusters and Zn(II) clusters in neuronal growth-inhibitory factor isolated from bovine brain.

P. Faller, D. Pountney, R. Bogumil, 1996, European journal of biochemistry.

Zinc(II) modulates specifically amyloid formation and structure in model peptides

S. Sayen, E. Guillon, P. Faller, 2011, JBIC Journal of Biological Inorganic Chemistry.

Reproducibility Problems of Amyloid-β Self-Assembly and How to Deal With Them

P. Faller, C. Hureau, 2021, Frontiers in Chemistry.

Modeling the Cu+ binding in the 1-16 region of the amyloid-β peptide involved in Alzheimer's disease.

S. Furlan, P. Faller, C. Hureau, 2010, The journal of physical chemistry. B.

Platinoid complexes to target monomeric disordered peptides: a forthcoming solution against amyloid diseases?

P. Faller, C. Hureau, 2014, Dalton transactions.

Pt(II) compounds interplay with Cu(II) and Zn(II) coordination to the amyloid-β peptide has metal specific consequences on deleterious processes associated to Alzheimer's disease.

P. Faller, C. Hureau, F. Collin, 2013, Chemical communications.

Insights into the mechanisms of amyloid formation of Zn(II)-Ab11-28: pH-dependent zinc coordination and overall charge as key parameters for kinetics and the structure of Zn(II)-Ab11-28 aggregates.

S. Sayen, E. Guillon, P. Faller, 2012, Inorganic chemistry.

The N-terminal 14-mer model peptide of human Ctr1 can collect Cu(ii) from albumin. Implications for copper uptake by Ctr1.

Kathryn L Haas, W. Bal, P. Faller, 2018, Metallomics : integrated biometal science.

Ascorbate oxidation by Cu(Amyloid- β ) complexes: determination of the intrinsic rate as function of alterations in the peptide sequence reveals key residues for ROS production

P. Faller, C. Hureau, M. Barrio, 2018 .

Identifying, by first-principles simulations, Cu[amyloid-β] species making Fenton-type reactions in Alzheimer's disease.

O. Andreussi, P. Faller, C. Hureau, 2013, The journal of physical chemistry. B.

Modeling copper binding to the amyloid-β peptide at different pH: toward a molecular mechanism for Cu reduction.

S. Furlan, P. Faller, C. Hureau, 2012, The journal of physical chemistry. B.

Two functions, one molecule: a metal-binding and a targeting moiety to combat Alzheimer's disease.

P. Faller, C. Hureau, I. Sasaki, 2010, Chembiochem : a European journal of chemical biology.

Mechanism of zinc(II)-promoted amyloid formation: zinc(II) binding facilitates the transition from the partially α-helical conformer to aggregates of amyloid β protein(1–28)

P. Faller, Christine Talmard, Rodrigue Leuma Yona, 2009, JBIC Journal of Biological Inorganic Chemistry.

Optical and TDPAC spectroscopy of Hg(II)-rubredoxin: model for a mononuclear tetrahedral [Hg(CysS)4]2− center

T. Butz, P. Faller, Isolde Collaboration, 2000, Journal of Biological Inorganic Chemistry.

Structural characterization of Cu(I) and Zn(II) sites in neuronal-growth-inhibitory factor by extended X-ray absorption fine structure (EXAFS).

P. Binz, J. Charnock, P. Faller, 1998, European Journal of Biochemistry.

Neuronal growth‐inhibitory factor (metallothionein‐3): reactivity and structure of metal–thiolate clusters *

P. Faller, 2010, The FEBS journal.

Evidence for a dynamic structure of human neuronal growth inhibitory factor and for major rearrangements of its metal-thiolate clusters.

D. Winge, O. Zerbe, P. Faller, 1999, Biochemistry.

Distinct metal-thiolate clusters in the N-terminal domain of neuronal growth inhibitory factor.

P. Faller, M. Vašák, 1997, Biochemistry.

Metal-thiolate clusters in neuronal growth inhibitory factor (GIF).

P. Faller, D. Hasler, M. Vašák, 2000, Journal of inorganic biochemistry.

Uptake of copper from hemopexin (HPX) in the absence and presence of heme by hepatic and mammary epithelial cells in culture

P. Faller, M. Linder, T. Kidane, 2020, The FASEB Journal.

Mutations of Histidine 13 to Arginine and Arginine 5 to Glycine Are Responsible for Different Coordination Sites of Zinc(II) to Human and Murine Peptides.

D. Testemale, S. Sayen, E. Guillon, 2018, Chemistry.

Dual Role of Glutathione as a Reducing Agent and Cu-Ligand Governs the ROS Production by Anticancer Cu-Thiosemicarbazone Complexes

P. Faller, E. Sicilia, B. Vileno, 2023, Inorganic chemistry.

Acrolein and Copper as Competitive Effectors of α-Synuclein.

P. Hellwig, F. Bellia, P. Faller, 2019, Chemistry.

Role of PTA in the prevention of Cu(amyloid-β) induced ROS formation and amyloid-β oligomerisation in the presence of Zn.

P. Faller, C. Hureau, M. Laguna, 2019, Metallomics : integrated biometal science.

Chemistry of mammalian metallothioneins and their interaction with amyloidogenic peptides and proteins.

Gabriele Meloni, P. Faller, C. Hureau, 2017, Chemical Society reviews.

Metal-thiolate clusters in the C-terminal domain of human neuronal growth inhibitory factor (GIF).

P. Faller, D. Hasler, M. Vašák, 1998, Biochemistry.

Revisiting the pro-oxidant activity of copper: interplay of ascorbate, cysteine, and glutathione

F. Stellato, S. Morante, P. Faller, 2023, Metallomics : integrated biometal science.

Ascorbate Oxidation by Cu(Amyloid-β) Complexes: Determination of the Intrinsic Rate as a Function of Alterations in the Peptide Sequence Revealing Key Residues for Reactive Oxygen Species Production.

P. Faller, C. Hureau, E. Atrián-Blasco, 2018, Analytical chemistry.

Derivatization of the Peptidic Xxx-Zzz-His Motif toward a Ligand with Attomolar CuII Affinity under Maintaining High Selectivity and Fast Redox Silencing.

P. Faller, C. Platas‐Iglesias, B. Vileno, 2023, Inorganic chemistry.

A luminescent ATCUN peptide variant with enhanced properties for copper(II) sensing in biological media.

P. Faller, L. Raibaut, B. Vileno, 2021, Journal of inorganic biochemistry.

Zn impacts Cu coordination to amyloid-β, the Alzheimer's peptide, but not the ROS production and the associated cell toxicity.

O. Proux, S. Sayen, E. Guillon, 2013, Chemical communications.

Nanoscale needle shaped histidine and narrow vibrational Raman bands using visible excitation

W. Bacsa, P. Faller, A. Estève, 2007 .

Raman study and DFT calculations of amino acids

A. Zwick, W. Bacsa, P. Faller, 2008 .

Amyloid-β/Drug Interactions from Computer Simulations and Cell-Based Assays.

A. Doig, P. Derreumaux, P. Nguyen, 2018, Journal of Alzheimer's disease : JAD.

Human serum albumin as a copper source for anticancer thiosemicarbazones

B. Keppler, G. Koellensperger, P. Heffeter, 2023, Metallomics : integrated biometal science.

Burning Amyloid-β with a Near-Infrared Photosensitizer

P. Faller, Vincent Lebrun, 2018 .

Molecular structure of the NQTrp inhibitor with the Alzheimer Aβ1-28 monomer.

A. Doig, P. Derreumaux, P. Nguyen, 2015, European journal of medicinal chemistry.

The catalytically active copper-amyloid-Beta state: coordination site responsible for reactive oxygen species production.

F. Nepveu, P. Faller, C. Hureau, 2013, Angewandte Chemie.

Correction: A Robust and Efficient Production and Purification Procedure of Recombinant Alzheimers Disease Methionine-Modified Amyloid-β Peptides

I. André, M. Remaud-Siméon, P. Faller, 2016, PloS one.

A Robust and Efficient Production and Purification Procedure of Recombinant Alzheimers Disease Methionine-Modified Amyloid-β Peptides

I. André, M. Remaud-Siméon, P. Faller, 2016, PloS one.

Combined experimental and simulation studies suggest a revised mode of action of the anti-Alzheimer disease drug NQ-Trp.

C. Rampon, A. Doig, P. Derreumaux, 2015, Chemistry.

Metal ions and intrinsically disordered proteins and peptides: from Cu/Zn amyloid-β to general principles.

P. Faller, C. Hureau, G. La Penna, 2014, Accounts of chemical research.

Modeling copper binding to the amyloid-β peptide at different pH: toward a molecular mechanism for Cu reduction.

S. Furlan, P. Faller, C. Hureau, 2012, The journal of physical chemistry. B.

Copper Transfer from Cu–Aβ to Human Serum Albumin Inhibits Aggregation, Radical Production and Reduces Aβ Toxicity

M. Maddelein, M. Miquel, P. Faller, 2009, Chembiochem : a European journal of chemical biology.

Cu transfer from amyloid-β4-16 to metallothionein-3: the role of the neurotransmitter glutamate and metallothionein-3 Zn(ii)-load states.

A. Krężel, Adam Pomorski, W. Bal, 2018, Chemical communications.

Thermodynamic study of Cu2+ binding to the DAHK and GHK peptides by isothermal titration calorimetry (ITC) with the weaker competitor glycine

M. Winterhalter, W. Bal, P. Faller, 2011, JBIC Journal of Biological Inorganic Chemistry.

Structural and biological studies on native bovine Cu,Zn-metallothionein-3

P. Binz, J. Charnock, P. Faller, 1999 .

Triggering Cu-coordination change in Cu(ii)-Ala-His-His by external ligands.

W. Bal, P. Hellwig, P. Faller, 2019, Chemical communications.