D. Harris

发表

Prion neurotoxicity: insights from prion protein mutants.

I. Solomon, Jessie A Schepker, D. Harris, 2010, Current issues in molecular biology.

Cell Surface Expression of the Prion Protein in Yeast Does Not Alter Copper Utilization Phenotypes*

D. Harris, Aimin Li, Jiaxin Dong, 2004, Journal of Biological Chemistry.

The binding and release of the inhibitor protein are governed independently by ATP and membrane potential in ox-heart submitochondrial vesicles.

G. Lippe, D. Harris, M. Sorgato, 1988, Biochimica et biophysica acta.

Glycolipid-anchored proteins in neuroblastoma cells form detergent- resistant complexes without caveolin

D. Harris, A. Gorodinsky, 1995, The Journal of cell biology.

Chapter 1 Cellular ATP

D. Harris, 1996 .

The possible role of tightly bound adenine nucleotides in oxidative and photosynthetic phosphorylation.

E. C. Slater, D. Harris, J. Rosing, 1975, Journal of supramolecular structure.

Mutant and Infectious Prion Proteins Display Common Biochemical Properties in Cultured Cells (*)

D. Harris, S. Lehmann, 1996, The Journal of Biological Chemistry.

A murine model of a familial prion disease.

B. Ghetti, D. Harris, R. Chiesa, 2003, Clinics in laboratory medicine.

Oxidative degradation of bilirubin produces vasoactive compounds.

D. Harris, C. Schofield, T. Claridge, 2000, European journal of biochemistry.

Primary structure and properties of the inhibitory protein of the mitochondrial ATPase (H(+)-ATP synthase) from potato.

J. Featherstone, D. Harris, A. Willis, 1995, Biochimica et biophysica acta.

An N-terminal Polybasic Domain and Cell Surface Localization Are Required for Mutant Prion Protein Toxicity*

I. Solomon, D. Harris, J. E. Huettner, 2011, The Journal of Biological Chemistry.

Prion protein with an octapeptide insertion has impaired neuroprotective activity in transgenic mice

B. Ghetti, D. Harris, Aimin Li, 2007, The EMBO journal.

The interactions of coupling ATPases with nucleotides.

D. Harris, 1978, Biochimica et biophysica acta.

A Mutant Prion Protein Displays an Aberrant Membrane Association When Expressed in Cultured Cells (*)

D. Harris, S. Lehmann, 1995, The Journal of Biological Chemistry.

Prion protein at the crossroads of physiology and disease

D. Harris, Jessie A. Turnbaugh, U. Unterberger, 2012, Trends in Neurosciences.

A transmembrane form of the prion protein contains an uncleaved signal peptide and is retained in the endoplasmic Reticulum.

R. S. Stewart, D. Harris, B. Drisaldi, 2001, Molecular biology of the cell.

Cell biological studies of the prion protein.

D. Harris, 1999, Current issues in molecular biology.

Familial Prion Diseases Modeled in Cell Culture

D. Harris, S. Lehmann, N. Daude, 1998 .

A wild-type prion protein does not acquire properties of the scrapie isoform when coexpressed with a mutant prion protein in cultured cells.

D. Harris, S. Lehmann, N. Daude, 1997, Brain research. Molecular brain research.

A glycolipid-anchored prion protein is endocytosed via clathrin-coated pits

D. Harris, S. Shyng, J. Heuser, 1994, The Journal of cell biology.

Wild-Type Mouse Prion Protein Neuroblastoma Cell Lines Overexpressing Mouse-Adapted Scrapie Strains to Murine Successful Transmission of Three

D. Harris, H. Laude, J. Grassi, 1999 .

GFP-tagged mutant prion protein forms intra-axonal aggregates in transgenic mice

D. Harris, S. Barmada, E. Biasini, 2008, Neurobiology of Disease.

The Prion Protein and Copper

D. Harris, L. R. Brown, 2002 .

Copper Stimulates Endocytosis of the Prion Protein*

D. Harris, P. Pauly, 1998, The Journal of Biological Chemistry.

Analysis of the mechanism of fast axonal transport by intracellular injection of potentially inhibitory macromolecules: evidence for a possible role of actin filaments.

J. H. Schwartz, D. Harris, D. Goldberg, 1980, Proceedings of the National Academy of Sciences of the United States of America.

Activation of zebrafish Src family kinases by the prion protein is an amyloid-β-sensitive signal that prevents the endocytosis and degradation of E-cadherin/β-catenin complexes in vivo

D. Harris, Alejandro Pinzón-Olejua, Emily Sempou, 2016, Molecular Neurodegeneration.

Mutation T318M in the CYP II B2 Gene Encoding P450c II AS (Aldosterone Synthase) Causes Corticosterone Methyl Oxidase 11 Deficiency

D. Harris, W. Miller, Guangren Zhang, 2007 .

Control of mitochondrial ATP synthase in rat cardiomyocytes: effects of thyroid hormone.

D. Harris, A. Das, 1991, Biochimica et biophysica acta.

The Neuroprotective Effect of Klotho is Mediated via Regulation of Members of the Redox System*

D. Harris, C. Abraham, Jennifer O. Liang, 2014, The Journal of Biological Chemistry.

An iPSC library from a family with Creutzfeldt-Jakob disease caused by the E200K mutation

Robert E. Mercer, D. Harris, G. Mostoslavsky, 2022 .

Mutant Prion Protein Expression Is Associated with an Alteration of the Rab GDP Dissociation Inhibitor α (GDI)/Rab11 Pathway*

D. Harris, M. Salmona, R. Chiesa, 2009, Molecular & Cellular Proteomics.

Acetylcholine receptor-inducing factor from chicken brain increases the level of mRNA encoding the receptor alpha subunit.

G. Fischbach, D. Harris, D. Falls, 1988, Proceedings of the National Academy of Sciences of the United States of America.

Control of mitochondrial ATP synthase in heart cells: inactive to active transitions caused by beating or positive inotropic agents.

D. Harris, A. Das, Anibh M. Das, 1990, Cardiovascular research.

Infectious and Pathogenic Forms of PrP

D. Harris, E. Biasini, 2013 .

Brain Copper Content and Cuproenzyme Activity Do Not Vary with Prion Protein Expression Level*

R. Casareno, J. Gitlin, D. Harris, 2000, The Journal of Biological Chemistry.

Localization of the mRNA for a chicken prion protein by in situ hybridization.

W. Snider, D. Harris, P. Lele, 1993, Proceedings of the National Academy of Sciences of the United States of America.

A Transmembrane Form of the Prion Protein Is Localized in the Golgi Apparatus of Neurons*

R. S. Stewart, D. Harris, 2005, Journal of Biological Chemistry.

Regulation of the mitochondrial ATP synthase is defective in rat heart during alcohol-induced cardiomyopathy.

D. Harris, A. Das, 1993, Biochimica et biophysica acta.

Identification of Anti-prion Compounds using a Novel Cellular Assay*

M. Glicksman, D. Harris, A. Beeler, 2016, The Journal of Biological Chemistry.

Microsoft Word-REV mss.docx

M. Glicksman, D. Harris, A. Beeler, 2016 .

PrP‐dependent cell adhesion in N2a neuroblastoma cells

A. Mangé, D. Harris, S. Lehmann, 2002, FEBS letters.

Non‐infectious aggregates of the prion protein react with several PrPSc‐directed antibodies

D. Harris, R. Chiesa, R. Williamson, 2008, Journal of neurochemistry.

Cytosolic Prion Protein (PrP) Is Not Toxic in N2a Cells and Primary Neurons Expressing Pathogenic PrP Mutations*

R. S. Stewart, G. Forloni, D. Harris, 2005, Journal of Biological Chemistry.

Characterization of brevin, a serum protein that shortens actin filaments.

J. H. Schwartz, D. Harris, 1981, Proceedings of the National Academy of Sciences of the United States of America.

Cellular prion protein targets amyloid-β fibril ends via its C-terminal domain to prevent elongation

J. Straub, D. Harris, Ryo Urano, 2017, The Journal of Biological Chemistry.

Mechanisms of prion-induced toxicity

Robert E. Mercer, D. Harris, 2022, Cell and Tissue Research.

A prion protein cycles between the cell surface and an endocytic compartment in cultured neuroblastoma cells.

D. Harris, S. Shyng, M. Huber, 1993, The Journal of biological chemistry.

The coupling ATPase complex: an evolutionary view.

D. Harris, 1981, Bio Systems.

A Naturally Occurring C-terminal Fragment of the Prion Protein (PrP) Delays Disease and Acts as a Dominant-negative Inhibitor of PrPSc Formation*

D. Harris, Jessie A. Turnbaugh, L. Westergard, 2011, The Journal of Biological Chemistry.

Azide as a probe of co-operative interactions in the mitochondrial F1-ATPase.

D. Harris, 1989, Biochimica et biophysica acta.

Tightly bound nucleotides of the energy-transducing ATPase of chloroplasts and their role in photophosphorylation.

D. Harris, E. Slater, 1975, Biochimica et biophysica acta.

Tight binding of adenine nucleotides to beef-heart mitochondrial ATPase.

E. C. Slater, D. Harris, J. Rosing, 1973, Biochimica et biophysica acta.

The SpoIIAA protein of Bacillus subtilis has GTP-binding properties

D. Harris, M. Yudkin, S. M. Najafi, 1996, Journal of bacteriology.

ROLE OF P38α MAP KINASE IN AMYLOID-β DERIVED DIFFUSIBLE LIGAND (ADDL) INDUCED DENDRITIC SPINE LOSS IN HIPPOCAMPAL NEURONS

D. Harris, U. Germann, J. Alam, 2019, Alzheimer's & Dementia.

Specificity of nucleotide binding and coupled reactions utilising the mitochondrial ATPase.

G. Radda, D. Harris, J. Gomez-Fernandez, 1978, Biochimica et biophysica acta.

Mr 42,000 ARIA: a protein that may regulate the accumulation of acetylcholine receptors at developing chick neuromuscular junctions.

G. Fischbach, G. Corfas, D. Harris, 1990, Cold Spring Harbor symposia on quantitative biology.

Fishing for Prion Protein Function

D. Harris, R. Chiesa, 2009, PLoS biology.

Interaction between F1-ATPase and its naturally occurring inhibitor protein. Studies using a specific anti-inhibitor antibody.

D. Harris, P. J. Jackson, I. Husain, 1985, Biochimica et biophysica acta.

Copper and zinc cause delivery of the prion protein from the plasma membrane to a subset of early endosomes and the Golgi

D. Harris, L. R. Brown, 2003, Journal of neurochemistry.

dissociation inhibitor alpha (GDI)/Rab11 pathway

D. Harris, M. Salmona, R. Chiesa, 2009 .

A deleted prion protein that is neurotoxic in vivo is localized normally in cultured cells

D. Harris, H. Christensen, 2009, Journal of neurochemistry.

Neurodegenerative Illness in Transgenic Mice Expressing a Transmembrane Form of the Prion Protein

R. S. Stewart, B. Ghetti, D. Harris, 2005, The Journal of Neuroscience.

The neurotoxicity of prion protein (PrP) peptide 106–126 is independent of the expression level of PrP and is not mediated by abnormal PrP species

R. S. Stewart, G. Forloni, D. Harris, 2005, Molecular and Cellular Neuroscience.

The Toxicity of a Mutant Prion Protein Is Cell-Autonomous, and Can Be Suppressed by Wild-Type Prion Protein on Adjacent Cells

G. Forloni, D. Harris, R. Chiesa, 2012, PloS one.

Studies of the kinetics of the isolated mitochondrial ATPase using dinitrophenol as a probe.

D. Harris, T. Dall-Larsen, L. Klungsøyr, 1981, Biochimica et biophysica acta.

Nerve Growth Factor‐Induced Differentiation Does Not Alter the Biochemical Properties of a Mutant Prion Protein Expressed in PC12 Cells

D. Harris, R. Chiesa, Roberto Chiesa, 2000, Journal of neurochemistry.

Kinetics of the release of the mitochondrial inhibitor protein. Correlation with synthesis and hydrolysis of ATP.

G. Lippe, D. Harris, M. Sorgato, 1988, Biochimica et biophysica acta.

The N-Terminal, Polybasic Region Is Critical for Prion Protein Neuroprotective Activity

D. Harris, Jessie A. Turnbaugh, U. Unterberger, 2011, PloS one.

Tightly bound nucleotides of the energy-transducing ATPase, and their role in oxidative phosphorylation. I. The Paracoccus denitrificans system.

G. Radda, D. Harris, P. John, 1977, Biochimica et biophysica acta.

The ATPase inhibitor protein in oxidative phosphorylation. The rate-limiting factor to phosphorylation in submitochondrial particles.

G. Radda, D. Harris, V. von Tscharner, 1979, Biochimica et biophysica acta.

Specific spin‐labelling of the energy‐coupling system of mitochondria

E. C. Slater, D. Harris, J. Rosing, 1974, FEBS letters.

Regulation of the mitochondrial ATP synthase in intact rat cardiomyocytes.

D. Harris, A. Das, 1990, The Biochemical journal.

A Drug-Based Cellular Assay (DBCA) for studying cytotoxic and cytoprotective activities of the prion protein: A practical guide.

D. Harris, Tania Massignan, E. Biasini, 2011, Methods.

Brevin, a serum protein that acts on the barbed end of actin filaments.

J. H. Schwartz, D. Harris, J. Wilkins, 1983, Cell biology international reports.

An inter-domain regulatory mechanism controls toxic activities of PrPC

D. Harris, Bei Wu, Alex J McDonald, 2017, Prion.

GFP-tagged prion protein is correctly localized and functionally active in the brains of transgenic mice

B. Ghetti, D. Harris, S. Barmada, 2004, Neurobiology of Disease.

A transgenic model of a familial prion disease.

B. Ghetti, D. Harris, R. Chiesa, 2000 .

Prion Protein Repeat Expansion Results in Increased Aggregation and Reveals Phenotypic Variability

H. True, D. Harris, Amar A. Desai, 2007, Molecular and Cellular Biology.

Prion protein with an insertional mutation accumulates on axonal and dendritic plasmalemma and is associated with distinctive ultrastructural changes.

D. Harris, M. Jeffrey, S. Barmada, 2009, The American journal of pathology.

Activation of zebrafish Src family kinases by the prion protein is an amyloid-β-sensitive signal that prevents the endocytosis and degradation of E-cadherin/β-catenin complexes in vivo

D. Harris, Alejandro Pinzón-Olejua, Emily Sempou, 2016, Molecular Neurodegeneration.

Multiple biochemical similarities between infectious and non‐infectious aggregates of a prion protein carrying an octapeptide insertion

D. Harris, R. Chiesa, S. Thellung, 2008, Journal of neurochemistry.

Identification of Intermediate Steps in the Conversion of a Mutant Prion Protein to a Scrapie-like Form in Cultured Cells*

D. Harris, S. Lehmann, N. Daude, 1997, The Journal of Biological Chemistry.

Altered Domain Structure of the Prion Protein Caused by Cu2+ Binding and Functionally Relevant Mutations: Analysis by Cross-Linking, MS/MS, and NMR.

P. Andrews, G. Millhauser, D. Harris, 2019, Structure.

Sulfated Glycans Stimulate Endocytosis of the Cellular Isoform of the Prion Protein, PrPC, in Cultured Cells (*)

K. Moulder, D. Harris, S. Shyng, 1995, The Journal of Biological Chemistry.

Dimerization of F0F1ATP synthase from bovine heart is independent from the binding of the inhibitor protein IF1.

I. Mavelli, G. Lippe, D. Harris, 2002, Biochimica et biophysica acta.

A prion-like protein from chicken brain copurifies with an acetylcholine receptor-inducing activity.

G. Fischbach, D. Harris, G D Fischbach, 1991, Proceedings of the National Academy of Sciences of the United States of America.

Mechanisms of prion-induced neurodegeneration

P. Saá, D. Harris, L. Cervenakova, 2016, Expert Reviews in Molecular Medicine.

Prion Diseases: What Is the Neurotoxic Molecule?

D. Harris, R. Chiesa, 2001, Neurobiology of Disease.

Control of mitochondrial ATP synthesis in the heart.

D. Harris, A. Das, A. Das, 1991, The Biochemical journal.

Evidence for a Six-transmembrane Domain Structure of Presenilin 1*

D. Harris, R. Chiesa, S. Lehmann, 1997, The Journal of Biological Chemistry.

New Insights into Prion Structure and Toxicity

H. True, D. Harris, 2006, Neuron.

Acute cellular uptake of abnormal prion protein is cell type and scrapie-strain independent.

D. Harris, I. Vorberg, S. Priola, 2008, Virology.

Prion protein lacks robust cytoprotective activity in cultured cells

D. Harris, H. Christensen, David A Harris, 2008, Molecular Neurodegeneration.

Bax deletion prevents neuronal loss but not neurological symptoms in a transgenic model of inherited prion disease.

B. Ghetti, K. Roth, D. Harris, 2005, Proceedings of the National Academy of Sciences of the United States of America.

The mitochondrial ATP synthase inhibitor protein binds near the C‐terminus of the F1 β‐subunit

D. Harris, P. J. Jackson, 1988, FEBS letters.

ATP synthesis and hydrolysis in submitochondrial particles subjected to an acid—base transition

D. Harris, I. Husain, 1983, FEBS letters.

The initial stages of photophosphorylation. Studies using excitation by saturating, short flashes of light.

A. Crofts, D. Harris, 1978, Biochimica et biophysica acta.

Two distinct types of ɛ‐binding site exist in chloroplast coupling factor (CF1)

D. Harris, P.J. Andralojc, 1988 .

An N-terminal Fragment of the Prion Protein Binds to Amyloid-β Oligomers and Inhibits Their Neurotoxicity in Vivo*

M. Gobbi, G. Forloni, D. Harris, 2013, The Journal of Biological Chemistry.

PrP is a central player in toxicity mediated by soluble aggregates of neurodegeneration-causing proteins

M. Frosch, J. Collinge, D. Walsh, 2019, Acta Neuropathologica.

Biochemical dysfunction in heart mitochondria exposed to ischaemia and reperfusion.

David A Harris, D. Harris, G. Solaini, 2005, The Biochemical journal.

The study of the pathogenic mechanism of mitochondrial diseases provides information on basic bioenergetics.

D. Harris, A. Baracca, G. Sgarbi, 2008, Biochimica et biophysica acta.

Blockade of Glycosylation Promotes Acquistion of Scrapie-like Properties by the Prion Protein in Cultured Cells*

D. Harris, S. Lehmann, 1997, The Journal of Biological Chemistry.

The N-terminal Domain of a Glycolipid-anchored Prion Protein Is Essential for Its Endocytosis via Clathrin-coated Pits (*)

K. Moulder, D. Harris, S. Shyng, 1995, The Journal of Biological Chemistry.

Processing of a cellular prion protein: identification of N- and C-terminal cleavage sites.

B. Chait, D. Harris, S. Shyng, 1993, Biochemistry.

The cellular prion protein (PrP(C)): its physiological function and role in disease.

D. Harris, H. Christensen, L. Westergard, 2007, Biochimica et biophysica acta.

Identification of anti-prion drugs and targets using toxicity-based assays.

D. Harris, Robert C. C. Mercer, 2019, Current opinion in pharmacology.

Immunopurification of Pathological Prion Protein Aggregates

M. Gobbi, D. Harris, R. Chiesa, 2009, PloS one.

Prion neurotoxicity

D. Harris, Bei Wu, N. Le, 2019, Brain pathology.

A Neuronal Culture System to Detect Prion Synaptotoxicity

D. Harris, H. Wille, Thibaut Imberdis, 2016, PLoS pathogens.

Synthetic Prions Provide Clues for Understanding Prion Diseases.

D. Harris, Thibaut Imberdis, 2016, The American journal of pathology.

Molecular Distinction between Pathogenic and Infectious Properties of the Prion Protein

B. Ghetti, D. Harris, R. Chiesa, 2003, Journal of Virology.

Aggregated, Wild-Type Prion Protein Causes Neurological Dysfunction and Synaptic Abnormalities

B. Ghetti, D. Harris, R. Chiesa, 2008, The Journal of Neuroscience.

Human prion proteins with pathogenic mutations share common conformational changes resulting in enhanced binding to glycosaminoglycans

Shaoman Yin, P. Tien, D. Harris, 2007, Proceedings of the National Academy of Sciences.

Neurological Illness in Transgenic Mice Expressing a Prion Protein with an Insertional Mutation

B. Ghetti, D. Harris, R. Chiesa, 1998, Neuron.

N-Terminally Deleted Forms of the Prion Protein Activate Both Bax-Dependent and Bax-Independent Neurotoxic Pathways

K. Roth, D. Harris, Aimin Li, 2007, The Journal of Neuroscience.

Mammalian Prion Protein Suppresses Bax-induced Cell Death in Yeast*

D. Harris, Aimin Li, 2005, Journal of Biological Chemistry.

Both N-Terminal and C-Terminal Histidine Residues of the Prion Protein are Essential for Copper Coordination and Neuroprotective Self-Regulation.

G. Millhauser, D. Harris, R. D. Britt, 2020, Journal of molecular biology.

Prions activate a p38 MAPK synaptotoxic signaling pathway

D. Harris, Bei Wu, Thibaut Imberdis, 2018, PLoS pathogens.

Size-exclusion high-performance liquid chromatography of proteins.

D. Harris, 1992, Methods in molecular biology.

Prion permissive pathways: extracellular matrix genes control susceptibility to prion infection

D. Harris, Thibaut Imberdis, 2014, The EMBO journal.

Differential activation of myotube nuclei following exposure to an acetylcholine receptor-inducing factor

David A. Harris, G. Fischbach, D. Harris, 1989, Nature.

Most Pathogenic Mutations Do Not Alter the Membrane Topology of the Prion Protein*

R. S. Stewart, D. Harris, D A Harris, 2001, The Journal of Biological Chemistry.

A Nine Amino Acid Domain Is Essential for Mutant Prion Protein Toxicity

D. Harris, Jessie A. Turnbaugh, L. Westergard, 2011, The Journal of Neuroscience.

Post‐transcriptional suppression of pathogenic prion protein expression in Drosophila neurons

M. Feany, S. Supattapone, D. Harris, 2003, Journal of neurochemistry.

Intrinsic toxicity of the cellular prion protein is regulated by its conserved central region

G. Millhauser, D. Harris, Bei Wu, 2020, FASEB journal : official publication of the Federation of American Societies for Experimental Biology.

Trafficking, turnover and membrane topology of PrP.

D. Harris, 2003, British medical bulletin.

Biosynthesis and cellular processing of the prion protein.

D. Harris, 2001, Advances in protein chemistry.

Cellular Biology of Prion Diseases

D. Harris, 1999, Clinical Microbiology Reviews.

Cell biology of the prion protein.

K. Moulder, D. Harris, S. Shyng, 1996, Current topics in microbiology and immunology.

Primary Myopathy and Accumulation of PrPSc-Like Molecules in Peripheral Tissues of Transgenic Mice Expressing a Prion Protein Insertional Mutation

A. Pestronk, B. Ghetti, R. Schmidt, 2001, Neurobiology of Disease.

Accumulation of protease-resistant prion protein (PrP) and apoptosis of cerebellar granule cells in transgenic mice expressing a PrP insertional mutation.

B. Ghetti, D. Harris, R. Chiesa, 2000, Proceedings of the National Academy of Sciences of the United States of America.

Cell-lysate conversion of prion protein into its protease-resistant isoform suggests the participation of a cellular chaperone.

C. Soto, D. Harris, E. Levy, 1999, Biochemical and biophysical research communications.

Successful Transmission of Three Mouse-Adapted Scrapie Strains to Murine Neuroblastoma Cell Lines Overexpressing Wild-Type Mouse Prion Protein

D. Harris, H. Laude, J. Grassi, 2000, Journal of Virology.

Cloning of non-polyadenylated RNAs from rat brain.

D. Harris, A. Sherbany, 1991, Brain research. Molecular brain research.

PrP-grafted antibodies bind certain amyloid β-protein aggregates, but do not prevent toxicity

M. Frosch, J. Collinge, D. Walsh, 2019, Brain Research.

Reversion of prion protein conformational changes by synthetic b-sheet breaker peptides

T. Wisniewski, C. Soto, F. Tagliavini, 2000, The Lancet.

Mad Cow Disease and Related Spongiform Encephalopathies

D. Harris, 2004, Current Topics in Microbiology and Immunology.

Nucleotide-binding properties of native and cold-treated mitochondrial ATPase.

E. C. Slater, J Rosing, A Kemp, 1975, Biochimica et biophysica acta.

Interaction between the soluble F1 ATPase and its naturally occurring inhibitor protein. Studies using hydrophilic high-performance liquid chromatography and immunoelectron microscopy.

D. Harris, G. Schäfer, H. Lünsdorf, 1986, European journal of biochemistry.

Interaction of F1-ATPase, from ox heart mitochondria with its naturally occurring inhibitor protein. Studies using radio-iodinated inhibitor protein.

R. L. Cross, D. Harris, J. Power, 1983, Biochimica et biophysica acta.

A thermodynamic analysis of the interaction between the mitochondrial coupling adenosine triphosphatase and its naturally occurring inhibitor protein.

D. Harris, J. Gomez-Fernandez, 1978, The Biochemical journal.

Tightly bound nucleotides of the energy-transducing ATPase, and their role in oxidative phosphorylation. II. The beef heart mitochondrial system.

E. C. Slater, G. Radda, D. Harris, 1977, Biochimica et biophysica acta.

The adenosine triphosphatase-inhibitor content of bovine heart submitochondrial particles. Influence of the inhibitor on adenosine triphosphate-dependent reactions.

G. Radda, D. Harris, S. Ferguson, 1977, The Biochemical journal.

The ectopic FOF1 ATP synthase of rat liver is modulated in acute cholestasis by the inhibitor protein IF1

Elena Bisetto, V. Giorgio, G. Lippe, 2010, Journal of bioenergetics and biomembranes.

Promotion and inhibition of catalytic cooperativity of the Ca2+-dependent ATPase activity of spinach chloroplast coupling factor 1 (CF1).

D. Harris, P. Andralojc, 1990, Biochimica et Biophysica Acta.

Catalytic cooperativity in the Ca2+-dependent ATPase activity of spinach chloroplast coupling factor (CF1)

D. Harris, P. Andralojc, 1994 .

Preparation and characterisation of an αβ heterodimer from the ATP synthase of Rhodospirillum rubrum

D. Harris, P. Andralojc, 1993 .

Hydrolysis of adenosine 5'-triphosphate by the isolated catalytic subunit of the coupling ATPase from Rhodospirillum rubrum

D. Harris, M. Baltscheffsky, J. Boork, 1985 .

Sites of protein-protein interaction on the mitochondrial F1-ATPase inhibitor protein.

D. Harris, P. J. Jackson, 1986, The Biochemical journal.

Mutant Prion Proteins Are Partially Retained in the Endoplasmic Reticulum*

Terrance T. Kummer, D. Harris, S. Barmada, 2001, The Journal of Biological Chemistry.

Doppel induces degeneration of cerebellar Purkinje cells independently of Bax.

D. Harris, Aimin Li, Jiaxin Dong, 2007, The American journal of pathology.

How ATP is made

D. Harris, 1982 .

Isolation of the Catalytic (β) Subunit of the Chloroplast ATP Synthase in a Hydrolytically Active Form

D. Harris, S. Nadanaciva, 1990 .

Isolation and characterisation of a functional αβ heterodimer from the ATP synthase of Rhodospirillum rubrum

D. Harris, P.J. Andralojc, 1992 .

Optimal promoter usage for lentiviral vector-mediated transduction of cultured central nervous system cells

D. Harris, M. Goldberg, B. Snider, 2010, Journal of Neuroscience Methods.

Ectopic F0F1 ATP synthase contains both nuclear and mitochondrially-encoded subunits

G. Lippe, D. Harris, A. Rai, 2013, Journal of Bioenergetics and Biomembranes.

Mutational Analysis of Topological Determinants in Prion Protein (PrP) and Measurement of Transmembrane and Cytosolic PrP during Prion Infection*

R. S. Stewart, D. Harris, 2003, Journal of Biological Chemistry.

Mutant PrP Is Delayed in Its Exit from the Endoplasmic Reticulum, but Neither Wild-type nor Mutant PrP Undergoes Retrotranslocation Prior to Proteasomal Degradation*

R. S. Stewart, D. Harris, R. Chiesa, 2003, Journal of Biological Chemistry.

In vitro and in vivo studies of F0F1ATP synthase regulation by inhibitor protein IF1 in goat heart

I. Mavelli, G. Lippe, D. Harris, 2004 .

Neonatal lethality in transgenic mice expressing prion protein with a deletion of residues 105–125

K. Roth, D. Harris, R. Chiesa, 2007, The EMBO journal.

Two mutant prion proteins expressed in cultured cells acquire biochemical properties reminiscent of the scrapie isoform.

D. Harris, S. Lehmann, 1996, Proceedings of the National Academy of Sciences of the United States of America.

Visualization of Prion Infection in Transgenic Mice Expressing Green Fluorescent Protein-Tagged Prion Protein

D. Harris, S. Barmada, 2005, The Journal of Neuroscience.

The N-Terminal, Polybasic Region of PrPC Dictates the Efficiency of Prion Propagation by Binding to PrPSc

P. Saá, S. Supattapone, D. Harris, 2012, The Journal of Neuroscience.

Aβ receptors specifically recognize molecular features displayed by fibril ends and neurotoxic oligomers

D. Harris, Ladan Amin, 2019, Nature Communications.

Ligands binding to the cellular prion protein induce its protective proteolytic release with therapeutic potential in neurodegenerative proteinopathies

S. Hornemann, A. Aguzzi, I. Zerr, 2021, bioRxiv.

The N-terminus of the prion protein is a toxic effector regulated by the C-terminus

David W. Colby, G. Millhauser, D. Harris, 2017, eLife.

A Mutant Prion Protein Sensitizes Neurons to Glutamate-Induced Excitotoxicity

J. Luebke, P. Toselli, I. Solomon, 2013, The Journal of Neuroscience.

Ion channels induced by the prion protein

I. Solomon, D. Harris, E. Biasini, 2012, Prion.

NMDA receptor misalignment in iPSC-derived neurons from a multi-generational family with inherited Creutzfeldt-Jakob disease

Robert E. Mercer, D. Harris, G. Mostoslavsky, 2022, bioRxiv.

Bound nucleotides and phosphorylation in Rhodospirillum rubrum.

D. Harris, M. Baltscheffsky, 1979, Biochemical and biophysical research communications.

The 'non-exchangeable' nucleotides of F1-F0ATP synthase. Cofactors in hydrolysis?

D. Harris, 1993, FEBS letters.

Copper Converts the Cellular Prion Protein into a Protease-resistant Species That Is Distinct from the Scrapie Isoform*

D. Harris, R. Chiesa, E. Quaglio, 2001, The Journal of Biological Chemistry.

A C-terminal Membrane Anchor Affects the Interactions of Prion Proteins with Lipid Membranes*

D. Harris, R. Lemmens‐Gruber, C. Becker, 2014, The Journal of Biological Chemistry.

Neurotoxic Mutants of the Prion Protein Induce Spontaneous Ionic Currents in Cultured Cells*

I. Solomon, D. Harris, J. E. Huettner, 2010, The Journal of Biological Chemistry.

Prion proteins carrying pathogenic mutations are resistant to phospholipase cleavage of their glycolipid anchors.

D. Harris, R. Narwa, 1999, Biochemistry.

Targeting the cellular prion protein to treat neurodegeneration.

D. Harris, E. Biasini, 2012, Future medicinal chemistry.

Regulation of the mitochondrial ATP synthase in rat heart.

D. Harris, 1993, Biochemical Society transactions.

160 Mutant prion proteins acquire PrP5c-like properties in cultured cells: an experimental model of familial prion diseases

D. Harris, S. Lehmann, 1996, Neurobiology of Aging.

The vital force — A study of bioenergetics: by Franklin M Harold. pp 577, WH Freeman, New York. 1986. £19.95

D. Harris, 1987 .

A Novel, Drug-based, Cellular Assay for the Activity of Neurotoxic Mutants of the Prion Protein*

R. S. Stewart, I. Solomon, D. Harris, 2009, The Journal of Biological Chemistry.

Defects in regulation of mitochondrial ATP synthase in cardiomyocytes from spontaneously hypertensive rats.

D. Harris, A. Das, 1990, The American journal of physiology.

N-glycosylation is a potent regulator of prion protein neurotoxicity

G. Millhauser, D. Harris, Kevin M. Schilling, 2023, bioRxiv.

A highly toxic cellular prion protein induces a novel, nonapoptotic form of neuronal death.

J. Olney, K. Dikranian, K. Roth, 2010, The American journal of pathology.

Mediators of neurotoxicity

I. Solomon, D. Harris, E. Biasini, 2012 .

PURIFICATION AND CHARACTERIZATION OF MUSCLE PROTEINS FROM APLYSIA CALIFORNICA

J. H. Schwartz, D. Harris, A. Sherbany, 1984 .