Dramatic Aggregation of Alzheimer Aβ by Cu(II) Is Induced by Conditions Representing Physiological Acidosis

Alzheimer's disease: Initial report of the purification and characterization of a novel cerebrovascular amyloid protein

Glenner, G. G., & Wong, C. W. (1984) · Biochemical and Biophysical Research Communications · doi:10.1016/s0006-291x(84)80190-4 · Cited by 5,404

The precursor of Alzheimer's disease amyloid A4 protein resembles a cell-surface receptor

Kang, J., Lemaire, H.-G., Unterbeck, A., Salbaum, J. M., Masters, C. L., Grzeschik, K.-H., Multhaup, G., Beyreuther, K., & Müller-Hill, B. (1987) · Nature · doi:10.1038/325733a0 · Cited by 4,619

Amyloid plaque core protein in Alzheimer disease and Down syndrome.

Masters, C. L., Simms, G., Weinman, N. A., Multhaup, G., McDonald, B. L., & Beyreuther, K. (1985) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.82.12.4245 · Cited by 4,431

Amyloid β-peptide is produced by cultured cells during normal metabolism

Haass, C., Schlossmacher, M. G., Hung, A. Y., Vigo-Pelfrey, C., Mellon, A., Ostaszewski, B. L., Lieberburg, I., Koo, E. H., Schenk, D., Teplow, D. B., et al. (1992) · Nature · doi:10.1038/359322a0 · Cited by 1,921

Isolation and quantification of soluble Alzheimer's β-peptide from biological fluids

Seubert, P., Vigo-Pelfrey, C., Esch, F., Lee, M., Dovey, H., Davis, D., Sinha, S., Schiossmacher, M., Whaley, J., Swindlehurst, C., et al. (1992) · Nature · doi:10.1038/359325a0 · Cited by 1,731

Amyloid β Protein Gene: cDNA, mRNA Distribution, and Genetic Linkage Near the Alzheimer Locus

Tanzi, R. E., Gusella, J. F., Watkins, P. C., Bruns, G. A. P., St George-Hyslop, P., Van Keuren, M. L., Patterson, D., Pagan, S., Kurnit, D. M., & Neve, R. L. (1987) · Science · doi:10.1126/science.2949367 · Cited by 1,611

Rapid induction of Alzheimer A beta amyloid formation by zinc

Bush, A., Pettingell, W., Multhaup, G., d Paradis, M., Vonsattel, J., Gusella, J., Beyreuther, K., Masters, C., & Tanzi, R. (1994) · Science · doi:10.1126/science.8073293 · Cited by 1,522

Production of the Alzheimer Amyloid β Protein by Normal Proteolytic Processing

Shoji, M., Golde, T. E., Ghiso, J., Cheung, T. T., Estus, S., Shaffer, L. M., Cai, X.-D., McKay, D. M., Tintner, R., Frangione, B., et al. (1992) · Science · doi:10.1126/science.1439760 · Cited by 1,447

The Wilson disease gene is a copper transporting ATPase with homology to the Menkes disease gene

Tanzi, R. E., Petrukhin, K. E., Чернов, И. П., Pellequer, J., Wasco, W., Ross, B., Romano, D., Parano, E., Pavone, P., Brzustowicz, L. M., et al. (1993) · Nature Genetics · doi:10.1038/ng1293-344 · Cited by 1,367

Binding of human apolipoprotein E to synthetic amyloid beta peptide: isoform-specific effects and implications for late-onset Alzheimer disease.

Strittmatter, W. J., Weisgraber, K. H., Huang, D. Y., Dong, L. M., Salvesen, G. S., Pericak-Vance, M., Schmechel, D., Saunders, A. M., Goldgaber, D., & Roses, A. D. (1993) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.90.17.8098 · Cited by 1,363

Characterization and Chromosomal Localization of a cDNA Encoding Brain Amyloid of Alzheimer's Disease

Goldgaber, D., Lerman, M. I., McBride, O. W., Saffiotti, U., & Gajdusek, D. C. (1987) · Science · doi:10.1126/science.3810169 · Cited by 1,359

Iron accumulation in Alzheimer disease is a source of redox-generated free radicals

Smith, M. A., Harris, P. L. R., Sayre, L. M., & Perry, G. L. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.18.9866 · Cited by 1,357

Acute phase proteins with special reference to C-reactive protein and related proteins (pentaxins) and serum amyloid A protein.

Pepys, M., & Baltz, M. (1983) · Advances in Immunology · doi:10.1016/s0065-2776(08)60379-x · Cited by 1,322

The cellular prion protein binds copper in vivo

Brown, D. R., Qin, K., Herms, J., Madlung, A., Manson, J., Strome, R., Fraser, P., Kruck, T., von Bohlen, A., Schulz-Schaeffer, W., et al. (1997) · Nature · doi:10.1038/37783 · Cited by 1,300

Neurobiology of Zinc and Zinc-Containing Neurons

Frederickson, C. J. (1989) · International review of neurobiology · doi:10.1016/s0074-7742(08)60279-2 · Cited by 1,070

Assembly and aggregation properties of synthetic Alzheimer's A4/beta amyloid peptide analogs.

Burdick, D., Soreghan, B., Kwon, M., Kosmoski, J., Knauer, M., Henschen, A., Yates, J., Cotman, C., & Glabe, C. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)48529-8 · Cited by 1,014

Apolipoprotein E allele–specific antioxidant activity and effects on cytotoxicity by oxidative insults and β–amyloid peptides

Miyata, M., & Smith, J. D. (1996) · Nature Genetics · doi:10.1038/ng0996-55 · Cited by 735

Reduction of β‐amyloid peptide42 in the cerebrospinal fluid of patients with Alzheimer's disease

Motter, R., Vigo‐Pelfrey, C., Kholodenko, D., Barbour, R., Johnson‐Wood, K., Galasko, D., Chang, L., Miller, B., Clark, C., Green, R., et al. (1995) · Annals of Neurology · doi:10.1002/ana.410380413 · Cited by 701

Solution conformations and aggregational properties of synthetic amyloid β-peptides of Alzheimer's disease

Barrow, C. J., Yasuda, A., Kenny, P. T. M., & Zagorski, M. G. (1992) · Journal of Molecular Biology · doi:10.1016/0022-2836(92)90106-t · Cited by 644

Biochemistry of Copper

Linder, M. C. (1991) · Springer eBooks · doi:10.1007/978-1-4757-9432-8 · Cited by 626

Water-soluble Aβ(N-40, N-42) oligomers in normal and Alzheimer disease brains

Kuo, Y.-M., Emmerling, M. R., Vigo-Pelfrey, C., Kasunic, T. C., Kirkpatrick, J. B., Murdoch, G. H., Ball, M. J., & Roher, A. E. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.8.4077 · Cited by 618

Beta amyloid protein deposition in the brain after severe head injury: implications for the pathogenesis of Alzheimer's disease.

Roberts, G. W., Gentleman, S. M., Lynch, A., Murray, L., Landon, M., & Graham, D. I. (1994) · Journal of Neurology, Neurosurgery & Psychiatry · doi:10.1136/jnnp.57.4.419 · Cited by 569

Generation of beta-amyloid in the secretory pathway in neuronal and nonneuronal cells.

Busciglio, J., Gabuzda, D. H., Matsudaira, P., & Yankner, B. A. (1993) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.90.5.2092 · Cited by 569

Solution Structures of β Peptide and Its Constituent Fragments: Relation to Amyloid Deposition

Barrow, C. J., & Zagorski, M. G. (1991) · Science · doi:10.1126/science.1853202 · Cited by 538

Morphology and Toxicity of Aβ-(1-42) Dimer Derived from Neuritic and Vascular Amyloid Deposits of Alzheimer's Disease

Roher, A. E., Chaney, M. O., Kuo, Y., Webster, S. D., Stine, W. B., Haverkamp, L. J., Woods, A. S., Cotter, R. J., Tuohy, J. M., Krafft, G. A., et al. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.34.20631 · Cited by 494

Analysis of Heterogeneous βA4 Peptides in Human Cerebrospinal Fluid and Blood by a Newly Developed Sensitive Western Blot Assay

Ida, N., Hartmann, T., Pantel, J., Schrüder, J., Zerfaß, R., Fürstl, H., Sandbrink, R., Masters, C. L., & Beyreuther, K. T. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.37.22908 · Cited by 478

Amyloid β-protein deposition in tissues other than brain in Alzheimer's disease

Joachim, C. L., Mori, H., & Selkoe, D. J. (1989) · Nature · doi:10.1038/341226a0 · Cited by 462

Alzheimer's disease amyloidogenic glycoprotein: expression pattern in rat brain suggests a role in cell contact.

Shivers, B. D., Hilbich, C., Multhaup, G., Salbaum, M., Beyreuther, K. T., & SEEBURG, P. H. (1988) · The EMBO Journal · doi:10.1002/j.1460-2075.1988.tb02952.x · Cited by 442

βA4 amyloid protein deposition in brain after head trauma

Roberts, G., Gentleman, S., Lynch, A., & Graham, D. I. (1991) · The Lancet · doi:10.1016/0140-6736(91)92724-g · Cited by 440

Amyloid β protein (Aβ) deposition: Aβ42(43) precedes Aβ40 in down Syndrome

Iwatsubo, T., Mann, D. M. A., Odaka, A., Suzuki, N., & Ihara, Y. (1995) · Annals of Neurology · doi:10.1002/ana.410370305 · Cited by 386

pH-dependent structural transitions of Alzheimer amyloid peptides

Fraser, P. E., Nguyen, J. T., Surewicz, W. K., & Kirschner, D. A. (1991) · Biophysical Journal · doi:10.1016/s0006-3495(91)82154-3 · Cited by 380

Physical, morphological and functional differences between ph 5.8 and 7.4 aggregates of the Alzheimer's amyloid peptide Abeta.

Wood, S. J., Maleeff, B., Hart, T., & Wetzel, R. (1996) · Journal of Molecular Biology · doi:10.1006/jmbi.1996.0133 · Cited by 337

Modulation of A beta adhesiveness and secretase site cleavage by zinc.

Bush, A. I., Pettingell, W. H., Paradis, M. D., & Tanzi, R. E. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)32694-7 · Cited by 331

Arthritis and Allied Conditions

Emery, P. (1990) · Annals of the Rheumatic Diseases · doi:10.1136/ard.49.7.492-c · Cited by 319

Zinc-induced Alzheimer's Aβ1–40 Aggregation Is Mediated by Conformational Factors

Huang, X., Atwood, C., Moir, R. D., Hartshorn, M. A., Vonsattel, J., Tanzi, R. E., & Bush, A. I. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.42.26464 · Cited by 317

Conservation of the sequence of the Alzheimer's disease amyloid peptide in dog, polar bear and five other mammals by cross-species polymerase chain reaction analysis

Johnstone, E. M., Chaney, M. O., Norris, F. H., Pascual, R. V., & Little, S. H. (1991) · Molecular Brain Research · doi:10.1016/0169-328x(91)90088-f · Cited by 315

Synovial fluid pH, lactate, oxygen and carbon dioxide partial pressure in various joint diseases

Treuhaft, P. S., & McCarty, D. J. (1971) · Arthritis & Rheumatism · doi:10.1002/art.1780140407 · Cited by 307

An important role of heparan sulfate proteoglycan (perlecan) in a model system for the deposition and persistence of fibrillar aβ-amyloid in rat brain

Snow, A. D., Sekiguchi, R., Nochlin, D., Fraser, P., Kimata, K., Mizutani, A., Arai, M., Schreier, W., & Morgan, D. G. (1994) · Neuron · doi:10.1016/0896-6273(94)90165-1 · Cited by 301

Surfactant properties of Alzheimer's A beta peptides and the mechanism of amyloid aggregation.

Soreghan, B. A., Kosmoski, J. V., & Glabe, C. G. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)61939-3 · Cited by 267

Enzyme Activities in Relation to pH and Lactate in Postmortem Brain in Alzheimer‐Type and Other Dementias

Yates, C. M., Butterworth, J., Tennant, M. C., & Gordon, A. (1990) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.1990.tb04948.x · Cited by 263

Isolation and characterization of amyloid P component from Alzheimer's disease and other types of cerebral amyloidosis.

Coria, F., Castaño, E., Prelli, F. C., Larrondo-Lillo, M., van Duinen, S. G., Shelanski, M. L., & Frangione, B. (1988) · PubMed · Cited by 245

Immunohistochemical characterization of alterations in the distribution of amyloid precursor proteins and beta-amyloid peptide after experimental brain injury in the rat

Pierce, J., Trojanowski, J., Graham, D., Smith, D., & McIntosh, T. (1996) · The Journal of Neuroscience · doi:10.1523/jneurosci.16-03-01083.1996 · Cited by 239

Glucose regulation and cognitive functions: relation to Alzheimer's disease and diabetes

Messier, C., & Gagnon, M. (1996) · Behavioural Brain Research · doi:10.1016/0166-4328(95)00153-0 · Cited by 237

Intrinsic stoichiometric equilibrium constants for the binding of zinc(II) and copper(II) to the high affinity site of serum albumin.

Masuoka, J., Hegenauer, J., Dyke, B. R. V., & Saltman, P. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(20)80574-2 · Cited by 215

NMR studies of amyloid .beta.-peptides: proton assignments, secondary structure, and mechanism of an .alpha.-helix .fwdarw. .beta.-sheet conversion for a homologous, 28-residue, N-terminal fragment

Zagorski, M. G., & Barrow, C. J. (1992) · Biochemistry · doi:10.1021/bi00139a028 · Cited by 188

Predominant deposition of amyloid-beta 42(43) in plaques in cases of Alzheimer's disease and hereditary cerebral hemorrhage associated with mutations in the amyloid precursor protein gene.

Mann, D. M. A., Iwatsubo, T., Ihara, Y., Cairns, N. J., Lantos, P. L., Bogdanović, N., Lannfelt, L., Winblad, B. G., Maat–Schieman, M. L. C., & Rossor, M. N. (1996) · Europe PMC (PubMed Central) · Cited by 184

Protein chemical and immunocytochemical studies of meningovascular β-amyloid protein in Alzheimer's disease and normal aging

Joachim, C. L., Duffy, L. K., Morris, J. H., & Selkoe, D. J. (1988) · Brain Research · doi:10.1016/0006-8993(88)90673-7 · Cited by 180

Proteins of iron storage and transport

Halliwell, B. B. (1986) · FEBS Letters · doi:10.1016/0014-5793(86)81206-6 · Cited by 177

Amyloid β‐Protein Induces Its Own Production in Cultured Degenerating Cerebrovascular Smooth Muscle Cells

Davis-Salinas, J., Saporito-Irwin, S. M., Cotman, C. W., & Nostrand, W. E. V. (1995) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.1995.65020931.x · Cited by 166

Structural Determinants of the Alzheimer's Amyloid β‐Peptide

Soto, C. A., Brañes, M. C., Alvarez, J., & Inestrosa, N. C. (1994) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.1994.63041191.x · Cited by 153

Insulin aggregation in artificial delivery systems

Lougheed, W. D., Woulfe-Flanagan, H., Clement, J. R., & Albisser, A. M. (1980) · Diabetologia · doi:10.1007/bf00258302 · Cited by 145

The Soluble Form of Alzheimer′s Amyloid β Protein Is Complexed to High Density Lipoprotein 3 and Very High Density Lipoprotein in Normal Human Plasma

Koudinov, A. R., Matsubara, E., Frangione, B., & Ghiso, J. A. (1994) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1994.2788 · Cited by 141

Distribution of β‐amyloid protein in the brain following severe head injury

Graham, D. I., Gentleman, S., Lynch, A., & Roberts, G. (1995) · Neuropathology and Applied Neurobiology · doi:10.1111/j.1365-2990.1995.tb01025.x · Cited by 140

The Effect of pH upon Human Transferrin: Selective Labelling of the Two Iron‐binding Sites

Lestas, A. N. (1976) · British Journal of Haematology · doi:10.1111/j.1365-2141.1976.tb00937.x · Cited by 140

Decreased RNA Polymerase Activity in Mammalian Zinc Deficiency

Terhune, M. W., & Sandstead, H. H. (1972) · Science · doi:10.1126/science.177.4043.68 · Cited by 130

Soluble Amyloid β-Protein Is a Marker of Alzheimer Amyloid in Brain But Not in Cerebrospinal Fluid

Tabaton, M., Nunzi, M. G., Xue, R., Usiak, M., AUTILIO‐GAMBETTI, L., & Gambetti, P. L. (1994) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1994.1634 · Cited by 126

Brain tissue accumulates 67copper by two ligand-dependent saturable processes. A high affinity, low capacity and a low affinity, high capacity process.

Hartter, D. E., & Barnea, A. (1988) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)35425-0 · Cited by 125

Metals and Oxidative Damage in Neurological Disorders

Connor, J. (1997) · Springer US · doi:10.1007/978-1-4899-0197-2 · Cited by 124

Aggregation and Metal‐Binding Properties of Mutant Forms of the Amyloid Aβ Peptide of Alzheimer's Disease

Clements, A., Allsop, D., Walsh, D. M., & Williams, C. H. (1996) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.1996.66020740.x · Cited by 116

Cerebrospinal fluid levels of amyloid β‐protein in alzheimer's disease: Inverse correlation with severity of dementia and effect of apolipoprotein e genotype

Nitsch, R. M., Rebeck, G. W., Deng, M., Richardson, U. I., Tennis, M., Schenk, D. B., Vigo‐Pelfrey, C., Lieberburg, I., Wurtman, R. J., Hyman, B. T., et al. (1995) · Annals of Neurology · doi:10.1002/ana.410370414 · Cited by 113

Characterization of the Binding of Amyloid‐β Peptide to Cell Culture‐Derived Native Apolipoprotein E2, E3, and E4 Isoforms and to Isoforms from Human Plasma

Yang, D., Smith, J. D., Zhou, Z., Gandy, S. E., & Martins, R. N. (1997) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.1997.68020721.x · Cited by 111

THE DISTRIBUTION OF COPPER IN HUMAN BRAIN

Warren, P. J., Earl, C., & Thompson, R. H. S. (1960) · Brain · doi:10.1093/brain/83.4.709 · Cited by 104

Amyloid β protein levels in cerebrospinal fluid are elevated in early‐onset Alzheimer's disease

Nakamura, T., Shoji, M., Harigaya, Y., 渡辺, 光., Hosoda, K., Cheung, T. T., Shaffer, L. M., Golde, T. E., Younkin, L. H., Younkin, S. G., et al. (1994) · Annals of Neurology · doi:10.1002/ana.410360616 · Cited by 103

Acidic pH enables caeruloplasmin to catalyse the modification of low‐density lipoprotein

Lamb, D. J., & Leake, D. S. (1994) · FEBS Letters · doi:10.1016/0014-5793(94)80348-x · Cited by 95

Assessment of Amyloid β Protein in Cerebrospinal Fluid as an Aid in the Diagnosis of Alzheimer's Disease

Southwick, P. C., Yamagata, S. K., Echols, C. L., Higson, G. J., Neynaber, S. A., Parson, R. E., & Munroe, W. A. (1996) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.1996.66010259.x · Cited by 89

New advances in inclusion-body myositis

Askanas, V., & Engel, K. W. (1993) · Current Opinion in Rheumatology · doi:10.1097/00002281-199305060-00007 · Cited by 83

Amyloidosis: a familiar problem in the light of current pathogenetic developments.

Kisilevsky, R. (1983) · PubMed · Cited by 83

Polyclonals to β-amyloid(1–42) identify most plaque and vascular deposits in Alzheimer cortex, but not striatum

Mak, K., Yang, F., Vinters, H. V., Frautschy, S. A., & Cole, G. M. (1994) · Brain Research · doi:10.1016/0006-8993(94)91725-6 · Cited by 80

The Structure of Neuritic Plaques in the Cerebral Cortex of Aged Rats

Vaughan, D. W., & Peters, A. (1981) · Journal of Neuropathology & Experimental Neurology · doi:10.1097/00005072-198107000-00009 · Cited by 78

Alzheimer Amyloid-β Peptide Forms Denaturant-Resistant Complex with Type ε3 but Not Type ε4 Isoform of Native Apolipoprotein E

Zhou, Z., Smith, J. D., Greengard, P., & Gandy, S. (1996) · Molecular Medicine · doi:10.1007/bf03401614 · Cited by 73

Alzheimer amyloid-beta peptide forms denaturant-resistant complex with type epsilon 3 but not type epsilon 4 isoform of native apolipoprotein E.

Zhou, Z., Smith, J. D., Greengard, P., & Gandy, S. (1996) · PubMed Central · Cited by 71

Studies on Inflammation: X. The Cytological Picture of an Inflammatory Exudate in Relation to its Hydrogen Ion Concentration.

MENKIN, V. (1934) · Europe PMC (PubMed Central) · Cited by 68

Native Complex Formation between Apolipoprotein E Isoforms and the Alzheimer's Disease Peptide Aβ

Chan, W., Fornwald, J. A., Brawner, M. E., & Wetzel, R. B. (1996) · Biochemistry · doi:10.1021/bi952852v · Cited by 57

pH-Dependent Conformations of the Amyloid .beta.(1-28) Peptide Fragment Explored Using Molecular Dynamics

Kirshenbaum, K., & Daggett, V. (1995) · Biochemistry · doi:10.1021/bi00023a009 · Cited by 53

The effect of pH on the kinetics of iron release from human transferrin

Baldwin, D. A., Sousa, D. M. R. D., & Wandruszka, R. M. A. V. (1982) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/0304-4165(82)90317-8 · Cited by 52

Ferrous iron release from transferrin by human neutrophil-derived superoxide anion: Effect of pH and iron saturation

Brieland, J. K., & Fantone, J. C. (1991) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(91)90266-l · Cited by 51

Zinc Deficiency and Incorporation of 14C-labeled Methionine into Tissue Proteins in Rats

Hsu, J. M., Anthony, W. L., & Buchanan, P. J. (1969) · Journal of Nutrition · doi:10.1093/jn/99.4.425 · Cited by 51

Molecular pathogenesis of beta-amyloidosis in Alzheimer's disease and other cerebral amyloidoses.

Maury, C. P. J. (1995) · PubMed · Cited by 45

Response : Zinc and Alzheimer's Disease

Bush, A. I., Moir, R. D., Rosenkranz, K. M., & Tanzi, R. E. (1995) · Science · doi:10.1126/science.268.5219.1921 · Cited by 45

Development of a monoclonal antibody specific for the COOH-terminal of beta-amyloid 1-42 and its immunohistochemical reactivity in Alzheimer's disease and related disorders.

Murphy, G. M., Forno, L. S., Higgins, L. S., Scardina, J. M., Eng, L. F., & Cordell, B. (1994) · PubMed Central · Cited by 44

The binding of transition metal ions in insulin crystals

Brill, A. S., & Venable, J. H. (1968) · Journal of Molecular Biology · doi:10.1016/0022-2836(68)90160-5 · Cited by 38

Effect of divalent metal ions and pH upon the binding reactivity of human serum amyloid P component, a C-reactive protein homologue, for zymosan. Preferential reactivity in the presence of copper and acidic pH.

Potempa, L. A., Kubak, B., & Gewurz, H. (1985) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)38998-6 · Cited by 36

Muscle fiber degeneration in distal myopathy with rimmed vacuole formation

Murakami, N., Ihara, Y., & Nonaka, I. (1995) · Acta Neuropathologica · doi:10.1007/bf00294256 · Cited by 33

Functional heterogeneity and pH-dependent dissociation properties of human transferrin

Princiotto, J. V. (1976) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/0304-4165(76)90207-5 · Cited by 31

Spectrophotometric determination of copper with N,N,N′,N′-tetraethylthiuram disulfide and an application of this method for studies on subcellular distribution of copper in rat brain

Matsuba, Y., & Takahashi, Y. (1970) · Analytical Biochemistry · doi:10.1016/0003-2697(70)90346-5 · Cited by 31

Molecular Mechanisms of Dementia

Rubinsztein, D. C. (1997) · Journal of Medical Genetics · doi:10.1136/jmg.34.9.791-a · Cited by 29

Myocardial zinc metabolism in experimental myocardial infarction.

Lindeman, R. D., Yunice, A. A., Baxter, D. J., Miller, L. R., & Nordquist, J. A. (1973) · PubMed · Cited by 29

Selective binding of soluble Abeta1-40 and Abeta1-42 to a subset of senile plaques.

Prior, R., D’Urso, D., Frank, R. W., Prikulis, I., Cleven, S., Ihl, R., & Pavlaković, G. (1996) · Europe PMC (PubMed Central) · Cited by 28

Zinc sulfate and wound healing

Haley, J. V. (1979) · Journal of Surgical Research · doi:10.1016/0022-4804(79)90127-6 · Cited by 28

Inflammation-associated amyloidogenesis

Kisilevsky, R. (1994) · Molecular Neurobiology · doi:10.1007/bf02778008 · Cited by 22

Chemical modification of glucosamine-6-phosphate synthase by diethyl pyrocarbonate: Evidence of histidine requirement for enzymatic activity

Badet‐Denisot, M., & Badet, B. (1992) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(92)90018-r · Cited by 22

Uptake of 67Cu by Ceruloplasmin In Vitro

Owen, C. A. (1975) · Experimental Biology and Medicine · doi:10.3181/00379727-149-38878 · Cited by 19

THE BIOLOGIC SIGNIFICANCE OF AMYLOID*

Gorevic, P. D., Cleveland, A. B., & Franklin, E. C. (1982) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.1982.tb22151.x · Cited by 16

Two‐dimensional NMR assignment of hyperfine‐shifted resonances of very fast relaxing metal binding sites of proteins by NOE spectroscopy

Sette, M., Paci, M., Desideri, A., & Rotilio, G. (1993) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1993.tb17773.x · Cited by 13

Immunohistochemical localization of amyloid beta-protein deposits in extracerebral tissues of patients with Alzheimer's disease.

Skodras, G., Peng, J. H., Parker, J. C., & Kragel, P. J. (1993) · PubMed · Cited by 8

Inflammatory diseases and copper

Gutteridge, J. C. (1985) · FEBS Letters · doi:10.1016/0014-5793(85)80459-2 · Cited by 4

The titration curve of insulin in the presence of various bivalent metal ions

Graae, J. (1968) · Biochemical Journal · doi:10.1042/bj1060777 · Cited by 4

Neurodegenerative diseases and oxidative stress

Barnham, K. J., Masters, C. L., & Bush, A. I. (2004) · Nature Reviews Drug Discovery · doi:10.1038/nrd1330 · Cited by 3,683

The neurobiology of zinc in health and disease

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Inhibitory Effect of Copper(II) on Zinc(II)-Induced Aggregation of Amyloid β-Peptide

Suzuki, K., Miura, T., & Takeuchi, H. (2001) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.2001.5263 · Cited by 90

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