Citation list rPeptide, LLC

Murray, I.V.J., Liu, L., Komatsu, H., Uryu, K., Xiao, G., Lawson, J.A., Axelsen, P.H. (2007) Membrane mediated amyloidogenesis and the promotion of oxidative lipid damage by amyloid β proteins. Journal of Biological Chemistry; 282(13):9335–9345

Garzon, D.J., Fahnestock, M. (2007) Oligomeric amyloid decreases basal levels of brain–derived neurotrophic factor (BDNF) mRNA via specific downregulation of BDNF transcripts IV and V in differentiated human neuroblastoma cells. The Journal of Neuroscience; 27(10):2628–2635.

Yan, Y., Wang, C. (2007) Aβ40 protects non–toxic Aβ42 monomer from aggregation. Journal of Molecular Biology; 369:909–916.

Chen, L., Jin, J., Davis, J., Zhou, Y., Wang, Y., Liu, J., Lockhart, P.J., Zhang, J. (2007) Oligomeric α–synuclein inhibits tubulin polymerization.Biochemical and Biophysical ResearchCommunications; 356:548–553.

Garai, K., Sureka, R., Maiti, S. (2007) Detecting amyloid–β aggregation with fiber–based fluorescence correlation spectroscopy. Biophysical Journal; 92:L55–L57.

Lacor, P.N., Buniel, M.C., Furlow, P.W., Clemente, A.S., Velasco, P.T., Wood, M, Viola, K.L., Klein, W.L. (2007) Aβ oligomer–induced aberrations in synapse composition, shape, and density provide a molecular basis for loss of connectivity in alzheimer’s disease. Neurobiology of Disease; 27(4):796–807.

De–Felice, F.G., Velasco, P.T., Lambert, M.P., Viola, K., Fernandez, S.J., Ferreira, S.T., Klein, W.L. (2007) Aβ oligomers induce neuronal oxidative stress through an N–methyl–D–aspartate receptor–dependent mechanism that is blocked by the alzheimer drug memantine. The Journal of Biological Chemistry; 282(15):11590–11601.

Scott Kim, W., Rahmanto, A.S., Kamili, A., Rye, K–A., Guillemin, G.J., Gelissen, I.C., Jessup, W., Hill, A.F., Garner, B. (2007) Role of ABCG1 and ABCA1 in regulation of neuronal cholesterol efflux to apolipoprotein E discs and suppression of amyloid–β peptide generation. The Journal of Biological Chemistry; 282(5):2851–2861.

Du, P., Wood, K.M., Rosner, M.H., Cunningham, D., Tate, B., Geoghegan, K.F. (2007) Dominance of amyloid precursor protein sequence over host cell secretases in determining β–amyloid profiles studies of interspecies variation and drug action by internally standardized immunoprecipitation/mass spectrometry. The Journal of Pharmacology and Experimental Therapeutics; 320(3):1144–1152.

Johansson, A–S., Garlind, A., Berglind–Dehlin, F., Karlsson, G., Edwards, K., Gellerfors, P., Ekholm–Pettersson, F., Palmblad, J., Lannfelt, L. (2007) Docosahexaenoic acid stabilizes soluble amyloid–β protofibrils and sustains amyloid–β–induced neurotoxicity in vitro. The FEBS Journal; 274: 990–1000.

Hu, M., Schurdak, M.E., Puttfarcken, P.S., Kouhen, R.E., Gopalakrishnan, M., Li, J. (2007) High content screen microscopy analysis of Aβ1–42–induced neurite outgrowth reduction in rat primary cortical neurons: Neuroprotective effects of α7 neuronal nicotinic acetylcholine receptor ligands. Brain Research; 1151:227–235.

Danielsson, J., Pierattelli, R., Banci, L., Graslund, A. (2007) High–resolution NMR studies of the zinc–binding site of the Alzheimer’s amyloid β–peptide. The FEBS Journal; 274:46–59.

Bharathi. Rao , K.S.J. (2007) Thermodynamics imprinting reveals deferential binding of metals to α–synuclein: Relevance to parkinson’s disease: Biochemical and Biophysical Research Communications; 359:15–120.

Suram, A., Hegde, M.L., Rao, K.S.J. (2007) A new evidence for DNA nicking property of amyloid β–peptide (1–42): Relevance to Alzheimer’s disease. Archives of Biochemistry and Biophysics; (In press).

Hegde, M.L., Rao, K.S.J. (2007) DNA induces folding in a–synuclein: Understanding the mechanism using chaperone property of osmolytes. Archives of Biochemistry and Biophysics; (In press).

Jin, J., Shie, F–S., Liu, J.,Wang,Y., Davis, J., Schantz, A.M., Montine, K.S., Montine, T.H., Zhang, J. (2007) Prostaglandin E2 receptor subtype 2 (EP2) regulates microglial activation and associated neurotoxicity induced by aggregated α–synuclein. Journal of Neuroinflammation; 4:2 doi: 10.1186/1742–2094–4–2.

Pym, J.L., Buckingham, D.S., Tsetlin, V., Boyd, C.A.R., Sattelle, D.B.S. (2007) The Aβ1–42M35C mutated amyloid peptide Aβ1–42 and the 25–35 fragment fail to mimic the subtype–specificity of actions on recombinant human nicotinic acetylcholine receptors (α7, α4β2, α3β4). Neuroscience Letters; 427(1):28–33.

Chen, L., Jin, J., Davis J., Zhou, Y., Wang, Y., Liu, J., Lockhart, P.J., and Zhag, J. (2007) Oligomeric α–synuclein inhibits tubulin polymerization. Biochemical and Biophysical Research Communications; 356(3):548–553.

Yan, Y., Liu, J., McCallum, S.A., Yang, D., Wang, C. (2007) Methyl dynamics of the amyloid–β peptides Aβ40 and Aβ42. Biochemical and Biophysical Research Communications; 362(2):410–414.

20. Diana, K., Gabriele, J., Markus, G., Markus, K., Mathias, J., Igor, M., Ingolf, Lary C.W., Heyo, K.K., Rolf, W.W., Silke, V. (2007) MDR1–P–Glycoprotein (ABCB1) Mediates Transport of Alzheimer’s Amyloid–β Peptides–Implications for the Mechanisms of Aβ Clearance at the Blood–Brain Barrier. Brain Pathology; 17(4):347–353.

Sahoo, B., Goswami, M., Nag, S., Maiti, S. (2007) Spontaneous formation of a protein corona prevents the loss of quantum dot fluorescence in physiological buffers. Chemical Physics Letters; 445(4–6):217–220.

Klegeris, A., McGeer, P.L. (2007) Complement activation by islet amyloid polypeptide (IAPP) and α–synuclein 112. Biochemical and Biophysical Research Communications; 357(4):1096–1099.

Wieneke J.A Van Geel., Abdo, W., F.,Melis, R., Williams, S., Verbeek, M., M. (2007) A more efficient enzyme–linked immunosorbent assay for measurement of α–synuclein in cerebrospinal fluid. Journal of Neuroscience Methods , Article in Press, Corrected Proof.

Englund. H., Sehlin.D., Johansson. A–S., Nilsson. L. N.G., Gellerfors. P., Pettersson. F.E. (2007) Sensitive ELISA detection of amyloid–β protofibrils in biological samples. Journal of Neurochemistry; 103(1):334–345.

Manelli. A.M., Bulfinch. L.C., Sullivan. P.M., LaDu. M.J. (2007) Aβ42 neurotoxicity in primary co–cultures: Effect of apoE isoform and Aβ conformation. Neurobiology of Aging; 28(8):1139–1147.

Boddaert. J., Kinugawa. K., Lambert. J–C., Boukhtouche. F., Zoll. J., Olivier. B–B., Mann. D., Berr. C., Vilar. J., Garabedian. B., Charue. D., Duyckaerts. C., Amouyel. P., Mariani. J., Tedgui. A., Mallat. Z. (2007) Evidence of a Role for Lactadherin in Alzheimer’s Disease. American Journal of Pathology; 170:921–929.

Udan. M.L.D., Ajit. D., Crouse. N.R., Nicholas. M.R. (2007) Toll–like receptors 2 and 4 mediate Aβ(1–42) activation of the innate immune response in a human monocytic cell line. Journal of Neurochemistry; 104(2):524–533.

Findeis. M.A. (2007) The role of amyloid β peptide 42 in Alzheimer’s disease. Pharmacology & Therapeutics; 116(2):266–286.

Bell. R.D., Sagare. A.P., Friedman. A.E., Bedi. G.S., Holtzman. D.M., Deane. R., Zlokovic.B.V. (2007) Transport pathways for clearance of human Alzheimer’s amyloid β–peptide and apolipoproteins E and J in the mouse central nervous system. Journal of Cerebral Blood Flow & Metabolism; 27: 909–918.

Walker, D.G., Link, J., Lue, L–F., Dalsing–Hernandez, J.E., Boyes, B. E. (2006) Gene expression changes by amyloid β peptide–stimulated human postmortem brain microglia identify activation of multiple inflammatory processes. Journal of Leukocyte Biology; 79:596–610.

Inoue, K., Garner, C., Ackermann, B.L., Oe, T., Blair, I. A. (2006) Liquid chromatography/tandem mass spectrometry characterization of oxidized amyloid beta peptides as potential biomarkers of Alzheimer’s disease. Rapid Commun. Mass Spectrometry; 20(5):911–918.

Craft, J.M., Watterson, D.M., Eldik, L.J.V. (2006) Human amyloid β–induced neuroinflammation is an early event in neurodegeneration. Glia; 53:484–490.

Floden, A.M., Combs, C.K., (2006) β–Amyloid Stimulates Murine Postnatal and Adult Microglia Cultures in a Unique Manner. Journal of Neuroscience; 26(17):4644–4648.

Simard, A.R., Soulet, D., Gowing, G., Julien, J–P., Rivest, S. (2006) Bone marrow–derived microglia play a critical role in restricting senile plaque formation in Alzheimer’s diseases. Neuron; 49: 489–502.

Johansson, A–S., Berglind–Dehlin, F., Karlsson, G., Edwards, K., Gellerfors, P., Lannfelt, L. (2006) Physiochemical characterization of the Alzheimer’s disease–related peptides Aβ1–42Arctic and Aβ1–42wt. The FEBS Journal; 273(12):2618–2630.

Bagriantsev, S., Liebman, S. (2006) Modulation of Aβ42 low–n oligomerization using a novel yeast reporter system. BMC Biology; 4:32.

Isaacs, A.M., Senn, D.B., Yuan, M., Shine, J.P., Yankner, B.A. (2006) Acceleration of amyloid β–peptide aggregation by physiological concentrations of calcium. Journal Biological Chemistry; 281(38):27916–27923.

Moses, G.S., Jensen, M.D., Lue, L–F., Walker, D.G., Sun, A.Y., Simonyi, A., Sun, G.Y. (2006) Secretory PLA2–IIA: a new inflammatory factor for Alzheimer’s disease. Journal of Neuroinflammation; 3:28.

Ingelsson, M., Ramasamy, K., Cantuti–Castelvetri, I., Skoglund, L., Matsui, T., Orne, J., Kowa, H., Raju, S., Vanderburg, C.R., Augustinack, J.C., Silva, R.D., Lees, A.J., Lannfelt, L., Growdon, J.H., Frosch, M.P., Standaert, D.G., Irizarry, M.C., Hyman, B.T. (2006) No alteration in tau exon 10 alternative splicing in tangle–bearing neurons of the Alzheimer’s disease brain. Acta Neuropathol; 112:439–449.

Williamson, M.P., Suzuki, Y., Bourne, N.T., Asakura, T. (2006) Binding of amyloid β to ganglioside micelles is dependent on histidine–13. Biochemical Journal; 397:483–490.

Sun, Z.P., Alpa, C., Yuan, J.M., Reinhard, S–S., Wei, Y. (2006) A novel method to study aggregation of amyloid β1–42 – A key peptide associated with Alzheimer’s disease. Abstracts of Papers, 231st ACS National Meeting, Atlanta, GA, United States, March 26–30, 2006, INOR–128. CODEN: 69HYEC AN2006: 247457 CAPLUS.

Oe, T., Ackermann, B.L., Inoue, K., Berna, M.J., Garner, C.O., Gelfanova, V., Dean, R.A., Siemers, E.R., Holtzman, D.M., Farlow, M.R., Blair, I.A. (2006) Quantitative analysis of amyloid β peptides in cerebrospinal fluid of Alzheimer’s disease patients by immunoaffinity purification and stable isotope dilution liquid chromatography–negative electrospray ionization/ tandem mass spectrometry. Rapid Communications in Mass Spectrometry; 20:3723–3735

Mueller–Steiner, S., Zhou, Y., Arai, H., Roberson, E.D., Sun, B., Chen, J., Wang, X., Yu, G., Esposito, L., Mucke, L., Gan, L. (2006) Antiamyloidogenic and neuroprotective Functions of cathepsin B: implications for alzheimer’s disease. Neuron; 51:703–714.

Lue, L– F., Yan, S.D., Stern, D.M., Walker, D.G. (2005) Preventing activation of receptor for advanced glycation endproducts in Alzheimer’s disease. Current Drug Targets – CNS & Neurological Disorders; 4(3):249–266.

Nichols, M.R., Moss, M.A., Reed, D.K., Cratic–McDaniel, S., Hoh, J.H., Rosenberry, T.L. (2005) Amyloid–β protofibrils differ from amyloid–β aggregates induced in dilute hexafluoroisopropanol in stability and morphology. Journal Biological Chemistry; 280(4):2471–2480.

Dickey, C.A., Gordon, M.N., Wilcock, D.M., Herber, D.L., Freeman, M.J., Morgan, D. (2005) Dysregulation of Na+/K+ ATPase by amyloid in APP+PS1 transgenic mice. BMC Neuroscience; 6:7.

Unlap, M.T., Williams, C., Morin, D., Siroky, B., Fintha, A., Fuson, A., Dodgen, L., Kovacs, G., Komlosi, P., Ferguson, W., Bell, P.D. (2005) Amyloid beta peptide 1–40 stimulates the Na+ / Ca2+ exchange activity of SNCX. Current Neurovascular Research; 2(1):3–12.

Chen, J., Zhou, Y., Mueller–Steiner, S., Chen, L–F., Kwon, H., Yi, S., Mucke, L., Gan, L. (2005) SIRT1 protects against microglia–dependent amyloid–β toxicity through inhibiting NF–?B signaling. Journal Biological Chemistry; 280(48):40364–40374.

Shie, F–S., Breyer, R.M., Montine, T.J. (2005) Microglia lacking E prostanoid receptor subtype 2 have enhanced Aβ phagocytosis yet lack Aβ–activated neurotoxicity. American Journal of Pathology; 166(4):1163–1172.

Shie, F–S., Montine, K.S., Breyer, R.M., Montine T.J. (2005) Microglial EP2 is critical to neurotoxicity from activated cerebral innate immunity. Glia; 52:70–76.

Lindberg, C., Crisby, M., Winblad, B., Schultzberg, M. (2005) Effects of statins on microglia. Journal of Neuroscience Research; 82:10–19.

Wiley, J.C., Hudson, M., Kanning, K.C., Schecterson, L.C., Bothwell, M. (2005) Familial Alzheimer’s disease mutations inhibit ?–secretase–mediated liberation of β–amyloid precursor protein carboxy–terminal fragment. Journal of Neurochemistry; 94(5):1189–1201.

Nichols, M.R., Moss, M.A., Reed, D.K., Hoh, J.H., Rosenberry, T.L. (2005) Amyloid–β aggregates formed at polar–nonpolar interfaces differ from amyloid–β protofibrils produced in aqueous buffers. Microscopy Research and Technique; 67:164–174.

Hu, Q., Wang, L., Yang, Z., Cool, B.H., Zitnik, G., Martin, G.M. (2005) Endoproteolytic cleavage of FE65 converts the adaptor protein to a potent suppressor of the sAPPα pathway in primates. Journal Biological Chemistry; 280(13):12548–12558.

Medina, M.G., Ledesma, M.D., Domínguez, J.E., Medina, M., Zafra, D., Alameda, F., Dotti, C.G., Navarro, P. (2005) Tissue plasminogen activator mediates amyloid–induced neurotoxicity via Erk1/2 activation. The EMBO Journal; 24(9):1706–1716.

Park, L., Anrather, J., Zhou, P., Frys, K., Pitstick, R., Younkin, S., Carlson, G.A., Iadecola, C. (2005) NADPH oxidase–derived reactive oxygen species mediate the cerebrovascular dysfunction induced by the amyloid β peptide. The Journal of Neuroscience; 25(7):1769–1777.

Lindberg, C., Selenica, M–L. B., Westlind–Danielsson, A., Schultzberg, M. (2005) β–Amyloid protein structure determines the nature of cytokine release from rat microglia. Journal Molecular Neuroscience; 27:1–12.

Murray, I.V., Sindoni, M.E., Axelsen, P.H. (2005) Promotion of oxidative lipid membrane damage by amyloid β proteins. Biochemistry; 44:12606–12613.

Ciccotosto, G.D., Tew, D., Curtain, C.C., Smith, D., Carrington, D., Masters, C.L., Bush, A.I., Cherny, R.A., Cappai, R., Barnham, K.J. (2004) Enhanced Toxicity and Cellular Binding of a Modified Amyloid Peptide with a methionine to valine substitution. Journal Biological Chemistry; 279: 42528–42534.

Hou, L., Shao, H., Zhang, Y., Li, H., Menon, N.K., Neuhaus, E.B., Brewer, J.M., Byeon, I.L., Ray, D.G., Vitek, M.P., Iwashita, T., Makula, R.A., Przybyla, A.B., Zagorski, M.G. (2004) Solution NMR studies of the Aβ(1–40) and Aβ(1–42) peptides establish that the Met35 oxidation state affects the mechanism of amyloid formation. J. Am. Chem. Soc; 126:1992–2005.

Mandal, P.K., Pettegrew, J.W., (2004) Alzheimer’s disease: NMR studies of asialo (GMI) and trisialo (GT1b) ganglioside interactions with Aβ(1–40) peptide in a membrane mimic environment. Neurochemical Research; 29(2):447–453.

El–Agnaf, O.M.A., Paleologou, K.E., Greer, B., Abogrein, A.M., King, J.E., Salem, S.A., Fullwood, N.J., Benson, F.E., Hewitt, R., Ford, K.J., Martin, F.L., Harriott, P., Cookson, M.R., Allsop, D. (2004) A strategy for designing inhibitors of alpha–synuclein aggregation and toxicity as a novel treatment for Parkinson’s disease and related disorders. The Faseb Journal; June 4, doi:10.1096/fj.03–1346fje.

Barnham, K.J., Haeffner, F., Ciccotosto, G.D., Curtain, C.C., Tew, D., Mavros, C., Beyreuther, K., Carrington, D., Masters, C.L., Cherny, R.A., Cappai, R., Bush, A.I. (2004) Tyrosine gated electron transfer is key to the toxic mechanism of Alzheimer’s disease β–amyloid. The Faseb Journal; July 1, doi:10.1096/fj.03–1346fje.

Wu, J., Kuo, Y–P., George, A.A., Xu, L., Hu, J., Lukas, R.J. (2004) β–amyloid directly inhibits human α4β2–nicotinic acetylcholine receptors heterologously expressed in human SH–EP1 cells. Journal of Biological Chemistry; 279(36):37842–37851.

Stine, W.B. Jr, Dahlgren, K.N., Krafft, G.K., and LaDu, M.J. (2003) In vitro characterization of conditions for amyloid–β peptide oligomerization and fibrillogenesis. Journal Biological Chemistry; 278:11612–11622.

LeVine III, H. (2003) Y10W b (1–40) fluorescence reflects epitope exposure in conformers of Alzheimer’s β peptide. Archives of Biochem and Biophys; 417(1):112–122.

Dahlgren, K. N., Manelli, A. M., Stine, W. B. J., Baker, L. K., Krafft, G. A., and LaDu, M. J. (2002) Oligomeric and fibrillar species of amyloid–β peptides differentially affect neuronal viability. J. Biol. Chem; 277:32046–32053.

Zeng, H., Zhang, Y., Peng, L.–J, Shao, H., Menon, N.K., Yang, J., Salomon, A.R., Friedland, R.P. and Zagorski, M.G. (2001) Nicotine and amyloid formation. Biological Psychiatry; 49:&c 248–257.

Chesneau, V., Vekrellis, K., Rosner, M.R., and Selkoe, D. (2000) Purified recombinant insulin–degrading enzyme degrades amyloid b protein but does not promote its oligomerization. Biochem. Journal; 351:509–516.


   
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