Peptides inhibiting specific cleaving activities of presenilins

Bibliography

• Wolfe MS. Shutting down Alzheimer's. Sci Am 2006;294(5):72-9
   PubMedGoogle Scholar
• Haass C, Selkoe DJ. Soluble protein oligomers in neurodegeneration: lessons from the Alzheimer's amyloid beta-peptide. Nat Rev Mol Cell Biol 2007;8(2):101-12
   PubMed Web of Science ®Google Scholar
• Tomita T, Iwatsubo T. Gamma-secretase as a therapeutic target for treatment of Alzheimer's disease. Curr Pharm Des 2006;12(6):661-70
   PubMed Web of Science ®Google Scholar
• Tomita T. At the frontline of Alzheimer's disease treatment: gamma-secretase inhibitor/modulator mechanism. Naunyn Schmiedebergs Arch Pharmacol 2008;377(4-6):70-8
   Google Scholar
• Selkoe DJ, Wolfe MS. Presenilin: running with scissors in the membrane. Cell 2007;131(2):215-21
   PubMed Web of Science ®Google Scholar
• Ilagan MX, Kopan R. SnapShot: notch signaling pathway. Cell 2007;128(6):1246
   PubMedGoogle Scholar
• Parks AL, Curtis D. Presenilin diversifies its portfolio. Trends Genet 2007;23(3):140-50
   PubMed Web of Science ®Google Scholar
• Searfoss GH, Jordan WH, Calligaro DO, et al. Adipsin, a biomarker of gastrointestinal toxicity mediated by a functional gamma-secretase inhibitor. J Biol Chem 2003;278(46):46107-16
   PubMed Web of Science ®Google Scholar
• Wong GT, Manfra D, Poulet FM, et al. Chronic treatment with the gamma-secretase inhibitor LY-411,575 inhibits beta-amyloid peptide production and alters lymphopoiesis and intestinal cell differentiation. J Biol Chem 2004;279(13):12876-82
   PubMed Web of Science ®Google Scholar
• Milano J, McKay J, Dagenais C, et al. Modulation of notch processing by gamma-secretase inhibitors causes intestinal goblet cell metaplasia and induction of genes known to specify gut secretory lineage differentiation. Toxicol Sci 2004;82(1):341-58
   PubMed Web of Science ®Google Scholar
• Langedijk JP. Transport peptides among which C-terminal Erns peptide and analogues thereof. WO0200882; 2002
   Google Scholar
• Langedijk JP. Translocation activity of C-terminal domain of pestivirus Erns and ribotoxin L3 loop. J Biol Chem 2002;277(7):5308-14
   PubMedGoogle Scholar
• Wolfe MS, Xia W, Ostaszewski BL, et al. Two transmembrane aspartates in presenilin-1 required for presenilin endoproteolysis and gamma-secretase activity. Nature 1999;398(6727):513-7
   PubMed Web of Science ®Google Scholar
• Li YM, Xu M, Lai MT, et al. Photoactivated gamma-secretase inhibitors directed to the active site covalently label presenilin 1. Nature 2000;405(6787):689-94
   PubMed Web of Science ®Google Scholar
• Tolia A, Chavez-Gutierrez L, De Strooper B. Contribution of presenilin transmembrane domains 6 and 7 to a water-containing cavity in the gamma-secretase complex. J Biol Chem 2006;281(37):27633-42
   PubMed Web of Science ®Google Scholar
• Sato C, Morohashi Y, Tomita T, Iwatsubo T. Structure of the catalytic pore of gamma-secretase probed by the accessibility of substituted cysteines. J Neurosci 2006;26(46):12081-8
   PubMed Web of Science ®Google Scholar
• Tian G, Sobotka-Briner CD, Zysk J, et al. Linear non-competitive inhibition of solubilized human gamma-secretase by pepstatin A methylester, L685458, sulfonamides, and benzodiazepines. J Biol Chem 2002;277(35):31499-505
   PubMed Web of Science ®Google Scholar
• Tian G, Ghanekar SV, Aharony D, et al. The mechanism of gamma-secretase: multiple inhibitor binding sites for transition state analogs and small molecule inhibitors. J Biol Chem 2003;278(31):28968-75
   PubMed Web of Science ®Google Scholar
• Kornilova AY, Bihel F, Das C, Wolfe MS. The initial substrate-binding site of gamma-secretase is located on presenilin near the active site. Proc Natl Acad Sci USA 2005;102(9):3230-5
   PubMed Web of Science ®Google Scholar
• Annaert WG, Esselens C, Baert V, et al. Interaction with telencephalin and the amyloid precursor protein predicts a ring structure for presenilins. Neuron 2001;32(4):579-89
   PubMed Web of Science ®Google Scholar
• Esselens C, Oorschot V, Baert V, et al. Presenilin 1 mediates the turnover of telencephalin in hippocampal neurons via an autophagic degradative pathway. J Cell Biol 2004;166(7):1041-54
   PubMed Web of Science ®Google Scholar
• Suzuki N, Cheung TT, Cai XD, et al. An increased percentage of long amyloid beta protein secreted by familial amyloid beta protein precursor (beta APP717) mutants. Science 1994;264(5163):1336-40
   PubMed Web of Science ®Google Scholar
• Maruyama K, Tomita T, Shinozaki K, et al. Familial Alzheimer's disease-linked mutations at Val717 of amyloid precursor protein are specific for the increased secretion of A beta 42(43). Biochem Biophys Res Commun 1996;227(3):730-5
   PubMedGoogle Scholar
• Karlstrom H, Bergman A, Lendahl U, et al. A sensitive and quantitative assay for measuring cleavage of presenilin substrates. J Biol Chem 2002;277(9):6763-6
   PubMedGoogle Scholar
• Herreman A, Serneels L, Annaert W, et al. Total inactivation of gamma-secretase activity in presenilin-deficient embryonic stem cells. Nat Cell Biol 2000;2(7):461-2
   PubMed Web of Science ®Google Scholar
• Espeseth AS, Xu M, Huang Q, et al. Compounds that bind APP and inhibit Abeta processing in vitro suggest a novel approach to Alzheimer disease therapeutics. J Biol Chem 2005;280(18):17792-7
   PubMed Web of Science ®Google Scholar
• Kukar TL, Ladd TB, Bann MA, et al. Substrate-targeting gamma-secretase modulators. Nature 2008;453(7197):925-9
   PubMed Web of Science ®Google Scholar
• Sato T, Dohmae N, Qi Y, et al. Potential link between amyloid beta-protein 42 and C-terminal fragment gamma 49-99 of beta-amyloid precursor protein. J Biol Chem 2003;278(27):24294-301
   PubMedGoogle Scholar
• Zhao G, Mao G, Tan J, et al. Identification of a new presenilin-dependent zeta-cleavage site within the transmembrane domain of amyloid precursor protein. J Biol Chem 2004;279(49):50647-50
   PubMedGoogle Scholar
• Qi-Takahara Y, Morishima-Kawashima M, Tanimura Y, et al. Longer forms of amyloid beta protein: implications for the mechanism of intramembrane cleavage by gamma-secretase. J Neurosci 2005;25(2):436-45
   PubMed Web of Science ®Google Scholar
• Zhao G, Cui MZ, Mao G, et al. Gamma-cleavage is dependent on zeta-cleavage during the proteolytic processing of amyloid precursor protein within its transmembrane domain. J Biol Chem 2005;280(45):37689-97
   PubMed Web of Science ®Google Scholar
• Lichtenthaler SF, Wang R, Grimm H, et al. Mechanism of the cleavage specificity of Alzheimer's disease gamma-secretase identified by phenylalanine-scanning mutagenesis of the transmembrane domain of the amyloid precursor protein. Proc Natl Acad Sci USA 1999;96(6):3053-8
   PubMedGoogle Scholar
• Sato T, Tanimura Y, Hirotani N, et al. Blocking the cleavage at midportion between gamma- and epsilon-sites remarkably suppresses the generation of amyloid beta-protein. FEBS Lett 2005;579(13):2907-12
   PubMedGoogle Scholar