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Items: 1 to 20 of 97

1.

Structural interactions between inhibitor and substrate docking sites give insight into mechanisms of human PS1 complexes.

Li Y, Lu SH, Tsai CJ, Bohm C, Qamar S, Dodd RB, Meadows W, Jeon A, McLeod A, Chen F, Arimon M, Berezovska O, Hyman BT, Tomita T, Iwatsubo T, Johnson CM, Farrer LA, Schmitt-Ulms G, Fraser PE, St George-Hyslop PH.

Structure. 2014 Jan 7;22(1):125-35. doi: 10.1016/j.str.2013.09.018. Epub 2013 Nov 7.

2.

Structural biology of presenilin 1 complexes.

Li Y, Bohm C, Dodd R, Chen F, Qamar S, Schmitt-Ulms G, Fraser PE, St George-Hyslop PH.

Mol Neurodegener. 2014 Dec 18;9:59. doi: 10.1186/1750-1326-9-59. Review.

3.

Toward the structure of presenilin/γ-secretase and presenilin homologs.

Wolfe MS.

Biochim Biophys Acta. 2013 Dec;1828(12):2886-97. doi: 10.1016/j.bbamem.2013.04.015. Review.

4.

Mutation analysis of the presenilin 1 N-terminal domain reveals a broad spectrum of gamma-secretase activity toward amyloid precursor protein and other substrates.

Gong P, Vetrivel KS, Nguyen PD, Meckler X, Cheng H, Kounnas MZ, Wagner SL, Parent AT, Thinakaran G.

J Biol Chem. 2010 Dec 3;285(49):38042-52. doi: 10.1074/jbc.M110.132613. Epub 2010 Oct 4.

5.

Identification of presenilin 1-selective γ-secretase inhibitors with reconstituted γ-secretase complexes.

Lee J, Song L, Terracina G, Bara T, Josien H, Asberom T, Sasikumar TK, Burnett DA, Clader J, Parker EM, Zhang L.

Biochemistry. 2011 Jun 7;50(22):4973-80. doi: 10.1021/bi200026m. Epub 2011 May 13.

PMID:
21528914
6.

Identification of gamma-secretase inhibitor potency determinants on presenilin.

Zhao B, Yu M, Neitzel M, Marugg J, Jagodzinski J, Lee M, Hu K, Schenk D, Yednock T, Basi G.

J Biol Chem. 2008 Feb 1;283(5):2927-38. Epub 2007 Nov 21.

7.

Molecular dynamics simulation study reveals potential substrate entry path into γ-secretase/presenilin-1.

Kong R, Chang S, Xia W, Wong ST.

J Struct Biol. 2015 Aug;191(2):120-9. doi: 10.1016/j.jsb.2015.07.001. Epub 2015 Jul 2.

PMID:
26142917
8.

Presenilin transmembrane domain 8 conserved AXXXAXXXG motifs are required for the activity of the γ-secretase complex.

Marinangeli C, Tasiaux B, Opsomer R, Hage S, Sodero AO, Dewachter I, Octave JN, Smith SO, Constantinescu SN, Kienlen-Campard P.

J Biol Chem. 2015 Mar 13;290(11):7169-84. doi: 10.1074/jbc.M114.601286. Epub 2015 Jan 22.

9.

Dissociation between the processivity and total activity of γ-secretase: implications for the mechanism of Alzheimer's disease-causing presenilin mutations.

Quintero-Monzon O, Martin MM, Fernandez MA, Cappello CA, Krzysiak AJ, Osenkowski P, Wolfe MS.

Biochemistry. 2011 Oct 25;50(42):9023-35. doi: 10.1021/bi2007146. Epub 2011 Sep 30.

10.

Participation of transmembrane domain 1 of presenilin 1 in the catalytic pore structure of the γ-secretase.

Takagi S, Tominaga A, Sato C, Tomita T, Iwatsubo T.

J Neurosci. 2010 Nov 24;30(47):15943-50. doi: 10.1523/JNEUROSCI.3318-10.2010.

11.

gamma-Secretase complexes containing N- and C-terminal fragments of different presenilin origin retain normal gamma-secretase activity.

Strömberg K, Hansson EM, Laudon H, Bergstedt S, Näslund J, Lundkvist J, Lendahl U.

J Neurochem. 2005 Nov;95(3):880-90. Epub 2005 Aug 31.

12.

Conformational Changes in Transmembrane Domain 4 of Presenilin 1 Are Associated with Altered Amyloid-β 42 Production.

Tominaga A, Cai T, Takagi-Niidome S, Iwatsubo T, Tomita T.

J Neurosci. 2016 Jan 27;36(4):1362-72. doi: 10.1523/JNEUROSCI.5090-14.2016.

13.

Generation of amyloid-β is reduced by the interaction of calreticulin with amyloid precursor protein, presenilin and nicastrin.

Stemmer N, Strekalova E, Djogo N, Plöger F, Loers G, Lutz D, Buck F, Michalak M, Schachner M, Kleene R.

PLoS One. 2013 Apr 9;8(4):e61299. doi: 10.1371/journal.pone.0061299. Print 2013.

14.

Allosteric modulation of PS1/gamma-secretase conformation correlates with amyloid beta(42/40) ratio.

Uemura K, Lill CM, Li X, Peters JA, Ivanov A, Fan Z, DeStrooper B, Bacskai BJ, Hyman BT, Berezovska O.

PLoS One. 2009 Nov 18;4(11):e7893. doi: 10.1371/journal.pone.0007893.

15.
16.

Cooperative roles of hydrophilic loop 1 and the C-terminus of presenilin 1 in the substrate-gating mechanism of γ-secretase.

Takagi-Niidome S, Sasaki T, Osawa S, Sato T, Morishima K, Cai T, Iwatsubo T, Tomita T.

J Neurosci. 2015 Feb 11;35(6):2646-56. doi: 10.1523/JNEUROSCI.3164-14.2015.

17.

The presenilin C-terminus is required for ER-retention, nicastrin-binding and gamma-secretase activity.

Kaether C, Capell A, Edbauer D, Winkler E, Novak B, Steiner H, Haass C.

EMBO J. 2004 Dec 8;23(24):4738-48. Epub 2004 Nov 18.

18.

Structural basis of human γ-secretase assembly.

Sun L, Zhao L, Yang G, Yan C, Zhou R, Zhou X, Xie T, Zhao Y, Wu S, Li X, Shi Y.

Proc Natl Acad Sci U S A. 2015 May 12;112(19):6003-8. doi: 10.1073/pnas.1506242112. Epub 2015 Apr 27.

19.

Mechanism of gamma-secretase cleavage activation: is gamma-secretase regulated through autoinhibition involving the presenilin-1 exon 9 loop?

Knappenberger KS, Tian G, Ye X, Sobotka-Briner C, Ghanekar SV, Greenberg BD, Scott CW.

Biochemistry. 2004 May 25;43(20):6208-18.

PMID:
15147205
20.

Novel gamma-secretase inhibitors uncover a common nucleotide-binding site in JAK3, SIRT2, and PS1.

Wu F, Schweizer C, Rudinskiy N, Taylor DM, Kazantsev A, Luthi-Carter R, Fraering PC.

FASEB J. 2010 Jul;24(7):2464-74. doi: 10.1096/fj.09-148031. Epub 2010 Mar 17.

PMID:
20237298

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