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Items: 1 to 20 of 152

1.

Alzheimer's disease associated presenilin-1 holoprotein and its 18-20 kDa C-terminal fragment are death substrates for proteases of the caspase family.

Grunberg J, Walter J, Loetscher H, Deuschle U, Jacobsen H, Haass C.

Biochemistry. 1998 Feb 24;37(8):2263-70.

PMID:
9485372
2.

The proteolytic fragments of the Alzheimer's disease-associated presenilin-1 form heterodimers and occur as a 100-150-kDa molecular mass complex.

Capell A, Grünberg J, Pesold B, Diehlmann A, Citron M, Nixon R, Beyreuther K, Selkoe DJ, Haass C.

J Biol Chem. 1998 Feb 6;273(6):3205-11.

3.

Expression of Alzheimer's disease-associated presenilin-1 is controlled by proteolytic degradation and complex formation.

Steiner H, Capell A, Pesold B, Citron M, Kloetzel PM, Selkoe DJ, Romig H, Mendla K, Haass C.

J Biol Chem. 1998 Nov 27;273(48):32322-31.

4.

Proteolytic processing of presenilin-1 (PS-1) is not associated with Alzheimer's disease with or without PS-1 mutations.

Okochi M, Ishii K, Usami M, Sahara N, Kametani F, Tanaka K, Fraser PE, Ikeda M, Saunders AM, Hendriks L, Shoji SI, Nee LE, Martin JJ, Van Broeckhoven C, St George-Hyslop PH, Roses AD, Mori H.

FEBS Lett. 1997 Nov 24;418(1-2):162-6.

5.

Proteolytic processing of the Alzheimer disease-associated presenilin-1 generates an in vivo substrate for protein kinase C.

Walter J, Grünberg J, Capell A, Pesold B, Schindzielorz A, Citron M, Mendla K, George-Hyslop PS, Multhaup G, Selkoe DJ, Haass C.

Proc Natl Acad Sci U S A. 1997 May 13;94(10):5349-54.

6.
7.

Proteolytic processing of Alzheimer's disease associated proteins.

Haass C, Grünberg J, Capell A, Wild-Bode C, Leimer U, Walter J, Yamazaki T, Ihara I, Zweckbronner I, Jakubek C, Baumeister R.

J Neural Transm Suppl. 1998;53:159-67. Review.

PMID:
9700654
8.

Presenilin proteins undergo heterogeneous endoproteolysis between Thr291 and Ala299 and occur as stable N- and C-terminal fragments in normal and Alzheimer brain tissue.

Podlisny MB, Citron M, Amarante P, Sherrington R, Xia W, Zhang J, Diehl T, Levesque G, Fraser P, Haass C, Koo EH, Seubert P, St George-Hyslop P, Teplow DB, Selkoe DJ.

Neurobiol Dis. 1997;3(4):325-37.

PMID:
9173929
9.
10.
11.

Zebrafish (Danio rerio) presenilin promotes aberrant amyloid beta-peptide production and requires a critical aspartate residue for its function in amyloidogenesis.

Leimer U, Lun K, Romig H, Walter J, Grünberg J, Brand M, Haass C.

Biochemistry. 1999 Oct 12;38(41):13602-9.

PMID:
10521267
12.

Caspase-mediated cleavage is not required for the activity of presenilins in amyloidogenesis and NOTCH signaling.

Brockhaus M, Grünberg J, Röhrig S, Loetscher H, Wittenburg N, Baumeister R, Jacobsen H, Haass C.

Neuroreport. 1998 May 11;9(7):1481-6.

PMID:
9631452
13.

Calsenilin is a substrate for caspase-3 that preferentially interacts with the familial Alzheimer's disease-associated C-terminal fragment of presenilin 2.

Choi EK, Zaidi NF, Miller JS, Crowley AC, Merriam DE, Lilliehook C, Buxbaum JD, Wasco W.

J Biol Chem. 2001 Jun 1;276(22):19197-204. Epub 2001 Mar 9.

14.

Different effects of Alzheimer-associated mutations of presenilin 1 on its processing.

Murayama O, Honda T, Mercken M, Murayama M, Yasutake K, Nihonmatsu N, Nakazato Y, Michel G, Song S, Sato K, Takahashi H, Takashima A.

Neurosci Lett. 1997 Jun 20;229(1):61-4.

PMID:
9224802
15.

The influence of endoproteolytic processing of familial Alzheimer's disease presenilin 2 on abeta42 amyloid peptide formation.

Jacobsen H, Reinhardt D, Brockhaus M, Bur D, Kocyba C, Kurt H, Grim MG, Baumeister R, Loetscher H.

J Biol Chem. 1999 Dec 3;274(49):35233-9.

16.

Amyloidogenic function of the Alzheimer's disease-associated presenilin 1 in the absence of endoproteolysis.

Steiner H, Romig H, Pesold B, Philipp U, Baader M, Citron M, Loetscher H, Jacobsen H, Haass C.

Biochemistry. 1999 Nov 2;38(44):14600-5.

PMID:
10545183
18.

Alternative cleavage of Alzheimer-associated presenilins during apoptosis by a caspase-3 family protease.

Kim TW, Pettingell WH, Jung YK, Kovacs DM, Tanzi RE.

Science. 1997 Jul 18;277(5324):373-6.

19.

Alzheimer's disease associated presenilin 1 interacts with HC5 and ZETA, subunits of the catalytic 20S proteasome.

Van Gassen G, De Jonghe C, Pype S, Van Criekinge W, Julliams A, Vanderhoeven I, Woodrow S, Beyaert R, Huylebroeck D, Van Broeckhoven C.

Neurobiol Dis. 1999 Oct;6(5):376-91.

PMID:
10527805
20.

The Alzheimer's disease-associated presenilins are differentially phosphorylated proteins located predominantly within the endoplasmic reticulum.

Walter J, Capell A, Grünberg J, Pesold B, Schindzielorz A, Prior R, Podlisny MB, Fraser P, Hyslop PS, Selkoe DJ, Haass C.

Mol Med. 1996 Nov;2(6):673-91.

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