Grünberg J - Search Results

1

Truncated presenilin 2 derived from differentially spliced mRNA does not affect the ratio of amyloid beta-peptide 1-42/1-40.

Grünberg J, Walter J, Eckman C, Capell A, Schindzielorz A, Younkin S, Mehta N, Hardy J, Haass C. Grünberg J, et al. Neuroreport. 1998 Oct 5;9(14):3293-9. doi: 10.1097/00001756-199810050-00027. Neuroreport. 1998. PMID: 9831466

2

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. Grunberg J, et al. Biochemistry. 1998 Feb 24;37(8):2263-70. doi: 10.1021/bi972106l. Biochemistry. 1998. PMID: 9485372

3

Proteolytic fragments of the Alzheimer's disease associated presenilins-1 and -2 are phosphorylated in vivo by distinct cellular mechanisms.

Walter J, Grünberg J, Schindzielorz A, Haass C. Walter J, et al. Among authors: grunberg j. Biochemistry. 1998 Apr 28;37(17):5961-7. doi: 10.1021/bi971763a. Biochemistry. 1998. PMID: 9558331

4

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. Haass C, et al. Among authors: grunberg j. J Neural Transm Suppl. 1998;53:159-67. doi: 10.1007/978-3-7091-6467-9_14. J Neural Transm Suppl. 1998. PMID: 9700654 Review.

5

Phosphorylation of presenilin-2 regulates its cleavage by caspases and retards progression of apoptosis.

Walter J, Schindzielorz A, Grünberg J, Haass C. Walter J, et al. Among authors: grunberg j. Proc Natl Acad Sci U S A. 1999 Feb 16;96(4):1391-6. doi: 10.1073/pnas.96.4.1391. Proc Natl Acad Sci U S A. 1999. PMID: 9990034 Free PMC article.

6

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. Leimer U, et al. Among authors: grunberg j. Biochemistry. 1999 Oct 12;38(41):13602-9. doi: 10.1021/bi991453n. Biochemistry. 1999. PMID: 10521267

7

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. Walter J, et al. Among authors: grunberg j. Mol Med. 1996 Nov;2(6):673-91. Mol Med. 1996. PMID: 8972483 Free PMC article.

8

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. Walter J, et al. Among authors: grunberg j. Proc Natl Acad Sci U S A. 1997 May 13;94(10):5349-54. doi: 10.1073/pnas.94.10.5349. Proc Natl Acad Sci U S A. 1997. PMID: 9144240 Free PMC article.

9

Cellular expression and proteolytic processing of presenilin proteins is developmentally regulated during neuronal differentiation.

Capell A, Saffrich R, Olivo JC, Meyn L, Walter J, Grünberg J, Mathews P, Nixon R, Dotti C, Haass C. Capell A, et al. Among authors: grunberg j. J Neurochem. 1997 Dec;69(6):2432-40. doi: 10.1046/j.1471-4159.1997.69062432.x. J Neurochem. 1997. PMID: 9375676 Free article.

10

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. Capell A, et al. Among authors: grunberg j. J Biol Chem. 1998 Feb 6;273(6):3205-11. doi: 10.1074/jbc.273.6.3205. J Biol Chem. 1998. PMID: 9452432 Free article.

This could explain the surprising finding that the Deltaexon 9 mutation is functionally active, although it cannot be proteolytically processed (Baumeister, R., Leimer, U., Zweckbronner, I., Jakubek, C., Grunberg, J., and Haass, C. (1997) Genes & Function 1, 149 …

This could explain the surprising finding that the Deltaexon 9 mutation is functionally active, although it cannot be proteolytically proces …

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