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Items: 16


Conditional gene expression systems in the transgenic rat brain.

Schönig K, Weber T, Frömmig A, Wendler L, Pesold B, Djandji D, Bujard H, Bartsch D.

BMC Biol. 2012 Sep 3;10:77. doi: 10.1186/1741-7007-10-77.


Quantitative analysis of conditional gene inactivation using rationally designed, tetracycline-controlled miRNAs.

Berger SM, Pesold B, Reber S, Schönig K, Berger AJ, Weidenfeld I, Miao J, Berger MR, Gruss OJ, Bartsch D.

Nucleic Acids Res. 2010 Sep;38(17):e168. doi: 10.1093/nar/gkq616. Epub 2010 Jul 17.


Reconstitution of gamma-secretase activity.

Edbauer D, Winkler E, Regula JT, Pesold B, Steiner H, Haass C.

Nat Cell Biol. 2003 May;5(5):486-8.


Association analysis of HTR6 and HTR2A polymorphisms in sporadic Alzheimer's disease.

Thome J, Retz W, Baader M, Pesold B, Hu M, Cowen M, Durany N, Adler G, Henn FA, Rösler M.

J Neural Transm (Vienna). 2001;108(10):1175-80.


Stress differentially regulates synaptophysin and synaptotagmin expression in hippocampus.

Thome J, Pesold B, Baader M, Hu M, Gewirtz JC, Duman RS, Henn FA.

Biol Psychiatry. 2001 Nov 15;50(10):809-12.


A pathogenic presenilin-1 deletion causes abberrant Abeta 42 production in the absence of congophilic amyloid plaques.

Steiner H, Revesz T, Neumann M, Romig H, Grim MG, Pesold B, Kretzschmar HA, Hardy J, Holton JL, Baumeister R, Houlden H, Haass C.

J Biol Chem. 2001 Mar 9;276(10):7233-9. Epub 2000 Nov 17.


Glycine 384 is required for presenilin-1 function and is conserved in bacterial polytopic aspartyl proteases.

Steiner H, Kostka M, Romig H, Basset G, Pesold B, Hardy J, Capell A, Meyn L, Grim ML, Baumeister R, Fechteler K, Haass C.

Nat Cell Biol. 2000 Nov;2(11):848-51.


Promoter polymorphism of the 5-HT transporter and Alzheimer's disease.

Hu M, Retz W, Baader M, Pesold B, Adler G, Henn FA, Rösler M, Thome J.

Neurosci Lett. 2000 Nov 10;294(1):63-5.


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.


A loss of function mutation of presenilin-2 interferes with amyloid beta-peptide production and notch signaling.

Steiner H, Duff K, Capell A, Romig H, Grim MG, Lincoln S, Hardy J, Yu X, Picciano M, Fechteler K, Citron M, Kopan R, Pesold B, Keck S, Baader M, Tomita T, Iwatsubo T, Baumeister R, Haass C.

J Biol Chem. 1999 Oct 1;274(40):28669-73.


The biological and pathological function of the presenilin-1 Deltaexon 9 mutation is independent of its defect to undergo proteolytic processing.

Steiner H, Romig H, Grim MG, Philipp U, Pesold B, Citron M, Baumeister R, Haass C.

J Biol Chem. 1999 Mar 19;274(12):7615-8.


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.


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.


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.


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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