Results 231 to 240 of about 14,023 (271)

Analysis of Amyloid Precursor Protein Processing Protease β‐Secretase: Tools for Memapsin 2 (β‐Secretase) Inhibition Studies

ChemInform, 2004
AbstractFor Abstract see ChemInform Abstract in Full Text.
Gerald Koelsch, Dongwoo Shin, Vajira Weerasena, Jordan Tang, Arun Ghosh   +4 more
openaire   +1 more source

“Secretase,” Alzheimer amyloid protein precursor secreting enzyme is not sequence-specific

Biochemical and Biophysical Research Communications, 1991
The major pathological change in Alzheimer's disease is the deposition of amyloid beta/A4-protein (beta P) in the brain. beta P is derived from a small part of the much larger amyloid protein precursor (APP). In the normal condition, APP is cleaved in the interior of beta P, preventing the formation of beta P, by a hypothetical proteinase "secretase ...
K, Maruyama, F, Kametani, M, Usami, W, Yamao-Harigaya, K, Tanaka   +4 more
openaire   +2 more sources

Heparin promotes ß-secretase cleavage of the Alzheimer's amyloid precursor protein

Neurochemistry International, 1997
In Alzheimer's disease, abnormal processing of the amyloid precursor protein (APP) is thought to play an important role in amyloid deposition. We investigated the effect of heparin, a highly sulfated glycosaminoglycan related to heparan sulfate, on the secretion of the beta-secretase cleavage product of APP (sAPP beta) in a human neuroblastoma cell ...
B, Leveugle, W, Ding, J T, Durkin, S, Mistretta, J, Eisle, M, Matic, R, Siman, B D, Greenberg, H M, Fillit   +8 more
openaire   +2 more sources

γ‐Secretase‐dependent cleavage of amyloid precursor protein regulates osteoblast behavior

The FASEB Journal, 2009
ABSTRACT γ‐Secretase cleaves amyloid precursor protein (APP) to generate amyloid‐β (Aβ) peptides, which aggregate in the brain in Alzheimer's disease (AD). γ‐Secretase also cleaves molecules that regulate osteoblast activity, such as Notch and ephrinB2. However, the role of APP in bone is unknown.
Curtis, Neil, Fagan, Michael J., McLeod, Jane, Lewis, Huw D., Good, Mark A., Genever, Paul G.   +5 more
openaire   +3 more sources

Role of Amyloid Precursor Protein, Amyloid-β and γ-Secretase in Cholesterol Maintenance

Neurodegenerative Diseases, 2006
Lipids play an important part as risk factors for Alzheimer’s disease. This article summarizes the current understanding of the molecular mechanism by which amyloid-β (Aβ) peptides regulate cholesterol and sphingomyelin metabolism, and how in return cholesterol and sphingomyelin regulate Aβ peptide production.
openaire   +2 more sources

Role of presenilin in γ-secretase cleavage of amyloid precursor protein

Experimental Gerontology, 2000
Cerebral accumulation of the amyloid beta-protein (Abeta) is an early and invariant event in the pathogenesis of Alzheimer's disease (AD). Mutations in the presenilin (PS) 1 and 2 genes that increase production of the highly amyloidogenic Abeta(42) are the most common cause of familial AD.
openaire   +2 more sources

Alzheimer's disease amyloid precursor protein (ApPP): proteolytic processing, secretases and βA4 amyloid production

Amyloid, 1994
The major component of Alzheimer's disease amyloid is the 4 kDa peptide βA4 which is produced from an integral membrane protein (amyloid beta precursor protein, AβPP) by proteolytic processing. Cleavage of the βA4 domain from the precursor protein is part of a complex process which results in the release of AβPP from the membrane.
Genevieve Evin, Konrad Beyreuther, Colin L. Masters   +2 more
openaire   +1 more source

Purification and cloning of amyloid precursor protein β-secretase from human brain

Nature, 1999
Proteolytic processing of the amyloid precursor protein (APP) generates amyloid beta (Abeta) peptide, which is thought to be causal for the pathology and subsequent cognitive decline in Alzheimer's disease. Cleavage by beta-secretase at the amino terminus of the Abeta peptide sequence, between residues 671 and 672 of APP, leads to the generation and ...
S, Sinha, J P, Anderson, R, Barbour, G S, Basi, R, Caccavello, D, Davis, M, Doan, H F, Dovey, N, Frigon, J, Hong, K, Jacobson-Croak, N, Jewett, P, Keim, J, Knops, I, Lieberburg, M, Power, H, Tan, G, Tatsuno, J, Tung, D, Schenk, P, Seubert, S M, Suomensaari, S, Wang, D, Walker, J, Zhao, L, McConlogue, V, John   +26 more
openaire   +2 more sources

Physiological functions of the amyloid precursor protein secretases ADAM10, BACE1, and Presenilin

Experimental Brain Research, 2011
Alzheimer's disease causing mutations in the amyloid precursor protein (APP) or in the Presenilin 1 (PS1) or Presenilin 2 (PS2) genes increase the production of amyloid peptides (Aβ) that precipitate in amyloid plaques. Since amyloid plaques are also a prominent feature of sporadic Alzheimer's disease (AD), abnormal proteolysis of APP and the ...
Johannes, Prox, Andrea, Rittger, Paul, Saftig   +2 more
openaire   +2 more sources

ASP1 (BACE2) Cleaves the Amyloid Precursor Protein at the β-Secretase Site

Molecular and Cellular Neuroscience, 2000
Sequential proteolytic processing of the Amyloid Precursor Protein (APP) by beta- and gamma-secretases generates the 4-kDa amyloid (A beta) peptide, a key component of the amyloid plaques seen in Alzheimer's disease (AD). We and others have recently reported the identification and characterisation of an aspartic proteinase, Asp2 (BACE), as beta ...
I, Hussain, D J, Powell, D R, Howlett, G A, Chapman, L, Gilmour, P R, Murdock, D G, Tew, T D, Meek, C, Chapman, K, Schneider, S J, Ratcliffe, D, Tattersall, T T, Testa, C, Southan, D M, Ryan, D L, Simmons, F S, Walsh, C, Dingwall, G, Christie   +18 more
openaire   +2 more sources