Results 231 to 240 of about 36,206 (272)

Successive cleavage of β-amyloid precursor protein by γ-secretase

Seminars in Cell & Developmental Biology, 2020
γ-Secretase is a multimeric aspartyl protease that cleaves the membrane-spanning region of the β-carboxyl terminal fragment (βCTF) generated from β-amyloid precursor protein. γ-Secretase defines the generated molecular species of amyloid β-protein (Aβ), a critical molecule in the pathogenesis of Alzheimer's disease (AD).
Satoru, Funamoto, Shinji, Tagami, Masayasu, Okochi, Maho, Morishima-Kawashima   +3 more
openaire   +4 more sources

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   +4 more sources

ADAMs family members as amyloid precursor protein α‐secretases

Journal of Neuroscience Research, 2003
AbstractIn the non‐amyloidogenic pathway, the Alzheimer's amyloid precursor protein (APP) is cleaved within the amyloid‐β domain by α‐secretase precluding deposition of intact amyloid‐β peptide. The large ectodomain released from the cell surface by the action of α‐secretase has several neuroprotective properties.
Allinson, Tobias M. J., Parkin, Edward T., Turner, Anthony J., Hooper, Nigel M.   +3 more
openaire   +2 more sources

Iron Levels Modulate α‐Secretase Cleavage of Amyloid Precursor Protein

Journal of Neurochemistry, 1995
Abstract: The amyloid precursor protein (APP) is a membrane‐spanning glycoprotein that is the source of βA4 peptides, which aggregate in Alzheimer's disease to form senile plaques. APP is cleaved within the βA4 sequence to release a soluble N‐terminal derivative (APPsol), which has a wide range of trophic and protective functions.
S, Bodovitz, M T, Falduto, D E, Frail, W L, Klein   +3 more
openaire   +2 more sources

β-Secretase Processing of the Alzheimer's Amyloid Protein Precursor (APP)

Journal of Molecular Neuroscience, 2003
An integral membrane aspartyl protease, BACE, is responsible for beta-secretase processing of the beta-amyloid precursor protein (APP) to the large secreted sAPPbeta and membrane-bound CTFbeta of 99 residues. CTFbeta is subsequently cleaved within the membrane by gamma-secretase to the amyloid beta protein (Abeta) that is deposited in the Alzheimer's ...
Laura, Marlow, Melissa, Cain, Miguel A, Pappolla, Kumar, Sambamurti   +3 more
openaire   +2 more sources

Soluble amyloid precursor proteins and secretases as Alzheimer's disease biomarkers

Trends in Molecular Medicine, 2014
Recently revised diagnostic guidelines for Alzheimer's disease (AD) emphasise the use of biomarkers, heralding a paradigm shift towards a more biological definition of the disorder. Currently available biomarkers offer added diagnostic accuracy in certain situations, but their performance in terms of early diagnostic sensitivity and specificity does ...
Robert, Perneczky, Panagiotis, Alexopoulos, Alexander, Kurz   +2 more
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Targeting amyloid precursor protein secretases: Alzheimer's disease and beyond

Drug News & Perspectives, 2010
This review evaluates past and present clinical trials, as well as the current preclinical drug candidates focused on treating Alzheimer's disease (AD), in order to better assess the trends in AD drug discovery in context with specific drug mechanisms.
openaire   +2 more sources

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