Results 171 to 180 of about 26,623 (217)

Blood-based proteomic signatures of spontaneous menopause: Implications for later-life brain aging and Alzheimer’s disease risk

Casaletto K, Alexander MW, Rabin J, Canuca M, Iadipaolo A, Cornelis L, Miolane N, Pham A, Borger J, Diaz V, Paolillo E, Kramer J, Pritschet L, Taylor C, Panizzon M, Reyes RR, Denkinger M, Ashton N, Johnson S, Jacobs E, Saloner R.   +20 more
europepmc   +1 more source

The β-Secretase BACE1 in Alzheimer’s Disease [PDF]

Biological Psychiatry, 2021
BACE1 (beta-site amyloid precursor protein cleaving enzyme 1) was initially cloned and characterized in 1999. It is required for the generation of all monomeric forms of amyloid-β (Aβ), including Aβ42, which aggregates into bioactive conformational species and likely initiates toxicity in Alzheimer's disease (AD).
Harald Hampel, Robert Vassar, Bart De Strooper   +2 more
exaly   +8 more sources

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The BACE1 inhibitor LY2886721 improves diabetic phenotypes of BACE1 knock-in mice

Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease, 2021
The β-site amyloid precursor protein (APP) cleaving enzyme 1 (BACE1) has been identified as the central initiator of amyloid β (Aβ) generation in the brain, the key hallmark of Alzheimer's disease (AD). However, recent studies provided evidence that BACE1 also plays a crucial role in metabolic regulation, and we have shown that neuronal human BACE1 ...
Dekeryte, Ruta, Franklin, Zara, Hull, Claire, Croce, Lorenzo, Kamli-Salino, Sarah, Helk, Oliver Walter, Hoffmann, Philip, Yang, Zhixiang, Riedel, Gernot, Delibegovic, Mirela, Platt, Bettina   +10 more
openaire   +3 more sources

BACE1-AS prevents BACE1 mRNA degradation through the sequestration of BACE1-targeting miRNAs

Journal of Chemical Neuroanatomy, 2019
Abnormal long noncoding RNAs (lncRNAs) and microRNAs (miRNAs) participate in the pathophysiology of Alzheimer's disease (AD). However, it remains unclear whether these two types of noncoding RNAs functionally interact and which factors mediate these interactions in AD.
Tao, Zeng, Haitao, Ni, Yue, Yu, Mingke, Zhang, Minjuan, Wu, Qiaoling, Wang, Liujun, Wang, Sha, Xu, Zhenyu, Xu, Chen, Xu, Jun, Xiong, Junfeng, Jiang, Yan, Luo, Yue, Wang, Houqi, Liu   +14 more
openaire   +2 more sources

BACE1 in Alzheimer's disease

Clinica Chimica Acta, 2012
Targeting BACE1 (β-site APP cleaving enzyme 1 or β-secretase) is the focus of Alzheimer's disease (AD) research because this aspartyl protease is involved in the abnormal production of β amyloid plaques (Aβ), the hallmark of its pathophysiology. Evidence suggests that there is a strong connection between AD and BACE1.
M, Sathya, P, Premkumar, C, Karthick, P, Moorthi, K S, Jayachandran, M, Anusuyadevi   +5 more
openaire   +2 more sources

BACE1 interacts with nicastrin

Biochemical and Biophysical Research Communications, 2002
Beta-amyloid peptide (Abeta) is generated through the proteolytic cleavage of beta-amyloid precursor protein (APP) by beta- and gamma-secretases. The beta-secretase, BACE1, initiates Abeta formation followed by gamma-cleavage within the APP transmembrane domain.
Chinatsu, Hattori, Masashi, Asai, Yoko, Oma, Yoshihiro, Kino, Noboru, Sasagawa, Takaomi C, Saido, Kei, Maruyama, Shoichi, Ishiura   +7 more
openaire   +2 more sources

BACE1 Dependent Neuregulin Processing: Review

Current Alzheimer Research, 2012
Neuregulin-1 (NRG1), known also as heregulin, acetylcholine receptor inducing activity (ARIA), glial growth factor (GGF), or sensory and motor neuron derived factor (SMDF), plays essential roles in several developmental processes, and is required also later in life.
Fleck, Daniel, Garratt, Alistair N, Haass, Christian, Willem, Michael   +3 more
openaire   +3 more sources

Licoflavonol Reduces Aβ Secretion by Increasing BACE1 Phosphorylation to Facilitate BACE1 Degradation

Molecular Nutrition & Food Research, 2019
ScopeIn the previous study, Glycyrrhiza uralensis Fisch extract (GUE) inhibited Aβ secretion by inhibiting β‐site APP‐cleaving enzyme 1 (BACE1) transcription, and the active compounds semilicoisoflavone B (SB) and licoflavonol (LF) inhibited Aβ secretion. SB corresponds to the same mechanism as GUE, but LF has a different mechanism.
Ming-Yao, Gu, Yoon Sun, Chun, Ryu Shi, Yong, Hyun Ok, Yang   +3 more
openaire   +2 more sources

Small-sized BACE1 inhibitors

Drugs of the Future, 2006
The determination of the three-dimensional X-ray crystal structure of b-secretase (BACE) complexed with an inhibitor has greatly facilitated the design of BACE inhibitors. Generally, BACE inhibitors can be grouped into two main families: substrate-based inhibitors designed as peptidomimetic inhibitors and nonpeptidomimetic inhibitors.
Zyta, Ziora, Tooru, KImura, Yoshiaki, Kiso   +2 more
openaire   +2 more sources