<HashMap><database>biostudies-literature</database><scores/><additional><submitter>Taylor HA</submitter><funding>British Heart Foundation</funding><funding>Biotechnology and Biological Sciences Research Council</funding><pagination>4568</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC9103286</full_dataset_link><repository>biostudies-literature</repository><omics_type>Unknown</omics_type><volume>23(9)</volume><pubmed_abstract>The β-site Amyloid precursor protein Cleaving Enzyme 1 (BACE1) is an extensively studied therapeutic target for Alzheimer's disease (AD), owing to its role in the production of neurotoxic amyloid beta (Aβ) peptides. However, despite numerous BACE1 inhibitors entering clinical trials, none have successfully improved AD pathogenesis, despite effectively lowering Aβ concentrations. This can, in part, be attributed to an incomplete understanding of BACE1, including its physiological functions and substrate specificity. We propose that BACE1 has additional important physiological functions, mediated through substrates still to be identified. Thus, to address this, we computationally analysed a list of 533 BACE1 dependent proteins, identified from the literature, for potential BACE1 substrates, </pubmed_abstract><journal>International journal of molecular sciences</journal><pubmed_title>PTPRD and DCC Are Novel BACE1 Substrates Differentially Expressed in Alzheimer's Disease: A Data Mining and Bioinformatics Study.</pubmed_title><pmcid>PMC9103286</pmcid><funding_grant_id>BB/V014358/1</funding_grant_id><funding_grant_id>FS/4yPhD/F/20/34130A</funding_grant_id><funding_grant_id>FS/4yPhD/F/20/34130</funding_grant_id><funding_grant_id>FS/4yPhD/F/20/34130C</funding_grant_id><funding_grant_id>FS/18/38/33659</funding_grant_id><pubmed_authors>Brown JM</pubmed_authors><pubmed_authors>Watt NT</pubmed_authors><pubmed_authors>Matthews LC</pubmed_authors><pubmed_authors>Taylor HA</pubmed_authors><pubmed_authors>Simmons KJ</pubmed_authors><pubmed_authors>Clavane EM</pubmed_authors><pubmed_authors>Trevelyan CJ</pubmed_authors><pubmed_authors>Meakin PJ</pubmed_authors><pubmed_authors>Przemylska L</pubmed_authors></additional><is_claimable>false</is_claimable><name>PTPRD and DCC Are Novel BACE1 Substrates Differentially Expressed in Alzheimer's Disease: A Data Mining and Bioinformatics Study.</name><description>The β-site Amyloid precursor protein Cleaving Enzyme 1 (BACE1) is an extensively studied therapeutic target for Alzheimer's disease (AD), owing to its role in the production of neurotoxic amyloid beta (Aβ) peptides. However, despite numerous BACE1 inhibitors entering clinical trials, none have successfully improved AD pathogenesis, despite effectively lowering Aβ concentrations. This can, in part, be attributed to an incomplete understanding of BACE1, including its physiological functions and substrate specificity. We propose that BACE1 has additional important physiological functions, mediated through substrates still to be identified. Thus, to address this, we computationally analysed a list of 533 BACE1 dependent proteins, identified from the literature, for potential BACE1 substrates, </description><dates><release>2022-01-01T00:00:00Z</release><publication>2022 Apr</publication><modification>2025-05-18T12:04:33.555Z</modification><creation>2025-04-05T20:38:52.51Z</creation></dates><accession>S-EPMC9103286</accession><cross_references><pubmed>35562959</pubmed><doi>10.3390/ijms23094568</doi></cross_references></HashMap>