Seizure protein 6 and its homolog seizure 6-like protein are physiological substrates of BACE1 in neurons

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Control of Peripheral Nerve Myelination by the ß-Secretase BACE1

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Bace1 modulates myelination in the central and peripheral nervous system

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BACE1 Deficiency Rescues Memory Deficits and Cholinergic Dysfunction in a Mouse Model of Alzheimer's Disease

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BACE1, a Major Determinant of Selective Vulnerability of the Brain to Amyloid-β Amyloidogenesis, is Essential for Cognitive, Emotional, and Synaptic Functions

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The Secreted β-Amyloid Precursor Protein Ectodomain APPsα Is Sufficient to Rescue the Anatomical, Behavioral, and Electrophysiological Abnormalities of APP-Deficient Mice

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Robust Central Reduction of Amyloid-β in Humans with an Orally Available, Non-Peptidic β-Secretase Inhibitor

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The Disintegrin/Metalloproteinase ADAM10 Is Essential for the Establishment of the Brain Cortex

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Phenotypic and Biochemical Analyses of BACE1- and BACE2-deficient Mice

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Function, therapeutic potential and cell biology of BACE proteases: current status and future prospects

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Secretome protein enrichment identifies physiological BACE1 protease substrates in neurons

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Temporal memory deficits in Alzheimer’s mouse models: Rescue by genetic deletion of BACE1

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Alteration of BACE1-dependent NRG1/ErbB4 signaling and schizophrenia-like phenotypes in <i>BACE1</i> -null mice

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Structure-Based Design of Potent and Selective Cell-Permeable Inhibitors of Human β-Secretase (BACE-1)

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A Technique for Serial Collection of Cerebrospinal Fluid from the Cisterna Magna in Mouse

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The Cell Adhesion Protein P-selectin Glycoprotein Ligand-1 Is a Substrate for the Aspartyl Protease BACE1

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Substrate and Inhibitor Profile of BACE (β-Secretase) and Comparison with Other Mammalian Aspartic Proteases

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Regulated intramembrane proteolysis - lessons from amyloid precursor protein processing

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Systematic substrate identification indicates a central role for the metalloprotease ADAM10 in axon targeting and synapse function

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The Neural Cell Adhesion Molecules L1 and CHL1 Are Cleaved by BACE1 Protease in Vivo*

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Proteomic Profiling of γ-Secretase Substrates and Mapping of Substrate Requirements

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BACE1 Physiological Functions May Limit Its Use as Therapeutic Target for Alzheimer's Disease.

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Sez-6 Proteins Affect Dendritic Arborization Patterns and Excitability of Cortical Pyramidal Neurons

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β-Site Amyloid Precursor Protein (APP)-cleaving Enzyme 1 (BACE1)-deficient Mice Exhibit a Close Homolog of L1 (CHL1) Loss-of-function Phenotype Involving Axon Guidance Defects

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Bace1 and Neuregulin‐1 cooperate to control formation and maintenance of muscle spindles

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Dual Cleavage of Neuregulin 1 Type III by BACE1 and ADAM17 Liberates Its EGF-Like Domain and Allows Paracrine Signaling

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LC–MS/MS Characterization of O-Glycosylation Sites and Glycan Structures of Human Cerebrospinal Fluid Glycoproteins

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Soluble amyloid precursor protein (APP) regulates transthyretin and Klotho gene expression without rescuing the essential function of APP

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Discovery of AZD3839, a Potent and Selective BACE1 Inhibitor Clinical Candidate for the Treatment of Alzheimer Disease*

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BACE1 gene deletion: Impact on behavioral function in a model of Alzheimer’s disease

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Systematic Proteomic Analysis Identifies β-Site Amyloid Precursor Protein Cleaving Enzyme 2 and 1 (BACE2 and BACE1) Substrates in Pancreatic β-Cells*

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Utilizing Structures of CYP2D6 and BACE1 Complexes To Reduce Risk of Drug–Drug Interactions with a Novel Series of Centrally Efficacious BACE1 Inhibitors

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Label-free Quantitative Proteomics of Mouse Cerebrospinal Fluid Detects β-Site APP Cleaving Enzyme (BACE1) Protease Substrates In Vivo

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Disturbance of cerebellar synaptic maturation in mutant mice lacking BSRPs, a novel brain‐specific receptor‐like protein family

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Constitutive α- and β-secretase cleavages of the amyloid precursor protein are partially coupled in neurons, but not in frequently used cell lines

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Antagonistic Effects of BACE1 and APH1B-γ-Secretase Control Axonal Guidance by Regulating Growth Cone Collapse

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Unsaturated Fatty Acids Drive Disintegrin and Metalloproteinase (ADAM)-dependent Cell Adhesion, Proliferation, and Migration by Modulating Membrane Fluidity

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Bepridil and Amiodarone Simultaneously Target the Alzheimer's Disease - and -Secretase via Distinct Mechanisms

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Febrile seizures are associated with mutation of seizure‐related (SEZ) 6, a brain‐specific gene

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BACE1 activity regulates cell surface contactin-2 levels

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Di-substituted pyridinyl aminohydantoins as potent and highly selective human β-secretase (BACE1) inhibitors

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Cloning and expression of SEZ-6, a brain-specific and seizure-related cDNA

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QARIP: a web server for quantitative proteomic analysis of regulated intramembrane proteolysis

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Polymorphisms in seizure 6-like gene are associated with bipolar disorder I: Evidence of gene×gender interaction

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The Role of Seizure-RelatedSEZ6as a Susceptibility Gene in Febrile Seizures

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Improvement of a sample preparation method assisted by sodium deoxycholate for mass‐spectrometry‐based shotgun membrane proteomics†

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Enhanced SDC-assisted digestion coupled with lipid chromatography-tandem mass spectrometry for shotgun analysis of membrane proteome

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The β-Secretase BACE1 in Alzheimer’s Disease

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The physiological roles of tau and Aβ: implications for Alzheimer’s disease pathology and therapeutics

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Proteolytic ectodomain shedding of membrane proteins in mammals—hardware, concepts, and recent developments

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The substrate repertoire of γ-secretase/presenilin

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The case for low-level BACE1 inhibition for the prevention of Alzheimer disease

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The role of membrane trafficking in the processing of amyloid precursor protein and production of amyloid peptides in Alzheimer's disease

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BACE1 Function and Inhibition: Implications of Intervention in the Amyloid Pathway of Alzheimer’s Disease Pathology

Koelsch, G. (2017) · Molecules · doi:10.3390/molecules22101723 · Cited by 125 · see citing works

Role of BACE1 in Alzheimer’s synaptic function

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Findings of Efficacy, Safety, and Biomarker Outcomes of Atabecestat in Preclinical Alzheimer Disease

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Beta-Site Amyloid Precursor Protein Cleaving Enzyme 1 Inhibition Impairs Synaptic Plasticity via Seizure Protein 6

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Physiological Functions of the β-Site Amyloid Precursor Protein Cleaving Enzyme 1 and 2

Yan, R. (2017) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2017.00097 · Cited by 105 · see citing works

BACE1: More than just a β‐secretase

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An optimized quantitative proteomics method establishes the cell type‐resolved mouse brain secretome

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Inhibition of PKCδ reduces amyloid-β levels and reverses Alzheimer disease phenotypes

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BACE2 distribution in major brain cell types and identification of novel substrates

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Modulation of γ- and β-secretases as early prevention against Alzheimer's disease

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Not all roads lead to the immune system: the genetic basis of multiple sclerosis severity

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Discovery of seven novel putative antigens in membranous nephropathy and membranous lupus nephritis identified by mass spectrometry

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The Metabolic Syndrome, Inflammation, and Colorectal Cancer Risk: An Evaluation of Large Panels of Plasma Protein Markers Using Repeated, Prediagnostic Samples

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Lack of Sez6 Family Proteins Impairs Motor Functions, Short-Term Memory, and Cognitive Flexibility and Alters Dendritic Spine Properties

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Consequences of Pharmacological BACE Inhibition on Synaptic Structure and Function

Zhu, K., Peters, F., Filser, S., & Herms, J. W. (2018) · Biological Psychiatry · doi:10.1016/j.biopsych.2018.04.022 · Cited by 50 · see citing works

The Alzheimer’s disease-linked protease BACE1 modulates neuronal IL-6 signaling through shedding of the receptor gp130

Müller, S. A., Shmueli, M. D., Feng, X. M., Tüshaus, J., Schumacher, N., Clark, R., Smith, B. E., Chi, A., Rose‐John, S., Kennedy, M. E., et al. (2023) · Molecular Neurodegeneration · doi:10.1186/s13024-023-00596-6 · Cited by 49 · see citing works

NrCAM is a marker for substrate‐selective activation of ADAM10 in Alzheimer's disease

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The neurobiology and therapeutic potential of multi-targeting β-secretase, glycogen synthase kinase 3β and acetylcholinesterase in Alzheimer’s disease

Fronza, M. G., Alves, D. A. C., Praticò, D., & Savegnago, L. (2023) · Ageing Research Reviews · doi:10.1016/j.arr.2023.102033 · Cited by 47 · see citing works

Shed CNTNAP2 ectodomain is detectable in CSF and regulates Ca2+ homeostasis and network synchrony via PMCA2/ATP2B2

Martin‐de‐Saavedra, M. D., Santos, M. D., Culotta, L., Varea, O., Spielman, B. P., Parnell, E., Forrest, M. P., Gao, R., Yoon, S., McCoig, E., et al. (2021) · Neuron · doi:10.1016/j.neuron.2021.11.025 · Cited by 46 · see citing works

AAV‐mediated delivery of an anti‐BACE1 VHH alleviates pathology in an Alzheimer's disease model

Marino, M., Zhou, L., Rincón, M. Y., Callaerts‐Vegh, Z., Verhaert, J., Wahis, J., Creemers, E., Yshii, L., Wierda, K. D. B., Saito, T., et al. (2022) · EMBO Molecular Medicine · doi:10.15252/emmm.201809824 · Cited by 45 · see citing works

A microglial activity state biomarker panel differentiates FTD-granulin and Alzheimer’s disease patients from controls

Pesämaa, I., Müller, S. A., Robinson, S., Darcher, A., Paquet, D., Zetterberg, H., Lichtenthaler, S. F., & Haass, C. (2023) · Molecular Neurodegeneration · doi:10.1186/s13024-023-00657-w · Cited by 42 · see citing works

Toxic amyloid-β oligomers induced self-replication in astrocytes triggering neuronal injury

Wang, W., Hou, T., Jia, L.-F., Wu, Q., Quan, M., & Jia, J. (2019) · EBioMedicine · doi:10.1016/j.ebiom.2019.03.049 · Cited by 42 · see citing works

Guanidine-based β amyloid precursor protein cleavage enzyme 1 (BACE-1) inhibitors for the Alzheimer's disease (AD): A review

Gehlot, P., Kumar, S., Vyas, V. K., Choudhary, B. S., Sharma, M., & Malik, R. (2022) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2022.117047 · Cited by 40 · see citing works

Impact of maternal obesity on placental transcriptome and morphology associated with fetal growth restriction in mice

Mucci, D. D. B., Kusinski, L. C., Wilsmore, P., Loche, E., Pantaleão, L. C., Ashmore, T. J., Blackmore, H. L., Fernandez‐Twinn, D. S., do Carmo, M. D. G. T., & Ozanne, S. E. (2020) · International Journal of Obesity · doi:10.1038/s41366-020-0561-3 · Cited by 40 · see citing works

Seizure protein 6 controls glycosylation and trafficking of kainate receptor subunits GluK2 and GluK3

Pigoni, M., Hsia, H., Hartmann, J., Njavro, J. R., Shmueli, M. D., Müller, S. A., Güner, G., Tüshaus, J., Kuhn, P., Kumar, R., et al. (2020) · The EMBO Journal · doi:10.15252/embj.2019103457 · Cited by 39 · see citing works

The Sez6 Family Inhibits Complement by Facilitating Factor I Cleavage of C3b and Accelerating the Decay of C3 Convertases

Qiu, W., Luo, S., Ma, S. A., Saminathan, P., Li, H., Gunnersen, J. M., Gelbard, H. A., & Hammond, J. W. (2021) · Frontiers in Immunology · doi:10.3389/fimmu.2021.607641 · Cited by 39 · see citing works

Click Chemistry-mediated Biotinylation Reveals a Function for the Protease BACE1 in Modulating the Neuronal Surface Glycoproteome

Herber, J., Njavro, J. R., Feederle, R., Schepers, U., Müller, U., Bräse, S., Müller, S. A., & Lichtenthaler, S. F. (2018) · Molecular & Cellular Proteomics · doi:10.1074/mcp.ra118.000608 · Cited by 37 · see citing works

BACE1 Inhibitor MK-8931 Alters Formation but Not Stability of Dendritic Spines

Blume, T., Filser, S., Jaworska, A. M., Blain, J., Koenig, G., Moschke, K., Lichtenthaler, S. F., & Herms, J. W. (2018) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2018.00229 · Cited by 36 · see citing works

LRRK2 G2019S kinase activity triggers neurotoxic NSF aggregation

Pischedda, F., Cirnaru, M., Ponzoni, L., Sandre, M., Biosa, A., Pérez‐Carrión, M. D., Marin, O., Morari, M., Pan, L., Greggio, E., et al. (2021) · Brain · doi:10.1093/brain/awab073 · Cited by 31 · see citing works

Kainate and AMPA receptors in epilepsy: Cell biology, signalling pathways and possible crosstalk

Henley, J. M., Nair, J. D., Seager, R., Yucel, B. P., Woodhall, G. L., Henley, B. S., Talandyte, K., Needs, H. I., & Wilkinson, K. A. (2021) · Neuropharmacology · doi:10.1016/j.neuropharm.2021.108569 · Cited by 30 · see citing works

Mouse brain proteomics establishes MDGA1 and CACHD1 as in vivo substrates of the Alzheimer protease BACE1

Njavro, J. R., Klotz, J., Dislich, B., Wanngren, J., Shmueli, M. D., Herber, J., Kuhn, P., Kumar, R., Koeglsperger, T., Conrad, M., et al. (2019) · The FASEB Journal · doi:10.1096/fj.201902347r · Cited by 29 · see citing works

Experimental evidence for temporal uncoupling of brain Aβ deposition and neurodegenerative sequelae

Rother, C., Uhlmann, R. E., Müller, S. A., Schelle, J., Skodras, A., Obermüller, U., Häsler, L. M., Lambert, M., Baumann, F., Xu, Y., et al. (2022) · Nature Communications · doi:10.1038/s41467-022-34538-5 · Cited by 28 · see citing works

BACE1 partial deletion induces synaptic plasticity deficit in adult mice

Lombardo, S., Chiacchiaretta, M., Tarr, A. J., Kim, W., Cao, T., Sigal, G., Rosahl, T. W., Xia, W., Haydon, P. G., Kennedy, M. E., et al. (2019) · Scientific Reports · doi:10.1038/s41598-019-56329-7 · Cited by 28 · see citing works

Iron Responsive Element-Mediated Responses to Iron Dyshomeostasis in Alzheimer’s Disease

Hin, N., Newman, M., Pederson, S., & Lardelli, M. (2021) · Journal of Alzheimer s Disease · doi:10.3233/jad-210200 · Cited by 28 · see citing works

Functional SELEX and Biomedical Applications of Aptamers: Beyond Molecular Recognition

He, M., Wang, Z., Wu, X., Du, Z. H., Cui, C., Zhao, Z., Sun, Y., Zhang, X., He, L., & Tan, W. (2025) · Angewandte Chemie International Edition · doi:10.1002/anie.202424687 · Cited by 27 · see citing works

JNJ-67569762, A 2-Aminotetrahydropyridine-Based Selective BACE1 Inhibitor Targeting the S3 Pocket: From Discovery to Clinical Candidate

Rombouts, F. J. R., Kusakabe, K., Alexander, R., Austin, N. E., Borghys, H., Cleyn, M. A. J. D., Dhuyvetter, D., Gijsen, H. J. M., Hrupka, B. J., Jacobs, T., et al. (2021) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.1c00935 · Cited by 26 · see citing works

Intercellular signaling by ectodomain shedding at the synapse

Martin‐de‐Saavedra, M. D., Santos, M. D., & Penzes, P. (2022) · Trends in Neurosciences · doi:10.1016/j.tins.2022.03.004 · Cited by 24 · see citing works

BACE Inhibitor Clinical Trials for Alzheimer’s Disease

Watkins, E. A., & Vassar, R. J. (2024) · Journal of Alzheimer s Disease · doi:10.3233/jad-231258 · Cited by 23 · see citing works

Current Advances in Aptamer-based Biomolecular Recognition and Biological Process Regulation

Chen, S., Zhang, L., Yuan, Q., & Tan, J. (2022) · Chemical Research in Chinese Universities · doi:10.1007/s40242-022-2087-9 · Cited by 23 · see citing works

An Alternative View of Familial Alzheimer’s Disease Genetics

Lardelli, M. T. (2023) · Journal of Alzheimer s Disease · doi:10.3233/jad-230313 · Cited by 23 · see citing works

Electric Stimulation of Neurogenesis Improves Behavioral Recovery After Focal Ischemia in Aged Rats

Bălşeanu, T. A., Grigore, M. M., Pinosanu, L. R., SLEVIN, M. A., Hermann, D. M., Glăvan, D., & Popa‐Wagner, A. (2020) · Frontiers in Neuroscience · doi:10.3389/fnins.2020.00732 · Cited by 22 · see citing works

Spatiotemporal processing of neural cell adhesion molecules 1 and 2 by BACE1 in vivo

Kim, W., Watanabe, H., Lomoio, S., & Tesco, G. (2021) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2021.100372 · Cited by 22 · see citing works

Meprin β knockout reduces brain Aβ levels and rescues learning and memory impairments in the APP/lon mouse model for Alzheimer’s disease

Marengo, L., Armbrust, F., Schoenherr, C., Storck, S. E., Schmitt, U., Zampar, S., Wirths, O., Altmeppen, H. C., Glatzel, M., Kaether, C., et al. (2022) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-022-04205-5 · Cited by 20 · see citing works

Regulation of beta‐amyloid for the treatment of Alzheimer's disease: Research progress of therapeutic strategies and bioactive compounds

Qiu, W., Liu, H., Liu, Y., Lü, X., Wang, L., Hu, Y., Feng, F., Li, Q., & Sun, H. (2023) · Medicinal Research Reviews · doi:10.1002/med.21947 · Cited by 20 · see citing works

Navigating the Maze of Alzheimer’s disease by exploring BACE1: Discovery, current scenario, and future prospects

Iram, F., Shahid, M., Ansari, J., Ashraf, G. M., Hassan, M. I., & Islam, A. (2024) · Ageing Research Reviews · doi:10.1016/j.arr.2024.102342 · Cited by 20 · see citing works

Exome sequencing in an Italian family with Alzheimer’s disease points to a role for seizure-related gene 6 (SEZ6) rare variant R615H

Paracchini, L., Beltrame, L., Boeri, L., Fusco, F., Caffarra, P., Marchini, S., Albani, D., & Forloni, G. (2018) · Alzheimer s Research & Therapy · doi:10.1186/s13195-018-0435-2 · Cited by 20 · see citing works

The Swedish dilemma - the almost exclusive use of APPswe-based mouse models impedes adequate evaluation of alternative β-secretases

Armbrust, F., Bickenbach, K., Marengo, L., Pietrzik, C. U., & Becker‐Pauly, C. (2021) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2021.119164 · Cited by 20 · see citing works

A 6‑gene risk score system constructed for predicting the clinical prognosis of pancreatic adenocarcinoma patients

Liu, Y., Zhu, D., Xing, H., Hou, Y., & Sun, Y. (2019) · Oncology Reports · doi:10.3892/or.2019.6979 · Cited by 19 · see citing works

BACE1-cleavage of Sez6 and Sez6L is elevated in Niemann-Pick type C disease mouse brains

Čaušević, M., Dominko, K., Malnar, M., Vidatic, L., Čermak, S., Pigoni, M., Kuhn, P.-H., Colombo, A., Havas, D., Flunkert, S., et al. (2018) · PLoS ONE · doi:10.1371/journal.pone.0200344 · Cited by 14 · see citing works

Failure, Success, and Future Direction of Alzheimer Drugs Targeting Amyloid‐β Cascade: Pros and Cons of Chemical and Biological Modalities

Kim, J., Jeon, H., Kim, H. Y., & Kim, Y. S. (2023) · ChemBioChem · doi:10.1002/cbic.202300328 · Cited by 16 · see citing works

The Alzheimer’s disease–linked protease BACE2 cleaves VEGFR3 and modulates its signaling

Schmidt, A., Hrupka, B. J., van Bebber, F., Kumar, S. S., Feng, X., Tschirner, S. K., Aßfalg, M., Müller, S. A., Hilger, L. S., Hofmann, L. I., et al. (2024) · Journal of Clinical Investigation · doi:10.1172/jci170550 · Cited by 16 · see citing works

Effects of microRNA-298 on APP and BACE1 translation differ according to cell type and 3′-UTR variation

Wang, R., & Lahiri, D. K. (2022) · Scientific Reports · doi:10.1038/s41598-022-05164-4 · Cited by 16 · see citing works

Beta secretase activity in peripheral nerve regeneration

Farah, M. H., & Tallon, C. (2017) · Neural Regeneration Research · doi:10.4103/1673-5374.217319 · Cited by 16 · see citing works

Beta-Secretase 1 Underlies Reactive Astrocytes and Endothelial Disruption in Neurodegeneration

Chacón-Quintero, M. V., Pineda-López, L. G., Villegas‐Lanau, C. A., Posada‐Duque, R., & Cardona‐Gómez, G. P. (2021) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2021.656832 · Cited by 15 · see citing works

ARL6IP1 mediates small-molecule-induced alleviation of Alzheimer pathology through FXR1-dependent BACE1 translation initiation

Zhou, G., Tang, J., Ma, Y., Fu, X., Liu, J., Yang, R.-Z., Zhang, H., Cai, X., Wang, J., Xie, X., et al. (2023) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2220148120 · Cited by 14 · see citing works

BACE1 Translation: At the Crossroads Between Alzheimer’s Disease Neurodegeneration and Memory Consolidation

Guix, F. X., Sartório, C. L., & ILL‐Raga, G. (2019) · Journal of Alzheimer s Disease Reports · doi:10.3233/adr-180089 · Cited by 13 · see citing works

PTPRD and DCC Are Novel BACE1 Substrates Differentially Expressed in Alzheimer’s Disease: A Data Mining and Bioinformatics Study

Taylor, H. A., Simmons, K. J., Clavane, E. M., Trevelyan, C. J., Brown, J., Przemyłska, L., Watt, N. T., Matthews, L. C., & Meakin, P. J. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23094568 · Cited by 13 · see citing works

New Highly Selective BACE1 Inhibitors and Their Effects on Dendritic Spine Density In Vivo

Pratsch, K., Unemura, C., Ito, M., Lichtenthaler, S. F., Horiguchi, N., & Herms, J. W. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms241512283 · Cited by 13 · see citing works

The β-Secretase Substrate Seizure 6–Like Protein (SEZ6L) Controls Motor Functions in Mice

Ong-Pålsson, E., Njavro, J. R., Wilson, Y. M., Pigoni, M., Schmidt, A., Müller, S. A., Meyer, M., Hartmann, J., Busche, M. A., Gunnersen, J. M., et al. (2021) · Molecular Neurobiology · doi:10.1007/s12035-021-02660-y · Cited by 12 · see citing works

Impaired Retromer Function in Niemann-Pick Type C Disease Is Dependent on Intracellular Cholesterol Accumulation

Dominko, K., Rastija, A., Sobočanec, S., Vidatic, L., Meglaj, S., Babic, A. L., Hutter‐Paier, B., Colombo, A.-V., Lichtenthaler, S. F., Tahirović, S., et al. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms222413256 · Cited by 12 · see citing works

Sez6 levels are elevated in cerebrospinal fluid of patients with inflammatory pain–associated conditions

Roitman, M., Edgington‐Mitchell, L. E., Mangum, J. E., Ziogas, J., Adamides, A. A., Myles, P. S., Choo-Bunnett, H., Bunnett, N. W., & Gunnersen, J. M. (2019) · PAIN Reports · doi:10.1097/pr9.0000000000000719 · Cited by 11 · see citing works

The pseudoprotease iRhom1 controls ectodomain shedding of membrane proteins in the nervous system

Tüshaus, J., Müller, S. A., Shrouder, J. J., Arends, M., Simons, M., Plesnila, N., Blobel, C., & Lichtenthaler, S. F. (2021) · The FASEB Journal · doi:10.1096/fj.202100936r · Cited by 11 · see citing works

Seizure-Related Homolog Protein 6 (SEZ6): Biology and Therapeutic Target in Neuroendocrine Carcinomas

Gezelius, E., Rekhtman, N., Baine, M. K., Rudin, C. M., Drilon, A. E. D. C., & Cooper, A. J. (2025) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-25-2090 · Cited by 10 · see citing works

Pharmacological BACE Inhibition Improves Axonal Regeneration in Nerve Injury and Disease Models

Tallon, C., Marshall, K. L., Kennedy, M. E., Hyde, L. A., & Farah, M. H. (2020) · Neurotherapeutics · doi:10.1007/s13311-020-00852-3 · Cited by 10 · see citing works

Induction of A Disintegrin and Metalloproteinase with Thrombospondin motifs 1 by a rare variant or cognitive activities reduces hippocampal amyloid-β and consequent Alzheimer’s disease risk

Qiu, Y., Sha, L., Zhang, X., Li, G., Zhu, W., & Xu, Q. (2022) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2022.896522 · Cited by 9 · see citing works

BACE inhibitor treatment of mice induces hyperactivity in a Seizure-related gene 6 family dependent manner without altering learning and memory

Nash, A., Gijsen, H. J. M., Hrupka, B. J., Teng, K. S.-L., Lichtenthaler, S. F., Takeshima, H., Gunnersen, J. M., & Munro, K. M. (2021) · Scientific Reports · doi:10.1038/s41598-021-94369-0 · Cited by 9 · see citing works

Prognostic significance of AP-2α/γ targets as cancer therapeutics

Kołat, D., Kałuzińska‐Kołat, Ż., Bednarek, A. K., & Płuciennik, E. (2022) · Scientific Reports · doi:10.1038/s41598-022-09494-1 · Cited by 9 · see citing works

β-secretase inhibition prevents structural spine plasticity deficits in AppNL-G-F mice

Blume, T., Filser, S., Sgobio, C., Peters, F., Neumann, U., Shimshek, D. R., Saito, T., Saido, T. C., Brendel, M., & Herms, J. W. (2022) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2022.909586 · Cited by 9 · see citing works

The emerging role of kainate receptor functional dysregulation in pain

Li, H., Li, J., Guan, Y., & Wang, Y. (2021) · Molecular Pain · doi:10.1177/1744806921990944 · Cited by 8 · see citing works

Therapeutic Potential of Targeting Regulated Intramembrane Proteolysis Mechanisms of Voltage-Gated Ion Channel Subunits and Cell Adhesion Molecules

Hodges, S. L., Bouza, A. A., & Isom, L. L. (2022) · Pharmacological Reviews · doi:10.1124/pharmrev.121.000340 · Cited by 7 · see citing works

Adenosine triphosphate Binding Cassette subfamily C member 1 (ABCC1) overexpression reduces APP processing and increases alpha- versus beta-secretase activity, in vitro

Jepsen, W. M., Both, M. D. D., Siniard, A. L., Ramsey, K. M., Piras, I. S., Naymik, M., Henderson-Smith, A., & Huentelman, M. J. (2020) · Biology Open · doi:10.1242/bio.054627 · Cited by 7 · see citing works

Endoglycan (PODXL2) is proteolytically processed by ADAM10 (a disintegrin and metalloprotease 10) and controls neurite branching in primary neurons

Hsia, H., Tüshaus, J., Feng, X. M., Hofmann, L. I., Wefers, B., Marciano, D. K., Wurst, W., & Lichtenthaler, S. F. (2021) · The FASEB Journal · doi:10.1096/fj.202100475r · Cited by 7 · see citing works

AAV mediated delivery of a novel anti-BACE1 VHH reduces Abeta in an Alzheimer’s disease mouse modelPreprint

Rincón, M. Y., Zhou, L., Marneffe, C., Voytyuk, I., Wouters, Y., Dewilde, M., Duqué, S. I., Vincke, C., Levites, Y., Golde, T. E., et al. (2019) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/698506 · Cited by 7 · see citing works

A novel mouse model for N-terminal truncated Aβ2-x generation through meprin β overexpression in astrocytes

Armbrust, F., Bickenbach, K., Altmeppen, H. C., Foggetti, A., Winkelmann, A., Wulff, P., Glatzel, M., Pietrzik, C. U., & Becker‐Pauly, C. (2024) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-024-05139-w · Cited by 6 · see citing works

Biological Mechanism-based Neurology and Psychiatry: A BACE1/2 and Downstream Pathway Model

Hampel, H. J., Lista, S., Caruso, G., Nisticò, R., Piccioni, G., Mercuri, N. B., Giorgi, F. S., Ferrarelli, F., Lemercier, P., Caraci, F., et al. (2021) · Current Neuropharmacology · doi:10.2174/1570159x19666211201095701 · Cited by 6 · see citing works

The BACE1-generated C-terminal fragment of the neural cell adhesion molecule 2 (NCAM2) promotes BACE1 targeting to Rab11-positive endosomes

Keable, R., Hu, S., Pfundstein, G., Kozlova, I., Su, F., Du, X., Yang, H., Gunnersen, J. M., Schachner, M., Leshchyns’ka, I., et al. (2022) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-022-04575-w · Cited by 6 · see citing works

HILAMA: High-dimensional multi-omics mediation analysis with latent confounding

Wang, X., Liu, J., Hu, S. S., Liu, Z., Lu, H. J., Liu, L., & Initiative, T. A. D. N. (2025) · BMC Medical Research Methodology · doi:10.1186/s12874-025-02686-z · Cited by 5 · see citing works

Detection of SEZ6, a Therapeutic Target, in Medullary Thyroid Carcinoma

Xu, B., Baine, M. K., Jungbluth, A. A., Alabkaa, A., Serrette, R., Roy, D., Rudin, C. M., Ho, A. L., Sherman, E. J., Doğan, S., et al. (2024) · The Journal of Clinical Endocrinology & Metabolism · doi:10.1210/clinem/dgae672 · Cited by 5 · see citing works

An Improved Method for Sampling and Quantitative Protein Analytics of Cerebrospinal Fluid of Individual Mice

Lourbopoulos, A. I., Müller, S. A., Jocher, G., Wick, M. W., Plesnila, N., & Lichtenthaler, S. F. (2025) · Molecular & Cellular Proteomics · doi:10.1016/j.mcpro.2025.100958 · Cited by 5 · see citing works

Postnatal neuronalBace1deletion impairs neuroblast and oligodendrocyte maturation

Benoit, M., Darboe, M., Das, B., Ge, Y., Zhou, J., Yao, A. Y., He, W., Yan, R., & Hu, X. (2022) · Human Molecular Genetics · doi:10.1093/hmg/ddac282 · Cited by 5 · see citing works

BACE1 Deficiency Causes Abnormal Neuronal Clustering in the Dentate Gyrus

Hou, H., Fan, Q., He, W., Suh, H., Hu, X., & Yan, R. (2017) · Stem Cell Reports · doi:10.1016/j.stemcr.2017.05.030 · Cited by 5 · see citing works

Seizure-6 proteins highlight BACE1 functions in neurobiology

Pigoni, M., Gunnersen, J. M., & Lichtenthaler, S. F. (2016) · Oncotarget · doi:10.18632/oncotarget.13801 · Cited by 5 · see citing works

The manipulator behind “Scissors”: γ -secretase and its modulators in Alzheimer’s disease

Ning, G., Fan, X., Du, J., wenxue, Z., Sijia, W., Meinei, C., Xiaolong, D., & Yiming, Q. (2025) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2025.1637671 · Cited by 4 · see citing works

BACE1 : Biological Functions and Involvement in the Pathophysiology of Alzheimer's Disease and Other Neurological Disorders

Bartolić, M., & Bosak, A. (2025) · BioFactors · doi:10.1002/biof.70071 · Cited by 4 · see citing works

Associations of CSF BACE1 with amyloid pathology, neurodegeneration, and cognition in Alzheimer’s disease

Gao, F., Zhang, M., Wang, Q., Ni, M., Liu, C., Deng, K., Xie, Q., Wang, S., Shi, J., & Shen, Y. (2024) · Acta Neuropathologica · doi:10.1007/s00401-024-02750-w · Cited by 4 · see citing works

Cytosolic sequestration of spatacsin by Protein Kinase A and 14-3-3 proteins

Cogo, S., Tomkins, J. E., Vavouraki, N., Giusti, V., Forcellato, F., Franchin, C., Tessari, I., Arrigoni, G., Cendron, L., Manzoni, C., et al. (2022) · Neurobiology of Disease · doi:10.1016/j.nbd.2022.105858 · Cited by 4 · see citing works

Functional SELEX and Biomedical Applications of Aptamers: Beyond Molecular Recognition

He, M., Wang, Z., Wu, X., Du, Z. H., Cui, C., Zhao, Z., Sun, Y., Zhang, X., He, L., & Tan, W. (2025) · Angewandte Chemie · doi:10.1002/ange.202424687 · Cited by 3 · see citing works

Proteomic-based evidence for adult neurogenesis in birds and mammals as indicated from cerebrospinal fluid

Voukali, E., & Vinkler, M. (2022) · Neural Regeneration Research · doi:10.4103/1673-5374.329002 · Cited by 3 · see citing works

It’s good to know what to BACE the specificity of your inhibitors on

Murray, A., Muñiz-García, A., Alić, I., & Nižetić, D. (2024) · Journal of Clinical Investigation · doi:10.1172/jci183677 · Cited by 3 · see citing works

Inhibition of striatal SEZ6 by miR-3594-5p is a drug-specific marker for late-stage heroin intake escalationPreprint

Lenoir, M., Bondi, I., Clémenceau, L., Nondier, I., Ballé, M., Jacques, S., Duché, A., Canestrelli, C., Martin‐Lannerée, S., Mouillet‐Richard, S., et al. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.07.26.453355 · Cited by 3 · see citing works

Identification of the enzymatic cleavage relationship between anti-aging protein α-Klotho and Alzheimer's disease biomarker BACE1

Gao, X., Sun, Z., Hu, J. H., Li, Y., Deng, Q., & Li, R. (2025) · Journal of Alzheimer s Disease · doi:10.1177/13872877251317730 · Cited by 2 · see citing works

Neuropathy-associated Tecpr2 mutation knock-in mice reveal endolysosomal loss of function phenotypes in neurons and microglia

Bhattacharya, D., da Silva‐Buttkus, P., Nalbach, K., Cheng, L., Garrett, L., Irmler, M., Kislinger, G., Werner, G., Rodde, R., Lengger, C., et al. (2025) · Cell Death and Disease · doi:10.1038/s41419-025-08168-w · Cited by 2 · see citing works

BACE1 regulates sleep–wake cycle through both enzymatic and non–enzymatic actions

Heininger, H., Feng, X., Altunkaya, A., Zheng, F., Stockinger, F., Wefers, B., Müller, S. A., Giesbertz, P., Tschirner, S. K., Shqau, D., et al. (2025) · EMBO Reports · doi:10.1038/s44319-025-00604-4 · Cited by 2 · see citing works

GalNAc-T13 maintains neurite architecture and memory retention via O-GalNAc glycosylation of seizure protein 6

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EC‐01‐04: Physiological Substrates of Bace1 and Adam10: Safety Issues or Biomarkers?

Lichtenthaler, S. F. (2016) · Alzheimer s & Dementia · doi:10.1016/j.jalz.2016.06.290

Additional file 3: Tables S1-S6. of Seizure protein 6 and its homolog seizure 6-like protein are physiological substrates of BACE1 in neurons

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Proteomics in neurons and animals: substrates and therapeutic potential of alpha-and beta-secretase

Lichtenthaler, S. F. (2013) · Molecular Neurodegeneration · doi:10.1186/1750-1326-8-s1-o6

O1‐06‐04: Therapeutic potential of BACE1/beta‐secretase: Proteome‐wide identification of physiological BACE1 substrates in primary neurons and mouse brain

Lichtenthaler, S. F., Dislich, B., Hogl, S., Colombo, A. V., Zeitschel, U., Willem, M., Haass, C., Volbracht, C., Roßner, S., & Kuhn, P. (2012) · Alzheimer s & Dementia · doi:10.1016/j.jalz.2012.05.236

Function and substrates of the Alzheimer´s disease protease BACE1

Njavro, J. R., & Jasenka (2019)