A mutation in the ovine cathepsin D gene causes a congenital lysosomal storage disease with profound neurodegeneration

β-Secretase Cleavage of Alzheimer's Amyloid Precursor Protein by the Transmembrane Aspartic Protease BACE

Vassar, R., Bennett, B. D., Babu-Khan, S., Kahn, S., Mendiaz, E. A., Denis, P., Teplow, D. B., Ross, S., Amarante, P., Loeloff, R., et al. (1999) · Science · doi:10.1126/science.286.5440.735 · Cited by 3,876

Handbook of Proteolytic Enzymes

(2004) · Elsevier eBooks · doi:10.1016/c2009-0-03628-9 · Cited by 2,623

[41] Cathepsin B, cathepsin H, and cathepsin L

Barrett, A. J., & Kirschke, H. (1981) · Methods in Enzymology · doi:10.1016/s0076-6879(81)80043-2 · Cited by 1,698

The Handbook of proteolytic enzymes

Barrett, A. J., Rawlings, N. D., & Woessner, J. F. (1998) · Cited by 1,119

Mutations in the palmitoyl protein thioesterase gene causing infantile neuronal ceroid lipofuscinosis

Vesa, J., Hellsten, E., Verkruyse, L. A., Camp, L. A., Rapola, J., Santavuori, P., Hofmann, S. L., & Peltonen, L. (1995) · Nature · doi:10.1038/376584a0 · Cited by 736

The Structure and Function of the Aspartic Proteinases

Davies, D. R. (1990) · Annual Review of Biophysics and Biophysical Chemistry · doi:10.1146/annurev.bb.19.060190.001201 · Cited by 658

Isolation of a novel gene underlying batten disease, CLN3

Lerner, T. J., Boustany, R., Anderson, J. W., D'Arigo, K. L., Schlumpf, K. S., Buckler, A., Gusella, J. F., & Haines, J. L. (1995) · Cell · doi:10.1016/0092-8674(95)90274-0 · Cited by 598

Association of Mutations in a Lysosomal Protein with Classical Late-Infantile Neuronal Ceroid Lipofuscinosis

Sleat, D. E., DONNELLY, R. J., Lackland, H., Liu, C., Sohár, I., Pullarkat, R. K., & Lobel, P. (1997) · Science · doi:10.1126/science.277.5333.1802 · Cited by 581

Mice deficient for the lysosomal proteinase cathepsin D exhibit progressive atrophy of the intestinal mucosa and profound destruction of lymphoid cells.

Säftig, P., Hetman, M., Schmahl, W. W., Weber, K., Heine, L., Mossmann, H., Köster, A., Heß, B., Evers, M., & FIGURA, K. V. (1995) · The EMBO Journal · doi:10.1002/j.1460-2075.1995.tb00029.x · Cited by 439

The Presenilins in Alzheimer's Disease--Proteolysis Holds the Key

Haass, C., & Strooper, B. D. (1999) · Science · doi:10.1126/science.286.5441.916 · Cited by 388

Oxidative damage of lysosomes in regulated cell death systems: Pathophysiology and pharmacologic interventions

Nagakannan, P., Tabeshmehr, P., & Eftekharpour, E. (2020) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2020.04.001 · Cited by 41

Stress-induced apoptosis is impaired in cells with a lysosomal targeting defect but is not affected in cells synthesizing a catalytically inactive cathepsin D

Tardy, C., Tyynelä, J., Hasilík, A., Levade, T., & Andrieu‐Abadie, N. (2003) · Cell Death and Differentiation · doi:10.1038/sj.cdd.4401272 · Cited by 38

The relevance of the storage of subunit c of ATP synthase in different forms and models of Batten disease (NCLs)

Palmer, D. N. (2015) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2015.06.014 · Cited by 37

Involvement of lysosomal storage-induced p38 MAP kinase activation in the overproduction of nitric oxide by microglia in cathepsin D-deficient mice

Yamasaki, R., Zhang, J., Koshiishi, I., Sastradipura, D. F. S., Wu, Z., Peters, C., Schwake, M., Uchiyama, Y., Kira, J., Säftig, P., et al. (2007) · Molecular and Cellular Neuroscience · doi:10.1016/j.mcn.2007.05.002 · Cited by 36

Medical bioremediation: Prospects for the application of microbial catabolic diversity to aging and several major age-related diseases

de Grey, A. D. N. J., Alvarez, P. J. J., Brady, R. O., Cuervo, A. M., Jerome, W. G., McCarty, P. L., Nixon, R. A., Rittmann, B. E., & Sparrow, J. R. (2005) · Ageing Research Reviews · doi:10.1016/j.arr.2005.03.008 · Cited by 38

Enhanced expression of manganese-dependent superoxide dismutase in human and sheep CLN6 tissues

Heine, C., Tyynelä, J., Cooper, J. D., Palmer, D. N., Elleder, M., Kohlschütter, A., & Braulke, T. (2003) · Biochemical Journal · doi:10.1042/bj20030598 · Cited by 36

A Dictyostelium Mutant with Reduced Lysozyme Levels Compensates by Increased Phagocytic Activity

Müller, I., Šubert, N., Otto, H., Herbst, R., Rühling, H., Maniak, M., & Leippe, M. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m411445200 · Cited by 35

The neuronal ceroid lipofuscinoses: Opportunities from model systems

Faller, K. M. E., Gutierrez‐Quintana, R., Mohammed, A., Rahim, A. A., Tuxworth, R. I., Wager, K., & Bond, M. (2015) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2015.04.022 · Cited by 35

Homozygous PPT1 Splice Donor Mutation in a Cane Corso Dog With Neuronal Ceroid Lipofuscinosis

Kolicheski, A., Heller, H. B., Arnold, S. A., Schnabel, R. D., Taylor, J. F., Brookhart-Knox, C. A., Mhlanga-Mutangadura, T., O’Brien, D. P., Johnson, G. S., Dreyfus, J. M., et al. (2016) · Journal of Veterinary Internal Medicine · doi:10.1111/jvim.14632 · Cited by 34

Novel rapid genotyping assays for neuronal ceroid lipofuscinosis in Border Collie dogs and high frequency of the mutant allele in Japan

Mizukami, K., Chang, H.-S., Yabuki, A., Kawamichi, T., Kawahara, N., Hayashi, D., Hossain, M. A., Rahman, M. M., Uddin, M. M., & Yamato, O. (2011) · Journal of Veterinary Diagnostic Investigation · doi:10.1177/1040638711425590 · Cited by 34

Morphologic and Functional Correlates of Synaptic Pathology in the Cathepsin D Knockout Mouse Model of Congenital Neuronal Ceroid Lipofuscinosis

Koch, S., Molchanova, S. M., Wright, A. K., Edwards, A., Cooper, J. D., Taira, T., Gillingwater, T. H., & Tyynelä, J. (2011) · Journal of Neuropathology & Experimental Neurology · doi:10.1097/nen.0b013e318238fc28 · Cited by 34

Murine cathepsin D deficiency is associated with dysmyelination/myelin disruption and accumulation of cholesteryl esters in the brain

Mutka, A., Haapanen, A., Käkelä, R., Lindfors, M., Wright, A. K., Inkinen, T., Hermansson, M., Rokka, A., Corthals, G., Jauhiainen, M., et al. (2010) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2009.06440.x · Cited by 34

Lysosomal Storage Diseases: Is Impaired Apoptosis a Pathogenic Mechanism?

Tardy, C., Andrieu‐Abadie, N., Salvayre, R., & Levade, T. (2004) · Neurochemical Research · doi:10.1023/b:nere.0000021232.05175.38 · Cited by 32

Cathepsin D: Analysis of its potential role as an amyloid beta degrading protease

Gallwitz, L., Schmidt, L., Marques, A. R. A., Tholey, A., Cassidy, L., Ulku, I., Multhaup, G., Spiezio, A. D., & Säftig, P. (2022) · Neurobiology of Disease · doi:10.1016/j.nbd.2022.105919 · Cited by 34

Neuronal ceroid lipofuscinosis (NCL) is caused by the entire deletion of CLN8 in the Alpenländische Dachsbracke dog

Hirz, M., Drögemüller, M., Schänzer, A., Jagannathan, V., Dietschi, E., Goebel, H. H., Hecht, W., Laubner, S., Schmidt, M. J., Steffen, F., et al. (2016) · Molecular Genetics and Metabolism · doi:10.1016/j.ymgme.2016.12.007 · Cited by 31

Discovery and Early Clinical Development of LY3202626, a Low-Dose, CNS-Penetrant BACE Inhibitor

McKinzie, D. L., Winneroski, L. L., Green, S. J., Hembre, E. J., Erickson, J. A., Willis, B. A., Monk, S. A., Aluise, C. D., Baker, T. K., López, J. E., et al. (2021) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.1c00489 · Cited by 31

Two novel CLN6 mutations in variant late‐infantile neuronal ceroid lipofuscinosis patients of Turkish origin

Siintola, E., Topçu, M., Kohlschütter, A., Salonen, T., Joensuu, T. H., Anttonen, A.-K., & Lehesjoki, A. (2005) · Clinical Genetics · doi:10.1111/j.1399-0004.2005.00471.x · Cited by 30

The origin of fluorescence in the neuronal ceroid lipofuscinoses (Batten disease) and neuron cultures from affected sheep for studies of neurodegeneration

Palmer, D. N., Oswald, M. J., Westlake, V. J., & Kay, G. W. (2002) · Archives of Gerontology and Geriatrics · doi:10.1016/s0167-4943(02)00011-0 · Cited by 30

Gene expression profiling in a mouse model of infantile neuronal ceroid lipofuscinosis reveals upregulation of immediate early genes and mediators of the inflammatory response

Qiao, X., Lu, J.-Y., & Hofmann, S. L. (2007) · BMC Neuroscience · doi:10.1186/1471-2202-8-95 · Cited by 30

Mutations in classical late infantile neuronal ceroid lipofuscinosis disrupt transport of tripeptidyl-peptidase I to lysosomes

Steinfeld, R., Steinke, H.-B., Isbrandt, D., Kohlschütter, A., & Gärtner, J. (2004) · Human Molecular Genetics · doi:10.1093/hmg/ddh264 · Cited by 30

In vivo MRI reveals the dynamics of pathological changes in the brains of cathepsin D-deficient mice and correlates changes in manganese-enhanced MRI with microglial activation

Haapanen, A., Ramadan, U. A., Autti, T. H., Joensuu, R., & Tyynelä, J. (2007) · Magnetic Resonance Imaging · doi:10.1016/j.mri.2007.03.012 · Cited by 29

Congenital ovine neuronal ceroid lipofuscinosis — acathepsin D deficiency with increased levels of the inactive enzyme

Tyynelä, J., Sohár, I., Sleat, D. E., Gin, R. M., Nelly, R. J. D., Baumann, M., Haltia, M., & Lobel, P. (2001) · European Journal of Paediatric Neurology · doi:10.1053/ejpn.2000.0433 · Cited by 29

The history of progressive myoclonus epilepsies

Genton, P., Striano, P., & Minassian, B. A. (2016) · Epileptic Disorders · doi:10.1684/epd.2016.0834 · Cited by 29

Status Epilepticus Induces Changes in the Expression and Localization of Endogenous Palmitoyl-Protein Thioesterase 1

Suopanki, J., Lintunen, M., Lahtinen, H., Haltia, M., Panula, P., Baumann, M., & Tyynelä, J. (2002) · Neurobiology of Disease · doi:10.1006/nbdi.2002.0503 · Cited by 29

Cathepsin D in the Tumor Microenvironment of Breast and Ovarian Cancers

Pranjol, M. Z. I., & Whatmore, J. L. (2020) · Advances in experimental medicine and biology · doi:10.1007/978-3-030-43093-1_1 · Cited by 29

The neuronal ceroid lipofuscinosis Cln8 gene expression is developmentally regulated in mouse brain and up-regulated in the hippocampal kindling model of epilepsy

Lonka, L., Aalto, A., Kopra, O., Kuronen, M., Kokaia, Z., Saarma, M., & Lehesjoki, A. (2005) · BMC Neuroscience · doi:10.1186/1471-2202-6-27 · Cited by 28

Early infantile neuronal ceroid lipofuscinosis (CLN10 disease) associated with a novel mutation in CTSD

Doccini, S., Sartori, S., Maeser, S., Pezzini, F., Rossato, S., Moro, F., Toldo, I., Przybylski, M., Santorelli, F. M., & Simonati, A. (2016) · Journal of Neurology · doi:10.1007/s00415-016-8111-6 · Cited by 27

Influence and interactions of cathepsin D, HLA‐DRB1 and APOE on cognitive abilities in an older non‐demented population

Payton, A., Boogerd, E. V. D., Davidson, Y. S., Gibbons, L., Ollier, W., Rabbitt, P., Worthington, J., Horan, M. A., & Pendleton, N. (2006) · Genes Brain & Behavior · doi:10.1111/j.1601-183x.2006.00191.x · Cited by 30

Differences in expression patterns of cathepsin C /dipeptidyl peptidase I in normal, pathological and aged mouse central nervous system

Koike, M., Shibata, M., Ezaki, J., Peters, C., Säftig, P., Kominami, E., & Uchiyama, Y. (2012) · European Journal of Neuroscience · doi:10.1111/ejn.12096 · Cited by 28

Neuronal ceroid lipofuscinosis in Australian Merino sheep: a new animal model

Tammen, I., Cook, R. W., Nicholas, F. W., & Raadsma, H. W. (2001) · European Journal of Paediatric Neurology · doi:10.1053/ejpn.2000.0432 · Cited by 27

Lysosomal degradation of cholecystokinin-(29–33)-amide in mouse brain is dependent on tripeptidyl peptidase-I: implications for the degradation and storage of peptides in classical late-infantile neuronal ceroid lipofuscinosis

Bernardini, F., & Warburton, M. J. (2002) · Biochemical Journal · doi:10.1042/bj20020467 · Cited by 27

Large Animal Models for Batten Disease

Weber, K. L., & Pearce, D. A. (2013) · Journal of Child Neurology · doi:10.1177/0883073813493666 · Cited by 26

Neuroectoderm-specific deletion of cathepsin D in mice models human inherited neuronal ceroid lipofuscinosis type 10

Ketscher, A., Ketterer, S., Dollwet-Mack, S., REIF, U. M., & Reinheckel, T. (2015) · Biochimie · doi:10.1016/j.biochi.2015.07.020 · Cited by 26

A replacement of the active-site aspartic acid residue 293 in mouse cathepsin D affects its intracellular stability, processing and transport in HEK-293 cells

Partanen, S., Storch, S., Löffler, H., Hasilík, A., Tyynelä, J., & Braulke, T. (2002) · Biochemical Journal · doi:10.1042/bj20021226 · Cited by 26

Cathepsin D deficiency induces cytoskeletal changes and affects cell migration pathways in the brain

Koch, S., Scifo, E., Rokka, A., Trippner, P., Lindfors, M., Korhonen, R., Corthals, G. L., Virtanen, I., Lalowski, M. M., & Tyynelä, J. (2012) · Neurobiology of Disease · doi:10.1016/j.nbd.2012.10.004 · Cited by 25

Knockdown of cathepsin D in zebrafish fertilized eggs determines congenital myopathy

Follo, C., Ozzano, M., Montalenti, C., Santoro, M. M., & Isidoro, C. (2013) · Bioscience Reports · doi:10.1042/bsr20120100 · Cited by 25

The effects of lysosomotropic agents on normal and INCL cells provide further evidence for the lysosomal nature of palmitoyl-protein thioesterase function

Lu, J.-Y., Verkruyse, L. A., & Hofmann, S. L. (2002) · Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids · doi:10.1016/s1388-1981(02)00158-0 · Cited by 25

The neuronal ceroid-lipofuscinoses (Batten disease)

Mole, S., Schulz, A., & Haltia, M. (2020) · Elsevier eBooks · doi:10.1016/b978-0-12-813866-3.00004-7 · Cited by 23

The function of CLN3P, the Batten disease protein

Rakheja, D., Narayan, S. B., & Bennett, M. J. (2008) · Molecular Genetics and Metabolism · doi:10.1016/j.ymgme.2008.01.001 · Cited by 23

Prominent tauopathy and intracellular β-amyloid accumulation triggered by genetic deletion of cathepsin D: implications for Alzheimer disease pathogenesis

Terron, H. M., Parikh, S. J., Abdul‐Hay, S. O., Sahara, T., Kang, D., Dickson, D. W., Säftig, P., LaFerla, F. M., Lane, S., & Leissring, M. A. (2024) · Alzheimer s Research & Therapy · doi:10.1186/s13195-024-01443-6 · Cited by 22

Lysosomal proteomics and disease

Sleat, D. E., Jadot, M., & Lobel, P. (2007) · PROTEOMICS - CLINICAL APPLICATIONS · doi:10.1002/prca.200700250 · Cited by 23

Mannose 6-Phosphorylated Proteins Are Required for Tumor Necrosis Factor-induced Apoptosis

Tardy, C., Autefage, H., Garcia, V., Levade, T., & Andrieu‐Abadie, N. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m408261200 · Cited by 22

Lysosomal Storage Diseases

Haskins, M. E., & Giger, U. (2008) · Elsevier eBooks · doi:10.1016/b978-0-12-370491-7.00024-6 · Cited by 22

An aspartyl cathepsin,CTH3, is essential for proprotein processing during secretory granule maturation inTetrahymena thermophila

Kumar, S., Briguglio, J. S., & Turkewitz, A. P. (2014) · Molecular Biology of the Cell · doi:10.1091/mbc.e14-03-0833 · Cited by 20

Detection of procathepsin D in rat milk

Beneš, P., Koelsch, G., Dvořák, B., Fusek, M., & Větvička, V. (2002) · Comparative Biochemistry and Physiology Part B Biochemistry and Molecular Biology · doi:10.1016/s1096-4959(02)00112-4 · Cited by 20

Developmental Changes in the Expression of Neuronal Ceroid Lipofuscinoses-Linked Proteins

Suopanki, J., Partanen, S., Ezaki, J., Baumann, M., Kominami, E., & Tyynelä, J. (2000) · Molecular Genetics and Metabolism · doi:10.1006/mgme.2000.3071 · Cited by 20

A novel intermediate mucolipidosis II/IIIαβ caused by GNPTAB mutation in the cytosolic N-terminal domain

Leroy, J. G., Sillence, D. O., Wood, T. C., Barnes, J. W., Lebel, R. R., Friez, M. J., Stevenson, R. E., Steet, R., & Cathey, S. S. (2013) · European Journal of Human Genetics · doi:10.1038/ejhg.2013.207 · Cited by 21

Aberrant Autophagy Impacts Growth and Multicellular Development in a Dictyostelium Knockout Model of CLN5 Disease

McLaren, M. D., Mathavarajah, S., Kim, W. D., Yap, S. Q., & Huber, R. J. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.657406 · Cited by 19

Neuronal ceroid lipofuscinosis: underlying mechanisms and emerging therapeutic targets

Ziółkowska, E., Takahashi, K., Dickson, P., Sardiello, M., Sands, M. S., & Cooper, J. D. (2025) · Nature Reviews Neurology · doi:10.1038/s41582-025-01132-4 · Cited by 21

The specific loss of GnRH-positive neurons from the hypothalamus of sheep with CLN6 neuronal ceroid lipofuscinosis occurs without glial activation and has only minor effects on reproduction

Kay, G. W., Jay, N. P., & Palmer, D. N. (2010) · Neurobiology of Disease · doi:10.1016/j.nbd.2010.11.008 · Cited by 18

The neuronal ceroid-lipofuscinoses (Batten disease)

Mole, S., & Schulz, A. (2024) · Elsevier eBooks · doi:10.1016/b978-0-443-19176-3.00018-2 · Cited by 19

The lysosomal degradation of neuromedin B is dependent on tripeptidyl peptidase-I: evidence for the impairment of neuropeptide degradation in late-infantile neuronal ceroid lipofuscinosis

Kopan, S., Sivasubramaniam, U., & Warburton, M. J. (2004) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2004.04.142 · Cited by 18

DNA Testing in Neurologic Diseases

O’Brien, D. P., & Leeb, T. (2014) · Journal of Veterinary Internal Medicine · doi:10.1111/jvim.12383 · Cited by 17

Analysis of NCL Proteins from an Evolutionary Standpoint

Muzaffar, N. E., & Pearce, D. A. (2008) · Current Genomics · doi:10.2174/138920208784139573 · Cited by 17

Experimental approaches for altering the expression of Abeta‐degrading enzymes

Loeffler, D. A. (2023) · Journal of Neurochemistry · doi:10.1111/jnc.15762 · Cited by 18

Manifestation of neuronal ceroid lipofuscinosis in Australian Merino sheep: Observations on altered behaviour and growth

Cronin, G. M., Beganovic, D. F., Sutton, A. L., Palmer, D. J., Thomson, P. C., & Tammen, I. (2015) · Applied Animal Behaviour Science · doi:10.1016/j.applanim.2015.11.012 · Cited by 17

Neuronal Ceroid Lipofuscinosis in a Domestic Cat Associated with a DNA Sequence Variant That Creates a Premature Stop Codon inCLN6

Katz, M. L., Buckley, R. M., Biegen, V. R., O’Brien, D. P., Johnson, G. C., Warren, W. C., & Lyons, L. A. (2020) · G3 Genes Genomes Genetics · doi:10.1534/g3.120.401407 · Cited by 15

Overexpression in colorectal carcinoma of two lysosomal enzymes, CLN2 and CLN1, involved in neuronal ceroid lipofuscinosis

Tsukamoto, T., Iida, J., Dobashi, Y., Furukawa, T., & Konishi, F. (2006) · Cancer · doi:10.1002/cncr.21764 · Cited by 15

Another disorder finds its gene

Ramirez‐Montealegre, D. (2006) · Brain · doi:10.1093/brain/awl132 · Cited by 16

Primary defects in lysosomal enzymes

WINCHESTER, B. G. (2004) · doi:10.1093/acprof:oso/9780198508786.003.0004 · Cited by 15

pdf1 , a Palmitoyl Protein Thioesterase 1 Ortholog in Schizosaccharomyces pombe : a Yeast Model of Infantile Batten Disease

Cho, S. K., & Hofmann, S. L. (2004) · Eukaryotic Cell · doi:10.1128/ec.3.2.302-310.2004 · Cited by 14

Neuronal ceroid-lipofuscinoses

Rakheja, D., & Bennett, M. J. (2018) · Translational Science of Rare Diseases · doi:10.3233/trd-180024 · Cited by 14

Genetic modifiers of degeneration in the cathepsin D deficient Drosophila model for neuronal ceroid lipofuscinosis

Kuronen, M., Talvitie, M., Lehesjoki, A., & Myllykangas, L. (2009) · Neurobiology of Disease · doi:10.1016/j.nbd.2009.09.001 · Cited by 14

Cathepsin D: A Candidate Link between Amyloid ?-protein and Tauopathy in Alzheimer Disease

Suire, C. N., & Leissring, M. A. (2021) · Journal of Experimental Neurology · doi:10.33696/neurol.2.029 · Cited by 15

Glial fibrillary acidic protein is elevated in the lysosomal storage disease classical late-infantile neuronal ceroid lipofuscinosis, but is not a component of the storage material

Xu, S., Sleat, D. E., Jadot, M., & Lobel, P. (2010) · Biochemical Journal · doi:10.1042/bj20100128 · Cited by 13

Picrotoxin-induced convulsions and lysosomal function in the rat brain

Acharya, M. M., Khamesra, S. H., & Katyare, S. S. (2005) · Indian Journal of Clinical Biochemistry · doi:10.1007/bf02893043 · Cited by 13

Haematopoietic development and immunological function in the absence of cathepsin D

Tulone, C., Uchiyama, Y., Novelli, M. R., Grosvenor, N., Säftig, P., & Chain, B. (2007) · BMC Immunology · doi:10.1186/1471-2172-8-22 · Cited by 13

Cathepsins: Getting in Shape for Lysosomal Proteolysis

Erickson, A. H., Isidoro, C., Mach, L., & Mort, J. S. (2013) · Springer eBooks · doi:10.1007/978-3-7091-0885-7_4 · Cited by 14

High yield synthesis and characterization of phosphorylated recombinant human procathepsin D expressed in mammalian cells

Démoz, M., Castino, R., Follo, C., Hasilík, A., Sloane, B. F., & Isidoro, C. (2005) · Protein Expression and Purification · doi:10.1016/j.pep.2005.07.024 · Cited by 13

An Alternative Splicing Variant in Clcn7 –/– Mice Prevents Osteopetrosis but Not Neural and Retinal Degeneration

Rajan, I., Read, R. W., Small, D. L., Perrard, J., & Vogel, P. (2010) · Veterinary Pathology · doi:10.1177/0300985810370164 · Cited by 12

Bioinformatic perspectives in the neuronal ceroid lipofuscinoses

Kmoch, S., Stránecký, V., Emes, R. D., & Mitchison, H. M. (2012) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2012.12.010 · Cited by 12

Cathepsin Deficiency as a Model for Neuronal Ceroid Lipofuscinoses

Shacka, J. J., & Roth, K. A. (2005) · American Journal Of Pathology · doi:10.1016/s0002-9440(10)61233-3 · Cited by 12

Lysosomal storage disease associated with a CNP sequence variant in Dalmatian dogs

Bullock, G., Johnson, G. S., Mhlanga-Mutangadura, T., Petesch, S. C., Thompson, S., Goebbels, S., & Katz, M. L. (2022) · Gene · doi:10.1016/j.gene.2022.146513 · Cited by 11

Characterization of Neuronal Ceroid-Lipofuscinosis in 3 Cats

Chalkley, M., Armién, A. G., Gilliam, D., Johnson, G. S., Zeng, R., Wünschmann, A., Kovi, R. C., & Katz, M. L. (2013) · Veterinary Pathology · doi:10.1177/0300985813502818 · Cited by 11

Batten disease through different in vivo and in vitro models: A review

Nittari, G., Tomassoni, D., Roy, P., Martinelli, I., Tayebati, S. K., & Amenta, F. (2022) · Journal of Neuroscience Research · doi:10.1002/jnr.25147 · Cited by 10

Genetic testing for phenotype-causing variants in sheep and goats

Lühken, G. (2012) · Molecular and Cellular Probes · doi:10.1016/j.mcp.2012.04.005 · Cited by 13

Neuronal Ceroid Lipofuscinosis in a Vietnamese Pot-bellied Pig (Sus scrofa)

Cesta, M. F., Mozzachio, K., Little, P. B., Olby, N. J., Sills, R. C., & Brown, T. T. (2006) · Veterinary Pathology · doi:10.1354/vp.43-4-556 · Cited by 10

Clinical and Pathologic Features of Neuronal Ceroid-Lipofuscinosis in a Ferret ( Mustela putorius furo )

Nibe, K., Miwa, Y., Matsunaga, S., CHAMBERS, J. K., Uetsuka, K., Nakayama, H., & Uchida, K. (2011) · Veterinary Pathology · doi:10.1177/0300985811400441 · Cited by 10

Systemic or Multifocal Signs

Lorenz, M. D., Coates, J. R., & Kent, M. (2011) · Elsevier eBooks · doi:10.1016/b978-1-4377-0651-2.10015-3 · Cited by 9

Characterization of Candidate Genes for Neuronal Ceroid Lipofuscinosis in Dog

Drögemüller, C., Wöhlke, A., & Distl, O. (2005) · Journal of Heredity · doi:10.1093/jhered/esi088 · Cited by 9

Genetic polymorphism in exon 2 of cathepsin D is not associated with vascular dementia

Jeong, B., Lee, K.-H., Lee, Y.-J., Yun, J., Park, Y.-J., Kim, Y.-H., Cho, Y.-S., Choi, E., Carp, R. I., & Kim, Y. (2010) · Acta Neurologica Scandinavica · doi:10.1111/j.1600-0404.2010.01400.x · Cited by 7

Similarities and differences in the biogenesis, processing and lysosomal targeting between zebrafish and human pro-Cathepsin D: Functional implications

Follo, C., Ozzano, M., Montalenti, C., Ekkapongpisit, M., & Isidoro, C. (2012) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2012.10.010 · Cited by 7

Neuronal Ceroid-Lipofuscinoses

Tyynelä, J. (2007) · Springer eBooks · doi:10.1007/0-387-28957-7_8 · Cited by 7

Gene Arrays, Cell Lines, Stem Cells, and Sensory Regeneration in Mammalian Ears

Rivolta, M. N., & Holley, M. C. (2008) · Springer eBooks · doi:10.1007/978-0-387-73364-7_7 · Cited by 6

Translating preclinical models of neuronal ceroid lipofuscinosis: progress and prospects

Nelvagal, H. R., & Cooper, J. D. (2017) · Expert Opinion on Orphan Drugs · doi:10.1080/21678707.2017.1360182 · Cited by 6

The canine CTSD gene as a candidate for late‐onset neuronal ceroid lipofuscinosis

Wöhlke, A., Distl, O., & Drögemüller, C. (2005) · Animal Genetics · doi:10.1111/j.1365-2052.2005.01375.x · Cited by 6

Neuronal Ceroid Lipofuscinosis in a Mallard Duck (Anas platyrhynchos)

Evans, E. E., Jones, M. P., Crews, A., & Newkirk, K. M. (2012) · Journal of Avian Medicine and Surgery · doi:10.1647/2010-045.1 · Cited by 6

Cathepsin D

Conner, G. E. (2004) · Handbook of Proteolytic Enzymes · doi:10.1016/b978-0-12-079611-3.50016-1 · Cited by 6

Neuronal Ceroid-Lipofuscinoses

Rakheja, D., & Bennett, M. J. (2017) · IOS Press eBooks · doi:10.3233/978-1-61499-718-4-499 · Cited by 5

The Impact of Assay Design on Medicinal Chemistry: Case Studies

Born, J. R., Chenniappan, V. K., Davis, D., Dahlin, J. L., Marugán, J., & Patnaik, S. (2021) · SLAS DISCOVERY · doi:10.1177/24725552211026238 · Cited by 5

A one-health approach to using sheep in research, with a focus on neuroscience studies

Chatzimanou, T., & Tsingotjidou, A. (2023) · One Health & Implementation Research · doi:10.20517/ohir.2023.13 · Cited by 3

Role of altered pH homeostasis and hypoxia in the phenotypic changes of cancer cells

Kokkonen, N. (2009) · Cited by 4

Neuronal ceroid lipofuscinosis in a Schapendoes dog is caused by a missense variant in CLN6

Bellamy, K. K. L., Skedsmo, F. S., Hultman, J., Jansen, J. H., & Lingaas, F. (2024) · Animal Genetics · doi:10.1111/age.13457 · Cited by 3

Exploring Systemic Functions of Lysosomal Proteases: The Perspective of Genetically Modified Mouse Models

Gansz, M., Kern, U., Peters, C., & Reinheckel, T. (2013) · Springer eBooks · doi:10.1007/978-3-7091-0885-7_6 · Cited by 3

Lysosomal diseases

Suzuki, K., & Suzuki, K. (2008) · CRC Press eBooks · doi:10.1201/b13319-8 · Cited by 3

Identifying Targets in α‐Synuclein Metabolism to Treat Parkinson Disease and Related Disorders

Tomlinson, J. J., Cullen, V., & Schlossmacher, M. G. (2010) · doi:10.1002/9780470572702.ch37 · Cited by 3

Neuronale Zeroidlipofuszinosen (NCL) im Tiermodell

Rüther, K. (2010) · Der Ophthalmologe · doi:10.1007/s00347-009-2108-9 · Cited by 2

Detection of cathepsin D in ewe’s milk by Western Blotting method

Špehar, I. D., Martinković, F., Havranek, J., Marinculić, A., Kalit, M. T., & Kalit, S. (2013) · Hrčak Portal of scientific journals of Croatia (University Computing Centre) · Cited by 2

Neuronal ceroid lipofuscinosis/Batten disease: the lysosomal proteinoses

Gupta, P. K., & Hofmann, S. L. (2002) · Molecular Psychiatry · doi:10.1038/sj.mp.4001127 · Cited by 2

Lysosomal Membrane Transport in the Central Nervous System

Morin, P., Sagné, C., & Gasnier, B. (2007) · Springer eBooks · doi:10.1007/978-0-387-30380-2_22 · Cited by 2

Cathepsin D-deficient Drosophila recapitulate the key features of neuronal ceroid lipofuscinoses

Myllykangas, L., Tyynelä, J., Page, A. W., Rubin, G. M., Haltia, M., & Feany, M. Β. (2005) · Neurobiology of Disease · doi:10.1016/j.nbd.2004.12.019 · Cited by 79

Congenital ovine neuronal ceroid lipofuscinosis — acathepsin D deficiency with increased levels of the inactive enzyme

Tyynelä, J., Sohár, I., Sleat, D. E., Gin, R. M., Nelly, R. J. D., Baumann, M., Haltia, M., & Lobel, P. (2001) · European Journal of Paediatric Neurology · doi:10.1053/ejpn.2000.0433 · Cited by 29

Cathepsin D deficiency underlies congenital human neuronal ceroid-lipofuscinosis

Siintola, E. (2006) · Brain · doi:10.1093/brain/awl107 · Cited by 389

Another disorder finds its gene

Ramirez‐Montealegre, D. (2006) · Brain · doi:10.1093/brain/awl132 · Cited by 16

Novel mutation and the first prenatal screening of cathepsin D deficiency (CLN10)

Fritchie, K., Siintola, E., Armao, D. M., Lehesjoki, A., Marino, T., Powell, C. M., Tennison, M. B., Booker, J., Koch, S., Partanen, S., et al. (2008) · Acta Neuropathologica · doi:10.1007/s00401-008-0426-7 · Cited by 79