Neuronal loss and brain atrophy in mice lacking cathepsins B and L

Identification of programmed cell death in situ via specific labeling of nuclear DNA fragmentation.

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Synaptic assembly of the brain in the absence of neurotransmitter secretion.

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Pycnodysostosis, a Lysosomal Disease Caused by Cathepsin K Deficiency

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Impaired osteoclastic bone resorption leads to osteopetrosis in cathepsin-K-deficient mice

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

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Cathepsin B contributes to TNF-α–mediated hepatocyte apoptosis by promoting mitochondrial release of cytochrome c

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Cathepsin L: Critical Role in Ii Degradation and CD4 T Cell Selection in the Thymus

Nakagawa, T. Y., Roth, W., Wong, P., Nelson, A., Farr, A. G., Deussing, J. M., Villadangos, J. A., Ploegh, H. L., Peters, C., & Rudensky, A. Y. (1998) · Science · doi:10.1126/science.280.5362.450 · Cited by 675

Cathepsin B Acts as a Dominant Execution Protease in Tumor Cell Apoptosis Induced by Tumor Necrosis Factor

Foghsgaard, L., Wissing, D., Mauch, D., Lademann, U. A., Bastholm, L., Boes, M. L., Elling, F., Leist, M., & Jäättelä, M. (2001) · The Journal of Cell Biology · doi:10.1083/jcb.153.5.999 · Cited by 629

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

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Cathepsin D in pancreatic acinar cells is implicated in cathepsin B and L degradation, but not in autophagic activity

Mehanna, S., Suzuki, C., Shibata, M., Sunabori, T., Imanaka, T., Araki, K., Yamamura, K., Uchiyama, Y., & Ohmuraya, M. (2015) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2015.12.002 · Cited by 20

Cathepsin Inhibition Prevents Autophagic Protein Turnover and Downregulates Insulin Growth Factor-1 Receptor–Mediated Signaling in Neuroblastoma

Soori, M. M., Lu, G., & Mason, R. W. (2015) · Journal of Pharmacology and Experimental Therapeutics · doi:10.1124/jpet.115.229229 · Cited by 20

Dual site‐controlled two‐photon fluorescent probe for the imaging of lysosomal pH in living cells

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From nucleus to mitochondria to lysosome selectivity switching in a cyanine probe: The phenolic to methoxy substituent conversion affects probe's selectivity.

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Analysis of cathepsin B and cathepsin L treatment to clear toxic lysosomal protein aggregates in neuronal ceroid lipofuscinosis

Spiezio, A. D., Marques, A. R. A., Schmidt, L., Thießen, N., Gallwitz, L., Fogh, J. M., Bartsch, U., & Säftig, P. (2021) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2021.166205 · Cited by 21

Cys-His proteases are among the wired proteins of the cell

Lockwood, T. D. (2004) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2004.09.011 · Cited by 20

Cystatin B-deficiency triggers ectopic histone H3 tail cleavage during neurogenesis

Daura, E., Tegelberg, S., Yoshihara, M., Jackson, C. B., Simonetti, F., Aksentjeff, K., Ezer, S., Hakala, P., Katayama, S., Kere, J., et al. (2021) · Neurobiology of Disease · doi:10.1016/j.nbd.2021.105418 · Cited by 19

Emergence of sex-specific transcriptomes in a sexually dimorphic brain nucleus

Friedrich, S. R., Nevue, A. A., Andrade, A. L. P., Velho, T., & Mello, C. V. (2022) · Cell Reports · doi:10.1016/j.celrep.2022.111152 · Cited by 19

Proteases in Cancer: Significance for Invasion and Metastasis

Sloane, B. F., List, K., Fingleton, B., & Matrisian, L. M. (2013) · Springer eBooks · doi:10.1007/978-3-7091-0885-7_15 · Cited by 21

Increased carcinogenic potential of myeloid tumor cells induced by aberrant TGF-β1-signaling and upregulation of cathepsin B

Reisenauer, A., Eickelberg, O., Wille, A., Heimburg, A., Reinhold, A., Sloane, B. F., Welte, T., & Bühling, F. (2007) · Biological Chemistry · doi:10.1515/bc.2007.072 · Cited by 20

Induction of cell death in neuroblastoma by inhibition of cathepsins B and L

Colella, R., Lu, G., Glazewski, L., Korant, B. D., Matlapudi, A., England, M. R., Craft, C. A., Frantz, C. N., & Mason, R. W. (2010) · Cancer Letters · doi:10.1016/j.canlet.2010.01.037 · Cited by 18

Toxoplasma Cathepsin Protease B and Aspartyl Protease 1 Are Dispensable for Endolysosomal Protein Digestion

McDonald, C., Smith, D. W., Cristina, M. D., Kannan, G., Dou, Z., & Carruthers, V. B. (2020) · mSphere · doi:10.1128/msphere.00869-19 · Cited by 18

Lysosomal integral membrane protein type-2 (LIMP-2/SCARB2) is a substrate of cathepsin-F, a cysteine protease mutated in type-B-Kufs-disease

Peters, J., Rittger, A., Weisner, R., Knabbe, J., Zunke, F., Rothaug, M., Daμμe, M., Berkovic, S. F., Blanz, J., Säftig, P., et al. (2015) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2014.12.111 · Cited by 18

Cathepsins in Neurological Diseases

Lewandowski, D., Konieczny, M., Różycka, A., Chrzanowski, K., Owecki, W., Kalinowski, J., Stepura, M., Jagodziński, P. P., & Dorszewska, J. (2025) · International Journal of Molecular Sciences · doi:10.3390/ijms26167886 · Cited by 17

The beneficial effects of l -cysteine on brain antioxidants of rats affected by sodium valproate

Hamza, R. Z., & Shenawy, N. S. E. (2017) · Human & Experimental Toxicology · doi:10.1177/0960327117695634 · Cited by 17

Neurexins play a crucial role in cerebellar granule cell survival by organizing autocrine machinery for neurotrophins

Uemura, T., Suzuki‐Kouyama, E., Kawase, S., Kurihara, T., Yasumura, M., Yoshida, T., Fukai, S., Yamazaki, M., Fei, P., Abe, M., et al. (2022) · Cell Reports · doi:10.1016/j.celrep.2022.110624 · Cited by 16

Lysosomal Modulatory Drugs for a Broad Strategy Against Protein Accumulation Disorders

Bahr, B. A. (2009) · Current Alzheimer Research · doi:10.2174/156720509789207903 · Cited by 17

Cathepsin B-A Neuronal Death Mediator in Alzheimer’s Disease Leading to Neurodegeneration

Singh, S. K., Sharma, A., Swetha, R., Bajad, N. G., Ganeshpurkar, A., Singh, R., & Kumar, A. (2022) · Mini-Reviews in Medicinal Chemistry · doi:10.2174/1389557522666220214095859 · Cited by 16

Double deficiency of cathepsin B and L in the mouse pancreas alters trypsin activity without affecting acute pancreatitis severity

Chen, W., Imasaka, M., Iwama, H., Nishiura, H., & Ohmuraya, M. (2022) · Pancreatology · doi:10.1016/j.pan.2022.08.011 · Cited by 16

Enhanced cystatin C and lysosomal protease expression following 6-hydroxydopamine exposure

Lee, D. C., Close, F. T., Goodman, C. B., Jackson, I. M., Mason, C. A. W., Wells, L. M., Womble, T. A., & Palm, D. E. (2006) · NeuroToxicology · doi:10.1016/j.neuro.2005.11.011 · Cited by 16

Human Mast Cells Upregulate Cathepsin B, a Novel Marker of Itch in Psoriasis

West, P., Tontini, C., Atmoko, H., Kiss, O., Garner, T., Bahri, R., Warren, R. B., Griffiths, C. E. M., Stevens, A., & Bulfone‐Paus, S. (2023) · Cells · doi:10.3390/cells12172177 · Cited by 15

Extracellular cathepsin L stimulates axonal growth in neurons

Tohda, C., & Tohda, M. (2017) · BMC Research Notes · doi:10.1186/s13104-017-2940-y · Cited by 15

Cathepsin L

Kirschke, H. (2012) · Handbook of Proteolytic Enzymes · doi:10.1016/b978-0-12-382219-2.00410-5 · Cited by 15

Recent insights into the networking of CLN genes and proteins in mammalian cells

Huber, R. J. (2023) · Journal of Neurochemistry · doi:10.1111/jnc.15822 · Cited by 14

Identification of a small molecule that induces ATG5-and-cathepsin-l-dependent cell death and modulates polyglutamine toxicity

Varma, H., Gangadhar, N. M., Letso, R. R., Wolpaw, A. J., Sriramaratnam, R., & Stockwell, B. R. (2013) · Experimental Cell Research · doi:10.1016/j.yexcr.2013.03.019 · Cited by 14

AAV8-mediated expression of N-acetylglucosamine-1-phosphate transferase attenuates bone loss in a mouse model of mucolipidosis II

Ko, A., Jin, D., Cho, S. Y., Park, S. W., Przybylska, M., Yew, N. S., Cheng, S. H., Kim, J.-S., Kwak, M. J., Kim, S. J., et al. (2016) · Molecular Genetics and Metabolism · doi:10.1016/j.ymgme.2016.02.001 · Cited by 15

An Autophagy Modifier Screen Identifies Small Molecules Capable of Reducing Autophagosome Accumulation in a Model of CLN3-Mediated Neurodegeneration

Petcherski, A., Chandrachud, U., Butz, E. S., Klein, M., Zhao, W., Reis, S. A., Haggarty, S. J., Ruonala, M. O., & Cotman, S. L. (2019) · Cells · doi:10.3390/cells8121531 · Cited by 15

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

Proteolysis of Amyloid β by Lysosomal Enzymes as a Function of Fibril Morphology

Lambeth, T. R., & Julian, R. R. (2021) · ACS Omega · doi:10.1021/acsomega.1c03915 · Cited by 14

Cellular Degradation Machineries in Age-Related Loss of Muscle Mass (Sarcopenia)

Altun, M., GrönholdtKlein, M., Wang, L., & Ulfhake, B. (2012) · InTech eBooks · doi:10.5772/34274 · Cited by 14

5-Aminopyrimidin-2-ylnitriles as Cathepsin K inhibitors

Morley, A., Kenny, P. W., Burton, B., Heald, R. A., MacFaul, P. A., Mullett, J., Page, K., Porres, S. S., Ribeiro, L. R., Smith, P., et al. (2009) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2009.01.110 · Cited by 13

Lysosomal Proteases

Brix, K. (2007) · Springer eBooks · doi:10.1007/0-387-28957-7_5 · 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

Elevated CTSL Gene Expression Correlated with Proinflammatory Cytokines in Omental Adipose Tissue of Patients with Obesity

Zhou, Q., Zhu, Y., Li, C., Li, Z., Tang, Z., Yuan, B., Wang, X., Zhang, S., & Wu, X. (2022) · Diabetes Metabolic Syndrome and Obesity · doi:10.2147/dmso.s373203 · Cited by 12

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

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

Wild type p53-dependent transcriptional upregulation of cathepsin L expression is mediated by C/EBPα in human glioblastoma cells

Katara, R., Mir, R. A., Shukla, A. A., Tiwari, A., Singh, N., & Chauhan, S. S. (2010) · Biological Chemistry · doi:10.1515/bc.2010.103 · Cited by 12

Cathepsin B knockout confers significant brain protection in the mouse model of stroke

Hu, K., Park, Y., Olivas-Garcia, Y., Chen, A. P., Liu, C., & Hu, B. R. (2023) · Experimental Neurology · doi:10.1016/j.expneurol.2023.114499 · Cited by 11

Neurobehavioral Impairments Predict Specific Cerebral Damage in Rat Model of Subarachnoid Hemorrhage

Lynch, D. G., Shah, K. A., Powell, K., Wadolowski, S., Tambo, W., Strohl, J. J., Unadkat, P., Eidelberg, D., Huerta, P. T., & Li, C. (2023) · Translational Stroke Research · doi:10.1007/s12975-023-01180-2 · Cited by 11

Expression mapping of cytotoxic T-lymphocyte antigen-2α gene transcripts in mouse brain

Luziga, C. D., Nakamura, O., Deshapriya, R. M. C., Usui, M., Miyaji, M., Wakimoto, M., Wada, N., & Yamamoto, Y. (2007) · Histochemistry and Cell Biology · doi:10.1007/s00418-007-0280-z · Cited by 11

An altered secretome is an early marker of the pathogenesis of CLN6 Batten disease

Best, H., Clare, A. J., McDonald, K. O., Wicky, H. E., & Hughes, S. (2020) · Journal of Neurochemistry · doi:10.1111/jnc.15285 · Cited by 8

A molten globule-to-ordered structure transition of Drosophila melanogaster crammer is required for its ability to inhibit cathepsin

Tseng, T., Cheng, C., Chen, D.-J., Shih, M.-F., Liu, Y.-N., Hsu, S. D., & Lyu, P. C. (2011) · Biochemical Journal · doi:10.1042/bj20111360 · Cited by 10

The human brain vasculature shows a distinct expression pattern of SARS-CoV-2 entry factorsPreprint

Ghobrial, M., Charish, J., Takada, S., Valiante, T. A., Monnier, P. P., Radovanovic, I., Bader, G. D., & Wälchli, T. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.10.10.334664 · Cited by 10

Best Practices for Development and Validation of Enzymatic Activity Assays to Support Drug Development for Inborn Errors of Metabolism and Biomarker Assessment

Azadeh, M., Good, J., Gunsior, M., Kulagina, N., Lu, Y., McNally, J., Myler, H. A., Ni, Y. G., Pelto, R., Quadrini, K. J., et al. (2024) · The AAPS Journal · doi:10.1208/s12248-024-00966-y · Cited by 10

Combined effects of social stress and liver fluke infection in a mouse model

Avgustinovich, D. F., Marenina, M. K., Zhanaeva, S. Y., Tenditnik, M. V., Katokhin, A. V., Pavlov, K. S., Sivkov, A. Y., Vishnivetskaya, G. B., Lvova, M. N., Tolstikova, T. G., et al. (2016) · Brain Behavior and Immunity · doi:10.1016/j.bbi.2016.01.012 · Cited by 10

Molecular targets and approaches to restore autophagy and lysosomal capacity in neurodegenerative disorders

Bastien, J., Menon, S., Messa, M., & Nyfeler, B. (2021) · Molecular Aspects of Medicine · doi:10.1016/j.mam.2021.101018 · Cited by 9

Proteases and Protease Inhibitors

Charron, M., & Wright, W. W. (2005) · Elsevier eBooks · doi:10.1016/b978-012647751-1/50010-6 · Cited by 9

Secreted caveolin-1 enhances periodontal inflammation by targeting gingival fibroblasts

Takizawa, N., Sawada, S., Chosa, N., Ishisaki, A., & Naruishi, K. (2013) · Biomedical Research · doi:10.2220/biomedres.34.1 · Cited by 8

A patient with pycnodysostosis presenting with seizures and porencephalic cysts

Kumar, S. (2014) · Journal of Neurosciences in Rural Practice · doi:10.4103/0976-3147.133606 · Cited by 8

RIT2 regulates autophagy lysosomal pathway induction and protects against α-synuclein pathology in a cellular model of Parkinson's disease

Gao, A. Y. L., Montagna, D. R., Hirst, W. D., & Temkin, P. A. (2024) · Neurobiology of Disease · doi:10.1016/j.nbd.2024.106568 · Cited by 7

Non-Canonical, Extralysosomal Activities of Lysosomal Peptidases in Physiological and Pathological Conditions: New Clinical Opportunities for Cancer Therapy

Conesa-Bakkali, R., Morillo‐Huesca, M., & Martínez‐Fábregas, J. (2025) · Cells · doi:10.3390/cells14020068 · Cited by 7

Protein processing by the placental protease, cathepsin P

Hassanein, M., Bojja, A. S., Glazewski, L., Lu, G., & Mason, R. W. (2009) · Molecular Human Reproduction · doi:10.1093/molehr/gap029 · Cited by 7

Cathepsin L coexists with Cytotoxic T-lymphocyte Antigen-2 alpha in distinct regions of the mouse brain

Luziga, C. D., Nga, B. T. T., Mbassa, G. K., & Yamamoto, Y. (2016) · Acta Histochemica · doi:10.1016/j.acthis.2016.08.003 · Cited by 6

Behavioral effects and inflammatory markers in the brain and periphery after repeated social defeat stress burdened by Opisthorchis felineus infection in mice

Avgustinovich, D. F., Tenditnik, M. V., Bondar, N. P., Marenina, M. K., Zhanaeva, S. Y., Lvova, M. N., Katokhin, A. V., Pavlov, K. S., Evseenko, V. I., & Tolstikova, T. G. (2022) · Physiology & Behavior · doi:10.1016/j.physbeh.2022.113846 · Cited by 7

The Transfer of Reductive Energy and Pace of Proteome Turnover: A Theory of Integrated Catabolic Control

Lockwood, T. D. (2005) · Antioxidants and Redox Signaling · doi:10.1089/ars.2005.7.982 · Cited by 6

Identification of KHS-101 as a Transcription Factor EB Activator to Promote α-Synuclein Degradation

Zhu, H.-Z., Ren, A., Li, T., Zhou, T., Li, A., Pan, X., Chen, L., & Chen, J. (2026) · International Journal of Molecular Sciences · doi:10.3390/ijms27020905 · Cited by 5

Expression of Cathepsin P mRNA, Protein and Activity in the Rat Choriocarcinoma Cell Line, Rcho-1, During Giant Cell Transformation

Hassanein, M., Korant, B. D., Lu, G., & Mason, R. W. (2007) · Placenta · doi:10.1016/j.placenta.2006.11.007 · Cited by 5

Design, Synthesis, and Biological Evaluation of 2-Arylaminopyrimidine Derivatives as Dual Cathepsin L and JAK Inhibitors for the Treatment of Acute Lung Injury

Shen, C., Mao, Z., Chen, T., Wei, Y., Zhou, T., Zhong, N., Zhu, G., Shi, Q., Xie, Z. W., Zhao, H., et al. (2024) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.4c02030 · Cited by 4

Golgi-Cox Staining Protocol for Medium Spiny Neurons in the Striatum of Neonatal and Early Postnatal Mouse Brain Using Cryosections

Ali, H. A., Mahmoud, W., Alzyoud, J. A. M., Aolymat, I., & Al‐Nassan, S. (2025) · International Journal of Molecular Sciences · doi:10.3390/ijms26167870 · Cited by 4

Recombinant cathepsins B and L promote α-synuclein clearance and restore lysosomal function in human and murine models with α-synuclein pathology

Balta, D., Varghese, A., Huarcaya, S. P., Spiezio, A. D., Marques, A. R. A., Akdaş, E. Y., Tabakacilar, D., Drobny, A., Werner, C. D., Xiang, W., et al. (2025) · Molecular Neurodegeneration · doi:10.1186/s13024-025-00886-1 · Cited by 4

Glioma-Associated Proteases

Bušek, P., Převorovský, M., Krepela, E., & Šedo, A. (2014) · Springer eBooks · doi:10.1007/978-3-7091-1431-5_12 · Cited by 4

Pathology of the Developing Mouse from Conception to Weaning

Bolon, B. N., & Carreira, V. (2015) · CRC Press eBooks · doi:10.1201/b18160-20 · Cited by 5

Cathepsin B deficiency disrupts cortical development via PEG3, leading to depression-like behavior

Xie, Z., Yang, Q., Lan, F., Kong, W., Zhao, S., Sun, J., Yan, Y., Quan, Z., Bai, Z., Qing, H., et al. (2025) · Communications Biology · doi:10.1038/s42003-025-08508-8 · Cited by 3

Dealing with damaged lysosomes : Impact of lysosomal membrane stability in health and disease

Eriksson, I. (2022) · Linköping University medical dissertations · doi:10.3384/9789179291792 · Cited by 3

Inflammasome Activation by Pathogenic Crystals and Particles

Re, F. (2011) · Springer eBooks · doi:10.1007/978-3-0348-0148-5_6 · 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

Proteolysis and proteolytic enzymes in structural plasticity of synapses

Kudryashova, I. V. (2009) · Neurochemical Journal · doi:10.1134/s1819712409030027 · Cited by 3

Self Organizing Map-Based Classification of Cathepsin k and S Inhibitors with Different Selectivity Profiles Using Different Structural Molecular Fingerprints: Design and Application for Discovery of Novel Hits

Ihmaid, S. K., Ahmed, H., Zayed, M. F., & Abadleh, M. M. (2016) · Molecules · doi:10.3390/molecules21020175 · Cited by 3

Whole-body single-cell sequencing of the Platynereis larva reveals a subdivision into apical versus non-apical tissuesPreprint

Achim, K., Eling, N., Vergara, H. M., Bertucci, P. Y., Brunet, T., Collier, P. G., Beneš, V., Marioni, J. C., & Arendt, D. (2017) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/167742 · Cited by 3

A lysosomal lipid transport pathway that enables cell survival under choline limitationPreprint

Scharenberg, S. G., Dong, W., Nyame, K., Levin‐Konigsberg, R., Krishnan, A. R., Rawat, E. S., Spees, K. K., Bassik, M. C., & Abu-Remaileh, M. (2022) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2022.11.27.517422 · Cited by 3

Reducing polypyrimidine tract‑binding protein 1 fails to promote neuronal transdifferentiation on HT22 and mouse astrocyte cells under physiological conditions

Li, Q., Zhang, W., Qiao, X.-Y., Liu, C., Dao, J.-J., Qiao, C.-M., Cui, C., Shen, Y., & Zhao, W. (2023) · Experimental and Therapeutic Medicine · doi:10.3892/etm.2023.12360 · Cited by 2

Molecular Differentiation of Cathepsins B and D, and of p53 Protein, and their Quantitative Assay in Biological Samples

Bratei, A. A., Staden, R. S., Ilie‐Mihai, R., & Gheorghe, D. (2023) · Journal of The Electrochemical Society · doi:10.1149/1945-7111/acf622 · Cited by 2

Uncovering the Unique Roles of Cathepsins B and L in Purkinje Cells Using Nervous System–Specific CTSB and CTSL Double-Deficient Mice

Sanada, T., Suzuki, C., Yamaguchi, J., Ueno, T., Trejo, J. A. O., Kakuta, S., Tada, N., Ohmuraya, M., Tanida, I., & Uchiyama, Y. (2025) · American Journal Of Pathology · doi:10.1016/j.ajpath.2025.04.011 · Cited by 2

Increased Immunoreactivity of Cathepsins in the Rat Esophagus under Chronic Acid Reflux Esophagitis

Suyama, M., Koike, M., Asaoka, D., Mori, H., Oguro, M., Ueno, T., Nagahara, A., Watanabe, S., & Uchiyama, Y. (2014) · Journal of Histochemistry & Cytochemistry · doi:10.1369/0022155414542300 · Cited by 2

Immunohistochemical study of microscopic globular bodies of normal human brain

Odagiri, S., Mori, F., Tanji, K., Kuroda, N., & Wakabayashi, K. (2011) · Biomedical Research · doi:10.2220/biomedres.32.337 · Cited by 2

Alteration of cathepsins and actin genes expression in rat brain during ageing

Львович, Р. Н., Topchieva, L. V., Vinogradova, I. A., & Немова, Н. Н. (2011) · Doklady Biological Sciences · doi:10.1134/s0012496611010157 · Cited by 2

Role of Lysosomal Cathepsins in Post-Myocardial Infarction Remodeling

Chen, H., Wang, J., & Shi, G. (2011) · North American Journal of Medicine and Science · doi:10.7156/v4i4p173 · Cited by 2

Proteolytic Mechanisms of Cell Death in the Central Nervous System

Larner, S. F., Hayes, R. L., & Wang, K. (2008) · Springer eBooks · doi:10.1007/978-0-387-30375-8_12 · Cited by 2

Trial of the cysteine cathepsin inhibitor JPM-OEt on early and advanced mammary cancer stages in the MMTV-PyMT-transgenic mouse model

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