Susceptibility of the cartilage collagens types II, IX and XI to degradation by the cysteine proteinases, cathepsins B and L

Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4

LAEMMLI, U. K. (1970) · Nature · doi:10.1038/227680a0 · Cited by 249,961 · see citing works

Cartilage contains mixed fibrils of collagen types II, IX, and XI.

Mendler, M., Eich-Bender, S. G., Vaughan, L., Winterhalter, K. H., & Brückner, P. (1989) · The Journal of Cell Biology · doi:10.1083/jcb.108.1.191 · Cited by 510 · see citing works

Cartilage collagens. What Is Their Function, and Are They Involved in Articular Disease?

Mayne, R. (1989) · Arthritis & Rheumatism · doi:10.1002/anr.1780320302 · Cited by 193 · see citing works

A comparison of four cathepsins (B, L, N and S) with collagenolytic activity from rabbit spleen

Maciewicz, R. A., & Etherington, D. J. (1988) · Biochemical Journal · doi:10.1042/bj2560433 · Cited by 160 · see citing works

Degradation of type IX collagen by matrix metalloproteinase 3 (stromelysin) from human rheumatoid synovial cells

Okada, Y., Konomi, H., Yada, T., Kimata, K., & Nagase, H. (1989) · FEBS Letters · doi:10.1016/0014-5793(89)80586-1 · Cited by 96 · see citing works

Immunodetection of cathepsins b and l present in and secreted from human pre‐malignant and malignant colorectal tumour cell lines

Maciewicz, R. A., Wardale, R. J., Etherington, D. J., & Paraskeva, C. (1989) · International Journal of Cancer · doi:10.1002/ijc.2910430323 · Cited by 96 · see citing works

Metalloproteinases and collagenase inhibitors in rheumatoid synovial fluid

Cawston, T. E., Mercer, E., Silva, M. D., & Hazleman, B. L. (1984) · Arthritis & Rheumatism · doi:10.1002/art.1780270306 · Cited by 87 · see citing works

Susceptibility of cartilage collagens type II, IX, X, and XI to human synovial collagenase and neutrophil elastase

Gadher, S. J., Eyre, D. R., Duance, V. C., Wotton, S. F., Heck, L. W., Schmid, T. M., & Woolley, D. E. (1988) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1988.tb14158.x · Cited by 73 · see citing works

Active center differences between cathepsins L and B: The S1 binding region

Kirschke, H., Wikström, P., & Shaw, E. N. (1988) · FEBS Letters · doi:10.1016/0014-5793(88)80600-8 · Cited by 70 · see citing works

From tadpole collagenase to a family of matrix metalloproteinases

Birkedal‐Hansen, H. (1988) · Journal of Oral Pathology and Medicine · doi:10.1111/j.1600-0714.1988.tb01313.x · Cited by 66 · see citing works

Collagenolytic Cathepsins of Rabbit Spleen: A Kinetic Analysis of Collagen Degradation and Inhibition by Chicken Cystatin

Maciewicz, R. A., Etherington, D. J., Kos, J., & Türk, V. (1987) · Collagen and Related Research · doi:10.1016/s0174-173x(87)80035-3 · Cited by 63 · see citing works

Type IX collagen: A possible function in articular cartilage

Wotton, S. F., Duance, V. C., & Fryer, P. R. (1988) · FEBS Letters · doi:10.1016/0014-5793(88)81307-3 · Cited by 53 · see citing works

Relationship of Procollagenase Activator, Stromelysin and Matrix Metalloproteinase 3

Murphy, G., Nagase, H., & Brinckerhoff, C. (1988) · Collagen and Related Research · doi:10.1016/s0174-173x(88)80009-8 · Cited by 51 · see citing works

The Structure of Type IX Collagena

Mayne, R., REST, M. V. D., Ninomiya, Y., & Olsen, B. R. (1985) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.1985.tb51155.x · Cited by 38 · see citing works

Isolation and characterization of the precursor of type M collagen

Duance, V. C., Wotton, S. F., Voyle, C. A., & Bailey, A. J. (1984) · Biochemical Journal · doi:10.1042/bj2210885 · Cited by 37 · see citing works

Protease susceptibilities of HMW, 1α, 2α, but not 3α cartilage collagens are similar to type V collagen

Liotta, L. A., Kalebic, T., Reese, C. A., & Mayne, R. (1982) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(82)90664-7 · Cited by 25 · see citing works

Enzyme immunoassay for cathepsins B and L in synovial fluids from patients with arthritis

Maciewicz, R. A., & Etherington, D. J. (1988) · Biochemical Society Transactions · doi:10.1042/bst0160812 · Cited by 19 · see citing works

Smart nanoparticles for cancer therapy

Sun, L., Liu, H., Ye, Y., Lei, Y., Islam, R., Tan, S., Tong, R., Miao, Y.-B., & Cai, L. (2023) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-023-01642-x · Cited by 1,073 · see citing works

Synovial fibroblasts of patients with rheumatoid arthritis attach to and invade normal human cartilage when engrafted into SCID mice.

Müller‐Ladner, U., Kriegsmann, J., Franklin, B. N., Matsumoto, S., Geiler, T., Gay, R. E., & Gay, S. (1996) · Europe PMC (PubMed Central) · Cited by 606 · see citing works

Degradation of extracellular-matrix proteins by human cathepsin B from normal and tumour tissues

Buck, M., Karustis, D. G., Day, N. A., Honn, K. V., & Sloane, B. F. (1992) · Biochemical Journal · doi:10.1042/bj2820273 · Cited by 424 · see citing works

Human cathepsin K cleaves native type I and II collagens at the N-terminal end of the triple helix

Kafienah, W., Brömme, D., Buttle, D. J., Croucher, L. J., & Hollander, A. P. (1998) · Biochemical Journal · doi:10.1042/bj3310727 · Cited by 358 · see citing works

Cathepsin cysteine proteases in cardiovascular disease

Lutgens, S. P. M., Cleutjens, K. B. J. M., Daemen, M. J. A. P., & Heeneman, S. (2007) · The FASEB Journal · doi:10.1096/fj.06-7924com · Cited by 351 · see citing works

The interglobular domain of cartilage aggrecan is cleaved by PUMP, gelatinases, and cathepsin B.

Fosang, A., Neame, P. J., Last, K., Hardingham, T., Murphy, G., & Hamilton, J. A. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)41799-1 · Cited by 297 · see citing works

Molecular and cellular mechanisms of joint destruction in rheumatoid arthritis: two cellular mechanisms explain joint destruction?

Gay, S., Gay, R. E., & Koopman, W. J. (1993) · Annals of the Rheumatic Diseases · doi:10.1136/ard.52.suppl_1.s39 · Cited by 262 · see citing works

Effects of dietary arginine supplementation on growth performance, flesh quality, muscle antioxidant capacity and antioxidant-related signalling molecule expression in young grass carp (Ctenopharyngodon idella)

Wang, B., Liu, Y., Feng, L., Jiang, W., Kuang, S., Jiang, J., Li, S., Tang, L. Y., & Zhou, X. (2014) · Food Chemistry · doi:10.1016/j.foodchem.2014.06.091 · Cited by 249 · see citing works

Regulation of Collagenase Activities of Human Cathepsins by Glycosaminoglycans

Li, Z., Yasuda, Y., Li, W., Bogyo, M. S., Katz, N., Gordon, R. E., Fields, G. B., & Brömme, D. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m310349200 · Cited by 235 · see citing works

Metabolic changes associated with tumor metastasis, part 1: tumor pH, glycolysis and the pentose phosphate pathway

Payen, V. L., Porporato, P. E., Baselet, B., & Sonveaux, P. (2015) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-015-2098-5 · Cited by 219 · see citing works

Bone formation and resorption biological markers in cosmonauts during and after a 180-day space flight (Euromir 95)

Caillot‐Augusseau, A., Lafage‐Proust, M., Soler, C., Pernod, J., Dubois, F., & Alexandre, C. (1998) · Clinical Chemistry · doi:10.1093/clinchem/44.3.578 · Cited by 218 · see citing works

Different effects of bisphosphonate and estrogen therapy on free and peptide-bound bone cross-links excretion

Garnero, P., Gineyts, É., Arbault, P., Christiansen, C., & Delmas, P. D. (1995) · Journal of Bone and Mineral Research · doi:10.1002/jbmr.5650100418 · Cited by 215 · see citing works

Cathepsin B expression in colorectal carcinomas correlates with tumor progression and shortened patient survival.

Campo, E., Muñoz, J., Miquel, R., Palacı́n, A., Cardesa, A., Sloane, B. F., & Emmert‐Buck, M. R. (1994) · PubMed Central · Cited by 214 · see citing works

Cathepsin L targeting in cancer treatment

Sudhan, D. R., & Siemann, D. W. (2015) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2015.08.007 · Cited by 210 · see citing works

Cathepsin B: A sellsword of cancer progression

Mijanović, O., Branković, A., Panin, A. N., Savchuk, S., Timashev, P., Ulasov, I., & Lesniak, M. S. (2019) · Cancer Letters · doi:10.1016/j.canlet.2019.02.035 · Cited by 205 · see citing works

Alterations in extracellular matrix composition during aging and photoaging of the skin

McCabe, M. C., Hill, R. C., Calderone, K., Cui, Y., Yan, Y., Quan, T., Fisher, G. J., & Hansen, K. C. (2020) · Matrix Biology Plus · doi:10.1016/j.mbplus.2020.100041 · Cited by 189 · see citing works

C ysteine P eptidases of M ammals: T heir B iological R oles and P otential E ffects in the O ral C avity and O ther T issues in H ealth and D isease

Dickinson, D. P. (2002) · Critical Reviews in Oral Biology & Medicine · doi:10.1177/154411130201300304 · Cited by 179 · see citing works

Molecular cloning of human cathepsin O, a novel endoproteinase and homologue of rabbit OC2

Shi, G., Chapman, H. A., Bhairi, S. M., DeLeeuw, C., Reddy, V. Y., & Weiss, S. J. (1995) · FEBS Letters · doi:10.1016/0014-5793(94)01349-6 · Cited by 174 · see citing works

An intracellular form of cathepsin B contributes to invasiveness in cancer.

Szpaderska, A. M., & Frankfater, A. (2001) · PubMed · Cited by 168 · see citing works

Effective activation of the proenzyme form of the urokinase‐type plasminogen activator (pro‐uPA) by the cysteine protease cathepsin L

Goretzki, L., Schmitt, M., Mann, K., Calvete, J. J., Chucholowski, N., Kramer, M. D., Günzler, W. A., Jänicke, F., & Graeff, H. (1992) · FEBS Letters · doi:10.1016/0014-5793(92)80339-i · Cited by 161 · see citing works

Cathepsin B in synovial cells at the site of joint destruction in rheumatoid arthritis

Trabandt, A., Gay, R. E., Fassbender, H., & Gay, S. (1991) · Arthritis & Rheumatism · doi:10.1002/art.1780341116 · Cited by 160 · see citing works

The Role of Cysteine Cathepsins in Cancer Progression and Drug Resistance

Rudzińska, M., Parodi, A., Soond, S. M., Винаров, А. З., Korolev, D. O., Morozov, A., Dağlıoğlu, C., Tutar, Y., & Zamyatnin, A. A. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20143602 · Cited by 155 · see citing works

Molecular Regulation of Human Cathepsin B: Implication in Pathologies

Yan, S., & Sloane, B. F. (2003) · Biological Chemistry · doi:10.1515/bc.2003.095 · Cited by 153 · see citing works

Expression of Rat Cathepsin S in Phagocytic Cells

Petanceska, S. S., Canoll, P., & Devi, L. A. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.8.4403 · Cited by 151 · see citing works

Exocytosis of active cathepsin B

Linebaugh, B. E., Sameni, M., Day, N. A., Sloane, B. F., & Keppler, D. (1999) · European Journal of Biochemistry · doi:10.1046/j.1432-1327.1999.00582.x · Cited by 148 · see citing works

Expression of the Collagenolytic and Ras-Induced Cysteine Proteinase Cathepsin L and Proliferation-Associated Oncogenes in Synovial Cells of MRL/I Mice and Patients with Rheumatoid Arthritis

Trabandt, A., Aicher, W. K., Gay, R. E., Sukhatme, V. P., Nilson-Hamilton, M., Hamilton, R. T., McGhee, J. R., Fassbender, H. G., & Gay, S. (1990) · Matrix · doi:10.1016/s0934-8832(11)80142-3 · Cited by 142 · see citing works

Nutritive values, flavor amino acids, healthcare fatty acids and flesh quality improved by manganese referring to up-regulating the antioxidant capacity and signaling molecules TOR and Nrf2 in the muscle of fish

Jiang, W., Wu, P., Tang, R.-J., Liu, Y., Kuang, S., Jiang, J., Tang, L. Y., Tang, W., Zhang, Y., Zhou, X., et al. (2016) · Food Research International · doi:10.1016/j.foodres.2016.09.020 · Cited by 128 · see citing works

The pathobiology of osteoarthritis and the rationale for the use of pentosan polysulfate for its treatment

Ghosh, P. B. (1999) · Seminars in Arthritis and Rheumatism · doi:10.1016/s0049-0172(99)80021-3 · Cited by 125 · see citing works

Aberrant cancer metabolism in epithelial–mesenchymal transition and cancer metastasis: Mechanisms in cancer progression

Huang, R., & Zong, X. (2017) · Critical Reviews in Oncology/Hematology · doi:10.1016/j.critrevonc.2017.04.005 · Cited by 115 · see citing works

Human tumour cathepsin B. Comparison with normal liver cathepsin B

Moin, K., Day, N. A., Sameni, M., Hasnain, S., Hirama, T., & Sloane, B. F. (1992) · Biochemical Journal · doi:10.1042/bj2850427 · Cited by 113 · see citing works

Cathepsin B aggravates coxsackievirus B3-induced myocarditis through activating the inflammasome and promoting pyroptosis

Wang, Y., Jia, L., Shen, J. H., Wang, Y., Fu, Z., Su, S., Cai, Z., Wang, J.-A., & Xiang, M. (2018) · PLoS Pathogens · doi:10.1371/journal.ppat.1006872 · Cited by 106 · see citing works

Selective induction of the secretion of cathepsins B and L by cytokines in synovial fibroblast-like cells.

Lemaire, R., Huet, G., Zerimech, F., Grard, G., Fontaine, C., Duquesnoy, B., & Flipo, R. (1997) · Lara D. Veeken · doi:10.1093/rheumatology/36.7.735 · Cited by 98 · see citing works

Dietary nucleotides supplementation affect the physicochemical properties, amino acid and fatty acid constituents, apoptosis and antioxidant mechanisms in grass carp (Ctenopharyngodon idellus) muscle

Tie, H., Wu, P., Jiang, W., Liu, Y., Kuang, S., Zeng, Y.-Y., Jiang, J., Tang, L. Y., Zhou, X., & Feng, L. (2018) · Aquaculture · doi:10.1016/j.aquaculture.2018.12.045 · Cited by 96 · see citing works

Cathepsin B Gene Knockout Improves Behavioral Deficits and Reduces Pathology in Models of Neurologic Disorders

Hook, G., Reinheckel, T., Ni, J., Wu, Z., Kindy, M. S., Peters, C., & HOOK, V. Y. H. (2022) · Pharmacological Reviews · doi:10.1124/pharmrev.121.000527 · Cited by 95 · see citing works

Epigenetic Silencing of the Tumor Suppressor Cystatin M Occurs during Breast Cancer Progression

Ai, L., Kim, W.-J., Kim, T., Fields, C. R., Massoll, N. A., Robertson, K. D., & Brown, K. D. (2006) · Cancer Research · doi:10.1158/0008-5472.can-06-0576 · Cited by 90 · see citing works

Comparative Localization of Cathepsin B Protein and Activity in Colorectal Cancer

Hazen, L. G. M., Bleeker, F. E., Lauritzen, B., Bahns, S., Song, J., Jonker, A., Driel, B. E. M. V., Lyon, H., Hansen, U., Köhler, A., et al. (2000) · Journal of Histochemistry & Cytochemistry · doi:10.1177/002215540004801012 · Cited by 90 · see citing works

Up regulation of cathepsin K expression in articular chondrocytes in a transgenic mouse model for osteoarthritis

Morko, J. P., Söderström, M., Säämänen, A.-M. K., Salminen, H. J., & Vuorio, E. I. (2004) · Annals of the Rheumatic Diseases · doi:10.1136/ard.2002.004671 · Cited by 89 · see citing works

Sequence analysis, tissue distribution, and expression of rat cathepsin S.

Petanceska, S. S., & Devi, L. A. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)35713-2 · Cited by 89 · see citing works

Detection of Multiple Autoantibodies in Patients with Ankylosing Spondylitis Using Nucleic Acid Programmable Protein Arrays

Wright, C., Sibani, S., Trudgian, D. C., Fischer, R., Kessler, B. M., LaBaer, J., & Bowness, P. (2012) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m9.00384 · Cited by 81 · see citing works

Cystatin M suppresses the malignant phenotype of human MDA-MB-435S cells

Shridhar, R., Zhang, J., Jin, S., Booth, B. A., Kevil, C. G., Sotiropoulou, G., Sloane, B. F., & Keppler, D. (2003) · Oncogene · doi:10.1038/sj.onc.1207340 · Cited by 77 · see citing works

Role of Cysteine Cathepsins in Extracellular Proteolysis

Brömme, D., & Wilson, S. C. (2011) · Springer eBooks · doi:10.1007/978-3-642-16861-1_2 · Cited by 75 · see citing works

Cathepsin L‐deficient mice exhibit abnormal skin and bone development and show increased resistance to osteoporosis following ovariectomy

Potts, W., Bowyer, J., Jones, H. B., Tucker, D. L., Freemont, A. J., Millest, A. J., Martin, C., Vernon, W., Neerunjun, D., Slynn, G., et al. (2004) · International Journal of Experimental Pathology · doi:10.1111/j.0959-9673.2004.00373.x · Cited by 75 · see citing works

The type II collagen fragments Helix-II and CTX-II reveal different enzymatic pathways of human cartilage collagen degradation

Tabassi, N. C.-B., Desmarais, S., Bay‐Jensen, A., Delaissé, J., Percival, M. D., & Garnero, P. (2008) · Osteoarthritis and Cartilage · doi:10.1016/j.joca.2008.02.008 · Cited by 73 · see citing works

Quantification of protease activities in synovial fluid from rheumatoid and osteoarthritis cases: comparison with antioxidant and free radical damage markers

Mantle, D., Falkous, G., & Walker, D. (1999) · Clinica Chimica Acta · doi:10.1016/s0009-8981(99)00055-8 · Cited by 72 · see citing works

The Potential Role of the Proteases Cathepsin D and Cathepsin L in the Progression and Metastasis of Epithelial Ovarian Cancer

Pranjol, M. Z. I., Gutowski, N. J., Hannemann, M. M., & Whatmore, J. L. (2015) · Biomolecules · doi:10.3390/biom5043260 · Cited by 71 · see citing works

The Role of Phagocyte Proteinases and Proteinase Inhibitors in Multiple Organ Failure

Jochum, M., Gippner‐Steppert, C., Machleidt, W., & Fritz, H. (1994) · American Journal of Respiratory and Critical Care Medicine · doi:10.1164/ajrccm/150.6_pt_2.s123 · Cited by 69 · see citing works

Matrix Metalloproteinase Dependent and Independent Collagen Degradation

Song, F. (2006) · Frontiers in bioscience · doi:10.2741/2036 · Cited by 67 · see citing works

Selective Neutral pH Inhibitor of Cathepsin B Designed Based on Cleavage Preferences at Cytosolic and Lysosomal pH Conditions

Yoon, M. C., Solania, A., Jiang, Z., Christy, M. P., Podvin, S., Mosier, C., Lietz, C. B., Ito, G., Gerwick, W. H., Wolan, D. W., et al. (2021) · ACS Chemical Biology · doi:10.1021/acschembio.1c00138 · Cited by 67 · see citing works

Dipeptidyl nitrile inhibitors of Cathepsin L

Asaad, N., Bethel, P. A., Coulson, M., Dawson, J. E., Ford, S. J., Gerhardt, S., Grist, M., Hamlin, G. A., James, M. J., Jones, E. V., et al. (2009) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2009.05.071 · Cited by 66 · see citing works

Identification of Key Genes and Pathways in Cervical Cancer by Bioinformatics Analysis

Wu, X., Peng, L., Zhang, Y., Chen, S., Lei, Q., Li, G., & Zhang, C. (2019) · International Journal of Medical Sciences · doi:10.7150/ijms.34172 · Cited by 66 · see citing works

Detecting cathepsin activity in human osteoarthritis via activity-based probes

Ben-Aderet, L., Merquiol, E., Fahham, D., Kumar, A., Reich, E., Ben‐Nun, Y., Kandel, L., Haze, A., Liebergall, M., Kosinska, M. K., et al. (2015) · Arthritis Research & Therapy · doi:10.1186/s13075-015-0586-5 · Cited by 65 · see citing works

Detection of collagenase-induced damage of collagen by 9A4, a monoclonal C-terminal neoepitope antibody

Otterness, I. G., Downs, J. T., Lane, C. L., Bliven, M. L., Stukenbrok, H., Scampoli, D. N., Milici, A. J., & Mézeš, P. (1999) · Matrix Biology · doi:10.1016/s0945-053x(99)00026-8 · Cited by 65 · see citing works

Cyclic AMP-dependent protein kinase activation of cystic fibrosis transmembrane conductance regulator chloride channels in planar lipid bilayers.

Tilly, B. C., Winter, M. C., Ostedgaard, L. S., O’Riordan, C. R., Smith, A. E., & Welsh, M. J. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)50113-2 · Cited by 61 · see citing works

Bone Disease in Rheumatological Disorders

Goldring, S. R., & Polisson, R. P. (1998) · Elsevier eBooks · doi:10.1016/b978-012068700-8/50022-0 · Cited by 58 · see citing works

Stimulation of the secretion of latent cysteine proteinase activity by tumor necrosis factor α and interleukin‐1

Huet, G., Flipo, R., Colin, C., Janin, A., Hémon, B., Collyn-d'Hooghe, M., Lafyatis, R., Duquesnoy, B., & Degand, P. (1993) · Arthritis & Rheumatism · doi:10.1002/art.1780360606 · Cited by 57 · see citing works

Targeting cathepsin L (CL) by specific ribozymes decreases CL protein synthesis and cartilage destruction in rheumatoid arthritis

Schedel, J., Seemayer, C. A., Pap, T., Neidhart, M., Kuchen, S., Michel, B. A., Gay, R. E., Müller‐Ladner, U., Gay, S., & Zacharias, W. (2004) · Gene Therapy · doi:10.1038/sj.gt.3302265 · Cited by 57 · see citing works

Characterisation of fibroblast-like cells in pannus lesions of patients with rheumatoid arthritis sharing properties of fibroblasts and chondrocytes

Xue, C., Takahashi, M., Hasunuma, T., Aono, H., Yamamoto, K., Yoshino, S., Sumida, T., & Nishioka, K. (1997) · Annals of the Rheumatic Diseases · doi:10.1136/ard.56.4.262 · Cited by 56 · see citing works

Synthesis and optimization of hyaluronic acid–methotrexate conjugates to maximize benefit in the treatment of osteoarthritis

Homma, A., Sato, H., Tamura, T., Okamachi, A., Emura, T., Ishizawa, T., Kato, T., Matsuura, T., Sato, S., Higuchi, Y., et al. (2009) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2009.12.053 · Cited by 53 · see citing works

Characterization of Type XI Collagen-Glycosaminoglycan Interactions

Vaughan‐Thomas, A., Young, R. D., Phillips, A. C., & Duance, V. C. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m008764200 · Cited by 53 · see citing works

Localization of Cathepsins D, K, and L in Degenerated Human Intervertebral Discs

Ariga, K., Yonenobu, K., Nakase, T., Kaneko, M., Okuda, S., Uchiyama, Y., & Yoshikawa, H. (2001) · Spine · doi:10.1097/00007632-200112150-00007 · Cited by 52 · see citing works

Cathepsin B: Basis Sequence: Mouse.

Cavallo‐Medved, D., Moin, K., & Sloane, B. F. (2011) · PubMed · Cited by 51 · see citing works

Peptidyl fluoromethyl ketones as inhibitors of cathepsin B

Ahmed, N. K., Martin, L. A., Watts, L. M., Palmer, J. T., Thornburg, L. P., Prior, J. J., & Esser, R. E. (1992) · Biochemical Pharmacology · doi:10.1016/0006-2952(92)90385-v · Cited by 51 · see citing works

Cathepsin B: The dawn of tumor therapy

Liu, F., Zhou, T., Zhang, S., Li, Y., Chen, Y., Miao, Z., Wang, X., Yang, G., Liu, Y., Zhang, L., et al. (2024) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2024.116329 · Cited by 50 · see citing works

Macrophage cathepsin L, a factor in the erosion of subchondral bone in rheumatoid arthritis

Iwata, Y., Mort, J. S., 立石, 博., & Lee, E. R. (1997) · Arthritis & Rheumatism · doi:10.1002/art.1780400316 · Cited by 50 · see citing works

Extracellular-matrix degradation at acid pH. Avian osteoclast acid collagenase isolation and characterization

Blair, H. C., Teitelbaum, S. L., Grosso, L. E., Lacey, D. L., Tan, H., McCourt, D. W., & Jeffrey, J. J. (1993) · Biochemical Journal · doi:10.1042/bj2900873 · Cited by 50 · see citing works

Cathepsins B and L in synovial fluids from patients with rheumatoid arthritis and the effect of cathepsin B on the activation of pro-urokinase.

Ikeda, Y., Ikata, T., Mishiro, T., Nakano, S., Ikebe, M., & Yasuoka, S. (2000) · PubMed · Cited by 49 · see citing works

Oncogene activation in rheumatoid synovium

Trabandt, A., Gay, R. E., & Gay, S. (1992) · Apmis · doi:10.1111/j.1699-0463.1992.tb04012.x · Cited by 49 · see citing works

Methylation-dependent silencing of CST6 in primary human breast tumors and metastatic lesions

Rivenbark, A. G., Livasy, C., Boyd, C., Keppler, D., & Coleman, W. B. (2007) · Experimental and Molecular Pathology · doi:10.1016/j.yexmp.2007.03.008 · Cited by 46 · see citing works

Complete degradation of type X collagen requires the combined action of interstitial collagenase and osteoclast-derived cathepsin-B.

Sires, U. I., Schmid, T. M., Fliszar, C. J., Wang, Z. Q., Gluck, S. L., & Welgus, H. G. (1995) · Journal of Clinical Investigation · doi:10.1172/jci117896 · Cited by 46 · see citing works

Identification and characterization of a novel human cathepsin L splice variant

Arora, S., & Chauhan, S. S. (2002) · Gene · doi:10.1016/s0378-1119(02)00700-x · Cited by 44 · see citing works

Evidence for Cross‐Talk Between Sertoli and Germ Cells Using Selected Cathepsins as Markers

Chung, S. S. W., Zhu, L.-J., Mo, M., Silvestrini, B., Lee, W. M., & Cheng, C. Y. (1998) · Journal of Andrology · doi:10.1002/j.1939-4640.1998.tb02078.x · Cited by 43 · see citing works

The relationship between gingival crevicular fluid cathepsin B activity and periodontal attachment loss in chronic periodontitis patients: a 2‐year longitudinal study

Eley, B. M., & Cox, S. W. (1996) · Journal of Periodontal Research · doi:10.1111/j.1600-0765.1996.tb00507.x · Cited by 39 · see citing works

Cathepsin B Dipeptidyl Carboxypeptidase and Endopeptidase Activities Demonstrated across a Broad pH Range

Yoon, M. C., HOOK, V. Y. H., & O’Donoghue, A. J. (2022) · Biochemistry · doi:10.1021/acs.biochem.2c00358 · Cited by 37 · see citing works

Cysteine and serine proteases of synovial tissue in rheumatoid arthritis and osteoarthritis

Solau‐Gervais, E., Zerimech, F., Lemaire, R., Fontaine, C., Huet, G., & Flipo, R. (2007) · Scandinavian Journal of Rheumatology · doi:10.1080/03009740701340172 · Cited by 36 · see citing works

Enhancement of flavor and healthcare substances, mouthfeel parameters and collagen synthesis in the muscle of on-growing grass carp (Ctenopharyngodon idella) fed with graded levels of glutamine

Ma, X., Feng, L., Wu, P., Liu, Y., Kuang, S., Tang, L. Y., Zhou, X., & Jiang, W. (2020) · Aquaculture · doi:10.1016/j.aquaculture.2020.735486 · Cited by 36 · see citing works

Cathepsin B in Osteoarthritis: Uncontrolled Proteolysis in the Wrong Place

Baici, A., Lang, A., Zwicky, R., & Müntener, K. (2004) · Seminars in Arthritis and Rheumatism · doi:10.1016/j.semarthrit.2004.03.008 · Cited by 36 · see citing works

Guanidinoacetic acid supplementation totally based on vegetable meal diet improved the growth performance, muscle flavor components and sensory characteristics of on-growing grass carp (Ctenopharygodon idella)

Yang, L.-L., Wu, P., Feng, L., Jiang, W., Liu, Y., Kuang, S., Tang, L., & Zhou, X. (2020) · Aquaculture · doi:10.1016/j.aquaculture.2020.735841 · Cited by 34 · see citing works

Synthesis and biochemical evaluation of benzoylbenzophenone thiosemicarbazone analogues as potent and selective inhibitors of cathepsin L

Parker, E. N., Song, J.-L., Kumar, G. D. K., Odutola, S. O., Chavarria, G. E., Charlton-Sevcik, A. K., Strecker, T. E., Barnes, A. L., Sudhan, D. R., Wittenborn, T. R., et al. (2015) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2015.09.036 · Cited by 33 · see citing works

Upregulation of distinct collagen transcripts in post-surgery scar tissue: a study of conjunctival fibrosis

Seet, L., Toh, L. Z., Chu, S. W. L., Finger, S. N., Chua, J., & Wong, T. T. L. (2017) · Disease Models & Mechanisms · doi:10.1242/dmm.028555 · Cited by 33 · see citing works

Expression of cathepsins B, D and L in mouse corneas infected withPseudomonas aeruginosa

Dong, Z., Katar, M., Linebaugh, B. E., Sloane, B. F., & Berk, R. S. (2001) · European Journal of Biochemistry · doi:10.1046/j.0014-2956.2001.02607.x · Cited by 33 · see citing works

Cathepsin L in metastatic bone disease: therapeutic implications

Leto, G., Sepporta, M. V., Crescimanno, M., Flandina, C., & Tumminello, F. M. (2010) · Biological Chemistry · doi:10.1515/bc.2010.069 · Cited by 32 · see citing works

Cathepsin B activity in normal human osteoblast-like cells and human osteoblastic osteosarcoma cells (MG-63) : regulation by interleukin-1 β and parathyroid hormone

Aisa, M. C. (1996) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/0304-4165(95)00182-4 · Cited by 31 · see citing works

Temporal pattern of cysteine endopeptidase (cathepsin B) expression in cartilage and synovium from rabbit knees with experimental osteoarthritis: gene expression in chondrocytes in response to interleukin-1 and matrix depletion

Mehraban, F., Tindal, M. H., Proffitt, M., & Moskowitz, R. W. (1997) · Annals of the Rheumatic Diseases · doi:10.1136/ard.56.2.108 · Cited by 29 · see citing works

Proteolytic Enzymes in Inflammatory Bowel Disease

MacDonald, T. T., & Pender, S. L. F. (1998) · Inflammatory Bowel Diseases · doi:10.1002/ibd.3780040211 · Cited by 29 · see citing works

DO NONIMMUNOLOGICALLY MEDIATED PATHWAYS PLAY A ROLE IN THE PATHOGENESIS OF RHEUMATOID ARTHRITIS?

Koopman, W. J., & Gay, S. (1993) · Rheumatic Disease Clinics of North America · doi:10.1016/s0889-857x(21)00170-8 · Cited by 29 · see citing works

Variation patterns of two degradation enzyme systems in articular cartilage in different stages of osteoarthritis: Regulation by dehydroepiandrosterone

Bao, J., Chen, W., Feng, J., Zhao, J., Shi, Z., Huang, K., & Wu, L. (2009) · Clinica Chimica Acta · doi:10.1016/j.cca.2009.06.040 · Cited by 28 · see citing works

Cysteine proteinases in arthritis and inflammation

Müller‐Ladner, U., Gay, R. E., & Gay, S. (1996) · Perspectives in Drug Discovery and Design · doi:10.1007/bf02174047 · Cited by 28 · see citing works

Purification of guinea pig YKl40 and modulation of its secretion by cultured articular chondrocytes

Ceuninck, F. D., Pastoureau, P., Bouet, F., Bonnet, J., & Vanhoutte, P. M. (1998) · Journal of Cellular Biochemistry · doi:10.1002/(sici)1097-4644(19980615)69:4 · Cited by 27 · see citing works

Monoclonal Antibodies Against Cathepsin L and Procathepsin L of Different Species

Weber, E., Bahn, H., & GÜNTHER, D. (1997) · Hybridoma · doi:10.1089/hyb.1997.16.159 · Cited by 27 · see citing works

Aziridine‐2,3‐dicarboxylic Acid Derivatives as Inhibitors of Papain

Schirmeister, T. (1996) · Archiv der Pharmazie · doi:10.1002/ardp.19963290504 · Cited by 24 · see citing works

Regulation of Collagenolytic Protease Secretion through c-Src in Osteoclasts

Furuyama, N., & Fujisawa, Y. (2000) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.2000.2698 · Cited by 24 · see citing works

Immunolocalization of cathepsin B in equinedyschondroplastic articular cartilage

Hernández-Vidal, G., Jeffcott, L. B., & Davies, M. (1998) · The Veterinary Journal · doi:10.1016/s1090-0233(98)80122-6 · Cited by 22 · see citing works

The application of scanning confocal microscopy in cartilage research

Wotton, S. F., Jeacocke, R. E., Maciewicz, R. A., Wardale, R. J., & Duance, V. C. (1991) · The Histochemical Journal · doi:10.1007/bf01044964 · Cited by 22 · see citing works

Cathepsin L plays an active role in involution of the mouse mammary gland

Burke, M. A., Hutter, D., Reshamwala, R. P., & Knepper, J. E. (2003) · Developmental Dynamics · doi:10.1002/dvdy.10313 · Cited by 21 · see citing works

Alternative splicing of the 5′ region of cathepsin B pre‐messenger RNA in rheumatoid synovial tissue

Lemaire, R., Flipo, R., Migаud, H., Fontaine, C., Huet, G., Dacquembronne, E., & Lafyatis, R. (1997) · Arthritis & Rheumatism · doi:10.1002/art.1780400824 · Cited by 21 · see citing works

Long-Lasting Tissue Inflammatory Processes Trigger Autoimmune Responses to Extracellular Matrix Molecules

Bei, R., Masuelli, L., Palumbo, C., Tresoldi, I., Scardino, A., & Modesti, A. (2008) · International Reviews of Immunology · doi:10.1080/08830180801939280 · Cited by 20 · see citing works

Cathepsin B in gingival crevicular fluid of adult periodontitis patients: Identification by immunological and enzymological methods

市丸, 英., Tanoue, M., Tani, M., Tani, Y., Kaneko, T., Iwasaki, Y., Kunimatsu, K., & Kato, I. (1996) · Inflammation Research · doi:10.1007/bf02280991 · Cited by 20 · see citing works

Selective increased presentation of type II collagen by leupeptin

Manoury, B. (1997) · International Immunology · doi:10.1093/intimm/9.4.581 · Cited by 20 · see citing works

Modification of the Composition of Articular Cartilage Collagen Fibrils with Increasing Age

Vaughan‐Thomas, A., Dudhia, J., Bayliss, M. T., Kadler, K. E., & Duance, V. C. (2008) · Connective Tissue Research · doi:10.1080/03008200802325417 · Cited by 17 · see citing works

Cathepsin L Induces Proangiogenic Changes in Human Omental Microvascular Endothelial Cells via Activation of the ERK1/2 Pathway

Pranjol, M. Z. I., Gutowski, N. J., Hannemann, M. M., & Whatmore, J. L. (2018) · Current Cancer Drug Targets · doi:10.2174/1568009618666180831123951 · Cited by 16 · see citing works

Degradation of cartilage matrix components by the cysteine proteinases, cathepsins B and L.

Maciewicz, R. A., & Wotton, S. F. (1991) · PubMed · Cited by 43 · see citing works

Susceptibility of cartilage collagens type II, IX, X, and XI to human synovial collagenase and neutrophil elastase

Gadher, S. J., Eyre, D. R., Duance, V. C., Wotton, S. F., Heck, L. W., Schmid, T. M., & Woolley, D. E. (1988) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1988.tb14158.x · Cited by 73 · see citing works

Cartilage proteoglycan aggregate is degraded more extensively by cathepsin L than by cathepsin B.

Nguyen, Q. K., Mort, J. S., & Roughley, P. J. (1990) · Europe PMC (PubMed Central) · Cited by 91 · see citing works

Cathepsin B1. A lysosomal enzyme that degrades native collagen

Burleigh, M. C., Barrett, A. J., & Lazarus, G. S. (1974) · Biochemical Journal · doi:10.1042/bj1370387 · Cited by 407 · see citing works

Cathepsin K and the degradation of cartilage

Huppé, G. (2003) · eScholarship@McGill (McGill) · doi:10.82308/50288