Cystatin C Antagonizes Transforming Growth Factor β Signaling in Normal and Cancer Cells

Role of Transforming Growth Factor β in Human Disease

Blobe, G. C., Schiemann, W. P., & Lodish, H. F. (2000) · New England Journal of Medicine · doi:10.1056/nejm200005043421807 · Cited by 2,430 · see citing works

TGFβ Signaling in Growth Control, Cancer, and Heritable Disorders

Massagué, J., Blain, S. W., & Lo, R. S. (2000) · Cell · doi:10.1016/s0092-8674(00)00121-5 · Cited by 2,386 · see citing works

The microenvironment of the tumour–host interface

Liotta, L. A., & Kohn, E. C. (2001) · Nature · doi:10.1038/35077241 · Cited by 2,322 · see citing works

TGF-β Signaling in Tumor Suppression and Cancer Progression

Derynck, R., Akhurst, R. J., & Balmain, A. (2001) · Nature Genetics · doi:10.1038/ng1001-117 · Cited by 2,275 · see citing works

How cells read TGF-β signals

Massagué, J. (2000) · Nature Reviews Molecular Cell Biology · doi:10.1038/35043051 · Cited by 1,882 · see citing works

TGFβ signals through a heteromeric protein kinase receptor complex

Wrana, J. L., Attisano, L., Cárcamo, J. M., Zentella‐Dehesa, A., Doody, J. F., Laiho, M., Wang, X.-F., & Massagué, J. (1992) · Cell · doi:10.1016/0092-8674(92)90395-s · Cited by 1,528 · see citing works

Lysosomal cysteine proteases: more than scavengers

Turk, B., Turk, D., & Türk, V. (2000) · Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology · doi:10.1016/s0167-4838(99)00263-0 · Cited by 844 · see citing works

Cystatin C: An Improved Estimator of Glomerular Filtration Rate?

Laterza, O., Price, C. P., & Scott, M. G. (2002) · Clinical Chemistry · doi:10.1093/clinchem/48.5.699 · Cited by 654 · see citing works

The 2.0 A X‐ray crystal structure of chicken egg white cystatin and its possible mode of interaction with cysteine proteinases.

Bode, W., Engh, R. A., Müsil, D., Thiele, U., Huber, R., Karshikov, A., Brzin, J., Kos, J., & Türk, V. (1988) · The EMBO Journal · doi:10.1002/j.1460-2075.1988.tb03109.x · Cited by 591 · see citing works

Heterotypic Signaling between Epithelial Tumor Cells and Fibroblasts in Carcinoma Formation

Elenbaas, B., & Weinberg, R. A. (2001) · Experimental Cell Research · doi:10.1006/excr.2000.5133 · Cited by 557 · see citing works

The refined 2.4 A X‐ray crystal structure of recombinant human stefin B in complex with the cysteine proteinase papain: a novel type of proteinase inhibitor interaction.

Stubbs, M. T., Laber, B., Bode, W., Huber, R., Jerala, R., Lenar≷cic̆, B., & Türk, V. (1990) · The EMBO Journal · doi:10.1002/j.1460-2075.1990.tb08321.x · Cited by 494 · see citing works

Cystatin C deficiency in human atherosclerosis and aortic aneurysms

Shi, G.-P., Sukhova, G. K., GRUBB, A. O., Ducharme, A., Rhode, L. H., Lee, R. T., Ridker, P. M., Libby, P., & Chapman, H. A. (1999) · Journal of Clinical Investigation · doi:10.1172/jci7709 · Cited by 456 · see citing works

Synergistic cooperation of TFE3 and Smad proteins in TGF-β-induced transcription of the plasminogen activator inhibitor-1 genePreprint

Hua, X., Liu, X., Ansari, D. O., & Lodish, H. F. (1998) · Genes & Development · doi:10.1101/gad.12.19.3084 · Cited by 283 · see citing works

Fetuin/α2-HS Glycoprotein Is a Transforming Growth Factor-β Type II Receptor Mimic and Cytokine Antagonist

Demetriou, M., Binkert, C. A., Sukhu, B., Tenenbaum, H. C., & Dennis, J. W. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.22.12755 · Cited by 271 · see citing works

Pericellular cathepsin B and malignant progression

Roshy, S., Sloane, B. F., & Moin, K. (2003) · Cancer and Metastasis Reviews · doi:10.1023/a:1023007717757 · Cited by 224 · see citing works

α2-HS Glycoprotein/Fetuin, a Transforming Growth Factor-β/Bone Morphogenetic Protein Antagonist, Regulates Postnatal Bone Growth and Remodeling

Szweras, M., Liu, D., Partridge, E. A., Pawling, J., Sukhu, B., Clokie, C. M. L., Jahnen‐Dechent, W., Tenenbaum, H. C., Swallow, C. J., Grynpas, M. D., et al. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m112234200 · Cited by 214 · see citing works

Soluble Transforming Growth Factor-β Type II Receptor Inhibits Negative Remodeling, Fibroblast Transdifferentiation, and Intimal Lesion Formation But Not Endothelial Growth

Smith, J. D., Bryant, S. R., Couper, L. L., Vary, C., Gotwals, P. J., Koteliansky, V., & Lindner, V. (1999) · Circulation Research · doi:10.1161/01.res.84.10.1212 · Cited by 197 · see citing works

Cell surface complex of cathepsin B/annexin II tetramer in malignant progression

Mai, J., Waisman, D. M., & Sloane, B. F. (2000) · Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology · doi:10.1016/s0167-4838(99)00274-5 · Cited by 196 · see citing works

Lysosomal cathepsins: structure, role in antigen processing and presentation, and cancer

Türk, V., Turk, B., Gunčar, G., Turk, D., & Kos, J. (2002) · Advances in Enzyme Regulation · doi:10.1016/s0065-2571(01)00034-6 · Cited by 184 · see citing works

Cathepsins B, H, and L and their inhibitors stefin A and cystatin C in sera of melanoma patients.

Kos, J., Štabuc, B., Schweiger, A., Krašovec, M., Cimerman, N. G., Kopitar‐Jerala, N., & Vrhovec, I. (1997) · PubMed · Cited by 181 · see citing works

Cysteine Proteinases and Their Inhibitors in Extracellular Fluids: Markers for Diagnosis and Prognosis in Cancer

Kos, J., Werle, B., Lah, T. T., & Brünner, N. (2000) · The International Journal of Biological Markers · doi:10.1177/172460080001500116 · Cited by 178 · see citing works

Friends and relations of the cystatin superfamily—new members and their evolution

Brown, W. M., & Dzięgielewska, K. M. (1997) · Protein Science · doi:10.1002/pro.5560060102 · Cited by 172 · see citing works

Activation of TGF-β by Leishmania chagasi : Importance for Parasite Survival in Macrophages

Gantt, K. R., Schultz‐Cherry, S., Rodríguez, N. E., Jerônimo, S. M. B., Nascimento, E. T., Goldman, T. L., Recker, T. J., Miller, M. A., & Wilson, M. E. (2003) · The Journal of Immunology · doi:10.4049/jimmunol.170.5.2613 · Cited by 171 · see citing works

Context-specific Effects of Fibulin-5 (DANCE/EVEC) on Cell Proliferation, Motility, and Invasion

Schiemann, W. P., Blobe, G. C., Kalume, D. E., Pandey, A., & Lodish, H. F. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m200148200 · Cited by 164 · see citing works

Immunomodulatory properties of cystatins

Vray, B., Hartmann, S., & Hoebeke, J. (2002) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-002-8525-4 · Cited by 161 · see citing works

SPARC Inhibits Epithelial Cell Proliferation in Part through Stimulation of the Transforming Growth Factor-β–Signaling System

Schiemann, B. J., Neil, J. R., & Schiemann, W. P. (2003) · Molecular Biology of the Cell · doi:10.1091/mbc.e03-01-0001 · Cited by 159 · see citing works

Imaging Proteolysis by Living Human Breast Cancer Cells

Sameni, M., Moin, K., & Sloane, B. F. (2000) · Neoplasia · doi:10.1038/sj.neo.7900116 · 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

Urokinase Plasminogen Activator System

Choong, P., & Nadesapillai, A. P. W. (2003) · Clinical Orthopaedics and Related Research · doi:10.1097/01.blo0000093845.72468.bd · Cited by 147 · see citing works

Intracellular and extracellular cathepsin B facilitate invasion of MCF-10A neoT cells through reconstituted extracellular matrix in vitro

Premzl, A., Zavašnik‐Bergant, V., Türk, V., & Kos, J. (2003) · Experimental Cell Research · doi:10.1016/s0014-4827(02)00055-1 · Cited by 139 · see citing works

Serum Cystatin C, a New Marker of Glomerular Filtration Rate, Is Increased during Malignant Progression

Kos, J., Štabuc, B., Cimerman, N. G., & Brünner, N. (1998) · Clinical Chemistry · doi:10.1093/clinchem/44.12.2556 · Cited by 135 · see citing works

Regulation of Osteogenesis by Fetuin

Binkert, C. A., Demetriou, M., Sukhu, B., Szweras, M., Tenenbaum, H. C., & Dennis, J. W. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.40.28514 · Cited by 130 · see citing works

A Deletion in the Gene for Transforming Growth Factor β Type I Receptor Abolishes Growth Regulation by Transforming Growth Factor β in a Cutaneous T-Cell Lymphoma

Schiemann, W. P., Pfeifer, W. M., Levi, E., Kadin, M. E., & Lodish, H. F. (1999) · Blood · doi:10.1182/blood.v94.8.2854.420k07_2854_2861 · Cited by 127 · see citing works

Decreased metastatic spread in mice homozygous for a null allele of the cystatin C protease inhibitor gene.

Huh, C. G., Håkansson, K., Nathanson, C. M., Thorgeirsson, U. P., Jonsson, N., Grubb, A., Abrahamson, M., & Karlsson, S. (1999) · Molecular Pathology · doi:10.1136/mp.52.6.332 · Cited by 119 · see citing works

The Soluble Exoplasmic Domain of the Type II Transforming Growth Factor (TGF)-β Receptor

Lin, H. Y.-F., Moustakas, A., Knaus, P. I., Wells, R. G., Henis, Y. I., & Lodish, H. F. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.6.2747 · Cited by 117 · see citing works

Functional Analysis of Cathepsin B-like Cysteine Proteases fromLeishmania donovani Complex

Somanna, A., Mundodi, V., & Gedamu, L. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m203034200 · Cited by 104 · see citing works

TGF-β Signaling in Mammary Gland Development and Tumorigenesis

Wakefield, L. M., Piek, E., & Böttinger, E. P. (2001) · Journal of Mammary Gland Biology and Neoplasia · doi:10.1023/a:1009568532177 · Cited by 99 · see citing works

Transforming growth factor beta regulates cystatin C in serum-free mouse embryo (SFME) cells

Solem, M. L., Rawson, C. L., Lindburg, K., & Barnes, D. W. (1990) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(90)90767-h · Cited by 91 · see citing works

Phorbol Ester Activation of a Proteolytic Cascade Capable of Activating Latent Transforming Growth Factor-β

Guo, M., Mathieu, P., Linebaugh, B. E., Sloane, B. F., & Reiners, J. J. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m108180200 · Cited by 87 · see citing works

Immunohistochemical localization of cathepsin B in neoplastic human prostate

Sinha, A. A., Wilson, M. J., Reddy, P. K., Gleason, D. F., Sameni, M., & Sloane, B. F. (1995) · The Prostate · doi:10.1002/pros.2990260402 · Cited by 80 · see citing works

Cystatin C and cathepsin B in human colon carcinoma: Expression by cell lines and matrix degradation

Coriicchiato, O., Cajot, J. F., Abrahamson, M., Chan, S. J., Keppler, D., & Sordat, B. (1992) · International Journal of Cancer · doi:10.1002/ijc.2910520425 · Cited by 76 · see citing works

Modulation of cystatin C expression impairs the invasive and tumorigenic potential of human glioblastoma cells

Konduri, S. D., Yanamandra, N., Siddique, K., Joseph, A., Dinh, D. H., Olivero, W. C., Gujrati, M., Kouraklis, G. P., Swaroop, A., Kyritsis, A. P., et al. (2002) · Oncogene · doi:10.1038/sj.onc.1205949 · Cited by 74 · see citing works

Growth stimulation of 3T3 fibroblasts by Cystatin

Sun, Q. X. (1989) · Experimental Cell Research · doi:10.1016/0014-4827(89)90219-x · Cited by 70 · see citing works

Cell-surface cathepsin B: Understanding its functional significance

Cavallo‐Medved, D., & Sloane, B. F. (2003) · Current topics in developmental biology/Current Topics in Developmental Biology · doi:10.1016/s0070-2153(03)54013-3 · Cited by 66 · see citing works

Two‐step mechanism of inhibition of cathepsin B by cystatin C due to displacement of the proteinase occluding loop

Nycander, M., Estrada, S., Mort, J. S., Abrahamson, M., & Björk, I. (1998) · FEBS Letters · doi:10.1016/s0014-5793(97)01604-9 · Cited by 64 · see citing works

Serum cystatin C as a marker of glomerular filtration rate

Dworkin, L. D. (2001) · Current Opinion in Nephrology & Hypertension · doi:10.1097/00041552-200109000-00001 · Cited by 61 · see citing works

Differential Localization of Cysteine Protease Inhibitors and a Target Cysteine Protease, Cathepsin B, by Immuno-Confocal Microscopy

Calkins, C. C., Sameni, M., Koblinski, J. E., Sloane, B. F., & Moin, K. (1998) · Journal of Histochemistry & Cytochemistry · doi:10.1177/002215549804600607 · Cited by 59 · see citing works

Recombinant chicken egg white cystatin variants of the QLVSG region

Auerswald, E. A., GENENGER, G., Assfalg‐Machleidt, I., Machleidt, W., Engh, R. A., & Fritz, H. (1992) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1992.tb17355.x · Cited by 59 · see citing works

The Molecular Pathology of Hereditary Cystatin C Amyloid Angiopathy Causing Brain Hemorrhage

Ólafsson, Í., Thorsteinsson, L., & Jensson, Ó. (1996) · Brain Pathology · doi:10.1111/j.1750-3639.1996.tb00795.x · Cited by 58 · see citing works

Cathepsin B/Cystatin C Complex Levels in Sera from Patients with Lung and Colorectal Cancer

Zore, I., Kraovec, M., Cimerman, N. G., Kuhelj, R., Werle, B., Nielsen, H. J., Brünner, N., & Kos, J. (2001) · Biological Chemistry · doi:10.1515/bc.2001.097 · Cited by 53 · see citing works

Phosphorylation of the human leukemia inhibitory factor (LIF) receptor by mitogen-activated protein kinase and the regulation of LIF receptor function by heterologous receptor activation.

Schiemann, W. P., Graves, L. M., Baumann, H., Morella, K. K., Gearing, D. P., Nielsen, M. D., Krebs, E. G., & Nathanson, N. M. (1995) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.92.12.5361 · Cited by 52 · see citing works

Constitutive expression of cytotoxic proteases and down-regulation of protease inhibitors in LGL leukemia

Kothapalli, R., Bailey, R. D., Kusmartseva, I., Mane, S., Epling‐Burnette, P. K., & Loughran, T. P. (2003) · International Journal of Oncology · doi:10.3892/ijo.22.1.33 · Cited by 50 · see citing works

Cystatin C secretion by rat glomerular mesangial cells: Autocrine loop for in vitro growth-promoting activity

Tavera, C., Leung-Tack, J., Prévot, D., Gensac, M.-C., Martínez, J., Fulcrand, P., & Collé, A. (1992) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(92)91842-e · Cited by 47 · see citing works

Inhibition of motility and invasion of B16 melanoma by the overexpression of cystatin C

Sexton, P. S., & Cox, J. L. (1997) · Melanoma Research · doi:10.1097/00008390-199704000-00002 · Cited by 40 · see citing works

Hairpin loop mutations of chicken cystatin have different effects on the inhibition of cathepsin B, cathepsin L and papain

Auerswald, E. A., Nägler, D. K., Assfalg‐Machleidt, I., Stubbs, M. T., Machleidt, W., & Fritz, H. (1995) · FEBS Letters · doi:10.1016/0014-5793(95)00175-9 · Cited by 40 · see citing works

Control and expression of cystatin C by mouse decidual cultures

Afonso, S., Tovar, C., Romagnano, L., & Babiarz, B. (2002) · Molecular Reproduction and Development · doi:10.1002/mrd.1142 · Cited by 28 · see citing works

Cystatin C and Cysteine Proteinases during the Development and Therapy of Lewis Lung Adenocarcinoma in Mice

Usova, T. A., Poteryaeva, O. N., Жанаева, С. Я., Ярыгина, Е. С., & Короленко, Т. А. (2003) · Bulletin of Experimental Biology and Medicine · doi:10.1023/a:1023462316317 · Cited by 7 · see citing works

Cystein Proteinase Inhibitor Stefin A as an Indicator of Efficiency of Tumor Treatment in Mice

Короленко, Т. А., Poteryaeva, O. N., Фаламеева, О. В., & Levina, O. A. (2003) · Bulletin of Experimental Biology and Medicine · doi:10.1023/a:1026084712399 · Cited by 5 · see citing works

Cystatin C in LS lymphosarcoma and HA-1 hepatoma treated with Ukrain and cyclophosphamide and involvement of apoptosis.

Короленко, Т. А., Poteryaeva, O. N., Djanayeva, S. J., Svechnikova, I., Каледин, В. И., Timofeyeva, O. A., Филипенко, М. Л., & Jw, N. (2000) · PubMed · Cited by 4 · see citing works

Untitled work

(1999) · doi:10.1002/(sici)1097-0215(19991112)83:4

multifunctional enzymes in cancer

Mohamed, M. M., & Sloane, B. F. (2006) · Nature reviews. Cancer · doi:10.1038/nrc1949 · Cited by 1,267 · see citing works

Role of transforming growth factor-β superfamily signaling pathways in human disease

Gordon, K. J., & Blobe, G. C. (2008) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2008.01.006 · Cited by 644 · see citing works

Cystatins: Biochemical and structural properties, and medical relevance

Türk, V. (2008) · Frontiers in bioscience · doi:10.2741/3089 · Cited by 361 · see citing works

Cathepsin S Controls Angiogenesis and Tumor Growth via Matrix-derived Angiogenic Factors

Wang, B., Sun, J., Kitamoto, S., Yang, M., GRUBB, A. O., Chapman, H. A., Kalluri, R., & Shi, G. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m509134200 · Cited by 291 · see citing works

A Helminth Immunomodulator Reduces Allergic and Inflammatory Responses by Induction of IL-10-Producing Macrophages

Schnoeller, C., Rausch, S., Pillai, S., Avagyan, A., Wittig, B. M., Loddenkemper, C., Hamann, A., Hamelmann, E. H., Lucius, R., & Hartmann, S. (2008) · The Journal of Immunology · doi:10.4049/jimmunol.180.6.4265 · Cited by 240 · see citing works

Critical Functions of the Lysosome in Cancer Biology

Davidson, S. M., & Heiden, M. G. V. (2016) · The Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev-pharmtox-010715-103101 · Cited by 209 · see citing works

Cystatin C: current position and future prospects

Séronie-Vivien, S., Delanaye, P., Piéroni, L., Mariat, C., Froissart, M., & Cristol, J. (2008) · Clinical Chemistry and Laboratory Medicine (CCLM) · doi:10.1515/cclm.2008.336 · Cited by 204 · see citing works

Glial influences on neural stem cell development: cellular niches for adult neurogenesis

Dengke, K., Ming, G., & Song, H. (2005) · Current Opinion in Neurobiology · doi:10.1016/j.conb.2005.08.003 · Cited by 202 · see citing works

Cystatins in Immune System

Magister, Š., & Kos, J. (2013) · Journal of Cancer · doi:10.7150/jca.5044 · Cited by 199 · see citing works

Tumor immunoediting and immunosculpting pathways to cancer progression

Reiman, J. M., Kmieciak, M., Manjili, M. H., & Knutson, K. L. (2007) · Seminars in Cancer Biology · doi:10.1016/j.semcancer.2007.06.009 · Cited by 196 · see citing works

Involvement of cystatin C in immunity and apoptosis

Zi, M., & Xu, Y. (2018) · Immunology Letters · doi:10.1016/j.imlet.2018.01.006 · Cited by 170 · see citing works

Mechanisms for Asporin Function and Regulation in Articular Cartilage

Nakajima, M., Kizawa, H., Saitoh, M., Kou, I., Miyazono, K., & Ikegawa, S. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m700522200 · Cited by 168 · see citing works

Fibulins 3 and 5 Antagonize Tumor Angiogenesis In vivo

Albig, A. R., Neil, J. R., & Schiemann, W. P. (2006) · Cancer Research · doi:10.1158/0008-5472.can-04-4096 · Cited by 162 · see citing works

Cystatin Superfamily

Ochieng, J., & Chaudhuri, G. (2010) · Journal of Health Care for the Poor and Underserved · doi:10.1353/hpu.0.0257 · Cited by 161 · see citing works

Towards novel anti-cancer strategies based on cystatin function

Keppler, D. (2006) · Cancer Letters · doi:10.1016/j.canlet.2005.04.001 · Cited by 147 · see citing works

Cysteine Cathepsins in Tumor-Associated Immune Cells

Jakoš, T., Pišlar, A. H., Jewett, A., & Kos, J. (2019) · Frontiers in Immunology · doi:10.3389/fimmu.2019.02037 · Cited by 145 · see citing works

Cystatin D is a candidate tumor suppressor gene induced by vitamin D in human colon cancer cells

Álvarez-Díaz, S., Valle, N., García, J. M., Peña, C., Freije, J. M. P., Quesada, V., Astudillo, A., Bonilla, F., López-Otı́n, C., & Múñoz, A. (2009) · Journal of Clinical Investigation · doi:10.1172/jci37205 · Cited by 134 · see citing works

A Helminth Immunomodulator Exploits Host Signaling Events to Regulate Cytokine Production in Macrophages

Klotz, C., Ziegler, T. R., Figueiredo, A. S., Rausch, S., Hepworth, M. R., Obsivac, N., Sers, C., Lang, R., Hammerstein, P., Lucius, R., et al. (2011) · PLoS Pathogens · doi:10.1371/journal.ppat.1001248 · Cited by 127 · see citing works

Differential gene expression profiling of short and long term denervated muscle

Batt, J. A. E., Bain, J. R., Gonçalves, J., Michalski, B., Plant, P. J., Fahnestock, M. L., & Woodgett, J. R. (2005) · The FASEB Journal · doi:10.1096/fj.04-3640fje · Cited by 119 · see citing works

Cystatin C is a disease‐associated protein subject to multiple regulation

Xu, Y., Ding, Y., Li, X., & Wu, X. (2015) · Immunology and Cell Biology · doi:10.1038/icb.2014.121 · Cited by 116 · see citing works

Hereditary Cystatin C Amyloid Angiopathy: Genetic, Clinical, and Pathological Aspects

Pálsdóttir, Á., Snorradóttir, Á. Ó., & Thorsteinsson, L. (2006) · Brain Pathology · doi:10.1111/j.1750-3639.2006.tb00561.x · Cited by 112 · see citing works

Cysteine Protease Cathepsins in Atherosclerotic Cardiovascular Diseases

Wu, H., Du, Q., Dai, Q., Ge, J., & Cheng, X. W. (2017) · Journal of Atherosclerosis and Thrombosis · doi:10.5551/jat.rv17016 · Cited by 111 · see citing works

Cystatins in cancer progression: More than just cathepsin inhibitors

Breznik, B., Mitrović, A., Lah, T. T., & Kos, J. (2019) · Biochimie · doi:10.1016/j.biochi.2019.05.002 · Cited by 106 · see citing works

Role of IL-10 in the progression of kidney disease

Sinuani, I., Beberashvili, I., Averbukh, Z., & Sandbank, J. (2013) · World Journal of Transplantation · doi:10.5500/wjt.v3.i4.91 · Cited by 102 · see citing works

Cathepsin S: investigating an old player in lung disease pathogenesis, comorbidities, and potential therapeutics

Brown, R., Nath, S., Lora, A., Samaha, G., Elgamal, Z., Kaiser, R., Taggart, C., Weldon, S., & Geraghty, P. (2020) · Respiratory Research · doi:10.1186/s12931-020-01381-5 · Cited by 82 · see citing works

LncRNA Snhg1, a non-degradable sponge for miR-338, promotes expression of proto-oncogene CST3 in primary esophageal cancer cells

Yan, Y., Fan, Q., Wang, L., Zhou, Y., Li, J., & Zhou, K. (2017) · Oncotarget · doi:10.18632/oncotarget.16189 · Cited by 100 · see citing works

Lysyl Oxidase Contributes to Mechanotransduction-Mediated Regulation of Transforming Growth Factor-β Signaling in Breast Cancer Cells

Taylor, M. A., Amin, J., Kirschmann, D. A., & Schiemann, W. P. (2011) · Neoplasia · doi:10.1593/neo.101086 · Cited by 95 · see citing works

On the role of cystatin C in cancer progression

Leto, G., Crescimanno, M., & Flandina, C. (2018) · Life Sciences · doi:10.1016/j.lfs.2018.04.013 · Cited by 84 · see citing works

Cystatin protease inhibitors and immune functions

Zavašnik‐Bergant, T. (2008) · Frontiers in bioscience · doi:10.2741/3028 · Cited by 83 · see citing works

The use of cystatin C to inhibit epithelial–mesenchymal transition and morphological transformation stimulated by transforming growth factor-β

Sokol, J. P., Neil, J. R., Schiemann, B. J., & Schiemann, W. P. (2005) · Breast Cancer Research · doi:10.1186/bcr1312 · Cited by 80 · see citing works

Role of Transforming Growth Factor-β In Cancer Progression

Galliher, A. J., Neil, J. R., & Schiemann, W. P. (2006) · Future Oncology · doi:10.2217/14796694.2.6.743 · Cited by 80 · see citing works

Cystatin C: A New Renal Marker and Its Potential Use in Small Animal Medicine

Ghys, L. F. E., Paepe, D., Smets, P. M. Y., Lefebvre, H., Delanghe, J., & Daminet, S. (2014) · Journal of Veterinary Internal Medicine · doi:10.1111/jvim.12366 · Cited by 79 · see citing works

Inhibitory properties of cystatin F and its localization in U937 promonocyte cells

Langerholc, T., Zavašnik‐Bergant, V., Turk, B., Türk, V., Abrahamson, M., & Kos, J. (2005) · FEBS Journal · doi:10.1111/j.1742-4658.2005.04594.x · Cited by 78 · see citing works

Mass spectrometric proteomics profiles of in vivo tumor secretomes: Capillary ultrafiltration sampling of regressive tumor masses

Huang, C., Ananthaswamy, H. N., Barnes, S., Ma, Y., Kawai, M., & Elmets, C. A. (2006) · PROTEOMICS · doi:10.1002/pmic.200600287 · Cited by 72 · see citing works

Association of Visceral and Subcutaneous Adiposity with Kidney Function

Young, J. A., Hwang, S., Sarnak, M. J., Hoffmann, U., Massaro, J. M., Levy, D. A., Benjamin, E. J., Larson, M. G., Vasan, R. S., O’Donnell, C. J., et al. (2008) · Clinical Journal of the American Society of Nephrology · doi:10.2215/cjn.02490508 · Cited by 71 · see citing works

Cathepsin L increases invasion and migration of B16 melanoma

Yang, Z. F., & Cox, J. L. (2007) · Cancer Cell International · doi:10.1186/1475-2867-7-8 · Cited by 70 · see citing works

Cystatins and cancer

James, L. C. (2009) · Frontiers in bioscience · doi:10.2741/3255 · Cited by 58 · see citing works

G-CSF induces a potentially tolerant gene and immunophenotype profile in T cells in vivo

Toh, H. C., Sun, L. J., Soe, Y., Wu, Y., Phoon, Y. P., Chia, W. K., Wu, J., Wong, K., & Tan, P. B. O. (2009) · Clinical Immunology · doi:10.1016/j.clim.2009.03.509 · Cited by 58 · see citing works

Cystatin C Rescues Degenerating Neurons in a Cystatin B-Knockout Mouse Model of Progressive Myoclonus Epilepsy

Kaur, G., Mohan, P. S., Pawlik, M., DeRosa, S., Fajiculay, J., Che, S., GRUBB, A. O., Ginsberg, S. D., Nixon, R. A., & Levy, E. (2010) · American Journal Of Pathology · doi:10.2353/ajpath.2010.100461 · Cited by 58 · see citing works

ERβ-mediated induction of cystatins results in suppression of TGFβ signaling and inhibition of triple-negative breast cancer metastasis

Reese, J. M., Bruinsma, E. S., Nelson, A. W., Chernukhin, I. V., Carroll, J. S., Li, Y., Subramaniam, M., Suman, V. J., Negron, V. C., Monroe, D. G., et al. (2018) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1807751115 · Cited by 58 · see citing works

Association of biological age with health outcomes and its modifiable factors

Liu, W., You, J., Ge, Y., Wu, B., Zhang, Y., Chen, S., Zhang, Y.-R., Huang, S., Ma, L., Feng, J., et al. (2023) · Aging Cell · doi:10.1111/acel.13995 · Cited by 56 · see citing works

Novel Egg White–based 3-D Cell Culture System

Kaipparettu, B. A., Kuiatse, I., Chan, B. T.-Y., Kaipparettu, M. B., Lee, A. V., & Oesterreich, S. (2008) · BioTechniques · doi:10.2144/000112883 · Cited by 55 · see citing works

High levels of cystatin C predict the metabolic syndrome: the prospective Malmö Diet and Cancer Study

Magnusson, M., Hedblad, B., Engström, G., Persson, M., Nilsson, P. M., & Melander, O. (2013) · Journal of Internal Medicine · doi:10.1111/joim.12051 · Cited by 54 · see citing works

Phosphoprotein Secretome of Tumor Cells as a Source of Candidates for Breast Cancer Biomarkers in Plasma

Zawadzka, A. M., Schilling, B., Cusack, M. P., Sahu, A. K., Drake, P. M., Fisher, S. J., Benz, C. C., & Gibson, B. W. (2014) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m113.035485 · Cited by 52 · see citing works

Is serum Cystatin-C a suitable marker of renal function in children?

Zaffanello, M., Franchini, M., & Fanos, V. (2007) · PubMed · Cited by 52 · see citing works

Macrophage responses to interferon-γ are dependent on cystatin C levels

Frendéus, K. H., Wallin, H., Janciauskiene, S., & Abrahamson, M. (2009) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2009.05.005 · Cited by 51 · see citing works

Reduction of Experimental Human Fibrosarcoma Lung Metastasis in Mice by Adenovirus-Mediated Cystatin C Overexpression in the Host

Kopitz, C., Anton, M., Gänsbacher, B., & Krüger, A. (2005) · Cancer Research · doi:10.1158/0008-5472.can-05-1572 · Cited by 51 · see citing works

Serum levels of cystatin C in patients with malignancy

Nakai, K., Kikuchi, M., Fujimoto, K., Kaneko, Y., Omori, S., Nakai, K., & Suwabe, A. (2008) · Clinical and Experimental Nephrology · doi:10.1007/s10157-008-0043-8 · Cited by 50 · see citing works

IL-10 Controls Cystatin C Synthesis and Blood Concentration in Response to Inflammation through Regulation of IFN Regulatory Factor 8 Expression

Xu, Y., Schnorrer, P., Proietto, A. I., Kowalski, G. M., Febbraio, M. A., Acha‐Orbea, H., Dickins, R. A., & Villadangos, J. A. (2011) · The Journal of Immunology · doi:10.4049/jimmunol.1001934 · Cited by 49 · see citing works

CST3 and GDF15 ameliorate renal fibrosis by inhibiting fibroblast growth and activation

Kim, Y.-I., Shin, H., Chun, Y., & Park, J. (2018) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2018.04.061 · Cited by 48 · see citing works

Cystatins – Extra- and intracellular cysteine protease inhibitors: High-level secretion and uptake of cystatin C in human neuroblastoma cells

Wallin, H., Bjarnadóttir, M., Vogel, L. K., Wassélius, J., Ekström, U., & Abrahamson, M. (2010) · Biochimie · doi:10.1016/j.biochi.2010.08.011 · Cited by 47 · see citing works

Cystatin F as a regulator of immune cell cytotoxicity

Kos, J., Nanut, M. P., Prunk, M., Sabotič, J., Dautović, E., & Jewett, A. (2018) · Cancer Immunology Immunotherapy · doi:10.1007/s00262-018-2165-5 · Cited by 46 · see citing works

Cystatin C as a p53‐inducible apoptotic mediator that regulates cathepsin L activity

Mori, J., Tanikawa, C., Funauchi, Y., Lo, P. H. Y., Nakamura, Y., & Matsuda, K. (2016) · Cancer Science · doi:10.1111/cas.12881 · Cited by 44 · see citing works

Epithelial cell-derived cytokines CST3 and GDF15 as potential therapeutics for pulmonary fibrosis

Kim, Y.-I., Shin, H., Chun, Y., Cho, C., Koh, J., Chung, D. H., & Park, J. (2018) · Cell Death and Disease · doi:10.1038/s41419-018-0530-0 · Cited by 43 · see citing works

Cystatins in non-small cell lung cancer: Tissue levels, localization and relation to prognosis

Werle, B., Schanzenbächer, U., Lah, T. T., Ebert, E., Jülke, B., Ébert, W., Fiehn, W., Kayser, K., Spieß, E., Abrahamson, M., et al. (2006) · Oncology Reports · doi:10.3892/or.16.4.647 · Cited by 42 · see citing works

Aging stem cells, latexin, and longevity

Liang, Y., & Zant, G. E. V. (2008) · Experimental Cell Research · doi:10.1016/j.yexcr.2008.01.032 · Cited by 42 · see citing works

Different Cysteine Proteinases Involved in Bone Resorption and Osteoclast Formation

Brage, M., Abrahamson, M., Lindström, V., GRUBB, A. O., & Lerner, U. H. (2005) · Calcified Tissue International · doi:10.1007/s00223-004-0043-y · Cited by 41 · see citing works

Influence of Thyroid Hormones and Transforming Growth Factor-β1 on Cystatin C Concentrations

Kotajima, N., Yanagawa, Y., Aoki, T., Tsunekawa, K., Morimura, T., Ogiwara, T., Nara, M., & Murakami, M. (2010) · Journal of International Medical Research · doi:10.1177/147323001003800418 · Cited by 41 · see citing works

Epigenetic regulation of cystatins in cancer

Ashley, G. R. (2009) · Frontiers in bioscience · doi:10.2741/3254 · Cited by 40 · see citing works

Moving from the Laboratory Bench to Patients’ Bedside: Considerations for Effective Therapy with Stem Cells

Sherman, L. S., Munoz, J. L., Patel, S. A., Dave, M. A., Paige, I., & Rameshwar, P. (2011) · Clinical and Translational Science · doi:10.1111/j.1752-8062.2011.00283.x · Cited by 39 · see citing works

Association Between Serum Cystatin C and Thyroid Diseases: A Systematic Review and Meta-Analysis

Xin, C., Xie, J., Fan, H., Sun, X., & Shi, B. (2021) · Frontiers in Endocrinology · doi:10.3389/fendo.2021.766516 · Cited by 39 · see citing works

Two Faces of Cathepsin D: Physiological Guardian Angel and Pathological Demon

Khalkhali‐Ellis, Z. (2014) · Biology and Medicine · doi:10.4172/0974-8369.1000206 · Cited by 38 · see citing works

Silencing of cystatin M in metastatic oral cancer cell line MDA-686Ln by siRNA increases cysteine proteinases and legumain activities, cell proliferation and in vitro invasion

Vigneswaran, N., Wu, J. G., Nagathihalli, N. S., James, R. I., Zeeuwen, P. L. J. M., & Zacharias, W. (2005) · Life Sciences · doi:10.1016/j.lfs.2005.05.096 · Cited by 34 · see citing works

Syndecan‐2 is a key regulator of transforming growth factor beta 2/smad2‐mediated adhesion in fibrosarcoma cells

Mytilinaiou, M. G., Bano, A., Nikitovic, D., Berdiaki, A., Voudouri, K., Kalogeraki, A. M., Karamanos, N. K., & Tzanakakis, G. N. (2013) · IUBMB Life · doi:10.1002/iub.1112 · Cited by 33 · see citing works

Cysteine proteinase inhibitors regulate human and mouse osteoclastogenesis by interfering with RANK signaling

Strålberg, F., Henning, P., Gjertsson, I., Kindlund, B., de Souza, P. C., Persson, E., Abrahamson, M., Kasprzykowski, F., GRUBB, A. O., & Lerner, U. H. (2013) · The FASEB Journal · doi:10.1096/fj.12-211748 · Cited by 33 · see citing works

Clinical Impact of Cystatin C/Cathepsin L and Follistatin/Activin A Systems in Breast Cancer Progression: A Preliminary Report

Leto, G., Incorvaia, L., Flandina, C., Ancona, C., Fulfaro, F., Crescimanno, M., Sepporta, M. V., & Badalamenti, G. (2016) · Cancer Investigation · doi:10.1080/07357907.2016.1222416 · Cited by 33 · see citing works

Cystatin C deficiency suppresses tumor growth in a breast cancer model through decreased proliferation of tumor cells

Završnik, J., Butinar, M., Prebanda, M. T., Krajnc, A., Vidmar, R., Fonovič, M., GRUBB, A. O., Türk, V., Turk, B., & Vasiljeva, O. S. (2017) · Oncotarget · doi:10.18632/oncotarget.17379 · Cited by 32 · see citing works

Circulating cathepsin K and cystatin C in patients with cancer related bone disease: Clinical and therapeutic implications

Tumminello, F. M., Flandina, C., Crescimanno, M., & Leto, G. (2007) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2007.07.001 · Cited by 32 · see citing works

Prognostic value of cystatin C in acute coronary syndromes: enhancer of atherosclerosis and promising therapeutic target

Ferraro, S., Marano, G., Biganzoli, E. M., Boracchi, P., & Bongo, A. S. (2011) · Clinical Chemistry and Laboratory Medicine (CCLM) · doi:10.1515/cclm.2011.607 · Cited by 32 · see citing works

Identification of the Amyloid β-Protein Precursor and Cystatin C as Novel Epidermal Growth Factor Receptor Regulated Secretory Proteins in Nasopharyngeal Carcinoma by Proteomics

Tang, C., Guan, Y., Yi, B., Li, X., Liang, K., Zou, H., Yi, H. L., Li, M., Zhang, P., Li, C., et al. (2010) · Journal of Proteome Research · doi:10.1021/pr100663p · Cited by 31 · see citing works

The protease inhibitor cystatin C down-regulates the release of IL-β and TNF-α in lipopolysaccharide activated monocytes

Gren, S. T., Janciauskiene, S. M., Salipalli, S., Jonigk, D. D., Kvist, P. H., Gerwien, J. G., Håkansson, K., & Grip, O. (2016) · Journal of Leukocyte Biology · doi:10.1189/jlb.5a0415-174r · Cited by 31 · see citing works

Clinicopathologic significance of cystatin C expression in gliomas

NAKABAYASHI, H., HARA, M., & Shimuzu, K. (2005) · Human Pathology · doi:10.1016/j.humpath.2005.06.021 · Cited by 31 · see citing works

Cathepsin S and its inhibitor cystatin C: imbalance in uveal melanoma

Paraoan, L. (2009) · Frontiers in bioscience · doi:10.2741/3393 · Cited by 29 · see citing works

The candidate tumor suppressor CST6 alters the gene expression profile of human breast carcinoma cells: Down-regulation of the potent mitogenic, motogenic, and angiogenic factor autotaxin

Song, J., Jie, C., Polk, P., Shridhar, R., Clair, T., Zhang, J., Yin, L., & Keppler, D. (2005) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2005.11.171 · Cited by 29 · see citing works

Cerebral malaria: insights from host-parasite protein-protein interactions

Rao, A., Kumar, M. K., Joseph, T., & Bulusu, G. (2010) · Malaria Journal · doi:10.1186/1475-2875-9-155 · Cited by 28 · see citing works

Cystatin C Deficiency Promotes Epidermal Dysplasia in K14-HPV16 Transgenic Mice

Yu, W., Liu, J., Shi, M. A., Wang, J., Xiang, M., Kitamoto, S., Wang, B., Sukhova, G. K., Murphy, G. F., Orasanu, G., et al. (2010) · PLoS ONE · doi:10.1371/journal.pone.0013973 · Cited by 28 · see citing works

Inhibition of invasion and metastasis of MHCC97H cells by expression of snake venom cystatin through reduction of proteinases activity and Epithelial-Mesenchymal Transition

Tang, N., Xie, Q., Wang, X., Li, X., Chen, Y., Lin, X., & Lin, J. (2011) · Archives of Pharmacal Research · doi:10.1007/s12272-011-0512-6 · Cited by 28 · see citing works

Berberine-loaded engineered nanoparticles attenuate TGF-β-induced remodelling in human bronchial epithelial cells

Rubis, G. D., Paudel, K. R., Liu, G., Agarwal, V., MacLoughlin, R. J., Pinto, T. D. J. A., Singh, S. K., Adams, J., Nammi, S., Chellappan, D. K., et al. (2023) · Toxicology in Vitro · doi:10.1016/j.tiv.2023.105660 · Cited by 27 · see citing works

Contribution of the MDRD Equation and of Cystatin C for Renal Function Estimates in Cancer Patients

Séronie-Vivien, S., Toullec, S., Malard, L., Thomas, F., Durrand, V., & Chatelut, É. (2006) · Medical Oncology · doi:10.1385/mo:23:1:63 · Cited by 27 · see citing works

Susceptibility to Salmonella carrier-state: A possible Th2 response in susceptible chicks

Chaussé, A., Grépinet, O., Bottreau, E., Robert, V., Hennequet‐Antier, C., Lalmanach, A.-C., Lecardonnel, J., Beaumont, C., & Velge, P. (2014) · Veterinary Immunology and Immunopathology · doi:10.1016/j.vetimm.2014.03.001 · Cited by 27 · see citing works

Low-level internalization of cystatin E/M affects legumain activity and migration of melanoma cells

Wallin, H., Apelqvist, J., Andersson, F., Ekström, U., & Abrahamson, M. (2017) · Journal of Biological Chemistry · doi:10.1074/jbc.m117.776138 · Cited by 26 · see citing works

Preoperative serum cystatin-C as a potential biomarker for prognosis of renal cell carcinoma

Guo, S., Xue, Y., He, Q., He, X., Guo, K., Dong, P., Yao, K., Yang, G., Chen, D., Li, Z., et al. (2017) · PLoS ONE · doi:10.1371/journal.pone.0178823 · Cited by 26 · see citing works

Type 2 Cystatins and Their Roles in the Regulation of Human Immune Response and Cancer Progression

Zhang, Z., & Zhan, F. (2023) · Cancers · doi:10.3390/cancers15225363 · Cited by 24 · see citing works

Preclinical Efficacy of Cystatin C to Target the Oncogenic Activity of Transforming Growth Factor β in Breast Cancer

Tian, M., & Schiemann, W. P. (2009) · Translational Oncology · doi:10.1593/tlo.09145 · Cited by 24 · see citing works

Isotope-coded protein label based quantitative proteomic analysis reveals significant up-regulation of apolipoprotein A1 and ovotransferrin in the myopic chick vitreous

Yu, F., Lam, T. C., Liu, L., Chun, R. K. M., Cheung, J. K.-W., Li, K. K., & To, C. H. (2017) · Scientific Reports · doi:10.1038/s41598-017-12650-7 · Cited by 24 · see citing works

The potential of cystatin C as a predictive biomarker in breast cancer

Leto, G., & Sepporta, M. V. (2020) · Expert Review of Anticancer Therapy · doi:10.1080/14737140.2020.1829481 · Cited by 24 · see citing works

Natural cystatin C fragments inhibit GPR15-mediated HIV and SIV infection without interfering with GPR15L signaling

Hayn, M., Blötz, A., Rodríguez, A., Vidal, S., Preising, N., Ständker, L., Wiese, S., Stürzel, C. M., Harms, M., Groß, R. M., et al. (2021) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2023776118 · Cited by 24 · see citing works

Targeted TGF-β chemotherapies: friend or foe in treating human malignancies?

Schiemann, W. P. (2007) · Expert Review of Anticancer Therapy · doi:10.1586/14737140.7.5.609 · Cited by 24 · see citing works

Aberrant cystatin‑C expression in blood from patients with breast cancer is a suitable marker for monitoring tumor burden

Kwon, W., Kim, T., Nahm, C., Moon, Y., & Kim, J. (2018) · Oncology Letters · doi:10.3892/ol.2018.9380 · Cited by 21 · see citing works

Detection of Cystatin C biomarker for clinical measurement of renal disease by developed ELISA diagnostic kits

Jiang, R., Xu, C., Zhou, X., Wang, T., & Yao, G. (2014) · Journal of Translational Medicine · doi:10.1186/1479-5876-12-205 · Cited by 21 · see citing works

Genetics of epilepsy: Epilepsy Research Foundation workshop report

Sisodiya, S. M., Cross, J. H., Blümcke, I., Chadwick, D. W., Craig, J. J., Crino, P. B., Debenham, P., Delanty, N., Elmslie, F., Gardiner, M., et al. (2007) · Epileptic Disorders · doi:10.1684/epd.2007.0107 · Cited by 21 · see citing works

Cystatin C level as a marker of renal function in allogeneic hematopoietic stem cell transplantation

Muto, H., Ohashi, K., Ando, M., Akiyama, H., & Sakamaki, H. (2010) · International Journal of Hematology · doi:10.1007/s12185-010-0521-0 · Cited by 20 · see citing works

Cystatins, cysteine peptidase inhibitors, as regulators of immune cell cytotoxicity

Prunk, M., Nanut, M. P., Sabotič, J., & Kos, J. (2017) · Periodicum Biologorum · doi:10.18054/pb.v118i4.4504 · Cited by 18 · see citing works

Cystatin C takes part in melanoma-microglia cross-talk: possible implications for brain metastasis

Moshe, A., Izraely, S., Sagi‐Assif, O., Prakash, R., Telerman, A., Meshel, T., Carmichael, S. T., & Witz, I. P. (2018) · Clinical & Experimental Metastasis · doi:10.1007/s10585-018-9891-0 · Cited by 18 · see citing works

Expression and significance of Cystatin-C in clear cell renal cell carcinoma

Guo, K., Chen, Q., He, X., Yao, K., Li, Z., Liu, Z., Chen, J., Liu, Z., Guo, C., Lu, J., et al. (2018) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2018.08.083 · Cited by 18 · see citing works

ISL2 is a putative tumor suppressor whose epigenetic silencing reprograms the metabolism of pancreatic cancer

Öztürk, H., Cingoz, H., Tufan, T., Yang, J., Adair, S. J., Tummala, K. S., Kuscu, C., Kinali, M., Cömertpay, G., Nagdas, S., et al. (2022) · Developmental Cell · doi:10.1016/j.devcel.2022.04.014 · Cited by 18 · see citing works

Urocortin 2 protects heart and kidney structure and function in an ovine model of acute decompensated heart failure: Comparison with dobutamine

Rademaker, M. T., Ellmers, L. J., Charles, C. J., & Richards, M. (2015) · International Journal of Cardiology · doi:10.1016/j.ijcard.2015.06.011 · Cited by 18 · see citing works

Structural Dynamics Investigation of Human Family 1 & 2 Cystatin-Cathepsin L1 Interaction: A Comparison of Binding Modes

Nandy, S. K., & Seal, A. (2016) · PLoS ONE · doi:10.1371/journal.pone.0164970 · Cited by 17 · see citing works

Variable expression of cystatin C in cultured trans-differentiating rat hepatic stellate cells

Gressner, A. M. (2006) · World Journal of Gastroenterology · doi:10.3748/wjg.v12.i5.731 · Cited by 16 · see citing works

Microcystin-LR-Induced Interaction between M2 Tumor-Associated Macrophage and Colorectal Cancer Cell Promotes Colorectal Cancer Cell Migration through Regulating the Expression of TGF-β1 and CST3

Jiang, X., Zhang, H., Zhang, H., Wang, F., Wang, X. C., Ding, T., Zhang, X., & Wang, T. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms241310527 · Cited by 15 · see citing works

Cystatin C antagonizes transforming growth factor beta signaling in normal and cancer cells.

Sokol, J. P., & Schiemann, W. P. (2004) · PubMed · Cited by 156 · see citing works

Cystatin C Antagonizes Transforming Growth Factor B Signaling in Normal and Cancer Cells

Sokol, J. P., & Schiemann, W. P. (2016)

Cystatin SN neutralizes the inhibitory effect of cystatin C on cathepsin B activity

Kim, J.-T., Lee, S.-J., Kang, M. A., Park, J. E., Kim, B.-Y., Dy, Y., Yang, Y. D., Lee, C.-H., Yeom, Y. I., Choe, Y.-K., et al. (2013) · Cell Death and Disease · doi:10.1038/cddis.2013.485 · Cited by 53 · see citing works

On the role of cystatin C in cancer progression

Leto, G., Crescimanno, M., & Flandina, C. (2018) · Life Sciences · doi:10.1016/j.lfs.2018.04.013 · Cited by 84 · see citing works

TGF-β Signaling, Activated Stromal Fibroblasts, and Cysteine Cathepsins B and L Drive the Invasive Growth of Human Melanoma Cells

Yin, M., Soikkeli, J., Jahkola, T., Virolainen, S., Saksela, O., & Hölttä, E. (2012) · American Journal Of Pathology · doi:10.1016/j.ajpath.2012.08.027 · Cited by 74 · see citing works