Cathepsin-sensitive nanoscale drug delivery systems for cancer therapy and other diseases

Magnetic iron oxide nanoparticles: Synthesis, stabilization, vectorization, physicochemical characterizations and biological applications

Laurent, S., Forge, D., Port, M., Roch, A., Robic, C., Vander Elst, L., & Muller, R. N. (2008) · Chemical Reviews · doi:10.1021/cr068445e · Cited by 6,852 · see citing works

Cancer nanomedicine: progress, challenges and opportunities

Shi, J., Kantoff, P. W., Wooster, R., & Farokhzad, O. C. (2017) · Nature Reviews Cancer · doi:10.1038/nrc.2016.108 · Cited by 5,873 · see citing works

On the size of the active site in proteases. I. Papain

Schechter, I., & Berger, A. (1967) · Biochemical and Biophysical Research Communications · doi:10.1016/s0006-291x(67)80055-x · Cited by 5,203 · see citing works

The golden age: gold nanoparticles for biomedicine

Dreaden, E. C., Alkilany, A. M., Huang, X., Murphy, C. J., & El‐Sayed, M. A. (2011) · Chemical Society Reviews · doi:10.1039/c1cs15237h · Cited by 3,572 · see citing works

Biodegradable nanoparticles for drug and gene delivery to cells and tissue

Panyam, J., & Labhasetwar, V. D. (2003) · Advanced Drug Delivery Reviews · doi:10.1016/s0169-409x(02)00228-4 · Cited by 3,365 · see citing works

The dawning era of polymer therapeutics

Duncan, R. (2003) · Nature Reviews Drug Discovery · doi:10.1038/nrd1088 · Cited by 3,273 · see citing works

Progress and challenges towards targeted delivery of cancer therapeutics

Rosenblum, D., Joshi, N., Tao, W., Karp, J. M., & Peer, D. (2018) · Nature Communications · doi:10.1038/s41467-018-03705-y · Cited by 2,220 · see citing works

Magnetic Nanoparticles: Design and Characterization, Toxicity and Biocompatibility, Pharmaceutical and Biomedical Applications

Reddy, L. H., Arias, J. L., Nicolas, J., & Couvreur, P. (2012) · Chemical Reviews · doi:10.1021/cr300068p · Cited by 2,106 · see citing works

Targeted Drug Delivery with Polymers and Magnetic Nanoparticles: Covalent and Noncovalent Approaches, Release Control, and Clinical Studies

Ulbrich, K., Holá, K., Šubr, V., Bakandritsos, A., Tuček, J., & Zbořil, R. (2016) · Chemical Reviews · doi:10.1021/acs.chemrev.5b00589 · Cited by 1,741 · see citing works

Four deaths and a funeral: from caspases to alternative mechanisms

Leist, M., & Jäättelä, M. (2001) · Nature Reviews Molecular Cell Biology · doi:10.1038/35085008 · Cited by 1,585 · see citing works

Cysteine cathepsins: From structure, function and regulation to new frontiers

Turk, V., Stoka, V., Vasiljeva, O., Renko, M., Sun, T., Turk, B., & Turk, D. (2012) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2011.10.002 · Cited by 1,377 · see citing works

Targeting proteases: successes, failures and future prospects

Turk, B. (2006) · Nature Reviews Drug Discovery · doi:10.1038/nrd2092 · Cited by 1,366 · see citing works

Biodegradable nanoparticles for drug delivery and targeting

Hans, M. L., & Lowman, A. M. (2002) · Current Opinion in Solid State and Materials Science · doi:10.1016/s1359-0286(02)00117-1 · Cited by 1,324 · see citing works

Drug targeting to tumors: Principles, pitfalls and (pre-) clinical progress

Lammers, T., Kiessling, F., Hennink, W. E., & Storm, G. (2012) · Journal of Controlled Release · doi:10.1016/j.jconrel.2011.09.063 · Cited by 1,324 · see citing works

Design, functionalization strategies and biomedical applications of targeted biodegradable/biocompatible polymer-based nanocarriers for drug delivery

Nicolas, J., Mura, S., Brambilla, D., Mackiewicz, N., & Couvreur, P. (2013) · Chem. Soc. Rev. · doi:10.1039/c2cs35265f · Cited by 1,270 · see citing works

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

Combinatorial drug therapy for cancer in the post-genomic era

Al-Lazikani, B., Banerji, U., & Workman, P. (2012) · Nature Biotechnology · doi:10.1038/nbt.2284 · Cited by 1,070 · see citing works

Designed synthesis of uniformly sized iron oxide nanoparticles for efficient magnetic resonance imaging contrast agents

Lee, N., & Hyeon, T. (2012) · Chem. Soc. Rev. · doi:10.1039/c1cs15248c · Cited by 995 · see citing works

Nanotechnology: Intelligent Design to Treat Complex Disease

Couvreur, P., & Vauthier, C. (2006) · Pharmaceutical Research · doi:10.1007/s11095-006-0284-8 · Cited by 950 · see citing works

Block copolymer micelles as vehicles for drug delivery

Kataoka, K., Kwon Glenn, S., Masayuki, Y., Teruo, O., & Sakurai, Y. (1993) · Journal of Controlled Release · doi:10.1016/0168-3659(93)90172-2 · Cited by 878 · see citing works

Sorting of lysosomal proteins

Braulke, T., & Bonifacino, J. S. (2008) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2008.10.016 · Cited by 873 · see citing works

Surface functionalization of nanoparticles for nanomedicine

Mout, R., Moyano, D. F., Rana, S., & Rotello, V. M. (2012) · Chemical Society Reviews · doi:10.1039/c2cs15294k · Cited by 806 · see citing works

Emerging roles of proteases in tumour suppression

López-Otı́n, C., & Matrisian, L. M. (2007) · Nature reviews. Cancer · doi:10.1038/nrc2228 · Cited by 805 · see citing works

The expanding role of prodrugs in contemporary drug design and development

Rautio, J., Meanwell, N. A., Di, L., & Hageman, M. J. (2018) · Nature Reviews Drug Discovery · doi:10.1038/nrd.2018.46 · Cited by 781 · see citing works

Cysteine cathepsin proteases: regulators of cancer progression and therapeutic response

Olson, O. C., & Joyce, J. A. (2015) · Nature reviews. Cancer · doi:10.1038/nrc4027 · Cited by 703 · see citing works

Phase I clinical and pharmacokinetic study of PK1 [N-(2-hydroxypropyl)methacrylamide copolymer doxorubicin]: first member of a new class of chemotherapeutic agents-drug-polymer conjugates. Cancer Research Campaign Phase I/II Committee.

Vasey, P. A., Kaye, S. B., Morrison, R. A., Twelves, C. J., Wilson, P., Duncan, R., Thomson, A. H., Murray, L. S., Hilditch, T. E., Murray, T., et al. (1999) · PubMed · Cited by 689 · see citing works

Nanoparticle-based combination therapy toward overcoming drug resistance in cancer

Hu, C. J., & Zhang, L. (2012) · Biochemical Pharmacology · doi:10.1016/j.bcp.2012.01.008 · Cited by 688 · see citing works

Dendrimers as Carriers for Delivery of Chemotherapeutic Agents

Medina, S. H., & ElSayed, M. E. H. (2009) · Chemical Reviews · doi:10.1021/cr900174j · Cited by 672 · see citing works

Phase I clinical trial and pharmacokinetic evaluation of NK911, a micelle-encapsulated doxorubicin

Matsumura, Y., Hamaguchi, T., Ura, T., Muro, K., Yamada, Y., Shimada, Y., Shirao, K., Okusaka, T., Ueno, H., Ikeda, M., et al. (2004) · British Journal of Cancer · doi:10.1038/sj.bjc.6602204 · Cited by 623 · see citing works

Self-assembled peptide-based nanostructures: Smart nanomaterials toward targeted drug delivery

Habibi, N., Kamaly, N., Memić, A., & Shafiee, H. (2016) · Nano Today · doi:10.1016/j.nantod.2016.02.004 · Cited by 622 · see citing works

Specialized roles for cysteine cathepsins in health and disease

Reiser, J., Adair, B. D., & Reinheckel, T. (2010) · Journal of Clinical Investigation · doi:10.1172/jci42918 · Cited by 582 · see citing works

Polymeric Conjugates for Drug Delivery

Larson, N., & Ghandehari, H. (2012) · Chemistry of Materials · doi:10.1021/cm2031569 · Cited by 580 · see citing works

HPMA copolymers: Origins, early developments, present, and future☆

Kopec̆ek, J., & Kopečková, P. (2009) · Advanced Drug Delivery Reviews · doi:10.1016/j.addr.2009.10.004 · Cited by 576 · see citing works

Development of the polymer micelle carrier system for doxorubicin

Nakanishi, T., Fukushima, S., Okamoto, K., Suzuki, M., Matsumura, Y., Yokoyama, M., Okano, T., Sakurai, Y., & Kataoka, K. (2001) · Journal of Controlled Release · doi:10.1016/s0168-3659(01)00341-8 · Cited by 570 · see citing works

HPMA copolymer–anticancer drug conjugates: design, activity, and mechanism of action

Kopeček, J. (2000) · European Journal of Pharmaceutics and Biopharmaceutics · doi:10.1016/s0939-6411(00)00075-8 · Cited by 561 · see citing works

Cathepsin B-Labile Dipeptide Linkers for Lysosomal Release of Doxorubicin from Internalizing Immunoconjugates: Model Studies of Enzymatic Drug Release and Antigen-Specific In Vitro Anticancer Activity

Dubowchik, G. M., Firestone, R. A., Padilla, L., Willner, D., Hofstead, S. J., Mosure, K. W., Knipe, J. O., Lasch, S. J., & Trail, P. A. (2002) · Bioconjugate Chemistry · doi:10.1021/bc025536j · Cited by 560 · see citing works

Recent advances on the use of biodegradable microparticles and nanoparticles in controlled drug delivery

Brannon‐Peppas, L. (1995) · International Journal of Pharmaceutics · doi:10.1016/0378-5173(94)00324-x · Cited by 528 · see citing works

Mechanisms of drug release in nanotherapeutic delivery systems

Wong, P. T., & Choi, S. K. (2015) · Chemical Reviews · doi:10.1021/cr5004634 · Cited by 507 · see citing works

Proteolytic Activity of Human Osteoclast Cathepsin K

Bossard, M. J., Tomaszek, T. A., Thompson, S. K., Amegadzie, B. Y., Hanning, C. R., Jones, C. S., Kurdyla, J., McNulty, D. E., Drake, F. H., Gowen, M., et al. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.21.12517 · Cited by 500 · see citing works

Peptide and protein nanoparticle conjugates: versatile platforms for biomedical applications

Spicer, C. D., Jumeaux, C., Gupta, B., & Stevens, M. M. (2018) · Chemical Society Reviews · doi:10.1039/c7cs00877e · Cited by 497 · see citing works

Polymeric anticancer drugs with pH-controlled activation

Ulbrich, K. (2004) · Advanced Drug Delivery Reviews · doi:10.1016/j.addr.2003.10.040 · Cited by 495 · see citing works

Oral lipid-based drug delivery systems – an overview

Kalepu, S., Manthina, M. V., & Padavala, V. S. (2013) · Acta Pharmaceutica Sinica B · doi:10.1016/j.apsb.2013.10.001 · Cited by 494 · see citing works

Selective Disruption of Lysosomes in HeLa Cells Triggers Apoptosis Mediated by Cleavage of Bid by Multiple Papain-like Lysosomal Cathepsins

Cirman, T., Bender, K. O., Droga-Mazovec, G., Türk, V., Reed, J. C., Myers, R., Salvesen, G. S., & Turk, B. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m308347200 · Cited by 479 · see citing works

Dendrimers in Oncology: An Expanding Horizon

Tekade, R. K., Kumar, P. V., & Jain, N. K. (2008) · Chemical Reviews · doi:10.1021/cr068212n · Cited by 474 · see citing works

Rational design of smart supramolecular assemblies for gene delivery: chemical challenges in the creation of artificial viruses

Miyata, K., Nishiyama, N., & Kataoka, K. (2011) · Chemical Society Reviews · doi:10.1039/c1cs15258k · Cited by 451 · see citing works

Polymer-drug conjugates: Recent development in clinical oncology

Li, C., & Wallace, S. (2008) · Advanced Drug Delivery Reviews · doi:10.1016/j.addr.2007.11.009 · Cited by 437 · see citing works

Hepatic Drug Targeting: Phase I Evaluation of Polymer-Bound Doxorubicin

Seymour, L. W., Ferry, D. R., Anderson, D., Hesslewood, S., Julyan, P. J., Poyner, R., Doran, J., Young, A., Burtles, S. S., & Kerr, D. J. (2002) · Journal of Clinical Oncology · doi:10.1200/jco.20.6.1668 · Cited by 435 · see citing works

Recent advances in dendrimer-based nanovectors for tumor-targeted drug and gene delivery

Kesharwani, P., & Iyer, A. K. (2014) · Drug Discovery Today · doi:10.1016/j.drudis.2014.12.012 · Cited by 382 · see citing works

Silica-based nanoprobes for biomedical imaging and theranostic applications

Vivero-Escoto, J. L., Huxford‐Phillips, R. C., & Lin, W. (2012) · Chemical Society Reviews · doi:10.1039/c2cs15229k · Cited by 382 · see citing works

In search of partners: linking extracellular proteases to substrates

Overall, C. M., & Blobel, C. (2007) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2120 · Cited by 350 · see citing works

New HPMA copolymers containing doxorubicin bound via pH-sensitive linkage: synthesis and preliminary in vitro and in vivo biological properties

Etrych, T., Jelínková, M., Řı́hová, B., & Ulbrich, K. (2001) · Journal of Controlled Release · doi:10.1016/s0168-3659(01)00281-4 · Cited by 340 · see citing works

Complete regression of well-established tumors using a novel water-soluble poly(L-glutamic acid)-paclitaxel conjugate.

Li, C., Yu, D. F., Newman, R. A., Cabral, F., Stephens, L. C., Hunter, N. R., Milas, L., & Wallace, S. (1998) · PubMed · Cited by 339 · see citing works

Lysosomal cathepsins and their regulation in aging and neurodegeneration

Stoka, V., Turk, V., & Turk, B. (2016) · Ageing Research Reviews · doi:10.1016/j.arr.2016.04.010 · Cited by 334 · see citing works

The pharmacological landscape and therapeutic potential of serine hydrolases

Bachovchin, D. A., & Cravatt, B. F. (2012) · Nature Reviews Drug Discovery · doi:10.1038/nrd3620 · Cited by 307 · see citing works

Cancer-associated lysosomal changes: friends or foes?

Kallunki, T., Olsen, O. D., & Jäättelä, M. (2012) · Oncogene · doi:10.1038/onc.2012.292 · Cited by 301 · see citing works

The role of cathepsins in osteoporosis and arthritis: Rationale for the design of new therapeutics

YASUDA, Y., KALETA, J., & Brömme, D. (2005) · Advanced Drug Delivery Reviews · doi:10.1016/j.addr.2004.12.013 · Cited by 301 · see citing works

Supramolecular Nanodevices: From Design Validation to Theranostic Nanomedicine

Cabral, H., Nishiyama, N., & Kataoka, K. (2011) · Accounts of Chemical Research · doi:10.1021/ar200094a · Cited by 290 · see citing works

Hepatic Drug Targeting: Phase I Evaluation of Polymer-Bound Doxorubicin

Seymour, L. W., Ferry, D. R., Anderson, D., et al. (2002) · Journal of Clinical Oncology · doi:10.1200/jco.2002.20.6.1668 · Cited by 287 · see citing works

Cathepsin K: its skeletal actions and role as a therapeutic target in osteoporosis

Costa, A. G., Cusano, N. E., Silva, B. C. C., Cremers, S., & Bilezikian, J. P. (2011) · Nature Reviews Rheumatology · doi:10.1038/nrrheum.2011.77 · Cited by 286 · see citing works

Nanoengineered Polymer Capsules: Tools for Detection, Controlled Delivery, and Site‐Specific Manipulation

Sukhorukov, G. B., Rogach, A. L., Zebli, B., Liedl, T., Skirtach, A. G., Köhler, K., Antipov, A. A., Gaponik, N. P., Susha, A. S., Winterhalter, M., et al. (2004) · Small · doi:10.1002/smll.200400075 · Cited by 280 · see citing works

Phase I clinical and pharmacokinetic study of PNU166945, a novel water-soluble polymer-conjugated prodrug of paclitaxel

Terwogt, J. M. M., Huinink, W. W. T. B., Schellens, J. H. M., Schot, M. E., Mandjes, I. A. M., Zurlo, M. G., Rocchetti, M., Rosing, H., Koopman, F. J., & Beijnen, J. H. (2001) · Anti-Cancer Drugs · doi:10.1097/00001813-200104000-00003 · Cited by 279 · see citing works

Noninvasive optical imaging of apoptosis by caspase-targeted activity-based probes

Edgington‐Mitchell, L. E., Berger, A. B., Blum, G., Albrow, V. E., Paulick, M. G., Lineberry, N. B., & Bogyo, M. S. (2009) · Nature Medicine · doi:10.1038/nm.1938 · Cited by 276 · see citing works

Poly (amino acid) micelle nanocarriers in preclinical and clinical studies

Matsumura, Y. (2008) · Advanced Drug Delivery Reviews · doi:10.1016/j.addr.2007.11.010 · Cited by 275 · see citing works

Lysosomal Membrane Proteins and Their Central Role in Physiology

Schwake, M., Schröder, B., & Säftig, P. (2013) · Traffic · doi:10.1111/tra.12056 · Cited by 258 · see citing works

Enzyme-Induced and Tumor-Targeted Drug Delivery System Based on Multifunctional Mesoporous Silica Nanoparticles

Cheng, Y.-J., Luo, G., Zhu, J., Xu, X., Zeng, X., Cheng, D., Li, Y., Wu, Y., Zhang, X., Zhuo, R., et al. (2015) · ACS Applied Materials & Interfaces · doi:10.1021/acsami.5b00752 · Cited by 253 · see citing works

Revised Definition of Substrate Binding Sites of Papain-Like Cysteine Proteases

Türk, V., Gunčar, G., Podobnik, M., & Turk, B. (1998) · Biological Chemistry · doi:10.1515/bchm.1998.379.2.137 · Cited by 252 · see citing works

Synthesis, Self-Assembly, and Biomedical Applications of Antimicrobial Peptide–Polymer Conjugates

Sun, H., Hong, Y., Xi, Y., Zou, Y., Gao, J., & Du, J. (2018) · Biomacromolecules · doi:10.1021/acs.biomac.8b00208 · Cited by 252 · see citing works

Noncaspase proteases in apoptosis

Johnson, D. (2000) · Leukemia · doi:10.1038/sj.leu.2401879 · Cited by 251 · see citing works

Proteolytic Cleavage—Mechanisms, Function, and “Omic” Approaches for a Near-Ubiquitous Posttranslational Modification

Klein, T., Eckhard, U., Dufour, A., Solis, N., & Overall, C. M. (2017) · Chemical Reviews · doi:10.1021/acs.chemrev.7b00120 · Cited by 229 · see citing works

Cysteine cathepsins are essential in lysosomal degradation of α-synuclein

McGlinchey, R. P., & Lee, J. C. (2015) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1500937112 · Cited by 227 · see citing works

The osteoclast-associated protease cathepsin K is expressed in human breast carcinoma.

Littlewood-Evans, A., Bilbe, G., Bowler, W. B., Farley, D. R., Wlodarski, B., Kokubo, T., Inaoka, T., Sloane, J. P., Evans, D. B., & Gallagher, J. A. (1997) · PubMed · Cited by 224 · 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

Peroral Route: An Opportunity for Protein and Peptide Drug Delivery

Sood, A., & Panchagnula, R. (2001) · Chemical Reviews · doi:10.1021/cr000700m · Cited by 222 · see citing works

A Phase I and Pharmacological Study of the Platinum Polymer AP5280 Given as an Intravenous Infusion Once Every 3 Weeks in Patients with Solid Tumors

Rademaker-Lakhai, J. M., Terret, C., Howell, S. B., Baud, C., de Boer, R. F., Pluim, D., Beijnen, J. H., Schellens, J. H. M., & Droz, J. (2004) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-03-0315 · Cited by 214 · see citing works

Improved Quenched Fluorescent Probe for Imaging of Cysteine Cathepsin Activity

Verdoes, M., Bender, K. O., Segal, E., van der Linden, W. A., Syed, S., Withana, N. P., Sanman, L. E., & Bogyo, M. S. (2013) · Journal of the American Chemical Society · doi:10.1021/ja4056068 · Cited by 213 · see citing works

Cysteine protease cathepsins in cardiovascular disease: from basic research to clinical trials

Liu, C.-L., Guo, J., Zhang, X., Sukhova, G. K., Libby, P., & Shi, G. (2018) · Nature Reviews Cardiology · doi:10.1038/s41569-018-0002-3 · Cited by 212 · see citing works

Enzyme‐Mediated Controlled Release Systems by Anchoring Peptide Sequences on Mesoporous Silica Supports

Coll, C., Mondragón, L., Martínez‐Máñez, R., Sancenón, F., Marcos, M. D., Soto, J., Amorós, P., & Pérez‐Payá, E. (2011) · Angewandte Chemie International Edition · doi:10.1002/anie.201004133 · Cited by 210 · see citing works

Amphiphilic peptide dendritic copolymer-doxorubicin nanoscale conjugate self-assembled to enzyme-responsive anti-cancer agent

Li, N., Li, N., Yi, Q., Luo, K., Guo, C., Pan, D., & Gu, Z. (2014) · Biomaterials · doi:10.1016/j.biomaterials.2014.07.059 · Cited by 210 · see citing works

Phase III Trial Comparing Paclitaxel Poliglumex (CT-2103, PPX) in Combination with Carboplatin Versus Standard Paclitaxel and Carboplatin in the Treatment of PS 2 Patients with Chemotherapy-Naïve Advanced Non-small Cell Lung Cancer

Langer, C. J., O'Byrne, K. J., Socinski, M. A., Mikhailov, S. M., Leśniewski-Kmak, K., Šmakal, M., Ciuleanu, T., Orlov, S., Dediu, M., Heigener, D. F., et al. (2008) · Journal of Thoracic Oncology · doi:10.1097/jto.0b013e3181753b4b · Cited by 203 · see citing works

Bone-targeting macromolecular therapeutics

WANG, D., Miller, S. C., Kopečková, P., & Kopeček, J. (2005) · Advanced Drug Delivery Reviews · doi:10.1016/j.addr.2004.12.011 · Cited by 203 · see citing works

The Future of Cysteine Cathepsins in Disease Management

Kramer, L., Türk, V., & Turk, B. (2017) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2017.06.003 · Cited by 194 · see citing works

Cysteine proteases as disease markers

Berdowska, I. (2004) · Clinica Chimica Acta · doi:10.1016/j.cccn.2003.12.016 · Cited by 193 · see citing works

Smart chemistry in polymeric nanomedicine

Tong, R., Tang, L., Ma, L., Tu, C., Baumgartner, R., & Cheng, J. (2014) · Chemical Society Reviews · doi:10.1039/c4cs00133h · Cited by 191 · see citing works

Critical role for cathepsin B in mediating caspase-1-dependent interleukin-18 maturation and caspase-1-independent necrosis triggered by the microbial toxin nigericin

Hentze, H., Lin, X. Y., Choi, M. S. K., & Porter, A. G. (2003) · Cell Death and Differentiation · doi:10.1038/sj.cdd.4401264 · Cited by 187 · see citing works

Targeting Heat Shock Proteins on Cancer Cells: Selection, Characterization, and Cell-Penetrating Properties of a Peptidic GRP78 Ligand

Kim, Y. S., Lillo, A. M., Steiniger, S. C. J., Liu, Y., Ballatore, C., Anichini, A., Mortarini, R., Kaufmann, G. F., Zhou, B., Felding‐Habermann, B., et al. (2006) · Biochemistry · doi:10.1021/bi060264j · Cited by 187 · see citing works

Dual Enzymatic Reaction-Assisted Gemcitabine Delivery Systems for Programmed Pancreatic Cancer Therapy

Han, H., Valdepérez, D., Jin, Q., Yang, B., Li, Z., Wu, Y., Pelaz, B., Parak, W. J., & Ji, J. (2017) · ACS Nano · doi:10.1021/acsnano.6b05541 · Cited by 186 · see citing works

Molecular imaging of gene therapy for cancer

Shah, K., Jacobs, A., Breakefield, X. O., & Weissleder, R. (2004) · Gene Therapy · doi:10.1038/sj.gt.3302278 · Cited by 185 · see citing works

Preliminary clinical study of the distribution of HPMA copolymers bearing doxorubicin and galactosamine

Julyan, P. J. (1999) · Journal of Controlled Release · doi:10.1016/s0168-3659(98)00124-2 · Cited by 181 · see citing works

Novel Peptide Linkers for Highly Potent Antibody−Auristatin Conjugate

Doronina, S. O., Bovee, T. D., Meyer, D. W., et al. (2008) · Bioconjugate Chemistry · doi:10.1021/bc800289a · Cited by 180 · see citing works

New approaches for dissecting protease functions to improve probe development and drug discovery

Deu, E., Verdoes, M., & Bogyo, M. S. (2012) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.2203 · Cited by 161 · see citing works

Targeting polymer therapeutics to bone

Low, S. A., & Kopec̆ek, J. (2012) · Advanced Drug Delivery Reviews · doi:10.1016/j.addr.2012.01.012 · Cited by 158 · see citing works

Synthesis and Evaluation of Water-Soluble Polymeric Bone-Targeted Drug Delivery Systems

Wang, D., Miller, S. C., Sima, M., et al. (2003) · Bioconjugate Chemistry · doi:10.1021/bc034090j · Cited by 156 · see citing works

Killing cancer cells by targeted drug-carrying phage nanomedicines

Bar, H., Yacoby, I., & Benhar, I. (2008) · BMC Biotechnology · doi:10.1186/1472-6750-8-37 · Cited by 149 · see citing works

Dendrimer–doxorubicin conjugate as enzyme-sensitive and polymeric nanoscale drug delivery vehicle for ovarian cancer therapy

Zhang, C., Pan, D., Luo, K., Li, N., Guo, C., Zheng, X., & Gu, Z. (2014) · Polymer Chemistry · doi:10.1039/c4py00601a · Cited by 142 · see citing works

Biodistribution and antitumour efficacy of long-circulating N-(2-hydroxypropyl)methacrylamide copolymer–doxorubicin conjugates in nude mice

Shiah, J.-G., Dvořák, M., Kopečková, P., Sun, Y., Peterson, C. M., & Kopec̆ek, J. (2001) · European Journal of Cancer · doi:10.1016/s0959-8049(00)00374-9 · Cited by 140 · see citing works

Paclitaxel poliglumex (XYOTAX; CT-2103): an intracellularly targeted taxane

Singer, J. W., Shaffer, S. A., Baker, B., Bernareggi, A., Stromatt, S. C., Nienstedt, D., & Besman, M. (2005) · Anti-Cancer Drugs · doi:10.1097/00001813-200503000-00003 · Cited by 138 · see citing works

Cysteine cathepsins in the immune response

Zavašnik‐Bergant, T., & Turk, B. (2006) · Tissue Antigens · doi:10.1111/j.1399-0039.2006.00585.x · Cited by 135 · see citing works

A Phase I and Pharmacokinetic Study of Pegylated Camptothecin as a 1-Hour Infusion Every 3 Weeks in Patients With Advanced Solid Malignancies

Rowinsky, E. K., Rizzo, J. D., Ochoa, L., Takimoto, C. H. M., Forouzesh, B., Schwartz, G. H., Hammond, L. A., Patnaik, A., Kwiatek, J., Goetz, A. D., et al. (2002) · Journal of Clinical Oncology · doi:10.1200/jco.2003.03.143 · Cited by 132 · see citing works

Polysaccharides based nanomaterials for targeted anti-cancer drug delivery

Dheer, D., Arora, D., Jaglan, S., Rawal, R. K., & Shankar, R. (2016) · Journal of drug targeting · doi:10.3109/1061186x.2016.1172589 · Cited by 132 · see citing works

Sequential combination therapy of ovarian cancer with degradable N -(2-hydroxypropyl)methacrylamide copolymer paclitaxel and gemcitabine conjugates

Zhang, R., Yang, J., Sima, M., Zhou, Y., & Kopec̆ek, J. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1406233111 · Cited by 131 · see citing works

Caveolin-1 mediates the expression and localization of cathepsin B, pro-urokinase plasminogen activator and their cell-surface receptors in human colorectal carcinoma cells

Cavallo‐Medved, D., Mai, J., Dosescu, J., Sameni, M., & Sloane, B. F. (2005) · Journal of Cell Science · doi:10.1242/jcs.02278 · Cited by 131 · see citing works

Fate of N-(2-hydroxypropyl)methacrylamide copolymers with pendent galactosamine residues after intravenous administration to rats

DUNCAN, R., Seymour, L. W., Scarlett, L., LLOYD, J., Rejmanová, P., & Kopeček, J. (1986) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/0304-4165(86)90120-0 · Cited by 130 · see citing works

Functional dendritic polymer architectures as stimuli-responsive nanocarriers

Calderón, M., Quadir, M., Strumia, M. C., & Haag, R. (2010) · Biochimie · doi:10.1016/j.biochi.2010.02.017 · Cited by 129 · see citing works

Down-regulation of cathepsin-D expression by antisense gene transfer inhibits tumor growth and experimental lung metastasis of human breast cancer cells

Glondu, M., Liaudet‐Coopman, E., Derocq, D., et al. (2002) · Oncogene · doi:10.1038/sj.onc.1205657 · Cited by 129 · see citing works

Proteolysis: A Biological Process Adapted in Drug Delivery, Therapy, and Imaging

Law, B., & Tung, C. (2009) · Bioconjugate Chemistry · doi:10.1021/bc800500a · Cited by 126 · see citing works

Mechanistic Studies of a Peptidic GRP78 Ligand for Cancer Cell-Specific Drug Delivery

Liu, Y. M., Steiniger, S. C. J., Kim, Y. S., Kaufmann, G. F., Felding‐Habermann, B., & Janda, K. D. (2007) · Molecular Pharmaceutics · doi:10.1021/mp060122j · Cited by 124 · see citing works

Endolysosomal proteases and their inhibitors in immunity

Bird, P. I., Trapani, J. A., & Villadangos, J. A. (2009) · Nature reviews. Immunology · doi:10.1038/nri2671 · Cited by 123 · see citing works

Phase II Study of CT-2103 in Patients With Recurrent Epithelial Ovarian, Fallopian Tube, or Primary Peritoneal Carcinoma

Sabbatini, P. J., Aghajanian, C. A., Dizon, D. S., et al. (2004) · Journal of Clinical Oncology · doi:10.1200/jco.2004.12.043 · Cited by 123 · see citing works

A phase I and pharmacokinetic study of MAG-CPT, a water-soluble polymer conjugate of camptothecin

Schoemaker, N. E., van Kesteren, C., Rosing, H., et al. (2002) · British Journal of Cancer · doi:10.1038/sj.bjc.6600516 · Cited by 121 · see citing works

Integrin-assisted drug delivery of nano-scaled polymer therapeutics bearing paclitaxel

Eldar-Boock, A., Miller, K., Sanchis, J., Lupu, R., Vicent, M., & Satchi-Fainaro, R. (2011) · Biomaterials · doi:10.1016/j.biomaterials.2011.01.073 · Cited by 120 · see citing works

Phase I and pharmacokinetic trial of AP5346, a DACH–platinum–polymer conjugate, administered weekly for three out of every 4 weeks to advanced solid tumor patients

Campone, M., Rademaker-Lakhai, J. M., Bennouna, J., Howell, S. B., Nowotnik, D. P., Beijnen, J. H., & Schellens, J. H. M. (2007) · Cancer Chemotherapy and Pharmacology · doi:10.1007/s00280-006-0397-0 · Cited by 115 · see citing works

A Nonpeptidic Cathepsin S Activity-Based Probe for Noninvasive Optical Imaging of Tumor-Associated Macrophages

Verdoes, M., Edgington‐Mitchell, L. E., Scheeren, F. A., Leyva, M. J., Blum, G., Weiskopf, K., Bachmann, M. H., Ellman, J. A., & Bogyo, M. S. (2012) · Chemistry & Biology · doi:10.1016/j.chembiol.2012.03.012 · Cited by 115 · see citing works

Lipid prodrug nanocarriers in cancer therapy

Mura, S., Bui, D. T., Couvreur, P., & Nicolas, J. (2015) · Journal of Controlled Release · doi:10.1016/j.jconrel.2015.01.021 · Cited by 114 · see citing works

Proteases in cancer drug delivery

Vandooren, J., Opdenakker, G., Loadman, P. M., & Edwards, D. R. (2016) · Advanced Drug Delivery Reviews · doi:10.1016/j.addr.2015.12.020 · Cited by 113 · see citing works

Drug delivery systems functionalized with bone mineral seeking agents for bone targeted therapeutics

Rotman, S. G., Grijpma, D. W., Richards, R. G., Moriarty, T. F., Eglin, D., & Guillaume, O. (2017) · Journal of Controlled Release · doi:10.1016/j.jconrel.2017.11.009 · Cited by 111 · see citing works

Cysteine cathepsin S as an immunomodulatory target: present and future trends

Gupta, S., Singh, R. K., Dastidar, S. G., et al. (2008) · Expert Opinion on Therapeutic Targets · doi:10.1517/14728222.12.3.291 · Cited by 110 · see citing works

Design of a multivalent galactoside ligand for selective targeting of HPMA copolymer–doxorubicin conjugates to human colon cancer cells

David, A., Kopečková, P., Minko, T., Rubinstein, A., & Kopec̆ek, J. (2003) · European Journal of Cancer · doi:10.1016/j.ejca.2003.07.001 · Cited by 110 · see citing works

Future directions of bone-targeted therapy for metastatic breast cancer

Onishi, T., Hayashi, N., Theriault, R. L., Hortobágyi, G. N., & Ueno, N. T. (2010) · Nature Reviews Clinical Oncology · doi:10.1038/nrclinonc.2010.134 · Cited by 109 · see citing works

Discovery of Peptidomimetic Antibody–Drug Conjugate Linkers with Enhanced Protease Specificity

Wei, B. Q., Gunzner, J. L., Yao, H., Wang, T., Wang, J., Xu, Z., Chen, J., Wai, J. S. M., Nonomiya, J., Tsai, S. P., et al. (2017) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.7b01430 · Cited by 109 · see citing works

Development of enzymatically cleavable prodrugs derived from dendritic polyglycerol

Calderón, M., Graeser, R., Kratz, F., & Haag, R. (2009) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2009.05.058 · Cited by 106 · see citing works

Cysteine Cathepsins as Regulators of the Cytotoxicity of NK and T Cells

Nanut, M. P., Sabotič, J., Jewett, A., & Kos, J. (2014) · Frontiers in Immunology · doi:10.3389/fimmu.2014.00616 · Cited by 103 · see citing works

Phase I Trial of Poly- l -Glutamate Camptothecin (CT-2106) Administered Weekly in Patients with Advanced Solid Malignancies

Homsi, J., Simon, G. R., Garrett, C. R., Springett, G. M., Conti, R. C. D., Chiappori, A., Münster, P. N., Burton, M. K., Stromatt, S. C., Allievi, C., et al. (2007) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-06-2821 · Cited by 103 · see citing works

Albumin-Binding Prodrugs of Camptothecin and Doxorubicin with an Ala-Leu-Ala-Leu-Linker That Are Cleaved by Cathepsin B: Synthesis and Antitumor Efficacy

Schmid, B., Chung, D., Warnecke, A., Fichtner, I., & Kratz, F. (2007) · Bioconjugate Chemistry · doi:10.1021/bc0602735 · Cited by 102 · see citing works

Lysosome-Targeting Fluorogenic Probe for Cathepsin B Imaging in Living Cells

Wang, Y., Li, J., Feng, L., Yu, J., Zhang, Y., Ye, D., & Chen, H. (2016) · Analytical Chemistry · doi:10.1021/acs.analchem.6b03717 · Cited by 98 · see citing works

Peptide-Based Biomaterials for Protease-Enhanced Drug Delivery

Law, B., Weissleder, R., & Tung, C. (2006) · Biomacromolecules · doi:10.1021/bm050920f · Cited by 96 · see citing works

Amphiphilic nanocarrier-induced modulation of PLK1 and miR-34a leads to improved therapeutic response in pancreatic cancer

Gibori, H., Eliyahu, S., Krivitsky, A., Ben‐Shushan, D., Epshtein, Y., Tiram, G., Blau, R., Ofek, P., Lee, J. S., Ruppin, E., et al. (2017) · Nature Communications · doi:10.1038/s41467-017-02283-9 · Cited by 96 · see citing works

PDEPT: Polymer-Directed Enzyme Prodrug Therapy. 2. HPMA Copolymer-β-lactamase and HPMA Copolymer-C-Dox as a Model Combination

Satchi‐Fainaro, R., Hailu, H., Davies, J. W., et al. (2003) · Bioconjugate Chemistry · doi:10.1021/bc020091k · Cited by 94 · see citing works

Enzyme‐Responsive Multifunctional Magnetic Nanoparticles for Tumor Intracellular Drug Delivery and Imaging

Yang, Y., Aw, J., Chen, K., Liu, F., Padmanabhan, P., Hou, Y., Cheng, Z., & Xing, B. (2011) · Chemistry - An Asian Journal · doi:10.1002/asia.201000905 · Cited by 93 · see citing works

Trafficking of lysosomal cathepsin B—green fluorescent protein to the surface of thyroid epithelial cells involves the endosomal/lysosomal compartment

Linke, M., Herzog, V., & Brix, K. (2002) · Journal of Cell Science · doi:10.1242/jcs.00184 · Cited by 88 · see citing works

Local and targeted drug delivery for bone regeneration

Newman, M. R., & Benoit, D. S. W. (2016) · Current Opinion in Biotechnology · doi:10.1016/j.copbio.2016.02.029 · Cited by 88 · see citing works

Phase I Pharmacokinetic, Food Effect, and Pharmacogenetic Study of Oral Irinotecan Given as Semisolid Matrix Capsules in Patients with Solid Tumors

Soepenberg, O., Dumez, H., Verweij, J., de Jong, F. A., de Jonge, M. J. A., Thomas, J., Eskens, F. A. L. M., van Schaik, R. H. N., Selleslach, J., ter Steeg, J., et al. (2005) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-04-1758 · Cited by 87 · see citing works

The light at the end of the tunnel—second generation HPMA conjugates for cancer treatment

Yang, J., & Kopec̆ek, J. (2017) · Current Opinion in Colloid & Interface Science · doi:10.1016/j.cocis.2017.07.003 · Cited by 86 · see citing works

Dipeptide-based highly potent doxorubicin antibody conjugates

Jeffrey, S. C., Nguyen, M. T., Andreyka, J. B., et al. (2005) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2005.09.081 · Cited by 85 · see citing works

Selective imaging of cathepsin L in breast cancer by fluorescent activity-based probes

Poręba, M., Rut, W., Vizovišek, M., Groborz, K. M., Kasperkiewicz, P., Finlay, D., Vuori, K., Türk, V., Turk, B., Salvesen, G. S., et al. (2018) · Chemical Science · doi:10.1039/c7sc04303a · Cited by 85 · see citing works

Deficiency and Inhibition of Cathepsin K Reduce Body Weight Gain and Increase Glucose Metabolism in Mice

Yang, M., Sun, J., Zhang, T., Liu, J., Zhang, J., Shi, M. A., Darakhshan, F., Guerre-Millo, M., Clément, K., Gelb, B. D., et al. (2008) · Arteriosclerosis Thrombosis and Vascular Biology · doi:10.1161/atvbaha.108.172320 · Cited by 84 · see citing works

The role of cathepsin X in cell signaling

Kos, J., Jevnikar, Z., & Obermajer, N. (2009) · Cell Adhesion & Migration · doi:10.4161/cam.3.2.7403 · Cited by 83 · 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

Cysteine cathepsins: their role in tumor progression and recent trends in the development of imaging probes

Löser, R., & Pietzsch, J. (2015) · Frontiers in Chemistry · doi:10.3389/fchem.2015.00037 · Cited by 79 · see citing works

Optical Imaging of Cancer-Related Proteases Using Near-Infrared Fluorescence Matrix Metalloproteinase-Sensitive and Cathepsin B-Sensitive Probes

Yhee, J. Y., Kim, S. A., Koo, H., et al. (2012) · Theranostics · doi:10.7150/thno.3716 · Cited by 79 · see citing works

Protein-Based Multifunctional Nanocarriers for Imaging, Photothermal Therapy, and Anticancer Drug Delivery

Pan, U. N., Khandelia, R., Sanpui, P., et al. (2016) · ACS Applied Materials & Interfaces · doi:10.1021/acsami.6b06099 · Cited by 76 · 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

Localization of nuclear cathepsin L and its association with disease progression and poor outcome in colorectal cancer

Sullivan, S., Tosetto, M., Kevans, D., Coss, A., Wang, L., O’Donoghue, D. P., Hyland, J. M., Sheahan, K. D., Mulcahy, H. E., & O'Sullivan, J. N. (2009) · International Journal of Cancer · doi:10.1002/ijc.24275 · Cited by 75 · see citing works

The role of cathepsin X in the migration and invasiveness of T lymphocytes

Jevnikar, Z., Obermajer, N., Bogyo, M. S., et al. (2008) · Journal of Cell Science · doi:10.1242/jcs.023721 · Cited by 75 · see citing works

Engineered Proteinticles for Targeted Delivery of siRNA to Cancer Cells

Lee, E. J., Lee, S. J., Kang, Y.-S., Ryu, J. H., Kwon, K. C., Jo, E., Yhee, J. Y., Kwon, I. C., Kim, K., & Lee, J. (2015) · Advanced Functional Materials · doi:10.1002/adfm.201403680 · Cited by 75 · see citing works

A cell-penetrating peptidic GRP78 ligand for tumor cell-specific prodrug therapy

Yoneda, Y., Steiniger, S. C. J., Čapková, K., et al. (2008) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2008.01.060 · Cited by 75 · see citing works

Degradation of Superparamagnetic Iron Oxide Nanoparticle-Induced Ferritin by Lysosomal Cathepsins and Related Immune Response

Laskar, A., Ghosh, M., Khattak, S. I., Li, W., & Yuan, X. (2012) · Nanomedicine · doi:10.2217/nnm.11.148 · Cited by 75 · see citing works

Enzyme-responsive doxorubicin release from dendrimer nanoparticles for anticancer drug delivery

Jeong, Y., Park, H. K., Lee, S. J., Oh, J., Lee, S., Lee, H. C., & Kang, D. H. (2015) · International Journal of Nanomedicine · doi:10.2147/ijn.s87145 · Cited by 74 · see citing works

Design of a Highly Selective Quenched Activity-Based Probe and Its Application in Dual Color Imaging Studies of Cathepsin S Activity Localization

Bender, K. O., Ofori, L. O., van der Linden, W. A., et al. (2015) · Journal of the American Chemical Society · doi:10.1021/jacs.5b00315 · Cited by 74 · see citing works

Phase I and Pharmacokinetic Study of DE-310 in Patients with Advanced Solid Tumors

Soepenberg, O., de Jonge, M. J. A., Sparreboom, A., et al. (2005) · Clinical Cancer Research · doi:10.1158/1078-0432.703.11.2 · Cited by 74 · see citing works

Biodistribution of free and N -(2-hydroxypropyl)methacrylamide copolymer-bound mesochlorin e 6 and adriamycin in nude mice bearing human ovarian carcinoma OVCAR-3 xenografts

Shiah, J.-G., Sun, Y., Peterson, C. M., & Kopeček, J. (1999) · Journal of Controlled Release · doi:10.1016/s0168-3659(99)00113-3 · Cited by 73 · see citing works

Selective Targeting of Tumor and Stromal Cells By a Nanocarrier System Displaying Lipidated Cathepsin B Inhibitor

Mikhaylov, G., Klimpel, D., Schaschke, N., Mikac, U., Vizovišek, M., Fonovič, M., Türk, V., Turk, B., & Vasiljeva, O. S. (2014) · Angewandte Chemie International Edition · doi:10.1002/anie.201402305 · Cited by 73 · see citing works

Proteases as regulators of pathogenesis: Examples from the Apicomplexa

Li, H., Child, M. A., & Bogyo, M. S. (2011) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2011.06.002 · Cited by 72 · see citing works

Cross-Linked Small-Molecule Micelle-Based Drug Delivery System: Concept, Synthesis, and Biological Evaluation

Liao, C., Chen, Y., Yao, Y., Zhang, S., Gu, Z., & Yu, X. (2016) · Chemistry of Materials · doi:10.1021/acs.chemmater.6b02965 · Cited by 70 · see citing works

Expression of Cathepsin B and L antigen and activity is associated with early colorectal cancer progression

Troy, A., Sheahan, K. D., Mulcahy, H. E., et al. (2004) · European Journal of Cancer · doi:10.1016/j.ejca.2004.03.011 · Cited by 68 · see citing works

Targeted drug delivery by in vivo coupling to endogenous albumin: an albumin-binding prodrug of methotrexate (MTX) is better than MTX in the treatment of murine collagen-induced arthritis

Fiehn, C., Kratz, F., Sass, G., Müller-Ladner, U., & Neumann, E. (2008) · Annals of the Rheumatic Diseases · doi:10.1136/ard.2007.086843 · Cited by 67 · see citing works

Cathepsin D in ovarian cancer: prognostic value and correlation with p53 expression and microvessel density

Lösch, A., Schindl, M., Kohlberger, P., et al. (2004) · Gynecologic Oncology · doi:10.1016/j.ygyno.2003.11.016 · Cited by 66 · see citing works

A novel cysteine cathepsin inhibitor yields macrophage cell death and mammary tumor regression

Salpeter, S. J., Pozniak, Y., Merquiol, E., Ben‐Nun, Y., Geiger, T., & Blum, G. (2015) · Oncogene · doi:10.1038/onc.2015.51 · Cited by 65 · see citing works

Mesoporous Silica Nanoparticles as an Antitumoral-Angiogenesis Strategy

Setyawati, M. I., & Leong, D. T. (2017) · ACS Applied Materials & Interfaces · doi:10.1021/acsami.6b12524 · Cited by 65 · see citing works

HPMA Copolymers Platinates Containing Dicarboxylato Ligands. Preparation, Characterisation and In Vitro and In Vivo Evaluation

Gianasi, E., Buckley, R. G., Latigo, J. R., et al. (2002) · Journal of drug targeting · doi:10.1080/1061186021000072456 · Cited by 64 · see citing works

FRET-trackable biodegradable HPMA copolymer-epirubicin conjugates for ovarian carcinoma therapy

Yang, J., Zhang, R., Radford, D. C., & Kopec̆ek, J. (2015) · Journal of Controlled Release · doi:10.1016/j.jconrel.2015.09.045 · Cited by 62 · see citing works

Polymeric nanotheranostics for real-time non-invasive optical imaging of breast cancer progression and drug release

Ferber, S., Baabur‐Cohen, H., Blau, R., et al. (2014) · Cancer Letters · doi:10.1016/j.canlet.2014.02.022 · Cited by 62 · see citing works

Proteinases and their receptors in inflammatory arthritis: an overview

Οικονομοπούλου, Κ., Diamandis, E. P., Hollenberg, M. D., & Chandran, V. (2018) · Nature Reviews Rheumatology · doi:10.1038/nrrheum.2018.17 · Cited by 61 · see citing works

Paclitaxel poliglumex for ovarian cancer

Galic, V., Wright, J. D., Lewin, S. N., et al. (2011) · Expert Opinion on Investigational Drugs · doi:10.1517/13543784.2011.576666 · Cited by 60 · see citing works

Combination cytotoxicity of backbone degradable HPMA copolymer gemcitabine and platinum conjugates toward human ovarian carcinoma cells

Duangjai, A., Luo, K., Zhou, Y., Yang, J., & Kopec̆ek, J. (2013) · European Journal of Pharmaceutics and Biopharmaceutics · doi:10.1016/j.ejpb.2013.11.008 · Cited by 59 · see citing works

Cathepsin B Expression and the Correlation with Clinical Aspects of Oral Squamous Cell Carcinoma

Yang, W., Ho, C., Yang, S., Lin, S., Yeh, K., Lin, C., & Chen, M. (2016) · PLoS ONE · doi:10.1371/journal.pone.0152165 · Cited by 59 · see citing works

Cathepsins in digestive cancers

Chen, S., Dong, H. F., Yang, S., & Guo, H. Y. (2017) · Oncotarget · doi:10.18632/oncotarget.16677 · Cited by 59 · see citing works

Enzyme-responsive pillar[5]arene-based polymer-substituted amphiphiles: synthesis, self-assembly in water, and application in controlled drug release

Gao, L., Zheng, B., Chen, W., & Schalley, C. A. (2015) · Chemical Communications · doi:10.1039/c5cc06207a · Cited by 58 · see citing works

Cathepsin‐B Induced Controlled Release from Peptide‐Capped Mesoporous Silica Nanoparticles

de la Torre, C., Mondragón, L., Coll, C., Sancenón, F., Marcos, M. D., Martínez‐Máñez, R., Amorós, P., Pérez‐Payá, E., & Orzáez, M. (2014) · Chemistry - A European Journal · doi:10.1002/chem.201404382 · Cited by 58 · see citing works

Tumor Detection by Imaging Proteolytic Activity

Darragh, M. R., Schneider, E. L., Lou, J., et al. (2010) · Cancer Research · doi:10.1158/0008-5472.can-09-1640 · Cited by 57 · see citing works

Orthogonally Functionalized Nanoscale Micelles for Active Targeted Codelivery of Methotrexate and Mitomycin C with Synergistic Anticancer Effect

Li, Y., Lin, J., Wu, H., Chang, Y., Yuan, C., Liu, C., Wang, S., Hou, Z., & Dai, L. (2015) · Molecular Pharmaceutics · doi:10.1021/mp5006068 · Cited by 57 · see citing works

Biodegradable multiblock poly(N-2-hydroxypropyl)methacrylamide gemcitabine and paclitaxel conjugates for ovarian cancer cell combination treatment

Larson, N., Yang, J., Ray, A., et al. (2013) · International Journal of Pharmaceutics · doi:10.1016/j.ijpharm.2013.06.046 · Cited by 56 · see citing works

Cisplatin-Induced Formation of Biocompatible and Biodegradable Polypeptide-Based Vesicles for Targeted Anticancer Drug Delivery

Shirbin, S. J., Ladewig, K., Fu, Q., et al. (2015) · Biomacromolecules · doi:10.1021/acs.biomac.5b00692 · Cited by 54 · see citing works

HPMA copolymer-based combination therapy toxic to both prostate cancer stem/progenitor cells and differentiated cells induces durable anti-tumor effects

Zhou, Y., Yang, J., Rhim, J. S., et al. (2013) · Journal of Controlled Release · doi:10.1016/j.jconrel.2013.09.005 · Cited by 53 · see citing works

Water-soluble HPMA copolymer—prostaglandin E1conjugates containing a cathepsin K sensitive spacer

Pan, H., Kopečková, P., Wang, D., et al. (2006) · Journal of drug targeting · doi:10.1080/10611860600834219 · Cited by 53 · see citing works

Cathepsin E Is a Marker of Gastric Differentiation and Signet-Ring Cell Carcinoma of Stomach: A Novel Suggestion on Gastric Tumorigenesis

Konno‐Shimizu, M., Yamamichi, N., Inada, K.-I., Kageyama‐Yahara, N., Shiogama, K., Takahashi, Y., Asada‐Hirayama, I., Yamamichi-Nishina, M., Nakayama, C., Ono, S., et al. (2013) · PLoS ONE · doi:10.1371/journal.pone.0056766 · Cited by 51 · see citing works

Development of Protein-Binding Bifunctional Linkers for a New Generation of Dual-Acting Prodrugs

Ajaj, K. A., Biniossek, M. L., & Kratz, F. (2009) · Bioconjugate Chemistry · doi:10.1021/bc800429q · Cited by 51 · see citing works

Phase 1 Study of Weekly Polyethylene Glycol-Camptothecin in Patients with Advanced Solid Tumors and Lymphomas

Posey, J. A., Saif, M. W., Carlisle, R. R., Goetz, A. D., Rizzo, J. D., Stevenson, S., Rudoltz, M. S., Kwiatek, J., Simmons, P., Rowinsky, E. K., et al. (2005) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-05-0783 · Cited by 51 · see citing works

Potential of targeted drug delivery system for the treatment of bone metastasis

Raichur, V., & Kusumdevi, V. (2014) · Drug Delivery · doi:10.3109/10717544.2014.913325 · Cited by 50 · see citing works

Cathepsin D non-proteolytically induces proliferation and migration in human omental microvascular endothelial cells via activation of the ERK1/2 and PI3K/AKT pathways

Pranjol, M. Z. I., Gutowski, N. J., Hannemann, M. M., et al. (2017) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2017.10.005 · Cited by 50 · see citing works

Cathepsin L in tumor angiogenesis and its therapeutic intervention by the small molecule inhibitor KGP94

Sudhan, D. R., Rabaglino, M. B., Wood, C. E., & Siemann, D. W. (2016) · Clinical & Experimental Metastasis · doi:10.1007/s10585-016-9790-1 · Cited by 49 · see citing works

Backbone Degradable N-(2-Hydroxypropyl)methacrylamide Copolymer Conjugates with Gemcitabine and Paclitaxel: Impact of Molecular Weight on Activity toward Human Ovarian Carcinoma Xenografts

Yang, J., Zhang, R., Pan, H., et al. (2017) · Molecular Pharmaceutics · doi:10.1021/acs.molpharmaceut.6b01005 · Cited by 49 · see citing works

Cathepsin Substrates as Cleavable Peptide Linkers in Bioconjugates, Selected from a Fluorescence Quench Combinatorial Library

Peterson, J. J., & Meares, C. F. (1998) · Bioconjugate Chemistry · doi:10.1021/bc980059j · Cited by 48 · see citing works

Paclitaxel poliglumex (PPX, CT-2103): macromolecular medicine for advanced non-small-cell lung cancer

Bonomi, P. (2007) · Expert Review of Anticancer Therapy · doi:10.1586/14737140.7.4.415 · Cited by 47 · see citing works

A cascade enzymatic reaction activatable gemcitabine prodrug with an AIE-based intracellular light-up apoptotic probe for in situ self-therapeutic monitoring

Han, H., Teng, W., Chen, T., Zhao, J., Jin, Q., Qin, Z., & Ji, J. (2017) · Chemical Communications · doi:10.1039/c7cc04872f · Cited by 47 · see citing works

Cathepsin B-sensitive nanoprobe for in vivo tumor diagnosis

Ryu, J. H., Kim, S. A., Koo, H., et al. (2011) · Journal of Materials Chemistry · doi:10.1039/c1jm13064a · Cited by 45 · see citing works

Identification of agents effective against multiple toxins and viruses by host-oriented cell targeting

Zilbermintz, L., Leonardi, W., Jeong, S., Sjodt, M., McComb, R. C., Ho, C.-L. C., Retterer, C. J., Gharaibeh, D. N., Zamani, R., Soloveva, V., et al. (2015) · Scientific Reports · doi:10.1038/srep13476 · Cited by 45 · see citing works

Suppressing IL-36-driven inflammation using peptide pseudosubstrates for neutrophil proteases

Sullivan, G. P., Henry, C. M., Clancy, D. M., Mametnabiev, T. E., Belotcerkovskaya, E., Davidovich, P. B., Sura‐Trueba, S., Garabadzhiu, A. V., & Martin, S. J. (2018) · Cell Death and Disease · doi:10.1038/s41419-018-0385-4 · Cited by 45 · see citing works

Targeting Cathepsin E in Pancreatic Cancer by a Small Molecule Allows In Vivo Detection

Keliher, E. J., Reiner, T., Earley, S., et al. (2013) · Neoplasia · doi:10.1593/neo.13276 · Cited by 43 · see citing works

Development of Activity-Based Probes for Cathepsin X

Paulick, M. G., & Bogyo, M. S. (2011) · ACS Chemical Biology · doi:10.1021/cb100392r · Cited by 43 · see citing works

Clinical and Pharmacologic Study of the Novel Prodrug Delimotecan (MEN 4901/T-0128) in Patients with Solid Tumors

Veltkamp, S. A., Witteveen, E. O., Capriati, A., Crea, A., Animati, F., Voogel-Fuchs, M., van den Heuvel, I. J. G. M., Beijnen, J. H., Voest, E. E., & Schellens, J. H. M. (2008) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-08-0438 · Cited by 43 · see citing works

Phase I Study of CT-2103, A Polymer-Conjugated Paclitaxel, and Carboplatin in Patients with Advanced Solid Tumors

Nemunaitis, J. J., Cunningham, C. C., Senzer, N. N., Gray, M., Oldham, F. B., Pippen, J., Mennel, R. G., & Eisenfeld, A. J. (2005) · Cancer Investigation · doi:10.1080/07357900500359935 · Cited by 41 · see citing works

Proteolytic cleavage of the disease-related lysosomal membrane glycoprotein CLN7

Steenhuis, P., Froemming, J., Reinheckel, T., & Storch, S. (2012) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2012.05.015 · Cited by 39 · see citing works

A lysosome-targeted drug delivery system based on sorbitol backbone towards efficient cancer therapy

Maniganda, S., Sankar, V., Nair, J. B., et al. (2014) · Organic & Biomolecular Chemistry · doi:10.1039/c4ob01153h · Cited by 39 · see citing works

Two-step polymer- and liposome-enzyme prodrug therapies for cancer: PDEPT and PELT concepts and future perspectives

Scomparin, A., Florindo, H. F., Tiram, G., Ferguson, E. L., & Satchi‐Fainaro, R. (2017) · Advanced Drug Delivery Reviews · doi:10.1016/j.addr.2017.09.011 · Cited by 39 · see citing works

Dipeptidyl Vinyl Sulfone as a Novel Chemical Tool to Inhibit HMGB1/NLRP3-Inflammasome and Inflamma-miRs in Aβ-Mediated Microglial Inflammation

Falcão, A. S., Carvalho, L. A. R., Lidónio, G. M. D. C., Vaz, A. R., Lucas, S. D., Moreira, R., & Brites, D. M. T. O. (2016) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.6b00250 · Cited by 38 · see citing works

Emerging functional roles of cathepsin E

Zaidi, N., Hermann, C., Herrmann, T., & Kalbacher, H. (2008) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2008.10.034 · Cited by 37 · see citing works

Dual-targeting delivery system for selective cancer cell death and imaging

Tian, X., Baek, K. H., & Shin, I. (2012) · Chemical Science · doi:10.1039/c2sc21777e · Cited by 36 · see citing works

Strategies on Nanodiagnostics and Nanotherapies of the Three Common Cancers

Leng, F., Liu, F., Yang, Y., Wu, Y., & Tian, W. (2018) · Nanomaterials · doi:10.3390/nano8040202 · Cited by 36 · 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

Targeting lysosomes in human disease: from basic research to clinical applications

Cao, M., Luo, X., Wu, K., & He, X. (2021) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-021-00778-y · Cited by 225 · see citing works

Identification of Dipeptidyl Nitriles as Potent and Selective Inhibitors of Cathepsin B through Structure-Based Drug Design

Greenspan, P. D., Clark, K., Tommasi, R., et al. (2001) · Journal of Medicinal Chemistry · doi:10.1021/jm010206q · Cited by 138 · see citing works

The activity and localization patterns of cathepsins B and X in cells of the mouse gastrointestinal tract differ along its length

Tamhane, T., Arampatzidou, M., Gerganova, V., et al. (2014) · Biological Chemistry · doi:10.1515/hsz-2014-0151 · Cited by 11 · see citing works

Neutrophil Elastase Up-Regulates Cathepsin B and Matrix Metalloprotease-2 Expression

Geraghty, P. M., Rogan, M. P., Greene, C. M., et al. (2007) · The Journal of Immunology · doi:10.4049/jimmunol.178.9.5871 · Cited by 125 · see citing works

Inhibitors of Cathepsin B

Gobec, S., & Frlan, R. (2006) · Current Medicinal Chemistry · doi:10.2174/092986706777935122 · Cited by 124 · see citing works

Development of Cathepsin Inhibitors and Structure-Based Design of Cathepsin B-Specific Inhibitor

Tomoo, K. (2010) · Current Topics in Medicinal Chemistry · doi:10.2174/156802610791113441 · Cited by 25 · see citing works