Tumor Microenvironment: Extracellular Matrix Alterations Influence Tumor Progression

Microenvironmental regulation of tumor progression and metastasis

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Molecular Mechanisms of Stress-Responsive Changes in Collagen and Elastin Networks in Skin

Aziz, J., Shezali, H., Radzi, Z., Yahya, N. A., Abu Kassim, N. H., Czernuszka, J., & Rahman, M. T. (2016) · Skin Pharmacology and Physiology · doi:10.1159/000447017 · Cited by 7,323 · see citing works

The biology and function of fibroblasts in cancer

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Matrix Crosslinking Forces Tumor Progression by Enhancing Integrin Signaling

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Microenvironmental regulation of metastasis

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Glypican-1 identifies cancer exosomes and detects early pancreatic cancer

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The tumor microenvironment at a glance

Balkwill, F. R., Capasso, M., & Hagemann, T. (2012) · Journal of Cell Science · doi:10.1242/jcs.116392 · Cited by 1,857 · see citing works

Metabolic Interactions in the Tumor Microenvironment

Lyssiotis, C. A., & Kimmelman, A. C. (2017) · Trends in Cell Biology · doi:10.1016/j.tcb.2017.06.003 · Cited by 853 · cited 1× · see citing works

Tumor-Associated Neutrophils: New Targets for Cancer Therapy

Gregory, A. D., & Houghton, A. M. (2011) · Cancer Research · doi:10.1158/0008-5472.can-10-2583 · Cited by 707 · see citing works

The extracellular matrix in tumor progression and metastasis

Eble, J. A., & Niland, S. (2019) · Clinical & Experimental Metastasis · doi:10.1007/s10585-019-09966-1 · Cited by 613 · see citing works

Therapeutic targeting of the tumor microenvironment

Joyce, J. A. (2005) · Cancer Cell · doi:10.1016/j.ccr.2005.05.024 · Cited by 580 · see citing works

Physiological levels of tumstatin, a fragment of collagen IV α3 chain, are generated by MMP-9 proteolysis and suppress angiogenesis via αVβ3 integrin

Hamano, Y., Zeisberg, M., Sugimoto, H., Lively, J. C., Maeshima, Y., Yang, C., Hynes, R. O., Werb, Z., Sudhakar, A., & Kalluri, R. (2003) · Cancer Cell · doi:10.1016/s1535-6108(03)00133-8 · Cited by 560 · see citing works

Improving diagnostic accuracy and interobserver concordance in the classification and grading of primary gliomas

Coons, S. W., Johnson, P. C., Scheithauer, B. W., Yates, A. J., & Pearl, D. K. (1997) · Cancer · doi:10.1002/(sici)1097-0142(19970401)79:7 · Cited by 559 · see citing works

Size Matters: Molecular Weight Specificity of Hyaluronan Effects in Cell Biology

Cyphert, J. M., Trempus, C. S., & Garantziotis, S. (2015) · International Journal of Cell Biology · doi:10.1155/2015/563818 · Cited by 405 · see citing works

Glypican‐3: A promising biomarker for hepatocellular carcinoma diagnosis and treatment

Zhou, F., Shang, W., Yu, X., & Tian, J. (2017) · Medicinal Research Reviews · doi:10.1002/med.21455 · Cited by 401 · see citing works

A microRNA signature in circulating exosomes is superior to exosomal glypican-1 levels for diagnosing pancreatic cancer

Lai, X., Wang, M., McElyea, S. D., Sherman, S., House, M. G., & Korc, M. (2017) · Cancer Letters · doi:10.1016/j.canlet.2017.02.019 · Cited by 386 · see citing works

Proteoglycan Chemical Diversity Drives Multifunctional Cell Regulation and Therapeutics

Karamanos, N. K., Piperigkou, Z., Theocharis, A. D., Watanabe, H., Franchi, M., Baud, S., Brézillon, S., Götte, M., Passi, A. G., Vigetti, D., et al. (2018) · Chemical Reviews · doi:10.1021/acs.chemrev.8b00354 · Cited by 372 · see citing works

Endorepellin, a Novel Inhibitor of Angiogenesis Derived from the C Terminus of Perlecan

Mongiat, M., Sweeney, S. M., Antonio, J. D. S., Fu, J., & Iozzo, R. V. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m210445200 · Cited by 341 · see citing works

The High and Low Molecular Weight Forms of Hyaluronan Have Distinct Effects on CD44 Clustering

Yang, C., Cao, M., Liu, H., He, Y., Xu, J., Du, Y., Liu, Y., Wang, W., Cui, L., Hu, J., et al. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.349209 · Cited by 310 · see citing works

Phase I Trial of a Glypican-3–Derived Peptide Vaccine for Advanced Hepatocellular Carcinoma: Immunologic Evidence and Potential for Improving Overall Survival

Sawada, Y., Yoshikawa, T., Nobuoka, D., Shirakawa, H., Kuronuma, T., Motomura, Y., Mizuno, S., Ishii, H., Nakachi, K., Konishi, M., et al. (2012) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-11-3044 · Cited by 302 · see citing works

Antiangiogenic Activity of Restin, NC10 Domain of Human Collagen XV: Comparison to Endostatin

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Melanoma cell-secreted exosomal miR-155-5p induce proangiogenic switch of cancer-associated fibroblasts via SOCS1/JAK2/STAT3 signaling pathway

Zhou, X., Yan, T., Huang, C., Xu, Z., Wang, L., Jiang, E., Wang, H., Yang, C., Liu, K., Shao, Z., et al. (2018) · Journal of Experimental & Clinical Cancer Research · doi:10.1186/s13046-018-0911-3 · Cited by 285 · see citing works

Syndecan-1 regulates αvβ3 and αvβ5 integrin activation during angiogenesis and is blocked by synstatin, a novel peptide inhibitor

Beauvais, D. M., Ell, B. J., McWhorter, A. R., & Rapraeger, A. C. (2009) · The Journal of Experimental Medicine · doi:10.1084/jem.20081278 · Cited by 280 · see citing works

Elastin-derived peptides enhance angiogenesis by promoting endothelial cell migration and tubulogenesis through upregulation of MT1-MMP

Robinet, A., Fahem, A., Cauchard, J.-H., Huet, E., Vincent, L., Lorimier, S., Antonicelli, F., Soria, C., Crépin, M., Hornebeck, W., et al. (2005) · Journal of Cell Science · doi:10.1242/jcs.01613 · Cited by 256 · see citing works

ADAMTS Metalloproteases Generate Active Versican Fragments that Regulate Interdigital Web Regression

McCulloch, D. R., Nelson, C. M., Dixon, L. J., Silver, D. L., Wylie, J. D., Lindner, V., Sasaki, T., Cooley, M. A., Argraves, W. S., & Apte, S. (2009) · Developmental Cell · doi:10.1016/j.devcel.2009.09.008 · Cited by 255 · see citing works

Biophysics of tumor microenvironment and cancer metastasis – a mini review

Emon, B., Bauer, J., Jain, Y., Jung, B., & Saif, T. (2018) · Computational and Structural Biotechnology Journal · doi:10.1016/j.csbj.2018.07.003 · Cited by 245 · see citing works

Cancer Associated Fibroblasts: The Architects of Stroma Remodeling

Santi, A., Kugeratski, F. G., & Zanivan, S. R. (2017) · PROTEOMICS · doi:10.1002/pmic.201700167 · Cited by 239 · see citing works

Procollagen II Amino Propeptide Processing by ADAMTS-3

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Two RGD-independent αvβ3 Integrin Binding Sites on Tumstatin Regulate Distinct Anti-tumor Properties

Maeshima, Y., Colorado, P. C., & Kalluri, R. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.c000186200 · Cited by 229 · see citing works

A current view of perlecan in physiology and pathology: A mosaic of functions

Gubbiotti, M. A., Neill, T., & Iozzo, R. V. (2016) · Matrix Biology · doi:10.1016/j.matbio.2016.09.003 · Cited by 216 · see citing works

mTORC1 as a Regulator of Mitochondrial Functions and a Therapeutic Target in Cancer

de la Cruz-López, K. G., Toledo-Guzmán, M. E., Sánchez, E. O., & Carrancá, A. G. (2019) · Frontiers in Oncology · doi:10.3389/fonc.2019.01373 · Cited by 215 · see citing works

Endostatin associates with integrin alpha5beta1 and caveolin-1, and activates Src via a tyrosyl phosphatase-dependent pathway in human endothelial cells.

Wickström, S. A., Alitalo, K. K., & Keski‐Oja, J. (2002) · PubMed · Cited by 207 · see citing works

Roles and targeting of the HAS/hyaluronan/CD44 molecular system in cancer

Karousou, E. G., Misra, S., Ghatak, S., Dobra, K., Götte, M., Vigetti, D., Passi, A. G., Karamanos, N. K., & Skandalis, S. S. (2016) · Matrix Biology · doi:10.1016/j.matbio.2016.10.001 · Cited by 202 · see citing works

GPC 1 exosome and its regulatory mi RNA s are specific markers for the detection and target therapy of colorectal cancer

Li, J., Chen, Y., Guo, X., Zhou, L., Jia, Z., Peng, Z., Tang, Y., Liu, W., Zhu, B., Wang, L., et al. (2017) · Journal of Cellular and Molecular Medicine · doi:10.1111/jcmm.12941 · Cited by 194 · see citing works

Endostatin's emerging roles in angiogenesis, lymphangiogenesis, disease, and clinical applications

Walia, A., Yang, J., Huang, Y.-H., Rosenblatt, M. I., Chang, J., & Azar, D. T. (2015) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2015.09.007 · Cited by 182 · see citing works

The multiple, complex roles of versican and its proteolytic turnover by ADAMTS proteases during embryogenesis

Nandadasa, S., Foulcer, S. J., & Apte, S. (2014) · Matrix Biology · doi:10.1016/j.matbio.2014.01.005 · Cited by 182 · see citing works

Phase II study of the GPC3-derived peptide vaccine as an adjuvant therapy for hepatocellular carcinoma patients

Sawada, Y., Yoshikawa, T., Ofuji, K., Yoshimura, M., Tsuchiya, N., Takahashi, M., Nobuoka, D., Gotohda, N., Takahashi, S., Kato, Y., et al. (2016) · OncoImmunology · doi:10.1080/2162402x.2015.1129483 · Cited by 178 · see citing works

Glypican-1 is enriched in circulating-exosomes in pancreatic cancer and correlates with tumor burden

Frampton, A. E., Prado, M. M., López-Jiménez, E. A., Fajardo-Puerta, A. B., Jawad, Z., Lawton, P., Giovannetti, E., Habib, N., Castellano, L., Stebbing, J., et al. (2018) · Oncotarget · doi:10.18632/oncotarget.24873 · Cited by 163 · see citing works

Laminin 332 processing impacts cellular behavior

Rousselle, P., & Beck, K. (2013) · Cell Adhesion & Migration · doi:10.4161/cam.23132 · Cited by 160 · see citing works

The cancer matrisome: From comprehensive characterization to biomarker discovery

Socovich, A. M., & Naba, A. (2018) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2018.06.005 · Cited by 158 · see citing works

Canstatin Acts on Endothelial and Tumor Cells via Mitochondrial Damage Initiated through Interaction with αvβ3 and αvβ5 Integrins

Magnon, C., Galaup, A., Mullan, B., Rouffiac, V., Bidart, J., Griscelli, F., Opolon, P., & Perricaudet, M. (2005) · Cancer Research · doi:10.1158/0008-5472.can-04-3536 · Cited by 152 · see citing works

Epithelial-to-mesenchymal transition and invadopodia markers in breast cancer: Lumican a key regulator

Καραμάνου, Κ., Franchi, M., Vynios, D. H., & Brézillon, S. (2019) · Seminars in Cancer Biology · doi:10.1016/j.semcancer.2019.08.003 · Cited by 152 · see citing works

Immunoregulatory roles of versican proteolysis in the myeloma microenvironment

Hope, C. L., Foulcer, S. J., Jagodinsky, J. C., Chen, S. X., Jensen, J. L., Patel, S., Leith, C. P., Maroulakou, I. G., Callander, N. S., Miyamoto, S., et al. (2016) · Blood · doi:10.1182/blood-2016-03-705780 · Cited by 147 · see citing works

MT2-MMP-Dependent Release of Collagen IV NC1 Domains Regulates Submandibular Gland Branching Morphogenesis

Rebustini, I. T., Myers, C., Lassiter, K. S., Surmak, A. J., Szabova, L., Holmbeck, K., Pedchenko, V. K., Hudson, B. G., & Hoffman, M. P. (2009) · Developmental Cell · doi:10.1016/j.devcel.2009.07.016 · Cited by 146 · see citing works

Fragments generated upon extracellular matrix remodeling: Biological regulators and potential drugs

Ricard‐Blum, S., & Vallet, S. D. (2017) · Matrix Biology · doi:10.1016/j.matbio.2017.11.005 · Cited by 143 · see citing works

Role of hyaluronan in pancreatic cancer biology and therapy: Once again in the spotlight

Sato, N., Kohi, S., Hirata, K., & Goggins, M. (2016) · Cancer Science · doi:10.1111/cas.12913 · Cited by 141 · see citing works

Next-Generation Cancer Immunotherapy Targeting Glypican-3

Shimizu, Y., Suzuki, T., Yoshikawa, T., Endo, I., & Nakatsura, T. (2019) · Frontiers in Oncology · doi:10.3389/fonc.2019.00248 · Cited by 136 · see citing works

Endostatin and endorepellin: A common route of action for similar angiostatic cancer avengers

Poluzzi, C., Iozzo, R. V., & Schaefer, L. (2015) · Advanced Drug Delivery Reviews · doi:10.1016/j.addr.2015.10.012 · Cited by 133 · see citing works

Laminin-111-derived peptides and cancer

Kikkawa, Y., Hozumi, K., Katagiri, F., Nomizu, M., Kleinman, H. K., & Koblinski, J. E. (2013) · Cell Adhesion & Migration · doi:10.4161/cam.22827 · Cited by 132 · see citing works

A Frizzled‐Like Cysteine‐Rich Domain in Glypican‐3 Mediates Wnt Binding and Regulates Hepatocellular Carcinoma Tumor Growth in Mice

Li, N., Wei, L., Liu, X., Bai, H., Ye, Y., Li, D., Li, N., Baxa, U., Wang, Q., Lv, L., et al. (2019) · Hepatology · doi:10.1002/hep.30646 · Cited by 127 · see citing works

The Tumor Microenvironment and Strategies to Improve Drug Distribution

Saggar, J. K., Yu, M., Tan, Q., & Tannock, I. F. (2013) · Frontiers in Oncology · doi:10.3389/fonc.2013.00154 · Cited by 124 · see citing works

αvβ3 and αvβ5 Integrins Bind Both the Proximal RGD Site and Non-RGD Motifs within Noncollagenous (NC1) Domain of the α3 Chain of Type IV Collagen

Pedchenko, V. K., Zent, R., & Hudson, B. G. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m311901200 · Cited by 123 · see citing works

Tumstatin, the NC1 domain of α3 chain of type IV collagen, is an endogenous inhibitor of pathological angiogenesis and suppresses tumor growth

Hamano, Y., & Kalluri, R. (2005) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2005.05.130 · Cited by 123 · see citing works

Syndecan-1 and Syndecan-4 Are Independent Indicators in Breast Carcinoma

Lendorf, M. E., Manon‐Jensen, T., Kronqvist, P., Multhaupt, H. A. B., & Couchman, J. (2011) · Journal of Histochemistry & Cytochemistry · doi:10.1369/0022155411405057 · Cited by 123 · see citing works

Elevated glypican‐1 expression is associated with an unfavorable prognosis in pancreatic ductal adenocarcinoma

Lu, H., Niu, F., Liu, F., Gao, J., Sun, Y., & Zhao, X. (2017) · Cancer Medicine · doi:10.1002/cam4.1064 · Cited by 119 · see citing works

Heparanase-induced shedding of syndecan-1/CD138 in myeloma and endothelial cells activates VEGFR2 and an invasive phenotype: prevention by novel synstatins

Jung, O., Trapp‐Stamborski, V., Purushothaman, A., Jin, H., Wang, H., Sanderson, R. D., & Rapraeger, A. C. (2016) · Oncogenesis · doi:10.1038/oncsis.2016.5 · Cited by 116 · see citing works

The Role of Glypican-3 in Regulating Wnt, YAP, and Hedgehog in Liver Cancer

Kolluri, A., & Ho, M. (2019) · Frontiers in Oncology · doi:10.3389/fonc.2019.00708 · Cited by 115 · see citing works

Excessive collagen turnover products are released during colorectal cancer progression and elevated in serum from metastatic colorectal cancer patients

Kehlet, S. N., Pamplona, R. S., Brix, S., Leeming, D. J., Karsdal, M. A., & Moreno, V. R. (2016) · Scientific Reports · doi:10.1038/srep30599 · Cited by 114 · see citing works

Locally generated VGVAPG and VAPG elastin‐derived peptides amplify melanoma invasion via the galectin‐3 receptor

Pócza, P., Süli‐Vargha, H., Darvas, Z., & Falus, A. (2007) · International Journal of Cancer · doi:10.1002/ijc.23296 · Cited by 113 · see citing works

Versican-Derived Matrikines Regulate Batf3–Dendritic Cell Differentiation and Promote T Cell Infiltration in Colorectal Cancer

Hope, C. L., Emmerich, P. B., Papadas, A., Pagenkopf, A. C., Matkowskyj, K. A., Hey, D. R. V. D., Payne, S. N., Clipson, L. J., Callander, N. S., Hematti, P., et al. (2017) · The Journal of Immunology · doi:10.4049/jimmunol.1700529 · Cited by 113 · see citing works

Degradation of tropoelastin by matrix metalloproteinases – cleavage site specificities and release of matrikines

Heinz, A., Jung, M. C., Duca, L., Sippl, W., Taddese, S., Ihling, C. H., Rusciani, A., Jahreis, G., Weiss, A. S., Neubert, R. H. H., et al. (2010) · FEBS Journal · doi:10.1111/j.1742-4658.2010.07616.x · Cited by 112 · see citing works

Matrikines from basement membrane collagens: A new anti-cancer strategy

Monboisse, J., Oudart, J., Ramont, L., Brassart‐Pasco, S., & Maquart, F. X. (2014) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2013.12.029 · Cited by 112 · see citing works

Lumican effects in the control of tumour progression and their links with metalloproteinases and integrins

Brézillon, S., Pietraszek‐Gremplewicz, K., Maquart, F., & Wegrowski, Y. (2013) · FEBS Journal · doi:10.1111/febs.12210 · Cited by 107 · see citing works

Synstatin: a selective inhibitor of the syndecan‐1‐coupled IGF 1 R –αvβ3 integrin complex in tumorigenesis and angiogenesis

Rapraeger, A. C. (2013) · FEBS Journal · doi:10.1111/febs.12160 · Cited by 104 · see citing works

Metastatin: a hyaluronan-binding complex from cartilage that inhibits tumor growth.

Liu, N., Lapcevich, R., Underhill, C. B., Han, Z., Gao, F., Swartz, G., Plum, S., Zhang, L., & Green, S. J. (2001) · PubMed · Cited by 101 · see citing works

Elastin-Derived Peptides Upregulate Matrix Metalloproteinase-2-ediated Melanoma Cell Invasion Through Elastin-Binding Protein

Ntayi, C., Labrousse, A.-L., Debret, R., Birembaut, P., Bellon, G., Antonicelli, F. D., Hornebeck, W., & Bernard, P. (2004) · Journal of Investigative Dermatology · doi:10.1046/j.0022-202x.2004.22228.x · Cited by 95 · see citing works

Lumican inhibits cell migration through α2β1 integrin

Zeltz, C., Brézillon, S., Käpylä, J., Eble, J. A., Bobichon, H., Terryn, C., Perreau, C., Franz, C. M., Heino, J., Maquart, F., et al. (2010) · Experimental Cell Research · doi:10.1016/j.yexcr.2010.08.002 · Cited by 91 · see citing works

Vascular endothelial‐cadherin stimulates syndecan‐1‐coupled insulin‐like growth factor‐1 receptor and cross‐talk between α V β3 integrin and vascular endothelial growth factor receptor 2 at the onset of endothelial cell dissemination during angiogenesis

Rapraeger, A. C., Ell, B. J., Roy, M., Li, X., Morrison, O. R., Thomas, G. M., & Beauvais, D. M. (2013) · FEBS Journal · doi:10.1111/febs.12134 · Cited by 83 · see citing works

The Antitumor Properties of the α3(IV)-(185-203) Peptide from the NC1 Domain of Type IV Collagen (Tumstatin) Are Conformation-dependent

Floquet, N., Brassart‐Pasco, S., Ramont, L., Derreumaux, P., Laronze, J. Y., Nuzillard, J., Maquart, F. X., Alix, A. J. P., & Monboisse, J. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m307736200 · Cited by 78 · see citing works

Lumican Binds ALK5 to Promote Epithelium Wound Healing

Yamanaka, O., Yuan, Y., Coulson‐Thomas, V. J., Gesteira, T. F., Call, M. K., Zhang, Y., Zhang, J., Chang, S., Xie, C., Liu, C., et al. (2013) · PLoS ONE · doi:10.1371/journal.pone.0082730 · Cited by 77 · see citing works

Lumican: A new inhibitor of matrix metalloproteinase‐14 activity

Pietraszek‐Gremplewicz, K., Chatron-Colliet, A., Brézillon, S., Perreau, C., Jakubiak-Augustyn, A., Krotkiewski, H., Maquart, F., & Wegrowski, Y. (2014) · FEBS Letters · doi:10.1016/j.febslet.2014.09.040 · Cited by 77 · see citing works

Syndecan-1 and Syndecan-4 Capture Epidermal Growth Factor Receptor Family Members and the α3β1 Integrin Via Binding Sites in Their Ectodomains

Wang, H., Jin, H., & Rapraeger, A. C. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m115.679084 · Cited by 75 · see citing works

Identification of circulating endorepellin LG3 fragment: Potential use as a serological biomarker for breast cancer

Chang, J. W., Kang, U., Kim, D., Yi, J. K., Lee, J. W., Noh, D., Lee, C., & Yu, M. (2007) · PROTEOMICS - CLINICAL APPLICATIONS · doi:10.1002/prca.200780049 · Cited by 73 · see citing works

The action of neutrophil serine proteases on elastin and its precursor

Heinz, A., Jung, M. C., Jahreis, G., Rusciani, A., Duca, L., Debelle, L., Weiss, A. S., Neubert, R. H. H., & Schmelzer, C. E. H. (2011) · Biochimie · doi:10.1016/j.biochi.2011.10.006 · Cited by 72 · see citing works

The clinical significance of circulating GPC1 positive exosomes and its regulative miRNAs in colon cancer patients

Li, J., Li, B., Ren, C., Chen, Y., Guo, X., Zhou, L., Peng, Z., Tang, Y., Chen, Y., Liu, W., et al. (2017) · Oncotarget · doi:10.18632/oncotarget.20516 · Cited by 71 · see citing works

Small leucine-rich proteoglycans and matrix metalloproteinase-14: Key partners?

Pietraszek‐Gremplewicz, K., Καραμάνου, Κ., Niang, A., Dauchez, M., Belloy, N., Maquart, F., Baud, S., & Brézillon, S. (2017) · Matrix Biology · doi:10.1016/j.matbio.2017.12.006 · Cited by 71 · see citing works

Extracellular matrix specific protein fingerprints measured in serum can separate pancreatic cancer patients from healthy controls

Willumsen, N., Bager, C. L., Leeming, D. J., Smith, V., Karsdal, M. A., Dornan, D., & Bay‐Jensen, A. (2013) · BMC Cancer · doi:10.1186/1471-2407-13-554 · Cited by 70 · see citing works

Quantitative Tissue Proteomics Analysis Reveals Versican as Potential Biomarker for Early-Stage Hepatocellular Carcinoma

Naboulsi, W., Megger, D. A., Bracht, T., Kohl, M., Turewicz, M., Eisenacher, M., Voss, D. M., Schlaak, J., Hoffmann, A.-C., Weber, F., et al. (2015) · Journal of Proteome Research · doi:10.1021/acs.jproteome.5b00420 · Cited by 70 · see citing works

The role of perlecan and endorepellin in the control of tumor angiogenesis and endothelial cell autophagy

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Clinical Significance of Serum COL6A3 in Pancreatic Ductal Adenocarcinoma

Kang, C. Y., Wang, J., Axell‐House, D. B., Soni, P., Chu, M., Chipitsyna, G. I., Sarosiek, K., Sendecki, J. A., Hyslop, T., Zoubi, M. S. A., et al. (2013) · Journal of Gastrointestinal Surgery · doi:10.1007/s11605-013-2326-y · Cited by 67 · see citing works

Glypican-1 in exosomes as biomarker for early detection of pancreatic cancer.

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Tetrastatin, the NC1 Domain of the α4(IV) Collagen Chain: A Novel Potent Anti-Tumor Matrikine

Brassart‐Pasco, S., Sénéchal, K., Thévenard, J., Ramont, L., Devy, J., Stefano, L. D., Dupont-Deshorgue, A., Brézillon, S., Feru, J., Jazeron, J.-F., et al. (2012) · PLoS ONE · doi:10.1371/journal.pone.0029587 · Cited by 66 · see citing works

Identification of novel short peptides derived from the α4, α5, and α6 fibrils of type IV collagen with anti-angiogenic properties

Karagiannis, E. D., & Popel, A. S. (2007) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2006.12.231 · Cited by 66 · see citing works

Targeting microenvironment in cancer therapeutics

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Lumican – Derived Peptides Inhibit Melanoma Cell Growth and Migration

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