Extracellular matrix and its therapeutic potential for cancer treatment

Global Cancer Statistics 2020: GLOBOCAN Estimates of Incidence and Mortality Worldwide for 36 Cancers in 185 Countries

Sung, H., Ferlay, J., Siegel, R. L., Laversanne, M., Soerjomataram, I., Jemal, A., & Bray, F. (2021) · CA: A Cancer Journal for Clinicians · doi:10.3322/caac.21660 · Cited by 108,699

Hallmarks of Cancer: The Next Generation

Hanahan, D., & Weinberg, R. A. (2011) · Cell · doi:10.1016/j.cell.2011.02.013 · Cited by 66,590

Stem cells, cancer, and cancer stem cells

Reya, T., Morrison, S. J., Clarke, M. F., & Weissman, I. L. (2001) · Nature · doi:10.1038/35102167 · Cited by 9,738

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

Mutational heterogeneity in cancer and the search for new cancer-associated genes

Lawrence, M. S., Stojanov, P., Polak, P., Kryukov, G. V., Cibulskis, K., Sivachenko, A., Carter, S. L., Stewart, C., Mermel, C. H., Roberts, S. A., et al. (2013) · Nature · doi:10.1038/nature12213 · Cited by 5,461

Targeting Hypoxia-Inducible Factors for the Treatment of Anemia in Chronic Kidney Disease Patients

Locatelli, F., Fishbane, S. N., Block, G. A., & Macdougall, I. C. (2017) · American Journal of Nephrology · doi:10.1159/000455166 · Cited by 4,836

Matrix Metalloproteinases and Tissue Inhibitors of Metalloproteinases: Structure, Function, and Biochemistry

Visse, R., & Nagase, H. (2003) · Circulation Research · doi:10.1161/01.res.0000070112.80711.3d · Cited by 4,575

Fibroblasts in cancer

Kalluri, R., & Zeisberg, M. (2006) · Nature Reviews Cancer · doi:10.1038/nrc1877 · Cited by 4,538

Atezolizumab and nab-paclitaxel in advanced triple-negative breast cancer

Schmid, P., Adams, S., Rugo, H. S., Schneeweiss, A., Barrios, C. H., Iwata, H., Diéras, V., Hegg, R., Im, S.-A., Shaw Wright, G., et al. (2018) · New England Journal of Medicine · doi:10.1056/nejmoa1809615 · Cited by 4,350

Matrix Crosslinking Forces Tumor Progression by Enhancing Integrin Signaling

Levental, K. R., Yu, H., Kass, L., Lakins, J. N., Egeblad, M., Erler, J. T., Fong, S. F. T., Csiszar, K., Giaccia, A., Weninger, W., et al. (2009) · Cell · doi:10.1016/j.cell.2009.10.027 · Cited by 4,101

Tensional homeostasis and the malignant phenotype

Paszek, M. J., Zahir, N., Johnson, K. R., Lakins, J. N., Rozenberg, G. I., Gefen, A., Reinhart-King, C. A., Margulies, S. S., Dembo, M., Boettiger, D., et al. (2005) · Cancer Cell · doi:10.1016/j.ccr.2005.08.010 · Cited by 3,941

The Extracellular Matrix: Not Just Pretty Fibrils

Hynes, R. O. (2009) · Science · doi:10.1126/science.1176009 · Cited by 3,527

Hepatogastroenterology

Chen, L., Li, N., & Ye, H. (2012) · Hepatogastroenterology · doi:10.5754/hge12469 · Cited by 3,208

Matrix Metalloproteinase Inhibitors and Cancer—Trials and Tribulations

Coussens, L. M., Fingleton, B., & Matrisian, L. M. (2002) · Science · doi:10.1126/science.1067100 · Cited by 2,761

Matrix metalloproteinases and the regulation of tissue remodelling

Page-McCaw, A., Ewald, A. J., & Werb, Z. (2007) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2125 · Cited by 2,630

EMT, CSCs, and drug resistance: the mechanistic link and clinical implications

Shibue, T., & Weinberg, R. A. (2017) · Nature Reviews Clinical Oncology · doi:10.1038/nrclinonc.2017.44 · Cited by 2,539

Transforming growth factor-beta stimulates the expression of fibronectin and collagen and their incorporation into the extracellular matrix.

Ignotz, R. A., & Massagué, J. (1986) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)35666-1 · Cited by 2,492

Cancer and the chemokine network

Balkwill, F. (2004) · Nature Reviews Cancer · doi:10.1038/nrc1388 · Cited by 2,343

Global Survey of Phosphotyrosine Signaling Identifies Oncogenic Kinases in Lung Cancer

Rikova, K., Guo, A., Zeng, Q., Possemato, A., Yu, J., Haack, H., Nardone, J., Lee, K., Reeves, C., Li, Y., et al. (2007) · Cell · doi:10.1016/j.cell.2007.11.025 · Cited by 2,317

The Collagen Family

Ricard-Blum, S. (2011) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a004978 · Cited by 2,305

Distinct role of macrophages in different tumor microenvironments

Lewis, C. E., & Pollard, J. W. (2006) · Cancer Research · doi:10.1158/0008-5472.can-05-4005 · Cited by 2,225

Identification of a subpopulation of cells with cancer stem cell properties in head and neck squamous cell carcinoma

Prince, M. E., Sivanandan, R., Kaczorowski, A., Wolf, G. T., Kaplan, M. J., Dalerba, P. D., Weissman, I. L., Clarke, M. F., & Ailles, L. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0610117104 · Cited by 2,205

Untitled work

(1999) · PubMed · Cited by 2,204

Fibronectin at a glance

Pankov, R. G., & Yamada, K. M. (2002) · Journal of Cell Science · doi:10.1242/jcs.00059 · Cited by 2,055

Nuclear Lamin-A Scales with Tissue Stiffness and Enhances Matrix-Directed Differentiation

Swift, J., Ivanovska, I. L., Buxboim, A., Harada, T., Dingal, P. C. D. P., Pinter, J., Pajerowski, J. D., Spinler, K. R., Shin, J., Tewari, M., et al. (2013) · Science · doi:10.1126/science.1240104 · Cited by 1,998

Matrix metalloproteinases as modulators of inflammation and innate immunity

Parks, W. C., Wilson, C. L., & López-Boado, Y. S. (2004) · Nature Reviews Immunology · doi:10.1038/nri1418 · Cited by 1,929

Basement membranes: structure, assembly and role in tumour angiogenesis

Kalluri, R. (2003) · Nature reviews. Cancer · doi:10.1038/nrc1094 · Cited by 1,840

Targeting BTK with ibrutinib in relapsed or refractory mantle-cell lymphoma

Wang, M. L., Rule, S., Martin, P., Goy, A., Auer, R., Kahl, B. S., Jurczak, W., Advani, R. H., Romaguera, J. E., Williams, M. E., et al. (2013) · New England Journal of Medicine · doi:10.1056/nejmoa1306220 · Cited by 1,685

The microRNA miR-34a inhibits prostate cancer stem cells and metastasis by directly repressing CD44

Liu, C., Kelnar, K., Liu, B., Chen, X., Calhoun‐Davis, T., Li, H., Patrawala, L., Yan, H., Jeter, C. R., Honorio, S., et al. (2011) · Nature Medicine · doi:10.1038/nm.2284 · Cited by 1,410

Biochemical and Biological Attributes of Matrix Metalloproteinases

Cui, N., Hu, M., & Khalil, R. A. (2017) · Progress in Molecular Biology and Translational Science · doi:10.1016/bs.pmbts.2017.02.005 · Cited by 1,359

The Matrisome: In Silico Definition and In Vivo Characterization by Proteomics of Normal and Tumor Extracellular Matrices

Naba, A., Clauser, K. R., Hoersch, S., Liu, H., Carr, S. A., & Hynes, R. O. (2012) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m111.014647 · Cited by 1,354

Strategies for MMP inhibition in cancer: innovations for the post-trial era

Overall, C. M., & López-Otín, C. (2002) · Nature Reviews Cancer · doi:10.1038/nrc884 · Cited by 1,349

The Expression and Distribution of the Hypoxia-Inducible Factors HIF-1α and HIF-2α in Normal Human Tissues, Cancers, and Tumor-Associated Macrophages

Talks, K. L., Turley, H., Gatter, K. C., Maxwell, P. H., Pugh, C. W., Ratcliffe, P. J., & Harris, A. L. (2000) · The American Journal of Pathology · doi:10.1016/s0002-9440(10)64554-3 · Cited by 1,312

Collagen family of proteins

REST, M. V. D., & Garrone, R. (1991) · The FASEB Journal · doi:10.1096/fasebj.5.13.1916105 · Cited by 1,302

Mechanotransduction in vascular physiology and atherogenesis

Hahn, C. S., & Schwartz, M. A. (2008) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2596 · Cited by 1,257

Oxygen Sensing, Hypoxia-Inducible Factors, and Disease Pathophysiology

Semenza, G. L. (2013) · Annual Review of Pathology Mechanisms of Disease · doi:10.1146/annurev-pathol-012513-104720 · Cited by 1,180

Role of extracellular matrix assembly in interstitial transport in solid tumors.

Netti, P. A., Berk, D. A., Swartz, M. A., Grodzinsky, A. J., & Jain, R. K. (2000) · PubMed · Cited by 1,165

Spherical Nucleic Acids

Cutler, J. I., Auyeung, E., & Mirkin, C. A. (2012) · Journal of the American Chemical Society · doi:10.1021/ja209351u · Cited by 1,151

The nanomechanical signature of breast cancer

Plodinec, M., Loparić, M., Monnier, C. A., Obermann, E. C., Zanetti‐Dällenbach, R., Oertle, P., Hyötylä, J. T., Aebi, U., Bentires‐Alj, M., Lim, R. Y. H., et al. (2012) · Nature Nanotechnology · doi:10.1038/nnano.2012.167 · Cited by 1,148

Matrix architecture defines the preferential localization and migration of T cells into the stroma of human lung tumors

Salmon, H., Franciszkiewicz, K., Damotte, D., Dieu-Nosjean, M.-C., Validire, P., Trautmann, A., Mami-Chouaib, F., & Donnadieu, E. (2012) · Journal of Clinical Investigation · doi:10.1172/jci45817 · Cited by 1,138

Progression to Malignancy in the Polyoma Middle T Oncoprotein Mouse Breast Cancer Model Provides a Reliable Model for Human Diseases

Lin, E. Y., Jones, J. G., Li, P., Zhu, L., Whitney, K. D., Muller, W. J., & Pollard, J. W. (2003) · American Journal Of Pathology · doi:10.1016/s0002-9440(10)63568-7 · Cited by 1,109

Glycosaminoglycans: molecular properties, protein interactions, and role in physiological processes

Jackson, R. L., Busch, S. J., & Cardin, A. D. (1991) · Physiological Reviews · doi:10.1152/physrev.1991.71.2.481 · Cited by 1,099

Identification of Gastric Cancer Stem Cells Using the Cell Surface Marker CD44

Takaishi, S., Okumura, T., Tu, S., Wang, S. S. W., Shibata, W., Ramanathan, V., Gordon, S. A. K., Shimada, Y., & Wang, T. C. (2009) · Stem Cells · doi:10.1002/stem.30 · Cited by 1,059

Signaling Properties of Hyaluronan Receptors

Turley, E. A., Noble, P. W., & Bourguignon, L. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.r100038200 · Cited by 1,041

Quantitative chemical proteomics reveals mechanisms of action of clinical ABL kinase inhibitors

Bantscheff, M., Eberhard, D., Abraham, Y., Bastuck, S., Böesche, M., Hobson, S., Mathieson, T., Perrin, J., Raida, M., Rau, C., et al. (2007) · Nature Biotechnology · doi:10.1038/nbt1328 · Cited by 1,036

Angiotensin inhibition enhances drug delivery and potentiates chemotherapy by decompressing tumour blood vessels

Chauhan, V. P., Martin, J. D., Liu, H., Lacorre, D. A., Jain, S. R., Kozin, S. V., Stylianopoulos, T., Mousa, A. S., Han, X., Adstamongkonkul, P., et al. (2013) · Nature Communications · doi:10.1038/ncomms3516 · Cited by 1,031

The Discoidin Domain Receptor Tyrosine Kinases Are Activated by Collagen

Vogel, W., Gish, G. D., Alves, F., & Pawson, T. (1997) · Molecular Cell · doi:10.1016/s1097-2765(00)80003-9 · Cited by 1,002

Highly purified CD44+ prostate cancer cells from xenograft human tumors are enriched in tumorigenic and metastatic progenitor cells

Patrawala, L., Calhoun, T., Schneider‐Broussard, R., Li, H., Bhatia, B., Tang, S., Reilly, J. G., Chandra, D., Zhou, J., Claypool, K., et al. (2006) · Oncogene · doi:10.1038/sj.onc.1209327 · Cited by 969

Causes, consequences, and remedies for growth-induced solid stress in murine and human tumors

Stylianopoulos, T., Martin, J. D., Chauhan, V. P., Jain, S. R., Diop-Frimpong, B., Bardeesy, N., Smith, B. L., Ferrone, C. R., Hornicek, F. J., Boucher, Y., et al. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1213353109 · Cited by 943

Periostin secreted by glioblastoma stem cells recruits M2 tumour-associated macrophages and promotes malignant growth

Zhou, W., Ke, S. Q., Huang, Z., Flavahan, W., Fang, X., Paul, J., Wu, L., Sloan, A. E., McLendon, R. E., Li, X., et al. (2015) · Nature Cell Biology · doi:10.1038/ncb3090 · Cited by 940

TGF-β Signaling from Receptors to SmadsPreprint

Hata, A., & Chen, Y. (2016) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a022061 · Cited by 929

A simplified laminin nomenclature

Aumailley, M., Bruckner‐Tuderman, L., Carter, W. G., Deutzmann, R., EDGAR, D., Ekblom, P., Engel, J., Engvall, E., Hohenester, E., & Jones, J. (2005) · Matrix Biology · doi:10.1016/j.matbio.2005.05.006 · Cited by 928

Platelet Membrane Glycoprotein IIb/IIIa: Member of a Family of Arg-Gly-Asp—Specific Adhesion Receptors

Pytela, R., Pierschbacher, M. D., Ginsberg, M. H., Plow, E. F., & Ruoslahti, E. I. (1986) · Science · doi:10.1126/science.2420006 · Cited by 924

Imaging cells and extracellular matrix in vivo by using second-harmonic generation and two-photon excited fluorescence

Zoumi, A., Yeh, A. T., & Tromberg, B. J. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.172368799 · Cited by 872

Structure of integrin, a glycoprotein involved in the transmembrane linkage between fibronectin and actin

Tamkun, J. W., DeSimone, D. W., Fonda, D., Patel‐King, R. S., Buck, C. A., Horwitz, A. F., & Hynes, R. O. (1986) · Cell · doi:10.1016/0092-8674(86)90744-0 · Cited by 871

Interactions between Hyaluronan and Its Receptors (CD44, RHAMM) Regulate the Activities of Inflammation and Cancer

Misra, S., Hascall, V. C., Markwald, R. R., & Ghatak, S. (2015) · Frontiers in Immunology · doi:10.3389/fimmu.2015.00201 · Cited by 830

Fibronectin fibrillogenesis, a cell-mediated matrix assembly process

Mao, Y., & Schwarzbauer, J. E. (2005) · Matrix Biology · doi:10.1016/j.matbio.2005.06.008 · Cited by 819

Bruton tyrosine kinase represents a promising therapeutic target for treatment of chronic lymphocytic leukemia and is effectively targeted by PCI-32765

Herman, S. E. M., Gordon, A. L., Hertlein, E., Ramanunni, A., Zhang, X., Jaglowski, S., Flynn, J., Jones, J., Blum, K. A., Buggy, J. J., et al. (2011) · Blood · doi:10.1182/blood-2011-01-328484 · Cited by 807

Collagen fibrillogenesis: fibronectin, integrins, and minor collagens as organizers and nucleators

Kadler, K. E., Hill, A., & Canty‐Laird, E. G. (2008) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2008.06.008 · Cited by 793

Specificity, versatility, and control of TGF-β family signaling

Derynck, R., & Budi, E. H. (2019) · Science Signaling · doi:10.1126/scisignal.aav5183 · Cited by 785

Growth Inhibitor from BSC-1 Cells Closely Related to Platelet Type β Transforming Growth Factor

Tucker, R. F., Shipley, G. D., Moses, H. L., & Holley, R. W. (1984) · Science · doi:10.1126/science.6093254 · Cited by 768

The role of collagen in cancer: from bench to bedside

Xu, S., Xu, H., Wang, W., Li, S., Li, H., Li, T., Zhang, W., Yu, X., & Liu, L. (2019) · Journal of Translational Medicine · doi:10.1186/s12967-019-2058-1 · Cited by 735

CD44v6 Is a Marker of Constitutive and Reprogrammed Cancer Stem Cells Driving Colon Cancer Metastasis

Todaro, M., Gaggianesi, M., Catalano, V., Benfante, A., Iovino, F., Biffoni, M., Apuzzo, T., Sperduti, I., Volpe, S., Cocorullo, G., et al. (2014) · Cell stem cell · doi:10.1016/j.stem.2014.01.009 · Cited by 733

Losartan inhibits collagen I synthesis and improves the distribution and efficacy of nanotherapeutics in tumors

Diop-Frimpong, B., Chauhan, V. P., Krane, S., Boucher, Y., & Jain, R. K. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1018892108 · Cited by 733

How is blood vessel growth regulated in normal and neoplastic tissue? G.H.A. Clowes memorial Award lecture.

Folkman, J. (1986) · PubMed · Cited by 732

Mechanically Activated Integrin Switch Controls α 5 β 1 Function

Friedland, J. C., Lee, M. H., & Boettiger, D. E. (2009) · Science · doi:10.1126/science.1168441 · Cited by 717

Fibrosis and cancer: A strained relationship

Piersma, B., Hayward, M.-K., & Weaver, V. M. (2020) · Biochimica et Biophysica Acta (BBA) - Reviews on Cancer · doi:10.1016/j.bbcan.2020.188356 · Cited by 715

Extracellular matrix (ECM) stiffness and degradation as cancer drivers

Najafi, M., Farhood, B., & Mortezaee, K. (2018) · Journal of Cellular Biochemistry · doi:10.1002/jcb.27681 · Cited by 711

The tenascin family of ECM glycoproteins: Structure, function, and regulation during embryonic development and tissue remodeling

Jones, F. S., & Jones, P. L. (2000) · Developmental Dynamics · doi:10.1002/(sici)1097-0177(200006)218:2 · Cited by 699

Inflammation and angiotensin II

Suzuki, Y., Ruiz‐Ortega, M., Lorenzo, Ó., Rupérez, M., Esteban, V., & Egido, J. (2003) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/s1357-2725(02)00271-6 · Cited by 696

Anti-angiogenesis for cancer revisited: Is there a role for combinations with immunotherapy?

Ramjiawan, R. R., Griffioen, A. W., & Duda, D. G. (2017) · Angiogenesis · doi:10.1007/s10456-017-9552-y · Cited by 680

Spherical Nucleic Acids*

Cutler, J. I., Auyeung, E., & Mirkin, C. A. (2020) · Spherical Nucleic Acids · doi:10.1201/9781003056676-5 · Cited by 676

Chromothripsis and Kataegis Induced by Telomere Crisis

Maciejowski, J., Li, Y., Bosco, N., Campbell, P. J., & de Lange, T. (2015) · Cell · doi:10.1016/j.cell.2015.11.054 · Cited by 675

Chemical proteomic profiles of the BCR-ABL inhibitors imatinib, nilotinib, and dasatinib reveal novel kinase and nonkinase targets

Rix, U., Hantschel, O. D., Dürnberger, G., Rix, L. L. R., Planyavsky, M., Fernbach, N. V., Kaupe, I., Bennett, K. L., Valent, P., Colinge, J., et al. (2007) · Blood · doi:10.1182/blood-2007-07-102061 · Cited by 671

Linkage of G Protein-Coupled Receptors to the MAPK Signaling Pathway Through PI 3-Kinase γ

Lopez-Ilasaca, M. A., Crespo, P., Pellici, P. G., Gutkind, J. S., & Wetzker, R. (1997) · Science · doi:10.1126/science.275.5298.394 · Cited by 670

Cilengitide: The First Anti-Angiogenic Small Molecule Drug Candidate. Design, Synthesis and Clinical Evaluation

Mas‐Moruno, C., Rechenmacher, F., & Kessler, H. (2010) · Anti-Cancer Agents in Medicinal Chemistry · doi:10.2174/187152010794728639 · Cited by 669

The role of stroma in pancreatic cancer: Diagnostic and therapeutic implications

Erkan, M., Hausmann, S., Michalski, C. W., Fingerle, A. A., Dobritz, M., Kleeff, J., & Friess, H. (2012) · Nature Reviews Gastroenterology & Hepatology · doi:10.1038/nrgastro.2012.115 · Cited by 662

Desmoplasia in Primary Tumors and Metastatic Lesions of Pancreatic Cancer

Whatcott, C. J., Diep, C. H., Jiang, P., Watanabe, A. T., Lobello, J. R., Sima, C., Hostetter, G. H., Shepard, H. M., Hoff, D. D. V., & Han, H. (2015) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-14-1051 · Cited by 658

Plasma and cellular fibronectin: distinct and independent functions during tissue repair

To, W. S., & Midwood, K. S. (2011) · Fibrogenesis & Tissue Repair · doi:10.1186/1755-1536-4-21 · Cited by 651

The Bruton tyrosine kinase inhibitor PCI-32765 thwarts chronic lymphocytic leukemia cell survival and tissue homing in vitro and in vivo

Ponader, S., Chen, S.-S., Buggy, J. J., Balakrishnan, K., Gandhi, V., Wierda, W. G., Keating, M. J., O'Brien, S., Chiorazzi, N., & Burger, J. A. (2012) · Blood · doi:10.1182/blood-2011-10-386417 · Cited by 640

CD44 is of Functional Importance for Colorectal Cancer Stem Cells

Du, L., Wang, H., He, L., Zhang, J., Ni, B., Wang, X., Jin, H., Cahuzac, N., Mehrpour, M., Lu, Y., et al. (2008) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-08-1034 · Cited by 613

Nuclear lamin stiffness is a barrier to 3D migration, but softness can limit survival

Harada, T., Swift, J., Irianto, J., Shin, J., Spinler, K. R., Athirasala, A., Diegmiller, R., Dingal, P. C. D. P., Ivanovska, I. L., & Discher, D. E. (2014) · The Journal of Cell Biology · doi:10.1083/jcb.201308029 · Cited by 611

Expression and Function of Laminins in the Embryonic and Mature Vasculature

Hallmann, R., Horn, N., Selg, M., Wendler, O., Pausch, F., & Sorokin, L. M. (2005) · Physiological Reviews · doi:10.1152/physrev.00014.2004 · Cited by 597

TGF-β Receptor Inhibitors Target the CD44high/Id1high Glioma-Initiating Cell Population in Human Glioblastoma

Anido, J., Sáez‐Borderías, A., Gonzàlez-Juncà, A., Rodón, L., Folch, G., Carmona, M. A., Prieto-Sánchez, R. M., Barba, I., Martínez-Sáez, E. A., Prudkin, L., et al. (2010) · Cancer Cell · doi:10.1016/j.ccr.2010.10.023 · Cited by 592

Amino acid sequence of the human fibronectin receptor.

Argraves, W. S., Suzuki, S., Arai, H., Thompson, K. A., Pierschbacher, M. D., & Ruoslahti, E. (1987) · The Journal of Cell Biology · doi:10.1083/jcb.105.3.1183 · Cited by 585

Collagen as a double-edged sword in tumor progression

Fang, M., Yuan, J., Peng, C., & Li, Y. (2014) · Tumor Biology · doi:10.1007/s13277-013-1511-7 · Cited by 580

Therapeutic implications of cancer stem cells

Al‐Hajj, M., Becker, M. W., Wicha, M. S., Weissman, I. L., & Clarke, M. F. (2003) · Current Opinion in Genetics & Development · doi:10.1016/j.gde.2003.11.007 · Cited by 570

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 566

Actomyosin-Mediated Cellular Tension Drives Increased Tissue Stiffness and β-Catenin Activation to Induce Epidermal Hyperplasia and Tumor Growth

Samuel, M. S., Lopez, J. I., McGhee, E. J., Croft, D. R., Strachan, D., Timpson, P., Munro, J., Schröder, E., Zhou, J., Brunton, V. G., et al. (2011) · Cancer Cell · doi:10.1016/j.ccr.2011.05.008 · Cited by 564

The clinically active BTK inhibitor PCI-32765 targets B-cell receptor– and chemokine-controlled adhesion and migration in chronic lymphocytic leukemia

de Rooij, M. F. M., Kuil, A., Geest, C. R., Eldering, E., Chang, B. Y., Buggy, J. J., Pals, S. T., & Spaargaren, M. (2012) · Blood · doi:10.1182/blood-2011-11-390989 · Cited by 558

Osteopontin-CD44 Signaling in the Glioma Perivascular Niche Enhances Cancer Stem Cell Phenotypes and Promotes Aggressive Tumor Growth

Pietras, A., Katz, A. M., Ekström, E. J., Wee, B., Halliday, J. J., Pitter, K. L., Werbeck, J. L., Amankulor, N., Huse, J. T., & Holland, E. C. (2014) · Cell stem cell · doi:10.1016/j.stem.2014.01.005 · Cited by 553

Targeting extracellular matrix stiffness to attenuate disease: from molecular mechanisms to clinical trials

Lampi, M. C., & Reinhart-King, C. A. (2018) · Science Translational Medicine · doi:10.1126/scitranslmed.aao0475 · Cited by 551

Collagens

Gordon, M. K., & Hahn, R. A. (2009) · Cell and Tissue Research · doi:10.1007/s00441-009-0844-4 · Cited by 548

Lymphocyte CD44 binds the COOH-terminal heparin-binding domain of fibronectin.

Jalkanen, S., & Jalkanen, M. (1992) · The Journal of Cell Biology · doi:10.1083/jcb.116.3.817 · Cited by 539

Extracellular matrix contains insulin-like growth factor binding protein-5: potentiation of the effects of IGF-I.

Jones, J. I., Gockerman, A., Busby, W. H., Camacho-Hübner, C., & Clemmons, D. R. (1993) · The Journal of Cell Biology · doi:10.1083/jcb.121.3.679 · Cited by 538

Abnormalities of Basement Membrane on Blood Vessels and Endothelial Sprouts in Tumors

Baluk, P., Morikawa, S., Haskell, A., Mancuso, M., & McDonald, D. M. (2003) · The American Journal of Pathology · doi:10.1016/s0002-9440(10)63540-7 · Cited by 528

Matrix stiffness induces epithelial–mesenchymal transition and promotes chemoresistance in pancreatic cancer cells

Rice, A. J., Cortes, E., Lachowski, D., Cheung, B. C. H., Karim, S. A., Morton, J. P., & Hernández, A. E. D. R. (2017) · Oncogenesis · doi:10.1038/oncsis.2017.54 · Cited by 526

HALO 202: Randomized Phase II Study of PEGPH20 Plus Nab-Paclitaxel/Gemcitabine Versus Nab-Paclitaxel/Gemcitabine in Patients With Untreated, Metastatic Pancreatic Ductal Adenocarcinoma

Hingorani, S. R., Zheng, L., Bullock, A. J., Seery, T. E., Harris, W. P., Sigal, D. S., Braiteh, F., Ritch, P. S., Zalupski, M. M., Bahary, N., et al. (2017) · Journal of Clinical Oncology · doi:10.1200/jco.2017.74.9564 · Cited by 522

Cloning of the $beta; subunit of the leukocyte adhesion proteins: Homology to an extracellular matrix receptor defines a novel supergene family

Kishimoto, T. K. (1987) · Cell · doi:10.1016/0092-8674(87)90246-7 · Cited by 517

Interleukin-1β and Tumor Necrosis Factor-α Decrease Collagen Synthesis and Increase Matrix Metalloproteinase Activity in Cardiac Fibroblasts In Vitro

Siwik, D. A., Chang, D. L. F., & Colucci, W. S. (2000) · Circulation Research · doi:10.1161/01.res.86.12.1259 · Cited by 517

Role of matrix metalloproteinases (MMPs) in colorectal cancer

Zucker, S., & Vacirca, J. L. (2003) · Cancer and Metastasis Reviews · doi:10.1023/a:1025867130437 · Cited by 509

Fibroblast heterogeneity: implications for human disease

Lynch, M. D., & Watt, F. M. (2018) · Journal of Clinical Investigation · doi:10.1172/jci93555 · Cited by 507

Laminins

Durbeej, M. (2009) · Cell and Tissue Research · doi:10.1007/s00441-009-0838-2 · Cited by 500

Coevolution of Solid Stress and Interstitial Fluid Pressure in Tumors During Progression: Implications for Vascular Collapse

Stylianopoulos, T., Martin, J. D., Snuderl, M., Mpekris, F., Jain, S. R., & Jain, R. K. (2013) · Cancer Research · doi:10.1158/0008-5472.can-12-4521 · Cited by 497

Tumor hypoxia and malignant progression

Vaupel, P., Mayer, A., & Höckel, M. (2004) · Methods in Enzymology · doi:10.1016/s0076-6879(04)81023-1 · Cited by 496

Hyaluronan–CD44 interactions as potential targets for cancer therapy

Misra, S., Heldin, P., Hascall, V. C., Karamanos, N. K., Skandalis, S. S., Markwald, R. R., & Ghatak, S. (2011) · The FEBS Journal · doi:10.1111/j.1742-4658.2011.08071.x · Cited by 494

Hyaluronan in Peritumoral Stroma and Malignant Cells Associates with Breast Cancer Spreading and Predicts Survival

Auvinen, P., Tammi, R., Parkkinen, J. J., Tammi, M., Ågren, U. M., Johansson, R. T., Hirvikoski, P. P., Eskelinen, M. J., & Kosma, V. (2000) · American Journal Of Pathology · doi:10.1016/s0002-9440(10)64757-8 · Cited by 494

Vascular and interstitial barriers to delivery of therapeutic agents in tumors

Jain, R. K. (1990) · Cancer and Metastasis Reviews · doi:10.1007/bf00046364 · Cited by 493

Determination of cellular shape by the extracellular matrix and its correlation with the control of cellular growth.

Gospodarowicz, D., Greenburg, G., & Birdwell, C. R. (1978) · PubMed · Cited by 491

TGF-β and cancer

Bierie, B., & Moses, H. (2005) · Cytokine & Growth Factor Reviews · doi:10.1016/j.cytogfr.2005.09.006 · Cited by 487

Phase I study of GC1008 (fresolimumab): a human anti‐transforming growth factor‐beta (TGFβ) monoclonal antibody in patients with advanced malignant melanoma or renal cell carcinoma

Morris, J. C., Tan, A. R., Olencki, T. E., Shapiro, G. I., Dezube, B. J., Reiss, M., Hsu, F. J., Berzofsky, J. A., & Lawrence, D. P. (2014) · PLoS ONE · doi:10.1371/journal.pone.0090353 · Cited by 487

Non-Small Cell Lung Cancer Cells Expressing CD44 Are Enriched for Stem Cell-Like Properties

Leung, E. L., Fiscus, R. R., Tung, J. W., Tin, V. P., Cheng, L. C., Sihoe, A. D., Fink, L. M., Ma, Y., & Wong, M. P. (2010) · PLoS ONE · doi:10.1371/journal.pone.0014062 · Cited by 484

Mutations in the DDR2 Kinase Gene Identify a Novel Therapeutic Target in Squamous Cell Lung Cancer

Hammerman, P. S., Sos, M. L., Ramos, A. H., Xu, C., Dutt, A., Zhou, W., Brace, L. E., Woods, B. A., Lin, W., Zhang, J., et al. (2011) · Cancer Discovery · doi:10.1158/2159-8274.cd-11-0005 · Cited by 482

Integrins as therapeutic targets: lessons and opportunities

Cox, D. M., Brennan, M., & Moran, N. M. (2010) · Nature Reviews Drug Discovery · doi:10.1038/nrd3266 · Cited by 478

The extracellular matrix in breast cancer

Insua-Rodríguez, J., & Oskarsson, T. (2016) · Advanced Drug Delivery Reviews · doi:10.1016/j.addr.2015.12.017 · Cited by 470

Glypican-3 Promotes the Growth of Hepatocellular Carcinoma by Stimulating Canonical Wnt Signaling

Capurro, M., Xiang, Y., Lobe, C. G., & Filmus, J. (2005) · Cancer Research · doi:10.1158/0008-5472.can-04-4244 · Cited by 470

Gemcitabine, Cisplatin, and nab-Paclitaxel for the Treatment of Advanced Biliary Tract Cancers: A Phase 2 Clinical Trial

Shroff, R. T., Javle, M. M., Xiao, L., Kaseb, A. O., Varadhachary, G. R., Wolff, R. A., Raghav, K. P. S., Iwasaki, M., Masci, P., Ramanathan, R. K., et al. (2019) · JAMA Oncology · doi:10.1001/jamaoncol.2019.0270 · Cited by 468

MINI REVIEW Keratan sulfate: structure, biosynthesis, and function

Funderburgh, J. L. (2000) · Glycobiology · doi:10.1093/glycob/10.10.951 · Cited by 451

Collagen promotes anti-PD-1/PD-L1 resistance in cancer through LAIR1-dependent CD8+ T cell exhaustion

Peng, D. H., Rodriguez, B. L., Diao, L., Chen, L., Wang, J., Byers, L. A., Wei, Y., Chapman, H. A., Yamauchi, M., Behrens, C., et al. (2020) · Nature Communications · doi:10.1038/s41467-020-18298-8 · Cited by 451

Degradation of decorin by matrix metalloproteinases: identification of the cleavage sites, kinetic analyses and transforming growth factor-β1 release

Imai, K., HIRAMATSU, A., Fukushima, D., Pierschbacher, M. D., & Okada, Y. (1997) · Biochemical Journal · doi:10.1042/bj3220809 · Cited by 445

Angiotensin receptors: a new role in cancer?

Deshayes, F., & Nahmias, C. (2005) · Trends in Endocrinology and Metabolism · doi:10.1016/j.tem.2005.07.009 · Cited by 437

Glypican-3 as a Serum Marker for Hepatocellular Carcinoma

Capurro, M., & Filmus, J. (2005) · Cancer Research · doi:10.1158/0008-5472.372.65.1 · Cited by 432

Hyaluronan catabolism: a new metabolic pathway

Stern, R. (2004) · European Journal of Cell Biology · doi:10.1078/0171-9335-00392 · Cited by 429

Permeation of the luminal capillary glycocalyx is determined by hyaluronan

Henry, C. B. S., & Duling, B. R. (1999) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.1999.277.2.h508 · Cited by 426

SB-505124 Is a Selective Inhibitor of Transforming Growth Factor-β Type I Receptors ALK4, ALK5, and ALK7

Byfield, S. D., Major, C. D., Laping, N. J., & Roberts, A. B. (2004) · Molecular Pharmacology · doi:10.1124/mol.65.3.744 · Cited by 424

Matrix stiffening promotes a tumor vasculature phenotype

Bordeleau, F., Mason, B. N., Lollis, E. M., Mazzola, M. C., Zanotelli, M. R., Somasegar, S., Califano, J. P., Montague, C. R., LaValley, D. J., Huynh, J., et al. (2016) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1613855114 · Cited by 419

VISTA is an acidic pH-selective ligand for PSGL-1

Johnston, R. J., Su, L. J., Pinckney, J., Critton, D., Boyer, E., Krishnakumar, A. M., Corbett, M. J., Rankin, A. L., DiBella, R. A., Campbell, L., et al. (2019) · Nature · doi:10.1038/s41586-019-1674-5 · Cited by 411

The Role of the Hyaluronan Receptor CD44 in Mesenchymal Stem Cell Migration in the Extracellular Matrix

Zhu, H., Mitsuhashi, N., Klein, A., Barsky, L. W., Weinberg, K. I., Barr, M. L., Demetriou, A. A., & Wu, G. D. (2005) · Stem Cells · doi:10.1634/stemcells.2005-0186 · Cited by 408

Platelet integrin αIIbβ3: signal transduction, regulation, and its therapeutic targeting

Huang, J., Li, X., Shi, X., Zhu, M. F., Wang, J., Huang, S., Huang, X., Wang, H., Li, L., Deng, H., et al. (2019) · Journal of Hematology & Oncology · doi:10.1186/s13045-019-0709-6 · Cited by 406

Cell Adhesion and Matrix Stiffness: Coordinating Cancer Cell Invasion and Metastasis

Gkretsi, V., & Stylianopoulos, T. (2018) · Frontiers in Oncology · doi:10.3389/fonc.2018.00145 · Cited by 404

Molecular cloning of a novel hyaluronan receptor that mediates tumor cell motility

Hardwick, C., Hoare, K., Owens, R. J., Hohn, H.-P., Höök, M., Moore, D. H., Cripps, V., Austen, L., Nance, D., & Turley, E. (1992) · The Journal of Cell Biology · doi:10.1083/jcb.117.6.1343 · Cited by 403

Discoidin Domain Receptor Functions in Physiological and Pathological Conditions

Leitinger, B. (2014) · International review of cytology · doi:10.1016/b978-0-12-800180-6.00002-5 · Cited by 401

Fibronectin, the extracellular glue

Zollinger, A. J., & Smith, M. L. (2016) · Matrix Biology · doi:10.1016/j.matbio.2016.07.011 · Cited by 400

Degradation of Fibrillar Collagen in a Human Melanoma Xenograft Improves the Efficacy of an Oncolytic Herpes Simplex Virus Vector

McKee, T. D., Grandi, P., Mok, W., Alexandrakis, G., Insin, N., Zimmer, J. P., Bawendi, M. G., Boucher, Y., Breakefield, X. O., & Jain, R. K. (2006) · Cancer Research · doi:10.1158/0008-5472.can-05-2242 · Cited by 397

Fibronectin and wound healing

Grinnell, F. (1984) · Journal of Cellular Biochemistry · doi:10.1002/jcb.240260206 · Cited by 387

‘Yin–Yang’ functions of transforming growth factor‐β and T regulatory cells in immune regulation

Wan, Y. Y., & Flavell, R. A. (2007) · Immunological Reviews · doi:10.1111/j.1600-065x.2007.00565.x · Cited by 386

Novel markers for differentiation of lobular and ductal invasive breast carcinomas by laser microdissection and microarray analysis

Turashvili, G., Bouchal, J., Baumforth, K. R. N., Wei, W., Dziechciarková, M., Ehrmann, J., Klein, J., Fridman, E., Škarda, J., Srovnal, J., et al. (2007) · BMC Cancer · doi:10.1186/1471-2407-7-55 · Cited by 385

Supramolecular organization of extracellular matrix glycosaminoglycans, in vitro and in the tissues

Scott, J. E. (1992) · The FASEB Journal · doi:10.1096/fasebj.6.9.1612287 · Cited by 380

Transcriptional activation of integrin β6 during the epithelial-mesenchymal transition defines a novel prognostic indicator of aggressive colon carcinoma

Bates, R. C., Bellovin, D. I., Brown, C. L., Maynard, E., Wu, B., Kawakatsu, H., Sheppard, D., Oettgen, P., & Mercurio, A. M. (2005) · Journal of Clinical Investigation · doi:10.1172/jci23183 · Cited by 380

Collective cell migration requires suppression of actomyosin at cell-cell contacts mediated by DDR1 and the cell polarity regulators Par3 and Par6

Hidalgo-Carcedo, C., Hooper, S., Chaudhry, S. I., Williamson, P., Harrington, K., Leitinger, B., & Sahai, E. (2010) · Nature Cell Biology · doi:10.1038/ncb2133 · Cited by 378

Alternative splicing of CD44 mRNA by ESRP1 enhances lung colonization of metastatic cancer cell

Yae, T., Tsuchihashi, K., Ishimoto, T., Motohara, T., Yoshikawa, M., Yoshida, G. J., Wada, T., Masuko, T., Mogushi, K., Tanaka, H., et al. (2012) · Nature Communications · doi:10.1038/ncomms1892 · Cited by 378

Hyaluronan-CD44 Interactions in Cancer: Paradoxes and Possibilities

Toole, B. P. (2009) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-09-0479 · Cited by 370

Targeted antiangiogenic therapy for cancer using Vitaxin: a humanized monoclonal antibody to the integrin alphavbeta3.

Gutheil, J. C., Campbell, T. N., Pierce, P. R., Watkins, J. D., Huse, W. D., Bodkin, D., & Cheresh, D. A. (2000) · PubMed · Cited by 369

Complexities of TGF-β Targeted Cancer Therapy

Connolly, E. C., Freimuth, J., & Akhurst, R. J. (2012) · International Journal of Biological Sciences · doi:10.7150/ijbs.4564 · Cited by 354

Transmembrane collagen receptors

Leitinger, B. (2011) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev-cellbio-092910-154013 · Cited by 354

MicroRNA-100 shuttled by mesenchymal stem cell-derived exosomes suppresses in vitro angiogenesis through modulating the mTOR/HIF-1α/VEGF signaling axis in breast cancer cells

Pakravan, K., Babashah, S., Sadeghizadeh, M., Mowla, S. J., Mohammadi, M. M., Ataei, F., Dana, N., & Javan, M. (2017) · Cellular Oncology · doi:10.1007/s13402-017-0335-7 · Cited by 354

Transforming growth factor β type 1 binds to collagen IV of basement membrane matrix: Implications for development

Paralkar, V. M., Vukičević, S., & Reddi, A. H. (1991) · Developmental Biology · doi:10.1016/0012-1606(91)90081-d · Cited by 352

Transcriptional Control by the SMADs

Hill, C. S. (2016) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a022079 · Cited by 351

A pan-cancer perspective of matrix metalloproteases (MMP) gene expression profile and their diagnostic/prognostic potential

Gobin, E., Bagwell, K., Wagner, J., Mysona, D., Sandirasegarane, S., Smith, N., Bai, S., Sharma, A. K., Schleifer, R. J., & She, J. (2019) · BMC Cancer · doi:10.1186/s12885-019-5768-0 · Cited by 349

Dense type I collagen matrices that support cellular remodeling and microfabrication for studies of tumor angiogenesis and vasculogenesis in vitro

Cross, V. L., Zheng, Y. Y., Choi, N., Verbridge, S. S., Sutermaster, B. A., Bonassar, L. J., Fischbach, C., & Stroock, A. D. (2010) · Biomaterials · doi:10.1016/j.biomaterials.2010.07.072 · Cited by 347

Role of host angiotensin II type 1 receptor in tumor angiogenesis and growth

Egami, K., Murohara, T., Shimada, T., Sasaki, K., Shintani, S., Sugaya, T., Ishii, M., Akagi, T., Ikeda, H., Matsuishi, T., et al. (2003) · Journal of Clinical Investigation · doi:10.1172/jci16645 · Cited by 345

Structure of integrin α5β1 in complex with fibronectin

Takagi, J., Strokovich, K., Springer, T. A., & Walz, T. (2003) · The EMBO Journal · doi:10.1093/emboj/cdg445 · Cited by 338

Mechanisms and impact of altered tumour mechanics

Mohammadi, H., & Sahai, E. (2018) · Nature Cell Biology · doi:10.1038/s41556-018-0131-2 · Cited by 336

TGF-β blockade improves the distribution and efficacy of therapeutics in breast carcinoma by normalizing the tumor stroma

Liu, J., Liao, S., Diop-Frimpong, B., Chen, W., Goel, S., Naxerova, K., Ancukiewicz, M., Boucher, Y., Jain, R. K., & Xu, L. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1117610109 · Cited by 332

Collagenase Nanoparticles Enhance the Penetration of Drugs into Pancreatic Tumors

Zinger, A., Koren, L., Adir, O., Poley, M., Alyan, M., Yaari, Z. A., Noor, N., Krinsky, N., Simon, A., Gibori, H., et al. (2019) · ACS Nano · doi:10.1021/acsnano.9b02395 · Cited by 330

Tumor cell-associated hyaluronan as an unfavorable prognostic factor in colorectal cancer.

Ropponen, K. M., Tammi, M., Parkkinen, J. J., Eskelinen, M., Tammi, R., Lipponen, P., Ågren, U. M., ALHAVA, E. M., & Kosma, V. (1998) · PubMed · Cited by 327

High levels of stromal hyaluronan predict poor disease outcome in epithelial ovarian cancer.

Anttila, M., Tammi, R., Tammi, M., Syrjänen, K. J., Saarikoski, S., & Kosma, V. (2000) · PubMed · Cited by 327

LY2109761, a novel transforming growth factor β receptor type I and type II dual inhibitor, as a therapeutic approach to suppressing pancreatic cancer metastasis

Melisi, D., Ishiyama, S., Sclabas, G. M., Fleming, J. B., Xia, Q., Tortora, G., Abbruzzese, J. L., & Chiao, P. J. (2008) · Molecular Cancer Therapeutics · doi:10.1158/1535-7163.mct-07-0337 · Cited by 324

A Multicolor Nanoprobe for Detection and Imaging of Tumor‐Related mRNAs in Living Cells

Li, N., Chang, C., Pan, W., et al. (2012) · Angewandte Chemie International Edition · doi:10.1002/anie.201203767 · Cited by 321

Fibronectin Regulates Latent Transforming Growth Factor-β (TGFβ) by Controlling Matrix Assembly of Latent TGFβ-binding Protein-1

Dallas, S. L., Sivakumar, P., Jones, C. J. P., Chen, Q., Peters, D. M. P., Mosher, D. F., Humphries, M. J., & Kielty, C. M. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m410762200 · Cited by 318

The 12th–14th type III repeats of fibronectin function as a highly promiscuous growth factor-binding domain

Martino, M. M., & Hubbell, J. A. (2010) · The FASEB Journal · doi:10.1096/fj.09-151282 · Cited by 317

Interplay of mevalonate and Hippo pathways regulates RHAMM transcription via YAP to modulate breast cancer cell motility

Wang, Z., Wu, Y., Wang, H., Zhang, Y., Mei, L., Fang, X., Zhang, X., Zhang, F., Chen, H., Liu, Y., et al. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1319190110 · Cited by 315

Role of fibronectin in collagen deposition: Fab' to the gelatin-binding domain of fibronectin inhibits both fibronectin and collagen organization in fibroblast extracellular matrix.

McDonald, J. A., Kelley, D. G., & Broekelmann, T. J. (1982) · The Journal of Cell Biology · doi:10.1083/jcb.92.2.485 · Cited by 315

A Phase I Dose Escalation Study with Anti-CD44v6 Bivatuzumab Mertansine in Patients with Incurable Squamous Cell Carcinoma of the Head and Neck or Esophagus

Tijink, B. M., Buter, J., de Bree, R., Giaccone, G., Lang, M. S., Staab, A., Leemans, C. R., & van Dongen, G. A. M. S. (2006) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-06-0910 · Cited by 315

The fibronectin isoform containing the ed‐b oncofetal domain: A marker of angiogenesis

Castellani, P., Viale, G., Dorcaratto, A., Nicolò, G., Kaczmarek, J., Querzé, G., & Zardi, L. (1994) · International Journal of Cancer · doi:10.1002/ijc.2910590507 · Cited by 312

Heparan Sulfate: Biosynthesis, Structure, and Function

Li, J.-P., & Kusche‐Gullberg, M. (2016) · International review of cytology · doi:10.1016/bs.ircmb.2016.02.009 · Cited by 312

Chimeric antigen receptor macrophage therapy for breast tumours mediated by targeting the tumour extracellular matrix

Zhang, W., Liu, L., Su, H., Liu, Q., Shen, J., Dai, H., Zheng, W., Lu, Y., Zhang, W., Bei, Y., et al. (2019) · British Journal of Cancer · doi:10.1038/s41416-019-0578-3 · Cited by 310

Proliferation and collagen production of human patellar tendon fibroblasts in response to cyclic uniaxial stretching in serum-free conditions

Yang, G., Crawford, R. C., & Wang, J. H. (2004) · Journal of Biomechanics · doi:10.1016/j.jbiomech.2004.01.005 · Cited by 308

Survey of Tyrosine Kinase Signaling Reveals ROS Kinase Fusions in Human Cholangiocarcinoma

Gu, T.-L., Deng, X., Huang, F., Tucker, M., Crosby, K., Rimkunas, V. M., Wang, Y., Deng, G., Zhu, L., Tan, Z., et al. (2011) · PLoS ONE · doi:10.1371/journal.pone.0015640 · Cited by 307

Heparin-II Domain of Fibronectin Is a Vascular Endothelial Growth Factor-Binding Domain

Wijelath, E. S., Rahman, S., Namekata, M., Murray, J., Nishimura, T., Mostafavi‐Pour, Z., Patel, Y., Suda, Y., Humphries, M. J., & Sobel, M. (2006) · Circulation Research · doi:10.1161/01.res.0000246849.17887.66 · Cited by 306

Hyaluronan-CD44v3 Interaction with Oct4-Sox2-Nanog Promotes miR-302 Expression Leading to Self-renewal, Clonal Formation, and Cisplatin Resistance in Cancer Stem Cells from Head and Neck Squamous Cell Carcinoma

Bourguignon, L., Wong, G., Earle, C., & Chen, L. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.308528 · Cited by 305

The on-off relationship of Rho and Rac during integrin-mediated adhesion and cell migration

Lawson, C. D., & Burridge, K. (2014) · Small GTPases · doi:10.4161/sgtp.27958 · Cited by 303

Fibroblast activation in cancer: when seed fertilizes soil

Kužet, S.-E., & Gaggioli, C. (2016) · Cell and Tissue Research · doi:10.1007/s00441-016-2467-x · Cited by 301

Targeting the LOX/hypoxia axis reverses many of the features that make pancreatic cancer deadly: inhibition of LOX abrogates metastasis and enhances drug efficacy

Miller, B. W., Morton, J. P., Pinese, M., Saturno, G., Jamieson, N. B., McGhee, E. J., Timpson, P., Leach, J. D. G., McGarry, L., Shanks, E. J., et al. (2015) · EMBO Molecular Medicine · doi:10.15252/emmm.201404827 · Cited by 299

Enhancement of the antitumor properties of interleukin-2 by its targeted delivery to the tumor blood vessel extracellular matrix

Carnemolla, B., Borsi, L., Balza, E., Castellani, P., Meazza, R., Berndt, A., Ferrini, S., Kosmehl, H., Neri, D., & Zardi, L. (2002) · Blood · doi:10.1182/blood.v99.5.1659 · Cited by 294

Immunoscintigraphic detection of the ED-B domain of fibronectin, a marker of angiogenesis, in patients with cancer.

Santimaria, M., Moscatelli, G., Viale, G. L., Giovannoni, L., Neri, G., Viti, F., Leprini, A., Borsi, L., Castellani, P., Zardi, L., et al. (2003) · PubMed · Cited by 293

An integrin αvβ3–c-Src oncogenic unit promotes anchorage-independence and tumor progression

Desgrosellier, J. S., Barnes, L. A., Shields, D. J., Huang, M., Lau, S. K., Prévost, N., Tarin, D., Shattil, S. J., & Cheresh, D. A. (2009) · Nature Medicine · doi:10.1038/nm.2009 · Cited by 293

Tenascins and the Importance of Adhesion ModulationPreprint

Chiquet‐Ehrismann, R., & Tucker, R. P. (2011) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a004960 · Cited by 284

Fibronectins in vascular morphogenesis

Astrof, S., & Hynes, R. O. (2009) · Angiogenesis · doi:10.1007/s10456-009-9136-6 · Cited by 280

The Extracellular Matrix and Pancreatic Cancer: A Complex Relationship

Weniger, M., Honselmann, K. C., & Liss, A. S. (2018) · Cancers · doi:10.3390/cancers10090316 · Cited by 280

YAP induces malignant mesothelioma cell proliferation by upregulating transcription of cell cycle-promoting genes

Mizuno, T., Murakami, H., Fujii, M., Ishiguro, F., Tanaka, I., Kondo, Y., Akatsuka, S., Toyokuni, S., Yokoi, K., Osada, H., et al. (2012) · Oncogene · doi:10.1038/onc.2012.5 · Cited by 278

Inhibition of collagen-induced discoidin domain receptor 1 and 2 activation by imatinib, nilotinib and dasatinib

Day, E., Waters, B., Spiegel, K., Alnadaf, T., Manley, P. W., Buchdunger, E., Walker, C., & Járai, G. (2008) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2008.10.014 · Cited by 278

Site-Directed Neovessel Formation in Vivo

Thompson, J. A., Anderson, K. D., DiPietro, J. M., Zwiebel, J. A., Zametta, M., Anderson, W. F., & Maciag, T. (1988) · Science · doi:10.1126/science.2457952 · Cited by 274

Defining the Role of Solid Stress and Matrix Stiffness in Cancer Cell Proliferation and Metastasis

Kalli, M., & Stylianopoulos, T. (2018) · Frontiers in Oncology · doi:10.3389/fonc.2018.00055 · Cited by 267

Transient tissue priming via ROCK inhibition uncouples pancreatic cancer progression, sensitivity to chemotherapy, and metastasis

Vennin, C., Chin, V. T., Warren, S. C., Lucas, M. C., Herrmann, D., Magenau, A., Mélénec, P., Walters, S. N., del Monte‐Nieto, G., Conway, J. R. W., et al. (2017) · Science Translational Medicine · doi:10.1126/scitranslmed.aai8504 · Cited by 266

Losartan treatment enhances chemotherapy efficacy and reduces ascites in ovarian cancer models by normalizing the tumor stroma

Zhao, Y., Cao, J., Melamed, A., Worley, M. J., Gockley, A. A., Jones, D., Nia, H. T., Zhang, Y., Stylianopoulos, T., Kumar, A. S., et al. (2019) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1818357116 · Cited by 265

The Hyaluronan Receptors CD44 and Rhamm (CD168) Form Complexes with ERK1,2 That Sustain High Basal Motility in Breast Cancer Cells

Hamilton, S. R., Fard, S. F., Paiwand, F. F., Tölg, C., Veiseh, M., Wang, C., McCarthy, J. B., Bissell, M. J., Koropatnick, J. D., & Turley, E. A. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m702078200 · Cited by 263

Anti-VEGF therapy induces ECM remodeling and mechanical barriers to therapy in colorectal cancer liver metastases

Rahbari, N. N., Kedrin, D., Incio, J., Liu, H., Ho, W. W., Nia, H. T., Edrich, C. M., Jung, K., Daubriac, J., Chen, I., et al. (2016) · Science Translational Medicine · doi:10.1126/scitranslmed.aaf5219 · Cited by 258

Distinct structural characteristics of discoidin I subfamily receptor tyrosine kinases and complementary expression in human cancer.

Alves, F., Vogel, W. F., Mossie, K. G., Millauer, B., Höfler, H., & Ullrich, A. (1995) · PubMed · Cited by 253

Regulation of MDR1 Expression and Drug Resistance by a Positive Feedback Loop Involving Hyaluronan, Phosphoinositide 3-Kinase, and ErbB2*♦

Misra, S., Ghatak, S., & Toole, B. P. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m500737200 · Cited by 251

Fibrillin Assembly Requires Fibronectin

Sabatier, L., Chen, D., Fagotto‐Kaufmann, C., Hubmacher, D., McKee, M. D., Annis, D. S., Mosher, D. F., & Reinhardt, D. P. (2008) · Molecular Biology of the Cell · doi:10.1091/mbc.e08-08-0830 · Cited by 250

Dual-targeting biomimetic delivery for anti-glioma activity via remodeling the tumor microenvironment and directing macrophage-mediated immunotherapy

Zhao, P., Wang, Y., Kang, X., Wu, A., Yin, W., Tang, Y., Wang, J., Zhang, M., Duan, Y., & Huang, Y. (2018) · Chemical Science · doi:10.1039/c7sc04853j · Cited by 249

Multi-organ Site Metastatic Reactivation Mediated by Non-canonical Discoidin Domain Receptor 1 Signaling

Gao, H., Chakraborty, G., Zhang, Z., Akalay, I., Gadiya, M. M., Gao, Y., Sinha, S., Hu, J. M., Jiang, C., Akram, M. M., et al. (2016) · Cell · doi:10.1016/j.cell.2016.06.009 · Cited by 247

Two cilengitide regimens in combination with standard treatment for patients with newly diagnosed glioblastoma and unmethylated MGMT gene promoter: results of the open-label, controlled, randomized phase II CORE study

Nabors, B., Fink, K., Mikkelsen, T., Grujičić, D., Tarnawski, R., Nam, D. H., Mazurkiewicz, M., Salacz, M. E., Ashby, L. S., Zagonel, V., et al. (2015) · Neuro-Oncology · doi:10.1093/neuonc/nou356 · Cited by 242

Functional Expression of the Angiotensin II Type1 Receptor in Human Ovarian Carcinoma Cells and Its Blockade Therapy Resulting in Suppression of Tumor Invasion, Angiogenesis, and Peritoneal Dissemination

Suganuma, T., Ino, K., Shibata, K., Kajiyama, H., Nagasaka, T., Mizutani, S., & Kikkawa, F. (2005) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-04-1946 · Cited by 237

Elastic Moduli of Collagen Gels Can Be Predicted from Two-Dimensional Confocal Microscopy

Yang, Y., Leone, L. M., & Kaufman, L. J. (2009) · Biophysical Journal · doi:10.1016/j.bpj.2009.07.035 · Cited by 234

Somatic mutations and germline sequence variants in the expressed tyrosine kinase genes of patients with de novo acute myeloid leukemia

Tomasson, M. H., Xiang, Z., Walgren, R. A., Zhao, Y., Kasai, Y., Miner, T. L., Ries, R. E., Lubman, O., Fremont, D. H., McLellan, M. D., et al. (2008) · Blood · doi:10.1182/blood-2007-09-113027 · Cited by 231

Blockade of angiotensin AT1a receptor signaling reduces tumor growth, angiogenesis, and metastasis

Fujita, M., Hayashi, I., Yamashina, S., Itoman, M., & Majima, M. (2002) · Biochemical and Biophysical Research Communications · doi:10.1016/s0006-291x(02)00496-5 · Cited by 231

Immune Checkpoint Inhibitors in Cancer Therapy

Shiravand, Y., Khodadadi, F., Kashani, S. M. A., Hosseini-Fard, S. R., Hosseini, S., Sadeghirad, H., Ladwa, R., O’Byrne, K., & Kulasinghe, A. (2022) · Current Oncology · doi:10.3390/curroncol29050247 · Cited by 1,353

Modulating extracellular matrix stiffness: A strategic approach to boost cancer immunotherapy

Mai, Z., Lin, Y., Lin, P., Zhao, X., & Cui, L. (2024) · Cell Death & Disease · doi:10.1038/s41419-024-06697-4 · Cited by 398

Tumor microenvironment signaling and therapeutics in cancer progression

Goenka, A., Khan, F., Verma, B., Sinha, P., Dmello, C. C., Jogalekar, M. P., Gangadaran, P., & Ahn, B. (2023) · Cancer Communications · doi:10.1002/cac2.12416 · Cited by 323

Extracellular matrix stiffness: Mechanisms in tumor progression and therapeutic potential in cancer

Zhang, M., & Zhang, B. (2025) · Experimental Hematology & Oncology · doi:10.1186/s40164-025-00647-2 · Cited by 269

Bioactive scaffolds for tissue engineering: A review of decellularized extracellular matrix applications and innovations

Liu, J., Song, Q., Yin, W., Li, C., An, N., Le, Y., Wang, Q., Feng, Y., Hu, Y., & Wang, Y. (2025) · Exploration · doi:10.1002/exp.20230078 · Cited by 140

Effects of Mechanotransduction on Stem Cell Behavior

Bilgen, B., & Odabaş, S. (2016) · doi:10.1002/9781119242642.ch3 · Cited by 4

Mechanotransduction in intervertebral discs

Tsai, T., Cheng, C., Chen, C., et al. (2014) · Journal of Cellular and Molecular Medicine · doi:10.1111/jcmm.12377 · Cited by 21

Cancer mechanobiology: interaction of biomaterials with cancer cells

Libring, S., & Solorio, L. (2020) · Elsevier eBooks · doi:10.1016/b978-0-08-102983-1.00016-8 · Cited by 8

The Driving Force: Nuclear Mechanotransduction in Cellular Function, Fate, and Disease

Maurer, M., & Lammerding, J. (2019) · Annual Review of Biomedical Engineering · doi:10.1146/annurev-bioeng-060418-052139 · Cited by 302

Review of cellular mechanotransduction on micropost substrates

Geng, Y., & Wang, Z. (2015) · Medical & Biological Engineering & Computing · doi:10.1007/s11517-015-1343-2 · Cited by 15