{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2025,2,21]],"date-time":"2025-02-21T18:46:50Z","timestamp":1740163610267,"version":"3.37.3"},"reference-count":48,"publisher":"Springer Science and Business Media LLC","issue":"1","license":[{"start":{"date-parts":[[2019,7,23]],"date-time":"2019-07-23T00:00:00Z","timestamp":1563840000000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0"},{"start":{"date-parts":[[2019,7,23]],"date-time":"2019-07-23T00:00:00Z","timestamp":1563840000000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0"}],"funder":[{"DOI":"10.13039\/501100003725","name":"National Research Foundation of Korea","doi-asserted-by":"publisher","award":["NRF-2016R1A6A3A04010213","NRF-2017R1A2B2008483","2017R1A2B4008680"],"award-info":[{"award-number":["NRF-2016R1A6A3A04010213","NRF-2017R1A2B2008483","2017R1A2B4008680"]}],"id":[{"id":"10.13039\/501100003725","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100003661","name":"Korea Institute for Advancement of Technology","doi-asserted-by":"publisher","award":["R0006245"],"award-info":[{"award-number":["R0006245"]}],"id":[{"id":"10.13039\/501100003661","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["link.springer.com"],"crossmark-restriction":false},"short-container-title":["Sci Rep"],"abstract":"<jats:title>Abstract<\/jats:title><jats:p>Although syndecan-2 is known to interact with the matrix metalloproteinase-7 (MMP-7), the details of their interaction were unknown. Our experiments with a series of syndecan-2 extracellular domain deletion mutants show that the interaction is mediated through an interaction of the extracellular domain of syndecan-2 (residues 41 to 60) with the \u03b12 helix-loop-\u03b13 helix in the pro-domain of MMP-7. NMR and molecular docking model show that Glu7 of the \u03b11 helix, Glu32 of the \u03b12 helix, and Gly48 and Ser52 of the \u03b12 helix-loop-\u03b13 helix of the MMP-7 pro-domain form the syndecan-2-binding pocket, which is occupied by the side chain of tyrosine residue 51 (Tyr51) of syndecan-2. Consistent with this notion, the expression of a syndecan-2 mutant in which Tyr51 was changed to Ala diminished the interaction between the syndecan-2 extracellular domain and the pro-domain of MMP-7. Furthermore, HT-29 colon adenocarcinoma cells expressing the interaction-defective mutant exhibited reductions in the cell-surface localization of MMP-7, the processing of pro-MMP-7 into active MMP-7, the MMP-7-mediated extracellular domain shedding of both syndecan-2 and E-cadherin, and syndecan-2-mediated anchorage-independent growth. Collectively, these data strongly suggest that Tyr51 of the syndecan-2 extracellular domain mediates its interaction with and activating processing of pro-MMP-7 and regulates MMP-7-dependent syndecan-2 functions.<\/jats:p>","DOI":"10.1038\/s41598-019-47140-5","type":"journal-article","created":{"date-parts":[[2019,7,23]],"date-time":"2019-07-23T10:03:15Z","timestamp":1563876195000},"update-policy":"https:\/\/doi.org\/10.1007\/springer_crossmark_policy","source":"Crossref","is-referenced-by-count":8,"title":["Tyrosine 51 residue of the syndecan-2 extracellular domain is involved in the interaction with and activation of pro-matrix metalloproteinase-7"],"prefix":"10.1038","volume":"9","author":[{"given":"Bohee","family":"Jang","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Ji-Hye","family":"Yun","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Sojoong","family":"Choi","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Jimin","family":"Park","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Dong Hae","family":"Shin","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-7300-9784","authenticated-orcid":false,"given":"Seung-Taek","family":"Lee","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Weontae","family":"Lee","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Eok-Soo","family":"Oh","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"297","published-online":{"date-parts":[[2019,7,23]]},"reference":[{"key":"47140_CR1","doi-asserted-by":"publisher","first-page":"957","DOI":"10.1038\/nrm2289","volume":"8","author":"MR Morgan","year":"2007","unstructured":"Morgan, M. R., Humphries, M. J. & Bass, M. D. Synergistic control of cell adhesion by integrins and syndecans. Nat Rev Mol Cell Biol. 8, 957\u2013969 (2007).","journal-title":"Nat Rev Mol Cell Biol."},{"key":"47140_CR2","doi-asserted-by":"publisher","first-page":"165","DOI":"10.1242\/dmm.004077","volume":"4","author":"TR Cox","year":"2011","unstructured":"Cox, T. R. & Erler, J. T. Remodeling and homeostasis of the extracellular matrix: implications for fibrotic diseases and cancer. Dis Model Mech. 4, 165\u2013178 (2011).","journal-title":"Dis Model Mech."},{"key":"47140_CR3","doi-asserted-by":"publisher","first-page":"119","DOI":"10.1146\/annurev.pathol.1.110304.100224","volume":"1","author":"TD Tlsty","year":"2006","unstructured":"Tlsty, T. D. & Coussens, L. M. Tumor stroma and regulation of cancer development. Annu Rev Pathol. 1, 119\u2013150 (2006).","journal-title":"Annu Rev Pathol."},{"key":"47140_CR4","doi-asserted-by":"publisher","first-page":"571","DOI":"10.1007\/s00280-008-0881-9","volume":"63","author":"F Mbeunkui","year":"2009","unstructured":"Mbeunkui, F. & Johann, D. J. Jr. Cancer and the tumor microenvironment: a review of an essential relationship. Cancer Chemother Pharmacol. 63, 571\u2013582 (2009).","journal-title":"Cancer Chemother Pharmacol."},{"key":"47140_CR5","doi-asserted-by":"publisher","first-page":"52","DOI":"10.1016\/j.cell.2010.03.015","volume":"141","author":"K Kessenbrock","year":"2010","unstructured":"Kessenbrock, K., Plaks, V. & Werb, Z. Matrix metalloproteinases: regulators of the tumor microenvironment. Cell. 141, 52\u201367 (2010).","journal-title":"Cell."},{"key":"47140_CR6","doi-asserted-by":"publisher","first-page":"383","DOI":"10.1513\/pats.200601-012TK","volume":"3","author":"A Pardo","year":"2006","unstructured":"Pardo, A. & Selman, M. Matrix metalloproteases in aberrant fibrotic tissue remodeling. Proc Am Thorac Soc. 3, 383\u2013388 (2006).","journal-title":"Proc Am Thorac Soc."},{"key":"47140_CR7","doi-asserted-by":"publisher","first-page":"454","DOI":"10.1002\/bjs.4868","volume":"92","author":"R Aihara","year":"2005","unstructured":"Aihara, R. et al. Clinical significance of mucin phenotype, \u03b2-catenin and matrix metalloproteinase 7 in early undifferentiated gastric carcinoma. Br J Surg. 92, 454\u2013462 (2005).","journal-title":"Br J Surg."},{"key":"47140_CR8","doi-asserted-by":"publisher","first-page":"239","DOI":"10.1016\/S0168-8278(00)00037-4","volume":"34","author":"R Lichtinghagen","year":"2001","unstructured":"Lichtinghagen, R. et al. Matrix metalloproteinase (MMP)-2, MMP-7, and tissue inhibitor of metalloproteinase-1 are closely related to the fibroproliferative process in the liver during chronic hepatitis C. J Hepatol. 34, 239\u2013247 (2001).","journal-title":"J Hepatol."},{"key":"47140_CR9","doi-asserted-by":"publisher","first-page":"2832","DOI":"10.1158\/1078-0432.CCR-1157-03","volume":"10","author":"LE Jones","year":"2004","unstructured":"Jones, L. E., Humphreys, M. J., Campbell, F., Neoptolemos, J. P. & Boyd, M. T. Comprehensive Analysis of Matrix Metalloproteinase and Tissue Inhibitor Expression in Pancreatic Cancer Increased Expression of Matrix Metalloproteinase-7 Predicts Poor Survival. Clin Cancer Res. 10, 2832\u20132845 (2004).","journal-title":"Clin Cancer Res."},{"key":"47140_CR10","doi-asserted-by":"publisher","first-page":"290","DOI":"10.1002\/1097-0215(200002)9999:9999<::AID-IJC1050>3.0.CO;2-1","volume":"95","author":"Y Adachi","year":"2001","unstructured":"Adachi, Y. et al. Clinicopathologic and prognostic significance of matrilysin expression at the invasive front in human colorectal cancers. Int J Cancer. 95, 290\u2013294 (2001).","journal-title":"Int J Cancer."},{"key":"47140_CR11","doi-asserted-by":"publisher","first-page":"439","DOI":"10.1016\/S0092-8674(00)80429-8","volume":"91","author":"Z Werb","year":"1997","unstructured":"Werb, Z. ECM and cell surface proteolysis: regulating cellular ecology. Cell. 91, 439\u2013442 (1997).","journal-title":"Cell."},{"key":"47140_CR12","doi-asserted-by":"publisher","first-page":"20","DOI":"10.1177\/153537020623100103","volume":"231","author":"M Ii","year":"2006","unstructured":"Ii, M., Yamamoto, H., Adachi, Y., Maruyama, Y. & Shinomura, Y. Role of matrix metalloproteinase-7 (matrilysin) in human cancer invasion, apoptosis, growth, and angiogenesis. Exp Biol Med (Maywood). 231, 20\u201327 (2006).","journal-title":"Exp Biol Med (Maywood)."},{"key":"47140_CR13","doi-asserted-by":"publisher","first-page":"145","DOI":"10.1023\/A:1023039230052","volume":"22","author":"T Shiomi","year":"2003","unstructured":"Shiomi, T. & Okada, Y. MT1-MMP and MMP-7 in invasion and metastasis of human cancers. Cancer Metastasis Rev. 22, 145\u2013152 (2003).","journal-title":"Cancer Metastasis Rev."},{"key":"47140_CR14","doi-asserted-by":"publisher","first-page":"683","DOI":"10.1016\/S0092-8674(00)81235-0","volume":"85","author":"PC Brooks","year":"1996","unstructured":"Brooks, P. C. et al. Localization of matrix metalloproteinase MMP-2 to the surface of invasive cells by interaction with integrin \u03b1v\u03b23. Cell. 85, 683\u2013693 (1996).","journal-title":"Cell."},{"key":"47140_CR15","doi-asserted-by":"publisher","first-page":"4782","DOI":"10.1093\/emboj\/20.17.4782","volume":"20","author":"Y Itoh","year":"2001","unstructured":"Itoh, Y. et al. Homophilic complex formation of MT1-MMP facilitates proMMP-2 activation on the cell surface and promotes tumor cell invasion. EMBO J. 20, 4782\u20134793 (2001).","journal-title":"EMBO J."},{"key":"47140_CR16","doi-asserted-by":"publisher","first-page":"35692","DOI":"10.1074\/jbc.M109.054254","volume":"284","author":"HY Ryu","year":"2009","unstructured":"Ryu, H. Y. et al. Syndecan-2 functions as a docking receptor for pro-matrix metalloproteinase-7 in human colon cancer cells. J Biol Chem. 284, 35692\u201335701 (2009).","journal-title":"J Biol Chem."},{"key":"47140_CR17","doi-asserted-by":"publisher","first-page":"2332","DOI":"10.1111\/febs.12198","volume":"280","author":"A Tocchi","year":"2013","unstructured":"Tocchi, A. & Parks, W. C. Functional interactions between matrix metalloproteinases and glycosaminoglycans. FEBS J. 280, 2332\u20132341 (2013).","journal-title":"FEBS J."},{"key":"47140_CR18","doi-asserted-by":"publisher","first-page":"27924","DOI":"10.1074\/jbc.M109.035147","volume":"284","author":"H-J Ra","year":"2009","unstructured":"Ra, H.-J. et al. Control of promatrilysin (MMP7) activation and substrate-specific activity by sulfated glycosaminoglycans. J Biol Chem. 284, 27924\u201327932 (2009).","journal-title":"J Biol Chem."},{"key":"47140_CR19","doi-asserted-by":"publisher","first-page":"27","DOI":"10.1111\/febs.13940","volume":"284","author":"NA Afratis","year":"2017","unstructured":"Afratis, N. A. et al. Syndecans\u2013key regulators of cell signaling and biological functions. FEBS J. 284, 27\u201341 (2017).","journal-title":"FEBS J."},{"key":"47140_CR20","doi-asserted-by":"publisher","first-page":"662","DOI":"10.1016\/j.ceb.2009.05.002","volume":"21","author":"K Lambaerts","year":"2009","unstructured":"Lambaerts, K., Wilcox-Adelman, S. A. & Zimmermann, P. The signaling mechanisms of syndecan heparan sulfate proteoglycans. Curr Opin Cell Biol. 21, 662\u2013669 (2009).","journal-title":"Curr Opin Cell Biol."},{"key":"47140_CR21","doi-asserted-by":"publisher","first-page":"89","DOI":"10.1146\/annurev-cellbio-100109-104126","volume":"26","author":"JR Couchman","year":"2010","unstructured":"Couchman, J. R. Transmembrane signaling proteoglycans. Annu Rev Cell Dev Biol. 26, 89\u2013114 (2010).","journal-title":"Annu Rev Cell Dev Biol."},{"key":"47140_CR22","doi-asserted-by":"publisher","first-page":"3904","DOI":"10.1111\/j.1742-4658.2010.07800.x","volume":"277","author":"AD Theocharis","year":"2010","unstructured":"Theocharis, A. D., Skandalis, S. S., Tzanakakis, G. N. & Karamanos, N. K. Proteoglycans in health and disease: novel roles for proteoglycans in malignancy and their pharmacological targeting. FEBS J. 277, 3904\u20133923 (2010).","journal-title":"FEBS J."},{"key":"47140_CR23","doi-asserted-by":"publisher","first-page":"93","DOI":"10.1016\/j.matbio.2010.10.006","volume":"30","author":"Y Choi","year":"2011","unstructured":"Choi, Y., Chung, H., Jung, H., Couchman, J. R. & Oh, E. S. Syndecans as cell surface receptors: unique structure equates with functional diversity. Matrix Biol. 30, 93\u201399 (2011).","journal-title":"Matrix Biol."},{"key":"47140_CR24","doi-asserted-by":"publisher","first-page":"31","DOI":"10.1007\/s00441-009-0829-3","volume":"339","author":"X Xian","year":"2010","unstructured":"Xian, X., Gopal, S. & Couchman, J. R. Syndecans as receptors and organizers of the extracellular matrix. Cell Tissue Res. 339, 31\u201346 (2010).","journal-title":"Cell Tissue Res."},{"key":"47140_CR25","doi-asserted-by":"publisher","first-page":"2870","DOI":"10.1111\/febs.12291","volume":"280","author":"N Malla","year":"2013","unstructured":"Malla, N. et al. In vitro reconstitution of complexes between pro\u2010matrix metalloproteinase\u20109 and the proteoglycans serglycin and versican. FEBS J. 280, 2870\u20132887 (2013).","journal-title":"FEBS J."},{"key":"47140_CR26","doi-asserted-by":"publisher","first-page":"669","DOI":"10.1006\/jmbi.2000.4235","volume":"304","author":"J-O Winberg","year":"2000","unstructured":"Winberg, J.-O., Kolset, S. O., Berg, E. & Uhlin-Hansen, L. Macrophages secrete matrix metalloproteinase-9 covalently linked to the core protein of chondroitin sulphate proteoglycans. J Mol Biol. 304, 669\u2013680 (2000).","journal-title":"J Mol Biol."},{"key":"47140_CR27","doi-asserted-by":"publisher","first-page":"581","DOI":"10.1093\/jb\/mvn006","volume":"143","author":"Y Koyama","year":"2008","unstructured":"Koyama, Y. et al. Matrix metalloproteinase-9 associated with heparan sulphate chains of GPI-anchored cell surface proteoglycans mediates motility of murine colon adenocarcinoma cells. J Biochem. 143, 581\u2013592 (2008).","journal-title":"J Biochem."},{"key":"47140_CR28","doi-asserted-by":"publisher","first-page":"29730","DOI":"10.1074\/jbc.M202435200","volume":"277","author":"H Park","year":"2002","unstructured":"Park, H., Kim, Y., Lim, Y., Han, I. & Oh, E. S. Syndecan-2 mediates adhesion and proliferation of colon carcinoma cells. J Biol Chem. 277, 29730\u201329736 (2002).","journal-title":"J Biol Chem."},{"key":"47140_CR29","doi-asserted-by":"publisher","first-page":"826","DOI":"10.1038\/sj.onc.1206068","volume":"22","author":"Y Kim","year":"2003","unstructured":"Kim, Y. et al. Decreased syndecan-2 expression correlates with trichostatin-A induced-morphological changes and reduced tumorigenic activity in colon carcinoma cells. Oncogene. 22, 826\u2013830 (2003).","journal-title":"Oncogene."},{"key":"47140_CR30","doi-asserted-by":"publisher","first-page":"2099","DOI":"10.1016\/j.str.2015.08.013","volume":"23","author":"SH Prior","year":"2003","unstructured":"Prior, S. H., Fulcher, Y. G., Koppisetti, R. K., Jurkevich, A. & Van Doren, S. R. Charge-triggered membrane insertion of matrix metalloproteinase-7, supporter of innate immunity and tumors. Structure. 23, 2099\u20132110 (2003).","journal-title":"Structure."},{"key":"47140_CR31","doi-asserted-by":"publisher","first-page":"2398","DOI":"10.1093\/bioinformatics\/btq444","volume":"26","author":"DW Ritchie","year":"2010","unstructured":"Ritchie, D. W. & Venkatraman, V. Ultra-fast FFT protein docking on graphics processors. Bioinformatics. 26, 2398\u20132405 (2010).","journal-title":"Bioinformatics."},{"key":"47140_CR32","doi-asserted-by":"publisher","first-page":"720","DOI":"10.1016\/j.jmb.2015.09.014","volume":"428","author":"GCP van Zundert","year":"2016","unstructured":"van Zundert, G. C. P. et al. The HADDOCK2.2 webserver: User-friendly integrative modeling of biomolecular complexes. J. Mol. Biol. 428, 720\u2013725 (2016).","journal-title":"J. Mol. Biol."},{"key":"47140_CR33","doi-asserted-by":"publisher","first-page":"297","DOI":"10.1017\/S003358359800345X","volume":"31","author":"M Buck","year":"1998","unstructured":"Buck, M. Trifluoroethanol and colleagues: cosolvents come of age. Recent studies with peptides and proteins. Q Rev Biophys. 31, 297\u2013355 (1998).","journal-title":"Q Rev Biophys."},{"key":"47140_CR34","doi-asserted-by":"publisher","first-page":"487","DOI":"10.1016\/j.bbrc.2014.02.142","volume":"446","author":"MJ Kwon","year":"2014","unstructured":"Kwon, M. J., Hong, E., Choi, Y., Kang, D. H. & Oh, E. S. Interleukin-1\u03b1 promotes extracellular shedding of syndecan-2 via induction of matrix metalloproteinase-7 expression. Biochem Biophys Res Commun. 446, 487\u2013492 (2014).","journal-title":"Biochem Biophys Res Commun."},{"key":"47140_CR35","doi-asserted-by":"publisher","first-page":"341","DOI":"10.1006\/excr.1997.3711","volume":"236","author":"DC Von Bredow","year":"1997","unstructured":"Von Bredow, D. C., Nagle, R. B., Bowden, G. T. & Cress, A. E. Cleavage of \u03b24 integrin by matrilysin. Exp Cell Res. 236, 341\u2013345 (1997).","journal-title":"Exp Cell Res."},{"key":"47140_CR36","doi-asserted-by":"crossref","first-page":"111","DOI":"10.1242\/jcs.114.1.111","volume":"114","author":"V No\u00eb","year":"2001","unstructured":"No\u00eb, V. et al. Release of an invasion promoter E-cadherin fragment by matrilysin and stromelysin-1. J Cell Sci. 114, 111\u2013118 (2001).","journal-title":"J Cell Sci."},{"key":"47140_CR37","doi-asserted-by":"crossref","first-page":"3874","DOI":"10.18632\/oncotarget.2885","volume":"6","author":"S Choi","year":"2015","unstructured":"Choi, S. et al. Shed syndecan-2 enhances tumorigenic activities of colon cancer cells. Oncotarget 6, 3874 (2015).","journal-title":"Oncotarget"},{"key":"47140_CR38","doi-asserted-by":"publisher","first-page":"47","DOI":"10.1016\/j.bbrc.2016.06.019","volume":"477","author":"B Jang","year":"2016","unstructured":"Jang, B., Jung, H., Chung, H., Moon, B. I. & Oh, E. S. Syndecan-2 enhances E-cadherin shedding and fibroblast-like morphological changes by inducing MMP-7 expression in colon cancer cells. Biochem Biophys Res Commun. 477, 47\u201353 (2016).","journal-title":"Biochem Biophys Res Commun."},{"key":"47140_CR39","doi-asserted-by":"publisher","first-page":"8133","DOI":"10.1074\/jbc.272.13.8133","volume":"272","author":"E-S Oh","year":"1997","unstructured":"Oh, E.-S., Woods, A. & Couchman, J. R. Syndecan-4 proteoglycan regulates the distribution and activity of protein kinase C. J Biol Chem. 272, 8133\u20138136 (1997).","journal-title":"J Biol Chem."},{"key":"47140_CR40","doi-asserted-by":"publisher","first-page":"370","DOI":"10.1110\/ps.8.2.370","volume":"8","author":"N Sreerama","year":"1999","unstructured":"Sreerama, N., Venyaminov, S. Y. & Woody, R. W. Estimation of the number of \u03b1-helical and \u03b2-strand segments in proteins using circular dichroism spectroscopy. Protein Sci. 8, 370\u2013380 (1999).","journal-title":"Protein Sci."},{"key":"47140_CR41","doi-asserted-by":"publisher","first-page":"252","DOI":"10.1006\/abio.2000.4880","volume":"287","author":"N Sreerama","year":"2000","unstructured":"Sreerama, N. & Woody, R. W. Estimation of protein secondary structure from circular dichroism spectra: comparison of CONTIN, SELCON, and CDSSTR methods with an expanded reference set. Anal Biochem. 287, 252\u2013260 (2000).","journal-title":"Anal Biochem."},{"key":"47140_CR42","doi-asserted-by":"publisher","first-page":"2844","DOI":"10.1063\/1.479562","volume":"111","author":"RW Woody","year":"1999","unstructured":"Woody, R. W. & Sreerama, N. Comment on \u201cImproving protein circular dichroism calculations in the far-ultraviolet through reparametrizing the amide chromophore\u201d. J. Chem. Phys. 109, 782 (1998). J Chem Phys. 111, 2844\u20132845 (1999).","journal-title":"J Chem Phys."},{"key":"47140_CR43","doi-asserted-by":"publisher","first-page":"4960","DOI":"10.1021\/bi00263a020","volume":"21","author":"D Mao","year":"1982","unstructured":"Mao, D., Wachter, E. & Wallace, B. A. Folding of the mitochondrial proton adenosine triphosphatase proteolipid channel in phospholipid vesicles. Biochemistry. 21, 4960\u20134968 (1982).","journal-title":"Biochemistry."},{"key":"47140_CR44","doi-asserted-by":"publisher","first-page":"5","DOI":"10.1002\/0471250953.bi0506s47","volume":"47","author":"B Webb","year":"2014","unstructured":"Webb, B. & Sali, A. Comparative protein structure modeling using MODELLER. Curr Protoc Bioinformatics. 47, 5\u20136 (2014).","journal-title":"Curr Protoc Bioinformatics."},{"key":"47140_CR45","doi-asserted-by":"publisher","first-page":"449","DOI":"10.1093\/nar\/gkw329","volume":"44","author":"A Lamiable","year":"2016","unstructured":"Lamiable, A. et al. PEP-FOLD3: faster de novo structure prediction for linear peptides in solution and in complex. Nucleic Acids Res. 44, 449\u2013454 (2016).","journal-title":"Nucleic Acids Res."},{"key":"47140_CR46","doi-asserted-by":"publisher","first-page":"1605","DOI":"10.1002\/jcc.20084","volume":"25","author":"EF Pettersen","year":"2004","unstructured":"Pettersen, E. F. et al. UCSF Chimera\u2014a visualization system for exploratory research and analysis. J Comput Chem. 25, 1605\u20131612 (2004).","journal-title":"J Comput Chem."},{"key":"47140_CR47","doi-asserted-by":"publisher","first-page":"33","DOI":"10.1016\/0263-7855(96)00018-5","volume":"14","author":"W Humphrey","year":"1996","unstructured":"Humphrey, W., Dalke, A. & Schulten, K. VMD: visual molecular dynamics. Journal of molecular graphics. J Mol Graph. 14, 33\u201338 (1996).","journal-title":"Journal of molecular graphics. J Mol Graph."},{"key":"47140_CR48","doi-asserted-by":"publisher","first-page":"16321","DOI":"10.1074\/jbc.M117.793752","volume":"292","author":"B Jang","year":"2017","unstructured":"Jang, B. et al. Syndecan-2 cytoplasmic domain up-regulates matrix metalloproteinase-7 expression via the protein kinase C\u03b3\u2013mediated FAK\/ERK signaling pathway in colon cancer. J Biol Chem. 292, 16321\u201316332 (2017).","journal-title":"J Biol Chem."}],"container-title":["Scientific Reports"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.nature.com\/articles\/s41598-019-47140-5.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/www.nature.com\/articles\/s41598-019-47140-5","content-type":"text\/html","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/www.nature.com\/articles\/s41598-019-47140-5.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2022,12,17]],"date-time":"2022-12-17T11:47:41Z","timestamp":1671277661000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.nature.com\/articles\/s41598-019-47140-5"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2019,7,23]]},"references-count":48,"journal-issue":{"issue":"1","published-online":{"date-parts":[[2019,12]]}},"alternative-id":["47140"],"URL":"https:\/\/doi.org\/10.1038\/s41598-019-47140-5","relation":{},"ISSN":["2045-2322"],"issn-type":[{"type":"electronic","value":"2045-2322"}],"subject":[],"published":{"date-parts":[[2019,7,23]]},"assertion":[{"value":"14 January 2019","order":1,"name":"received","label":"Received","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"11 July 2019","order":2,"name":"accepted","label":"Accepted","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"23 July 2019","order":3,"name":"first_online","label":"First Online","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"The authors declare no competing interests.","order":1,"name":"Ethics","group":{"name":"EthicsHeading","label":"Competing Interests"}}],"article-number":"10625"}}