Effects of Tenascin C on the Integrity of Extracellular Matrix and Skin Aging

A Mechanism for Regulating Pulmonary Inflammation and Fibrosis: The Integrin αvβ6 Binds and Activates Latent TGF β1

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Introduction to Skin Aging

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Mice develop normally without tenascin.Preprint

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Sensing the Environment: Regulation of Local and Global Homeostasis by the Skin's Neuroendocrine System

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Untitled work

Slominski (2012) · doi:10.1007/978-3-642-19683-6_1 · Cited by 461 · see citing works

Tenascin-C at a glance

Midwood, K. S., Chiquet, M., Tucker, R. P., & Orend, G. (2016) · Journal of Cell Science · doi:10.1242/jcs.190546 · Cited by 432 · see citing works

Modulation of Skin Collagen Metabolism in Aged and Photoaged Human Skin In Vivo

Chung, J. H., Seo, J. Y., Choi, H. R., Lee, M. K., Youn, C. S., Rhie, G., Cho, K. H., Kim, K. H., Park, K. C., & Eun, H. C. (2001) · Journal of Investigative Dermatology · doi:10.1046/j.0022-202x.2001.01544.x · Cited by 410 · see citing works

Revisiting the matricellular concept

Murphy-Ullrich, J. E., & Sage, E. H. (2014) · Matrix Biology · doi:10.1016/j.matbio.2014.07.005 · Cited by 393 · see citing works

Advances in tenascin-C biology

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Tenascin-C drives persistence of organ fibrosis

Bhattacharyya, S., Wang, W., Morales‐Nebreda, L., Feng, G., Wu, M., Zhou, X., Lafyatis, R., Lee, J. J., Hinchcliff, M., Feghali‐Bostwick, C. A., et al. (2016) · Nature Communications · doi:10.1038/ncomms11703 · Cited by 293 · see citing works

Epidermal growth factor (EGF)-like repeats of human tenascin-C as ligands for EGF receptor

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Reduced Expression of Connective Tissue Growth Factor (CTGF/CCN2) Mediates Collagen Loss in Chronologically Aged Human Skin

Quan, T., Shao, Y., He, T., Voorhees, J. J., & Fisher, G. J. (2010) · Journal of Investigative Dermatology · doi:10.1038/jid.2009.224 · Cited by 239 · see citing works

Skin wounds and severed nerves heal normally in mice lacking tenascin-C.

Forsberg, E., Hirsch, E., Fröhlich, L., Meyer, M., Ekblom, P., Aszódi, A., Werner, S., & Fässler, R. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.13.6594 · Cited by 235 · see citing works

Cell- and heparin-binding domains of the hexabrachion arm identified by tenascin expression proteins.

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Mitogenesis, cell migration, and loss of focal adhesions induced by tenascin-C interacting with its cell surface receptor, annexin II.

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Tenascin-C and integrins in cancer

Yoshida, T., Akatsuka, T., & Imanaka‐Yoshida, K. (2015) · Cell Adhesion & Migration · doi:10.1080/19336918.2015.1008332 · Cited by 180 · see citing works

Characterization of multiple adhesive and counteradhesive domains in the extracellular matrix protein cytotactin.

Prieto, A. L., Andersson-Fisone, C., & Crossin, K. L. (1992) · The Journal of Cell Biology · doi:10.1083/jcb.119.3.663 · Cited by 171 · see citing works

Tenascin variants: differential binding to fibronectin and distinct distribution in cell cultures and tissues.

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Neuroendocrine Aspects of Skin Aging

Bocheva, G., Slominski, R. M., & Slominski, A. T. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20112798 · Cited by 137 · see citing works

Tenascin-C May Accelerate Cardiac Fibrosis by Activating Macrophages via the Integrin αVβ3/Nuclear Factor–κB/Interleukin-6 Axis

Shimojo, N., Hashizume, R., Kanayama, K., Hara, M., Suzuki, Y., Nishioka, T., Hiroe, M., Yoshida, T., & Imanaka‐Yoshida, K. (2015) · Hypertension · doi:10.1161/hypertensionaha.115.06004 · Cited by 137 · see citing works

Deficiency of tenascin‐C attenuates liver fibrosis in immune‐mediated chronic hepatitis in mice

El-Karef, A., Yoshida, T., Gabazza, E. C., Nishioka, T., Inada, H., Sakakura, T., & Imanaka‐Yoshida, K. (2006) · The Journal of Pathology · doi:10.1002/path.2099 · Cited by 120 · see citing works

Tenascin-C: Its functions as an integrin ligand

Tucker, R. P., & Chiquet‐Ehrismann, R. (2015) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2015.06.003 · Cited by 119 · see citing works

A positive feedback loop bi-stably activates fibroblasts

Yeo, S.-Y., Lee, K.-W., Shin, D., An, S., Cho, K.-H., & Kim, S.-H. (2018) · Nature Communications · doi:10.1038/s41467-018-05274-6 · Cited by 115 · see citing works

The role of integrins in TGFβ activation in the tumour stroma

Khan, Z. A., & Marshall, J. F. (2016) · Cell and Tissue Research · doi:10.1007/s00441-016-2474-y · Cited by 115 · see citing works

Tenascin-C deficiency attenuates TGF-β-mediated fibrosis following murine lung injury

Carey, W. A., Taylor, G. D., Dean, W. B., & Bristow, J. D. (2010) · American Journal of Physiology-Lung Cellular and Molecular Physiology · doi:10.1152/ajplung.00385.2009 · Cited by 102 · see citing works

Transforming growth factor β inhibitory element in the rabbit matrix metalloproteinase-1 (collagenase-1) gene functions as a repressor of constitutive transcription

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Binding of αvβ1 and αvβ6 integrins to tenascin-C induces epithelial–mesenchymal transition-like change of breast cancer cells

Katoh, D., Nagaharu, K., Shimojo, N., Hanamura, N., Yamashita, M., Kozuka, Y., Imanaka‐Yoshida, K., & Yoshida, T. (2013) · Oncogenesis · doi:10.1038/oncsis.2013.27 · Cited by 90 · see citing works

Tenascin-C in cardiac disease: a sophisticated controller of inflammation, repair, and fibrosis

Imanaka‐Yoshida, K., Tawara, I., & Yoshida, T. (2020) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00353.2020 · Cited by 89 · see citing works

Tenascin-C blocks cell-cycle progression of anchorage-dependent fibroblasts on fibronectin through inhibition of syndecan-4

Orend, G., Huang, W., Olayioye, M. A., Hynes, N. E., & Chiquet‐Ehrismann, R. (2003) · Oncogene · doi:10.1038/sj.onc.1206618 · Cited by 88 · see citing works

Tenascin-C Enhances Pancreatic Cancer Cell Growth and Motility and Affects Cell Adhesion through Activation of the Integrin Pathway

Paron, I., Berchtold, S., Vörös, J., Shamarla, M., Erkan, M., Höfler, H., & Esposito, I. (2011) · PLoS ONE · doi:10.1371/journal.pone.0021684 · Cited by 76 · see citing works

Endothelin Receptor Type B Counteracts Tenascin-C–Induced Endothelin Receptor Type A–Dependent Focal Adhesion and Actin Stress Fiber Disorganization

Lange, K., Kammerer, M., Hegi, M. E., Grotegut, S., Dittmann, A., Huang, W., Fluri, E., Yip, G. W., Götte, M., Ruiz, C. F., et al. (2007) · Cancer Research · doi:10.1158/0008-5472.can-06-3348 · Cited by 73 · see citing works

MAP-kinase activity necessary for TGFβ1-stimulated mesangial cell type I collagen expression requires adhesion-dependent phosphorylation of FAK tyrosine 397

Hayashida, T., Wu, M.-H., Pierce, A. A., Poncelet, A.-C., Varga, J., & Schnaper, H. W. (2007) · Journal of Cell Science · doi:10.1242/jcs.03492 · Cited by 70 · see citing works

Tenascin-C Induces Phenotypic Changes in Fibroblasts to Myofibroblasts with High Contractility through the Integrin αvβ1/Transforming Growth Factor β/SMAD Signaling Axis in Human Breast Cancer

Katoh, D., Kozuka, Y., Noro, A., Ogawa, T., Imanaka‐Yoshida, K., & Yoshida, T. (2020) · American Journal Of Pathology · doi:10.1016/j.ajpath.2020.06.008 · Cited by 69 · see citing works

Tenascin-C deficiency ameliorates Alzheimer's disease-related pathology in mice

Xie, K., Liu, Y., Hao, W., Walter, S., Penke, B., Hartmann, T., Schachner, M., & Fassbender, K. C. (2013) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2013.04.013 · Cited by 68 · see citing works

Human Epidermal Keratinocytes Are a Source of Tenascin-C during Wound Healing

Latijnhouwers, M., Bergers, M., Ponec, M., Dijkman, H. B. P. M., Andriessen, M. P. M., & Schalkwijk, J. (1997) · Journal of Investigative Dermatology · doi:10.1111/1523-1747.ep12292170 · Cited by 63 · see citing works

Tenascins in fibrotic disorders—from bench to bedside

Kasprzycka, M., Hammarström, C. L., & Haraldsen, G. (2015) · Cell Adhesion & Migration · doi:10.4161/19336918.2014.994901 · Cited by 56 · see citing works

Skullcapflavone II Inhibits Degradation of Type I Collagen by Suppressing MMP-1 Transcription in Human Skin Fibroblasts

Lee, Y. H., Seo, E. K., & Lee, S. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20112734 · Cited by 50 · see citing works

Impaired cornea wound healing in a tenascin C-deficient mouse model

Sumioka, T., Kitano, A., Flanders, K. C., Okada, Y., Yamanaka, O., Fujita, N., Iwanishi, H., Kao, W. W. ‐., & Saika, S. (2012) · Laboratory Investigation · doi:10.1038/labinvest.2012.157 · Cited by 47 · see citing works

Tenascins and their implications in diseases and tissue mechanics

Brellier, F., Tucker, R. P., & Chiquet‐Ehrismann, R. (2009) · Scandinavian Journal of Medicine and Science in Sports · doi:10.1111/j.1600-0838.2009.00916.x · Cited by 45 · see citing works

UV-induced inhibition of adipokine production in subcutaneous fat aggravates dermal matrix degradation in human skin

Kim, E. J., Kim, Y. K., Kim, M. K., Kim, S., Kim, J. Y., Lee, D. H., & Chung, J. H. (2016) · Scientific Reports · doi:10.1038/srep25616 · Cited by 44 · see citing works

Bone Marrow-Derived Tenascin-C Attenuates Cardiac Hypertrophy by Controlling Inflammation

Song, L., Wang, L., Li, F., Yukht, A., Qin, M., Ruther, H., Yang, M., Chaux, A., Shah, P. K., & Sharifi, B. G. (2017) · Journal of the American College of Cardiology · doi:10.1016/j.jacc.2017.07.789 · Cited by 42 · see citing works

Extra-Cellular Matrix Proteins Induce Matrix Metalloproteinase-1 (MMP-1) Activity and Increase Airway Smooth Muscle Contraction in Asthma

Rogers, N. K., Clements, D., Dongre, A., Harrison, T. W., Shaw, D. E., & Johnson, S. R. (2014) · PLoS ONE · doi:10.1371/journal.pone.0090565 · Cited by 40 · see citing works

Tenascin-C Splice Variant Adhesive/anti-Adhesive Effects on Chondrosarcoma Cell Attachment to Fibronectin.

Ghert, M. A., Qi, W., Erickson, H., Block, J. A., & Scully, S. P. (2001) · Cell Structure and Function · doi:10.1247/csf.26.179 · Cited by 39 · see citing works

Tenascin-C is upregulated in the skin lesions of patients with atopic dermatitis

Ogawa, K., Ito, M., Takeuchi, K., Nakada, A., Heishi, M., Suto, H., Mitsuishi, K., Sugita, Y., Ogawa, H., & Ra, C. (2005) · Journal of Dermatological Science · doi:10.1016/j.jdermsci.2005.06.001 · Cited by 38 · see citing works

Tenascin-C and carcinoma cell invasion in oral and urinary bladder cancer

Berndt, A., Richter, P., Kosmehl, H., & Franz, M. (2015) · Cell Adhesion & Migration · doi:10.1080/19336918.2015.1005463 · Cited by 36 · see citing works

Upregulation of Tenascin-C Expression by IL-13 in Human Dermal Fibroblasts via the Phosphoinositide 3-kinase/Akt and the Protein Kinase C Signaling Pathways

Jinnin, M., Ihn, H., Asano, Y., Yamane, K., Trojanowska, M., & Tamaki, K. (2005) · Journal of Investigative Dermatology · doi:10.1038/sj.jid.5700090 · Cited by 33 · see citing works

Expression of tenascin-C splice variants by human skin cells

Latijnhouwers, M., de Jongh, G. J., Bergers, M., de Rooij, M. J. M., & Schalkwijk, J. (2000) · Archives of Dermatological Research · doi:10.1007/s004030000152 · Cited by 30 · see citing works

Transcriptional Regulation of Proteoglycans and Glycosaminoglycan Chain-synthesizing Glycosyltransferases by UV Irradiation in Cultured Human Dermal Fibroblasts

Shin, J., Oh, J., Kim, Y. K., Jung, J.-Y., & Chung, J. H. (2011) · Journal of Korean Medical Science · doi:10.3346/jkms.2011.26.3.417 · Cited by 26 · see citing works

The catalytically defective receptor protein tyrosine kinase EphA10 promotes tumorigenesis in pancreatic cancer cells

Shin, W., Park, M. K., Lee, Y. H., Kim, K., Lee, H., & Lee, S. (2020) · Cancer Science · doi:10.1111/cas.14568 · Cited by 22 · see citing works

The Adhesion Modulating Properties of Tenascin-W

Brellier, F., Martina, E., Chiquet, M., Ferralli, J., van der Heyden, M., Orend, G., Schittny, J. C., Chiquet‐Ehrismann, R., & Tucker, R. P. (2012) · International Journal of Biological Sciences · doi:10.7150/ijbs.8.187 · Cited by 20 · see citing works

Catalytically inactive receptor tyrosine kinase PTK7 activates FGFR1 independent of FGF

Shin, W., Lee, H. W., & Lee, S. (2019) · The FASEB Journal · doi:10.1096/fj.201900932r · Cited by 17 · see citing works

Tenascin-C in human cardiac pathology

Niebrój-Dobosz, I. (2012) · Clinica Chimica Acta · doi:10.1016/j.cca.2012.06.011 · Cited by 16 · see citing works

Molecular mechanism of tenascin-C action on matrix metalloproteinase-1 invasive potential.

Galoian, K. A., Garamszegi, N., Garamszegi, S. P., & Scully, S. P. (2007) · PubMed · Cited by 14 · see citing works

Tenascin-C promotes migration of hepatic stellate cells and production of type I collagen

Ma, J., Huang, X., Shen, Y., Chen, Z., Su, Q.-H., Xu, J., & Zhao, J. (2016) · Bioscience Biotechnology and Biochemistry · doi:10.1080/09168451.2016.1165600 · Cited by 12 · see citing works

Dermal extracellular matrix molecules in skin development, homeostasis, wound regeneration and diseases

Huang, J., Heng, S., Zhang, W., Liu, Y., Xia, T., Ji, C., & Zhang, L.-J. (2022) · Seminars in Cell & Developmental Biology · doi:10.1016/j.semcdb.2022.02.027 · Cited by 238 · see citing works

Principles of Tissue Engineering

Meesane, J. (2022) · Engineering materials · doi:10.1007/978-981-19-7830-2_2 · Cited by 135 · see citing works

Spatial transcriptomics combined with single‐cell RNA ‐sequencing unravels the complex inflammatory cell network in atopic dermatitis

Mitamura, Y., Reiger, M., Kim, J., Xiao, Y., Zhakparov, D., Tan, G., Rückert, B., Rinaldi, A. O., Baerenfaller, K., Akdiş, M., et al. (2023) · Allergy · doi:10.1111/all.15781 · Cited by 119 · see citing works

Skin Epidermis and Barrier Function

Lim, K. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22063035 · Cited by 67 · see citing works

Shared and Compartment‐Specific Processes in Nucleus Pulposus and Annulus Fibrosus During Intervertebral Disc Degeneration

Swahn, H., Mertens, J., Olmer, M., Myers, K., Mondala, T. S., Natarajan, P., Head, S. R., Álvarez-García, Ó., & Lotz, M. (2024) · Advanced Science · doi:10.1002/advs.202309032 · Cited by 62 · see citing works

Mechanotransduction in Skin Inflammation

Shutova, M. S., & Boehncke, W. (2022) · Cells · doi:10.3390/cells11132026 · Cited by 60 · see citing works

Tenascin-C in fibrosis in multiple organs: Translational implications

Bhattacharyya, S., Midwood, K. S., & Varga, J. (2022) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2022.03.019 · Cited by 57 · see citing works

Role of the Extracellular Matrix in Cancer: Insights into Tumor Progression and Therapy

Desai, N., Sahel, D. K., Sawant, B. K. S., Postwala, H. I., Shah, Y. B., Chavda, V. P., Fernandes, C., Khatri, D. K., & Vora, L. K. (2025) · Advanced Therapeutics · doi:10.1002/adtp.202400370 · Cited by 54 · see citing works

Research Progress in Skin Aging, Metabolism, and Related Products

He, X., Gao, X., & Xie, W. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms242115930 · Cited by 53 · see citing works

SOD3 Suppresses the Expression of MMP-1 and Increases the Integrity of Extracellular Matrix in Fibroblasts

Kim, J. H., Jeong, H. D., Song, M. J., Lee, D. H., Chung, J. H., & Lee, S. (2022) · Antioxidants · doi:10.3390/antiox11050928 · Cited by 36 · see citing works

Human Umbilical Cord Mesenchymal Stromal Cell-Derived Extracellular Vesicles Induce Fetal Wound Healing Features Revealed by Single-Cell RNA Sequencing

Liu, Y., Zhang, M., Wang, C., Chen, H., Su, D., Yang, C. H., Tao, Y., Lv, X., Zhou, Z., Li, J., et al. (2024) · ACS Nano · doi:10.1021/acsnano.4c01401 · Cited by 34 · see citing works

TGFβ1 Secreted by Cancer-Associated Fibroblasts as an Inductor of Resistance to Photodynamic Therapy in Squamous Cell Carcinoma Cells

Gallego-Rentero, M., Gutiérrez-Pérez, M., Fernández-Guarino, M., Mascaraque, M., Portillo-Esnaola, M., Gilaberte, Y., Carrasco, E., & Juarranz, Á. (2021) · Cancers · doi:10.3390/cancers13225613 · Cited by 33 · see citing works

Strategic outline of interventions targeting extracellular matrix for promoting healthy longevity

Park, J. Y. C., King, A., Björk, V., English, B. W., Fedintsev, A., & Ewald, C. Y. (2023) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00060.2023 · Cited by 29 · see citing works

SPARC Is Highly Expressed in Young Skin and Promotes Extracellular Matrix Integrity in Fibroblasts via the TGF-β Signaling Pathway

Ham, S. M., Song, M. J., Yoon, H., Lee, D. H., Chung, J. H., & Lee, S. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms241512179 · Cited by 29 · see citing works

LRG1 Promotes ECM Integrity by Activating the TGF-β Signaling Pathway in Fibroblasts

Park, H. N., Song, M. J., Choi, Y. E., Lee, D. H., Chung, J. H., & Lee, S. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms241512445 · Cited by 29 · see citing works

Role of integrin β1 and tenascin C mediate TGF-SMAD2/3 signaling in chondrogenic differentiation of BMSCs induced by type I collagen hydrogel

Huang, Y.-J., Sun, M., Lu, Z., Zhong, Q., Tan, M., Wei, Q., & Li, Z. (2024) · Regenerative Biomaterials · doi:10.1093/rb/rbae017 · Cited by 26 · see citing works

Intercellular communication analysis of the human retinal pigment epithelial and choroidal cells predicts pathways associated with aging, cellular senescence and age-related macular degeneration

Dhirachaikulpanich, D., Lagger, C., Chatsirisupachai, K., de Magalhães, J. P., & Paraoan, L. (2022) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2022.1016293 · Cited by 24 · see citing works

Understanding of mouse and human bladder at single‐cell resolution: integrated analysis of trajectory and cell‐cell interactive networks based on multiple scRNA‐seq datasets

Shi, B., Wu, Y., Chen, H., Ding, J., & Qi, J. (2021) · Cell Proliferation · doi:10.1111/cpr.13170 · Cited by 23 · see citing works

Target acquisition of anti-aging manno-oligosaccharide that triggers ECM process via TGF-β/Smads-SIRT1 signalling pathway

Liu, Y., Zi, C., Chen, D., Li, J., He, R., & Hu, J. (2022) · Carbohydrate Polymers · doi:10.1016/j.carbpol.2022.120380 · Cited by 23 · see citing works

The extracellular matrix fibulin 7 maintains epidermal stem cell heterogeneity during skin aging

Raja, E., Changarathil, G., Oinam, L., Ngo, Y. X., Tsunezumi, J., Ishii, R., Sasaki, T., Imanaka‐Yoshida, K., Yanagisawa, H., & Sada, A. (2022) · EMBO Reports · doi:10.15252/embr.202255478 · Cited by 22 · see citing works

Withania somnifera root extract inhibits MGO-induced skin fibroblast cells dysfunction via ECM-integrin interaction

Liu, X., Chen, C., Lin, Y., Liu, Y., Cai, S., Li, D., Li, L., Xiao, P., & Yi, F. (2024) · Journal of Ethnopharmacology · doi:10.1016/j.jep.2023.117699 · Cited by 19 · see citing works

Asthma and Post-Asthmatic Fibrosis: A Search for New Promising Molecular Markers of Transition from Acute Inflammation to Pulmonary Fibrosis

Savin, I. A., Markov, A. V., Аркадьевна, З. М., & Васильевна, С. А. (2022) · Biomedicines · doi:10.3390/biomedicines10051017 · Cited by 18 · see citing works

Metalloproteinases in dermal homeostasis

Kümper, M., Steinkamp, J., & Zigrino, P. (2022) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00450.2021 · Cited by 18 · see citing works

Tissue Mechanics in Haired Murine Skin: Potential Implications for Skin Aging

Harn, H. I., Chen, C., Wang, S., Lei, M., & Chuong, C. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.635340 · Cited by 18 · see citing works

Extracellular Matrix Remodeling in Atopic Dermatitis Harnesses the Onset of an Asthmatic Phenotype and Is a Potential Contributor to the Atopic March

Graff, P., Wörz, D., Wilzopolski, J., Voß, A., Sarrazin, J., Blimkie, T. M., Weiner, J. M., Kershaw, O., Panwar, P., Hackett, T., et al. (2023) · Journal of Investigative Dermatology · doi:10.1016/j.jid.2023.09.278 · Cited by 16 · see citing works

Expression of Polyamine Oxidase in Fibroblasts Induces MMP-1 and Decreases the Integrity of Extracellular Matrix

Jeong, H. D., Kim, J. H., Kwon, G. E., & Lee, S. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms231810487 · Cited by 16 · see citing works

Matrisomal components involved in regenerative wound healing in axolotl and Acomys : implications for biomaterial development

Avila-Martinez, N., Gansevoort, M., Verbakel, J., Haarshaadri, J., Araújo, I. M., Vitorino, M., Tiscórnia, G., Kuppevelt, T. H. V., & Daamen, W. F. (2023) · Biomaterials Science · doi:10.1039/d3bm00835e · Cited by 15 · see citing works

Matrikines in the skin: Origin, effects, and therapeutic potential

Sirois, J. P., & Heinz, A. (2024) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2024.108682 · Cited by 15 · see citing works

Anti-PTK7 Monoclonal Antibodies Inhibit Angiogenesis by Suppressing PTK7 Function

Oh, S. W., Shin, W., & Lee, S. (2022) · Cancers · doi:10.3390/cancers14184463 · Cited by 15 · see citing works

Involvement of Matricellular Proteins in Cellular Senescence: Potential Therapeutic Targets for Age-Related Diseases

Fujita, M., Sasada, M., Iyoda, T., & Fukai, F. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms25126591 · Cited by 14 · see citing works

Cellular senescence in human liver under normal aging and cancer

Karpova, A., Li, X., Peng, C.-W., Gallant, K. L., Rapp, D. R., Alligood, D. M., Houston, A. J., Park, A., Targino da Costa, A. L. N., Chou, W.-H., et al. (2026) · Cell Genomics · doi:10.1016/j.xgen.2025.101133 · Cited by 13 · see citing works

Tenascin-C: Friend or Foe in Lung Aging?

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HSP47 Increases the Expression of Type I Collagen in Fibroblasts through IRE1α Activation, XBP1 Splicing, and Nuclear Translocation of β-Catenin

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