Membrane-anchored and soluble forms of betaglycan, a polymorphic proteoglycan that binds transforming growth factor-beta.

Transforming growth factor type beta: rapid induction of fibrosis and angiogenesis in vivo and stimulation of collagen formation in vitro.

Roberts, A. B., Sporn, M. B., Assoian, R. K., Smith, J. M., Roche, N. S., Wakefield, L. M., Heine, U., Liotta, L. A., Falanga, V., & Kehrl, J. H. (1986) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.83.12.4167 · Cited by 2,867

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

The Toll gene of drosophila, required for dorsal-ventral embryonic polarity, appears to encode a transmembrane protein

Hashimoto, C., Hudson, K., & Anderson, K. V. (1988) · Cell · doi:10.1016/0092-8674(88)90516-8 · Cited by 1,097

Role of transforming growth factor-beta in the development of the mouse embryo.

Heine, U., Munoz, E. F., Flanders, K. C., Ellingsworth, L. R., Lam, H. Y., Thompson, N. L., Roberts, A. B., & Sporn, M. B. (1987) · The Journal of Cell Biology · doi:10.1083/jcb.105.6.2861 · Cited by 739

Deduced protein sequence of bone small proteoglycan I (biglycan) shows homology with proteoglycan II (decorin) and several nonconnective tissue proteins in a variety of species

Fisher, L. W., Termine, J. D., & Young, M. F. (1989) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)83781-4 · Cited by 703

The transforming growth factor-β system, a complex pattern of cross-reactive ligands and receptors

Cheifetz, S., Weatherbee, J. A., Tsang, M., Anderson, J. K., Mole, J. E., Lucas, R., & Massagué, J. (1987) · Cell · doi:10.1016/0092-8674(87)90192-9 · Cited by 701

The TGF-β family of growth and differentiation factors

Massagué, J. (1987) · Cell · doi:10.1016/0092-8674(87)90443-0 · Cited by 672

A lymphocyte molecule implicated in lymph node homing is a member of the cartilage link protein family

Stamenkovic, I., Amiot, M., Pesando, J. M., & Seed, B. (1989) · Cell · doi:10.1016/0092-8674(89)90638-7 · Cited by 672

Type beta transforming growth factor is an inhibitor of myogenic differentiation.

Massagué, J., Cheifetz, S., Endo, T., & Nadal‐Ginard, B. (1986) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.83.21.8206 · Cited by 560

A human lymphocyte homing receptor, the Hermes antigen, is related to cartilage proteoglycan core and link proteins

Goldstein, L. A., Zhou, D., Picker, L. J., Minty, C., Bargatze, R. F., Ding, J., & Butcher, E. C. (1989) · Cell · doi:10.1016/0092-8674(89)90639-9 · Cited by 556

Binding of transforming growth factor-β1 to methylamine-modified α2-macroglobulin and to binary and ternary α2-macroglobulin-proteinase complexes

Hall, S. W., LaMarre, J., Marshall, L., Hayes, M. A., & Gonias, S. L. (1992) · Biochemical Journal · doi:10.1042/bj2810569 · Cited by 36

Roles for transforming growth factors-β in the genesis, prevention, and treatment of breast cancer

Wakefield, L. M., Colletta, A. A., McCune, B. K., & Sporn, M. B. (1991) · Cancer treatment and research · doi:10.1007/978-1-4615-3500-3_6 · Cited by 36

The Balance of Cell Surface and Soluble Type III TGF-β Receptor Regulates BMP Signaling in Normal and Cancerous Mammary Epithelial Cells

Gatza, C. E., Elderbroom, J. L., Oh, S. Y., Starr, M. D., Nixon, A. B., & Blobe, G. C. (2014) · Neoplasia · doi:10.1016/j.neo.2014.05.008 · Cited by 35

PDGF-BB and TGF-α rescue gastrulation, spiculogenesis, and LpS1 expression in collagen-disrupted embryos of the sea urchin genus Lytechinus

RAMACHANDRAN, R., Seid, C. A., LEE, H., & Tomlinson, C. R. (1993) · Mechanisms of Development · doi:10.1016/0925-4773(93)90014-o · Cited by 35

Two novel patterns of transforming growth factor beta (TGF-beta) binding to cell surface proteins are dependent upon the binding of TGF-beta 1 and indicate a mechanism of positive cooperativity.

Segarini, P. R., Ziman, J. M., Kane, C. J. M., & Dasch, J. R. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)48393-7 · Cited by 34

Transforming Growth Factor β1

Ruscetti, F. W., Birchenall-Roberts, M. C., McPherson, J. M., & Wiltrout, R. H. (1998) · Elsevier eBooks · doi:10.1016/b978-012498340-3/50029-4 · Cited by 33

Heparan Sulfate Proteoglycan Expression Is Induced During Early Erythroid Differentiation of Multipotent Hematopoietic Stem Cells

Drzeniek, Z., Stöcker, G., Siebertz, B., Just, U., Schroeder, T., Ostertag, W., & Haubeck, H.-D. (1999) · Blood · doi:10.1182/blood.v93.9.2884 · Cited by 33

Transforming growth factor-beta signaling in breast cancer

Chang, C.-F. (2007) · Frontiers in bioscience · doi:10.2741/2396 · Cited by 33

Vascular endothelial growth factor is involved in neoangiogenesis in Hirudo medicinalis (Annelida, Hirudinea)

Tettamanti, G. (2003) · Cytokine · doi:10.1016/s1043-4666(03)00176-5 · Cited by 32

TGF-β receptors: a complicated system of multiple binding proteins

Segarini, P. R. (1993) · Biochimica et Biophysica Acta (BBA) - Reviews on Cancer · doi:10.1016/0304-419x(93)90009-2 · Cited by 32

Serglycin and betaglycan proteoglycans are expressed in the megakaryocytic cell line CHRF 288‐11 and normal human megakaryocytes

Schick, B. P., & Jacoby, J. A. (1995) · Journal of Cellular Physiology · doi:10.1002/jcp.1041650113 · Cited by 31

Turnover in periodontal connective tissues: dynamic homeostasis of cells, collagen and ground substances

Bartold, P. M. (1995) · Oral Diseases · doi:10.1111/j.1601-0825.1995.tb00189.x · Cited by 31

Activated α2‐Macroglobulin Promotes Mitogenesis in Rat Vascular Smooth Muscle Cells by a Mechanism that is Independent of Growth‐Factor‐Carrier Activity

Webb, D. J., Hussaini, I. M., Weaver, A. M., Atkins, T. L., Chu, C. T., Pizzo, S. V., Owens, G. K., & Gonias, S. L. (1995) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1995.714_a.x · Cited by 30

Anatomy, pathophysiology and basic mechanisms of disease

Crawford, J. M., & Burt, A. D. (2011) · Elsevier eBooks · doi:10.1016/b978-0-7020-3398-8.00001-5 · Cited by 32

Interaction of specifically chemically modified dextrans with transforming growth factor β1: potentiation of its biological activity

Logeart‐Avramoglou, D., Huynh, R., Chaubet, F., Sedel, L., & Meunier, A. (2002) · Biochemical Pharmacology · doi:10.1016/s0006-2952(01)00834-6 · Cited by 29

Extracellular calcium regulates distribution and transport of heparan sulfate proteoglycans in a rat parathyroid cell line.

Takeuchi, Y., Sakaguchi, K., Yanagishita, M., Aurbach, G. D., & Hascall, V. (1990) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)77400-0 · Cited by 29

The Role of TGFBR3 in the Development of Lung Cancer

Deng, X., Ma, N., He, J., Xu, F., & Zou, G. (2024) · Protein and Peptide Letters · doi:10.2174/0109298665315841240731060636 · Cited by 28

Isolation and purification of proteoglycans

Fedarko, N. S. (1993) · Cellular and Molecular Life Sciences · doi:10.1007/bf01923582 · Cited by 28

Thrombin adhesive properties: induction by plasmin and heparan sulfate.

Bar‐Shavit, R., Eskohjido, Y., Fenton, J. W., Esko, J. D., & Vlodavsky, I. (1993) · The Journal of Cell Biology · doi:10.1083/jcb.123.5.1279 · Cited by 28

Characterization of transforming growth factor-beta (TGF-beta) receptors on BeWo choriocarcinoma cells including the identification of a novel 38-kDa TGF-beta binding glycoprotein.

Mitchell, E. J., Lee, K., & O'Connor‐McCourt, M. D. (1992) · Molecular Biology of the Cell · doi:10.1091/mbc.3.11.1295 · Cited by 28

Dual Action of a Carbohydrate Epitope on Afferent and Efferent Axons in Cortical Development

Henke‐Fahle, S., Mann, F., Götz, M., Wild, K., & Bolz, J. (1996) · Journal of Neuroscience · doi:10.1523/jneurosci.16-13-04195.1996 · Cited by 28

Structure, Function, and Responses to Injury

Crawford, J. M., Bioulac‐Sage, P., & Hytiroglou, P. (2017) · Elsevier eBooks · doi:10.1016/b978-0-7020-6697-9.00001-7 · Cited by 28

The type III TGF-β receptor betaglycan transmembrane–cytoplasmic domain fragment is stable after ectodomain cleavage and is a substrate of the intramembrane protease γ-secretase

Blair, C. R., Stone, J. B., & Wells, R. G. (2010) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2010.12.005 · Cited by 27

Decrease in transforming growth factor beta 1 binding during differentiation of rat adipocyte precursors in primary culture.

Serrero, G., & Mills, D. (1991) · PubMed · Cited by 27

Stable expression of human platelet-derived growth factor B chain by bovine aortic endothelial cells. Matrix association and selective proteolytic cleavage by thrombin

Soyombo, A. A., & DiCorleto, P. E. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)32502-4 · Cited by 26

The t(1;10)(p22;q24) TGFBR3/MGEA5 Translocation in Pleomorphic Hyalinizing Angiectatic Tumor, Myxoinflammatory Fibroblastic Sarcoma, and Hemosiderotic Fibrolipomatous Tumor

Liu, H., Sukov, W. R., & Ro, J. Y. (2018) · Archives of Pathology & Laboratory Medicine · doi:10.5858/arpa.2017-0412-ra · Cited by 25

Proteoglycan synthesis in human erythroleukaemia (HEL) cells

Schick, B. P., & Senkowski-Richardson, S. (1992) · Biochemical Journal · doi:10.1042/bj2820651 · Cited by 25

Hypoxia affects cytokine production and proliferative responses by human peripheral mononuclear cells

Naldini, A., Carraro, F., Silvestri, S., & Bocci, V. A. (1997) · Journal of Cellular Physiology · doi:10.1002/(sici)1097-4652(199712)173:3 · Cited by 118

Mechanisms in TGF‐β Action

Massagué, J., Heino, J., & Laiho, M. (2007) · Novartis Foundation symposium · doi:10.1002/9780470514061.ch4 · Cited by 25

Human Chorionic Gonadotrophin as a Possible Mediator of Leiomyoma Growth during Pregnancy: Molecular Mechanisms

Sarais, V., Cermisoni, G. C., Schimberni, M., Alteri, A., Papaleo, E., Somigliana, E., & Viganò, P. (2017) · International Journal of Molecular Sciences · doi:10.3390/ijms18092014 · Cited by 24

Endoglin Trafficking/Exosomal Targeting in Liver Cells Depends on N-Glycosylation

Meurer, S. K., Wimmer, A. E., de Leur, E. V., & Weiskirchen, R. (2019) · Cells · doi:10.3390/cells8090997 · Cited by 23

Binding of transforming growth factor-β1 to immobilized human α2-macroglobulin

Webb, D. J., Crookston, K. P., Hall, S. W., & Gonias, S. L. (1992) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(92)90020-w · Cited by 24

Stromal accumulation of chondroitin sulphate in mammary tumours of dogs

Hinrichs, U., Rutteman, G. R., & Nederbragt, H. (1999) · British Journal of Cancer · doi:10.1038/sj.bjc.6690529 · Cited by 23

Transforming growth factor-β effects on morphology of immature rat Leydig cells

Dickson, C. P., Webster, D. R., Johnson, H., Millena, A. C., & Khan, S. A. (2002) · Molecular and Cellular Endocrinology · doi:10.1016/s0303-7207(02)00216-2 · Cited by 23

Apoptosis in mouse embryos: Elevated levels in pregastrulae and in the distal anterior region of gastrulae of normal and mutant mice

Manova, K., Tomihara-Newberger, C., Wang, S., Godelman, A., Kalantry, S., Whitty, K. B., Leon, V. D., Chen, W. S., Lacy, E., & Bachvarova, R. F. (1998) · Developmental Dynamics · doi:10.1002/(sici)1097-0177(199811)213:3 · Cited by 56

Proteoglycan–collagen associations in the non-lactating human breast connective tissue during the menstrual cycle

Stoeckelhuber, M., Stumpf, P., Hoefter, E., & WELSCH, U. N. (2002) · Histochemistry and Cell Biology · doi:10.1007/s00418-002-0438-7 · Cited by 22

Scar Wars Strategies

LOW, S. Q., & Moy, R. L. (1992) · The Journal of Dermatologic Surgery and Oncology · doi:10.1111/j.1524-4725.1992.tb02770.x · Cited by 22

Interactions Between CD44 and Hyaluronic Acid: Their Role in Tumor Growth and Metastasis

Sy, M. S., Liu, D., Schiavone, R., Ma, J., Mori, H., & Guo, Y. (1996) · Current topics in microbiology and immunology · doi:10.1007/978-3-642-80071-9_9 · Cited by 22

Mutual regulation between glycosylation and transforming growth factor-β isoforms signaling pathway

Chen, Z., Yu, H., Chen, X., Chen, W., Song, W., & Li, Z. (2023) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2023.123818 · Cited by 23

Connective tissue growth factor antagonizes transforming growth factor-β1/Smad signalling in renal mesangial cells

O'Donovan, H. C., Hickey, F. B., Brazil, D. P., Kavanagh, D. H., Oliver, N., Martin, F., Godson, C., & Crean, J. K. G. (2011) · Biochemical Journal · doi:10.1042/bj20110910 · Cited by 21

Oral ingestion of colostrum alters intestinal transforming growth factor-beta receptor intensity in newborn pigs

Mei, J., Zhang, Y., Wang, T. Z., Sangild, P. T., & Xu, R. (2006) · Livestock Science · doi:10.1016/j.livsci.2006.06.017 · Cited by 21

Role of glypican-1 in the trophic activity on PC12 cells induced by cultured sciatic nerve conditioned medium: identification of a glypican-1–neuregulin complex

Malavé, C., Villegas, G. M., Hernández, M., Martı́nez, J. C., Castillo, C., de Mata, Z. S., & Villegas, R. (2003) · Brain Research · doi:10.1016/s0006-8993(03)03031-2 · Cited by 21

Expression of transforming growth factor‐beta receptors types II and III within various cells in the rat periodontium

Gao, J., Symons, A. L., & Bartold, P. M. (1999) · Journal of Periodontal Research · doi:10.1111/j.1600-0765.1999.tb02230.x · Cited by 21

The Proteins of Bone

Delmas, P. D., & Malaval, L. (1993) · Handbook of experimental pharmacology · doi:10.1007/978-3-642-77991-6_19 · Cited by 21

The interaction of vascular endothelial cells and dorsal root ganglion neurites is mediated by vitronectin and heparan sulfate proteoglycans

Isahara, K., & Yamamoto, M. (1995) · Developmental Brain Research · doi:10.1016/0165-3806(94)00160-2 · Cited by 20

Proteoglycan Gene Families

Hassell, J. R., Blochberger, T. C., Rada, J. A., Chakravarti, S., & Noonan, D. M. (1993) · Advances in molecular and cell biology · doi:10.1016/s1569-2558(08)60199-x · Cited by 20

Ectodomain cleavage and shedding of the type III transforming growth factor‐β receptor in lung membranes

Philip, A., Hannah, R. R., & O'Connor‐McCourt, M. D. (1999) · European Journal of Biochemistry · doi:10.1046/j.1432-1327.1999.00298.x · Cited by 20

Cytokines and proteoglycans

Nietfeld, J. J., Huber-Bruning, O., & Bÿlsma, J. W. (1994) · Birkhäuser Basel eBooks · doi:10.1007/978-3-0348-7545-5_13 · Cited by 20

TβRIII is induced by TCR signaling and downregulated in FoxP3+ regulatory T cells

Ortega‐Francisco, S., Fuente, M. D. L., Alvarez-Salazar, E. K., Castro, L. A. B., Fonseca‐Camarillo, G., Olguín‐Alor, R., Alemán-Muench, G. R., López‐Casillas, F., Raman, C., García-Zepeda, E. A., et al. (2017) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2017.10.081 · Cited by 19

Effect of Heparin on Production of Basic Fibroblast Growth Factor and Transforming Growth Factor-Beta1 by Human Normal Skin and Hyperplastic Scar Fibroblasts

Fan, S.-Q., Qin, L.-Y., Cai, J.-L., Zhu, G.-Y., Bin, X., & Yan, H.-S. (2007) · Journal of Burn Care & Research · doi:10.1097/bcr.0b013e318148c9d0 · Cited by 19

TGF-β Superfamily Receptors—Targets for Antiangiogenic Therapy?

Otten, J., Bokemeyer, C., & Fiedler, W. (2010) · Journal of Oncology · doi:10.1155/2010/317068 · Cited by 19

Structural analysis of proteoglycan macrophage colony-stimulating factor.

Kimura, F., Suzu, S., Nakamura, Y., Wakimoto, N., Kanatani, Y., Yanai, N., Nagata, N., & Motoyoshi, K. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)32085-9 · Cited by 19

Proteoglycans – Structure and Functions

Kresse, H. (1996) · doi:10.1002/9783527614738.ch11 · Cited by 19

Changes in the connective tissue sheath of Wistar rat nerve with aging

Esquisatto, M. A. M., de Aro, A. A., Fêo, H. B., & Gomes, L. (2014) · Annals of Anatomy - Anatomischer Anzeiger · doi:10.1016/j.aanat.2014.08.005 · Cited by 18

The Role of Transforming Growth Factors–Beta in Cutaneous Scarring

Shah, M., Rorison, P., & Ferguson, M. W. J. (2000) · CRC Press eBooks · doi:10.3109/9780203909652-14 · Cited by 18

Changes in the Intraocular Cytokine Levels after Intravitreal Bevacizumab in Uveitic Macular Edema

Jeon, S., Lee, W. K., & Jung, Y. (2012) · Ocular Immunology and Inflammation · doi:10.3109/09273948.2012.709576 · Cited by 17

Acidity increases the uptake of native LDL by human monocyte-derived macrophages

Plihtari, R., Kovanen, P. T., & Öörni, K. (2011) · Atherosclerosis · doi:10.1016/j.atherosclerosis.2011.04.013 · Cited by 17

Reprint of: Betaglycan: A multifunctional accessory

Bilandzic, M., & Stenvers, K. L. (2012) · Molecular and Cellular Endocrinology · doi:10.1016/j.mce.2012.03.020 · Cited by 17

Monoclonal antibody MT2 identifies an extracellular matrix glycoprotein that is co-localized with tenascin during adult newt limb regeneration

Klatt, K. P., Yang, E. V., & Tassava, R. A. (1992) · Differentiation · doi:10.1111/j.1432-0436.1992.tb00668.x · Cited by 17

The synthesis of 5α ‐ dihydrotestosterone from androgens by human gingival tissues and fibroblasts in culture in response to TGIF‐β and PDGF

Kasasa, S. C., & Soory, M. (1996) · Journal of Periodontal Research · doi:10.1111/j.1600-0765.1996.tb00498.x · Cited by 17

Decreased transforming growth factor‐(β) response and binding in insulin‐independent teratoma‐derived cell lines with increased tumorigenic properties

Serrero, G., Zhou, J., Mills, D., & Lepak, N. M. (1991) · Journal of Cellular Physiology · doi:10.1002/jcp.1041490321 · Cited by 17

Extracellular Matrix and Bone Morphogenetic Proteins in Cartilage and Bone Development and Repair

Vukičević, S., Paralkar, V. M., & Reddi, A. H. (1993) · Advances in molecular and cell biology · doi:10.1016/s1569-2558(08)60203-9 · Cited by 17

Multidomain Proteins of the Extracellular Matrix and Cellular Growth

End, P., & Engel, J. (1991) · Elsevier eBooks · doi:10.1016/b978-0-12-483365-4.50008-6 · Cited by 16

Soluble type III TGFβ receptor in diagnosis and follow-up of patients with breast cancer.

Jurišić, D., Erjavec, I., Trkulja, V., Dumić-Čule, I., Hadžibegović, I., Kovačević, L., Svaguša, T., Stanec, Z., Vukičević, S., & Grgurević, L. (2015) · PubMed · doi:10.3109/08977194.2015.1055740 · Cited by 15

Cultured incisors display major modifications in basal lamina deposition without further effect on odontoblast differentiation

Meyer, J.-M., Ruch, J. V., Kubler, M. D., Kupferle, C., & Lesot, H. (1995) · Cell and Tissue Research · doi:10.1007/bf00300700 · Cited by 15

Abrogation of betaglycan attenuates TGF-β-mediated inhibition of embryonic murine lung branching morphogenesis in culture

Zhao, J., Tefft, J. D., Lee, M., Smith, S. M., & Warburton, D. (1998) · Mechanisms of Development · doi:10.1016/s0925-4773(98)00083-5 · Cited by 15

The Role of Transforming Growth Factors–Beta in Cutaneous Scarring

Shah, M., Rorison, P., & Ferguson, M. W. J. (2000) · CRC Press eBooks · doi:10.1201/b14004-11 · Cited by 15

CNS / PNS proteoglycans functionalize neuronal and astrocyte niche microenvironments optimizing cellular activity by preserving membrane polarization dynamics, ionic microenvironments, ion fluxes, neuronal activation, and network neurotransductive capacity

Melrose, J. (2024) · Journal of Neuroscience Research · doi:10.1002/jnr.25361 · Cited by 15

Role of Betaglycan in TGF-β Signaling and Wound Healing in Human Endometriotic Epithelial Cells and in Endometriosis

Mwaura, A. N., Riaz, M. A., Maoga, J. B., Mecha, E. O., Omwandho, C. O. A., Scheiner‐Bobis, G., Meinhold-Heerlein, I. M., & Konrad, L. (2022) · Biology · doi:10.3390/biology11040513 · Cited by 14

Glucocorticoid Regulation of Transforming Growth Factor β1 Activity and Binding in Osteoblast-Enriched Cultures from Fetal Rat Bone

Centrella, M., McCarthy, T. L., & CANALIS, E. M. (1991) · Molecular and Cellular Biology · doi:10.1128/mcb.11.9.4490-4496.1991 · Cited by 14

Evidence that heparin binding autocrine factors modulate testosterone production by the adult rat Leydig cell

McFarlane, J. R., Laslett, A. L., de Kretser, D., & Risbridger, G. P. (1996) · Molecular and Cellular Endocrinology · doi:10.1016/0303-7207(96)03766-5 · Cited by 14

Proteoglycan and glycosaminoglycan free chain expression in keratinocytes, endothelium, and mesenchymal cells

Piepkorn, M. W., Hovingh, P., & Linker, A. (1991) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(91)91712-l · Cited by 14

A tumor-promoting role for soluble TβRIII in glioblastoma

Burghardt, I., Schroeder, J. J., Weiß, T., Gramatzki, D., & Weller, M. (2021) · Molecular and Cellular Biochemistry · doi:10.1007/s11010-021-04128-y · Cited by 14

Effect of Heparin on Production of Transforming Growth Factor (TGF)-β1 and TGF-β1 mRNA Expression by Human Normal Skin and Hyperplastic Scar Fibroblasts

Fan, S.-Q., Cai, J.-L., Qin, L., Wang, Z., Liu, Z., & Sun, M. (2008) · Annals of Plastic Surgery · doi:10.1097/sap.0b013e318061d310 · Cited by 13

Agrin-like proteins of the neuromuscular junction

Patthy, L., & Nikolics, K. (1994) · Neurochemistry International · doi:10.1016/0197-0186(94)90108-2 · Cited by 13

Early Carcinogenesis Involves the Establishment of Immune Privilege via Intrinsic and Extrinsic Regulation of Indoleamine 2,3-dioxygenase-1: Translational Implications in Cancer Immunotherapy

Holtzhausen, A., Zhao, F. L., Evans, K. S., & Hanks, B. A. (2014) · Frontiers in Immunology · doi:10.3389/fimmu.2014.00438 · Cited by 12

One step preparation of multifunctional poly (ether sulfone) thin films with potential for wound dressing

Wang, L., Gong, T., Ming, W., Qiao, X., Ye, W., Zhang, L., & Pan, C. (2022) · Biomaterials Advances · doi:10.1016/j.bioadv.2022.212758 · Cited by 12

Nervous tissue proteoglycans

Margolis, R. K., & Margolis, R. U. (1994) · Birkhäuser Basel eBooks · doi:10.1007/978-3-0348-7545-5_9 · Cited by 12

A spoonful of sugar makes the melanoma go: the role of heparan sulfate proteoglycans in melanoma metastasis

O’Connell, M. P., & Weeraratna, A. T. (2011) · Pigment Cell & Melanoma Research · doi:10.1111/j.1755-148x.2011.00918.x · Cited by 11

Matrix Receptors to Cytokines: From Concept to Control of Tissue Fibrosis Dynamics

Grimaud, J.-A., & Lortat‐Jacob, H. (1994) · Pathology - Research and Practice · doi:10.1016/s0344-0338(11)80991-x · Cited by 11

Phosphorothioate Oligonucleotides Cause Degradation of Secretory but Not Intracellular Serglycin Proteoglycan Core Protein in a Sequence-Independent Manner in Human Megakaryocytic Tumor Cells

Schick, B. P., ERAS, J. L., & MINTZ, P. S. (1995) · Antisense Research and Development · doi:10.1089/ard.1995.5.59 · Cited by 11

Transforming growth factor β1 and adrenocorticortropin differentially regulate the synthesis of adrenocortical cell heparan sulfate proteoglycans and their binding of basic fibroblast growth factor

Jiang, Z., Savona‐Baron, C., CHAMBAZ, E. M., & Feige, J. (1992) · Journal of Cellular Physiology · doi:10.1002/jcp.1041530206 · Cited by 10

Isolation and partial characterization of a cell‐surface heparan sulfate proteoglycan from embryonic rat spinal cord

Guiseppetti, J. M., McCarthy, J. B., & Letourneau, P. C. (1994) · Journal of Neuroscience Research · doi:10.1002/jnr.490370505 · Cited by 10

Isolation and purification of proteoglycans

Fedarko, N. S. (1994) · Birkhäuser Basel eBooks · doi:10.1007/978-3-0348-7545-5_3 · Cited by 10

The Antiproliferative Effects of Enzymatic Deglycosylation and Metabolic Undersulfation of Proteoglycans from the Cell Surface

Ahmed, I., & Piepkorn, M. W. (1991) · Journal of Investigative Dermatology · doi:10.1111/1523-1747.ep12477957 · Cited by 10

Fibrogenic and anti-fibrogenic factors in wound repair

Ghahary, A., Pannu, R., & Tredget, E. E. (1996) · Advances in structural biology · doi:10.1016/s1064-6000(96)80010-x · Cited by 9

CrossTalkeR: Analysis and Visualisation of Ligand Receptor NetworksPreprint

Nagai, J. S., Leimkühler, N. B., Schaub, M. T., Schneider, R. K., & Costa, I. G. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.01.20.427390 · Cited by 9

Receptors for the TGF-β Ligand Family

Bassing, C. H., Yingling, J. M., & Wang, X. (1994) · Vitamins and hormones · doi:10.1016/s0083-6729(08)60497-5 · Cited by 9

Clearing the light path: Proteoglycans and their important roles in the lens and cornea

Stepp, M. A., & Menko, A. S. (2024) · Proteoglycan Research · doi:10.1002/pgr2.20 · Cited by 8

Transforming Growth Factor β Receptor Expression in Hyperstimulated Human Granulosa Cells and Cleavage Potential of the Zygotes1

Roy, S. K., Kurz, S. G., Carlson, A. M., Jonge, C. J. D., Ramey, J. W., & Maclin, V. M. (1998) · Biology of Reproduction · doi:10.1095/biolreprod59.6.1311 · Cited by 8

Rat Sertoli cell extracellular matrix regulates glycosaminoglycan synthesis by peritubular myoid cells in vitro

RAYCHOUDHURY, S. S., BLACKSHAW, A. W., & Irving, M. G. (1993) · Molecular Reproduction and Development · doi:10.1002/mrd.1080350208 · Cited by 8

Glycosaminoglycan modifications of betaglycan regulate ectodomain shedding to fine-tune TGF-β signaling responses in ovarian cancer

Choi, A. S., Jenkins, L. M., Barton, W. C., Kumari, A., Lancaster, C. L., Raulerson, C., Ji, H., Altomare, D., Starr, M. D., Whitaker, R. S., et al. (2024) · Cell Communication and Signaling · doi:10.1186/s12964-024-01496-y · Cited by 7

Transforming Growth Factor-Beta-1 Latency-Associated Peptide and Soluble Betaglycan Prevent a Glucose-Induced Increase in Fibronectin Production in Cultured Human Mesangial Cells

Nomura, K., Tada, H., Kuboki, K., & Inokuchi, T. (2002) · The Nephron journals/Nephron journals · doi:10.1159/000065020 · Cited by 7

Transforming growth factor β

Howe, P. H. (2003) · Elsevier eBooks · doi:10.1016/b978-012689663-3/50053-3 · Cited by 8

Heparin, a possible therapy for diabetic complications: The effect on mesangial and myomedial cells in vivo and in vitro, especially in relation to extracellular matrix

Yokoyama, H., Myrup, B., Oturai, P., & Deckert, T. (1995) · Journal of Diabetes and its Complications · doi:10.1016/1056-8727(94)00003-7 · Cited by 7

Inflammatory Cytokines: An Overview

Brandes, M. E., & Wahl, S. M. (1994) · Elsevier eBooks · doi:10.1016/b978-0-12-628930-5.50008-4 · Cited by 7

Activin A Modulates Betaglycan Shedding via the ALK4-SMAD3-Dependent Pathway in Endometriotic Cells

Mwaura, A. N., Riaz, M. A., Maoga, J. B., Mecha, E. O., Omwandho, C. O. A., Scheiner‐Bobis, G., Meinhold-Heerlein, I. M., & Konrad, L. (2022) · Biomolecules · doi:10.3390/biom12121749 · Cited by 7

Significance of TGFBR3 allelic loss in the deregulation of TGFβ signaling in primary human endometrial carcinomas

Zakrzewski, P. K., Nowacka‐Zawisza, M., Semczuk, A., Rechberger, T., Gałczyński, K., & Krajewska, W. M. (2015) · Oncology Reports · doi:10.3892/or.2015.4400 · Cited by 6

Ovarian transforming growth factor-b (TGF-b) receptors: in-vitro effects of follicle stimulating hormone, epidermal growth factor and TGF-b on receptor expression in human preantral follicles*

Leland, J. P. (1998) · Cited by 6

Characterization of radioiodinated recombinant human TGF-β1 binding to bone matrix within rabbit skull defects

Richardson, L., Zioncheck, T. F., Amento, E. P., Deguzmanè, L., Leeè, W. P., Xuè, Y., & Beckè, L. S. (1993) · Journal of Bone and Mineral Research · doi:10.1002/jbmr.5650081115 · Cited by 6

Membrane-anchored and soluble forms of betaglycan, a polymorphic proteoglycan that binds transforming growth factor-P

Andres, J., Stanley, K., Cheifetz, S., & Massagu�, J. (1989)

Membrane-anchored and soluble forms of betaglycan, a polymorphic proteoglycan that binds transforming growth factor-3

Andres, J., Stanley, K., Cheifetz, S., & Massagu�, J. (1989)

Purification of the transforming growth factor-beta (TGF-beta) binding proteoglycan betaglycan.

Andres, J., Rönnstrand, L., Cheifetz, S., & Massagué, J. (1991) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)54494-x · Cited by 73

Structure and expression of the membrane proteoglycan betaglycan, a component of the TGF-β receptor system

López‐Casillas, F., Cheifetz, S., Doody, J. F., Andres, J., Lane, W. S., & Massagué, J. (1991) · Cell · doi:10.1016/0092-8674(91)90073-8 · Cited by 677

Transforming growth factor-β receptors and binding proteoglycans

Boyd, F. T., Cheifetz, S., Andres, J., Laiho, M., & Massagué, J. (1990) · Journal of Cell Science · doi:10.1242/jcs.1990.supplement_13.12 · Cited by 38