Chondroitin Sulfate Perlecan Enhances Collagen Fibril Formation

Determination of hydroxyproline

Stegemann, H., & Stalder, K. (1967) · Clinica Chimica Acta · doi:10.1016/0009-8981(67)90167-2 · Cited by 1,588 · see citing works

A Direct Spectrophotometric Microassay for Sulfated Glycosaminoglycans in Cartilage Cultures

Farndale, R. W., Sayers, C. A., & Barrett, A. J. (1982) · Connective Tissue Research · doi:10.3109/03008208209160269 · Cited by 1,346 · see citing works

Specific inhibition of type I and type II collagen fibrillogenesis by the small proteoglycan of tendon

Vogel, K. G., Paulsson, M., & Heinegård, D. K. (1984) · Biochemical Journal · doi:10.1042/bj2230587 · Cited by 862 · see citing works

Supramolecular assembly of basement membranes

Timpl, R., & Brown, J. C. (1996) · BioEssays · doi:10.1002/bies.950180208 · Cited by 701 · see citing works

Perlecan Maintains the Integrity of Cartilage and Some Basement Membranes

Costell, M., Gustafsson, E., Aszódi, A., Mörgelin, M., Bloch, W., Hunziker, E. B., Addicks, K., Timpl, R., & Fässler, R. (1999) · The Journal of Cell Biology · doi:10.1083/jcb.147.5.1109 · Cited by 672 · see citing works

Perlecan, basal lamina proteoglycan, promotes basic fibroblast growth factor-receptor binding, mitogenesis, and angiogenesis.

Aviezer, D., Hecht, D., Safran, M., Eisinger, M., David, G., & Yayon, A. (1994) · Cell · doi:10.1016/0092-8674(94)90031-0 · Cited by 546 · see citing works

Perlecan is essential for cartilage and cephalic development

Arikawa‐Hirasawa, E., Watanabe, H., Takami, H., Hassell, J. R., & Yamada, Y. (1999) · Nature Genetics · doi:10.1038/15537 · Cited by 542 · see citing works

Phenotypic stability of bovine articular chondrocytes after long-term culture in alginate beads

Häuselmann, H. J., Fernandes, R. J., Mok, S. S., Schmid, T. M., Block, J. A., Aydelotte, M. B., Kuettner, K. E., & Thonar, E. J. ‐. A. (1994) · Journal of Cell Science · doi:10.1242/jcs.107.1.17 · Cited by 533 · see citing works

Culture and Growth Characteristics of Chondrocytes Encapsulated in Alginate Beads

Guo, J., Jourdian, G. W., & MacCallum, D. K. (1989) · Connective Tissue Research · doi:10.3109/03008208909043901 · Cited by 513 · see citing works

Mice deficient in small leucine-rich proteoglycans: novel in vivo models for osteoporosis, osteoarthritis, Ehlers-Danlos syndrome, muscular dystrophy, and corneal diseases

Ameye, L., & Young, M. F. (2002) · Glycobiology · doi:10.1093/glycob/cwf065 · Cited by 431 · see citing works

Interaction of a 59-kDa Connective Tissue Matrix Protein with Collagen I and Collagen II

Hedbom, E., & Heinegård, D. K. (1989) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)83516-5 · Cited by 333 · see citing works

Perlecan, the major proteoglycan of basement membranes, is altered in patients with Schwartz-Jampel syndrome (chondrodystrophic myotonia)

Nicole, S., Davoine, C.-S., Topaloğlu, H., Cattolico, L., Barral, D. C., Beighton, P., Hamida, C. B., Hammouda, H., Cruaud, C., White, P. S., et al. (2000) · Nature Genetics · doi:10.1038/82638 · Cited by 294 · see citing works

[7] Isolation and characterization of connective tissue polysaccharides

Rodén, L., Baker, J. R., Cifonelli, J. A., & Mathews, M. B. (1972) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/0076-6879(72)28009-0 · Cited by 281 · see citing works

The Determination of Collagen and Elastin

Jackson, D. S., & Cleary, E. G. (1967) · Methods of biochemical analysis · doi:10.1002/9780470110331.ch2 · Cited by 245 · see citing works

Dyssegmental dysplasia, Silverman-Handmaker type, is caused by functional null mutations of the perlecan gene

Arikawa‐Hirasawa, E., Wilcox, W. R., Le, A. H., Silverman, N. S., Govindraj, P., Hassell, J. R., & Yamada, Y. (2001) · Nature Genetics · doi:10.1038/86941 · Cited by 238 · see citing works

Heparan sulfate chains of perlecan are indispensable in the lens capsule but not in the kidney

Rossi, M., Morita, H., Sormunen, R., Airenne, S., Kreivi, M., Wang, L., Fukai, N., Olsen, B. R., Tryggvason, K., & Soininen, R. (2003) · The EMBO Journal · doi:10.1093/emboj/cdg019 · Cited by 237 · see citing works

The formation of fibrils from collagen solutions. 3. Effect of chondroitin sulphate and some other naturally occurring polyanions on the rate of formation

Wood, G. C. (1960) · Biochemical Journal · doi:10.1042/bj0750605 · Cited by 237 · see citing works

Structural and Functional Mutations of the Perlecan Gene Cause Schwartz-Jampel Syndrome, with Myotonic Myopathy and Chondrodysplasia

Arikawa‐Hirasawa, E., Le, A. H., Nishino, I., Nonaka, I., Ho, N. C., Francomano, C. A., Govindraj, P., Hassell, J. R., Devaney, J. M., Spranger, J. W., et al. (2002) · The American Journal of Human Genetics · doi:10.1086/340390 · Cited by 194 · see citing works

[17] Isolation and characterization of proteoglycans

Heinegård, D. K., & Sommarin, Y. (1987) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/0076-6879(87)44186-4 · Cited by 189 · see citing works

Hyperplastic Conotruncal Endocardial Cushions and Transposition of Great Arteries in Perlecan-Null Mice

Costell, M., Carmona, R., Gustafsson, E., González‐Iriarte, M., Fässler, R., & Muñoz‐Chápuli, R. (2002) · Circulation Research · doi:10.1161/01.res.0000026056.81424.da · Cited by 179 · see citing works

Cartilage oligomeric matrix protein (COMP) and collagen IX are sensitive markers for the differentiation state of articular primary chondrocytes

Zaucke, F., Dinser, R., Maurer, P., & Paulsson, M. (2001) · Biochemical Journal · doi:10.1042/bj3580017 · Cited by 178 · see citing works

The Leucine-rich Repeat Protein PRELP Binds Perlecan and Collagens and May Function as a Basement Membrane Anchor

Bengtsson, E., Mörgelin, M., Sasaki, T., Timpl, R., Heinegård, D. K., & Aspberg, A. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m108285200 · Cited by 171 · see citing works

Electron microscopy and other physical methods for the characterization of extracellular matrix components: Laminin, fibronectin, collagen IV, collagen VI, and proteoglycans

Engel, J., & Furthmayr, H. (1987) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/0076-6879(87)45003-9 · Cited by 170 · see citing works

Absence of acetylcholinesterase at the neuromuscular junctions of perlecan-null mice

Arikawa‐Hirasawa, E., Rossi, S. G., Rotundo, R. L., & Yamada, Y. (2002) · Nature Neuroscience · doi:10.1038/nn801 · Cited by 166 · see citing works

The C‐Terminal Domain V of Perlecan Promotes β1 Integrin‐Mediated Cell Adhesion, Binds Heparin, Nidogen and Fibulin‐2 and Can be Modified by Glycosaminoglycans

Brown, J. C., Sasaki, T., Göhring, W., Yamada, Y., & Timpl, R. (1997) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1997.t01-1-00039.x · Cited by 164 · see citing works

Perlecan is a component of cartilage matrix and promotes chondrocyte attachment

SundarRaj, N., Fite, D., Ledbetter, S. R., Chakravarti, S., & Hassell, J. R. (1995) · Journal of Cell Science · doi:10.1242/jcs.108.7.2663 · Cited by 156 · see citing works

Expression of the Heparan Sulfate Proteoglycan, Perlecan, during Mouse Embryogenesis and Perlecan Chondrogenic Activity In Vitro

French, M. M., Smith, S. E., Akanbi, K. A., Sanford, T., Hecht, J. T., Farach‐Carson, M. C., & Carson, D. D. (1999) · The Journal of Cell Biology · doi:10.1083/jcb.145.5.1103 · Cited by 154 · see citing works

The effect of acid mucopolysaccharides and acid mucopolysaccharide–proteins on fibril formation from collagen solutions

Mathews, M. B., & Decker, L. (1968) · Biochemical Journal · doi:10.1042/bj1090517 · Cited by 150 · see citing works

Expression ofreelin, the gene responsible for the reeler mutation, in embryonic development and adulthood in the mouse

Ikeda, Y., & Terashima, T. (1997) · Developmental Dynamics · doi:10.1002/(sici)1097-0177(199710)210:2 · Cited by 138 · see citing works

The Influence of Glycosaminoglycans on the Formation of Fibers from Monomeric Tropocollagen in vitro

Öbrink, B. (1973) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1973.tb02739.x · Cited by 128 · see citing works

Oversulfated Dermatan Sulfate Exhibits Neurite Outgrowth-promoting Activity toward Embryonic Mouse Hippocampal Neurons

Hikino, M., Mikami, T., Faissner, A., Vilela-Silva, A.-C. E. S., Pavão, M. S. G., & Sugahara, K. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m308169200 · Cited by 124 · see citing works

A Novel Interaction between Perlecan Protein Core and Progranulin

González, E. M., Mongiat, M., Slater, S. J., Baffa, R., & Iozzo, R. V. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.c300310200 · Cited by 124 · see citing works

Perlecan and Basement Membrane-Chondroitin Sulfate Proteoglycan (Bamacan) Are Two Basement Membrane Chondroitin/Dermatan Sulfate Proteoglycans in the Engelbreth-Holm-Swarm Tumor Matrix

Couchman, J., Kapoor, R., Sthanam, M., & Wu, R. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.16.9595 · Cited by 85 · see citing works

Structural basis of glycosaminoglycan modification and of heterotypic interactions of perlecan domain V 1 1Edited by I. B. Holland

Friedrich, M. V. K., Göhring, W., Mörgelin, M., Brancaccio, A., David, G., & Timpl, R. (1999) · Journal of Molecular Biology · doi:10.1006/jmbi.1999.3259 · Cited by 84 · see citing works

Chondrogenic Activity of the Heparan Sulfate Proteoglycan Perlecan Maps to the N-terminal Domain I

French, M. M., Gomes, R. R., Timpl, R., Höök, M., Czymmek, K. J., Farach‐Carson, M. C., & Carson, D. D. (2002) · Journal of Bone and Mineral Research · doi:10.1359/jbmr.2002.17.1.48 · Cited by 75 · see citing works

Characterization of Recombinant Perlecan Domain I and Its Substitution by Glycosaminoglycans and Oligosaccharides

Costell, M., Manni, K., Yamada, Y., & Timpl, R. (1997) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1997.t01-1-00115.x · Cited by 74 · see citing works

A fingerprinting method for chondroitin/dermatan sulfate and hyaluronan oligosaccharides

Lauder, R. M., Huckerby, T. N., & Nieduszynski, I. A. (2000) · Glycobiology · doi:10.1093/glycob/10.4.393 · Cited by 69 · see citing works

Domain IV of mouse laminin β1 and β2 chains

Sasaki, T., Mann, K., Miner, J. H., Miosge, N., & Timpl, R. (2002) · European Journal of Biochemistry · doi:10.1046/j.0014-2956.2001.02663.x · Cited by 68 · see citing works

Tyrosine-rich acidic matrix protein (TRAMP) accelerates collagen fibril formation in vitro.

Macbeath, J. R. E., Shackleton, D. R., & HULMES, D. J. S. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)36588-3 · Cited by 67 · see citing works

Localization of Glycosaminoglycan Substitution Sites on Domain V of Mouse Perlecan

Tapanadechopone, P., Hassell, J. R., Rigatti, B. W., & Couchman, J. (1999) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1999.1714 · Cited by 66 · see citing works

Domain Structure of Chondroitin Sulfate E Octasaccharides Binding to Type V Collagen

Takagaki, K., Munakata, H., Kakizaki, I., Iwafune, M., Itabashi, T., & Endo, M. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m106479200 · Cited by 66 · see citing works

Isolation and Identification of the Major Heparan Sulfate Proteoglycans in the Developing Bovine Rib Growth Plate

Govindraj, P., West, L. A., Koob, T. J., Neame, P. J., Doege, K. J., & Hassell, J. R. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m200786200 · Cited by 64 · see citing works

Role of Collagen Type II and Perlecan in Skeletal Development

Gustafsson, E., Aszódi, A., Ortéga, N., Hunziker, E. B., Denker, H., Werb, Z., & Fässler, R. (2003) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.2003.tb03217.x · Cited by 56 · see citing works

The B cell response to autologous type II collagen: biased V gene repertoire with V gene sharing and epitope shift

Mo, J., & Holmdahl, R. (1996) · The Journal of Immunology · doi:10.4049/jimmunol.157.6.2440 · Cited by 43 · see citing works

Inhibition of glycosaminoglycan modification of perlecan domain I by site‐directed mutagenesis changes protease sensitivity and laminin‐1 binding activity

Sasaki, T., Costell, M., Mann, K., & Timpl, R. (1998) · FEBS Letters · doi:10.1016/s0014-5793(98)01063-1 · Cited by 39 · see citing works

Lysolecithin enhancement of glycoprotein:glucosyl transferase activity

Kirschbaum, B. B., & Bosmann, H. B. (1973) · FEBS Letters · doi:10.1016/0014-5793(73)80773-2 · Cited by 34 · see citing works

Inhibition by heparin of the oxidation of lysine in collagen by lysyl oxidase

Gavriel, P., & Kagan, H. M. (1988) · Biochemistry · doi:10.1021/bi00408a022 · Cited by 32 · see citing works

Influence of Cartilage Proteoglycans on Type II Collagen Fibrillogenesis

Kuijer, R., van de Stadt, R. J., Koning, M. H. M. T. D., Kampen, G. P. J. V., & Korst, J. K. V. D. (1988) · Connective Tissue Research · doi:10.3109/03008208809015022 · Cited by 21 · see citing works

Cartilage homeostasis in health and rheumatic diseases

Goldring, M. B., & Marcu, K. B. (2009) · Arthritis Research & Therapy · doi:10.1186/ar2592 · Cited by 756 · see citing works

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 757 · see citing works

The nature and biology of basement membranes

Pozzi, A., Yurchenco, P. D., & Iozzo, R. V. (2016) · Matrix Biology · doi:10.1016/j.matbio.2016.12.009 · Cited by 575 · see citing works

The extracellular matrix as a multitasking player in disease

Theocharis, A., Manou, D., & Karamanos, N. (2019) · The FEBS Journal · doi:10.1111/febs.14818 · Cited by 403 · see citing works

Survey of the year 2003 commercial optical biosensor literature

Rich, R. L., & Myszka, D. G. (2004) · Journal of Molecular Recognition · doi:10.1002/jmr.726 · Cited by 505 · see citing works

The structure and function of the pericellular matrix of articular cartilage

Wilusz, R. E., Sanchez‐Adams, J., & Guilak, F. (2014) · Matrix Biology · doi:10.1016/j.matbio.2014.08.009 · Cited by 363 · see citing works

Developmental and Pathogenic Mechanisms of Basement Membrane Assembly

Yurchenco, P. D., & Patton, B. L. (2009) · Current Pharmaceutical Design · doi:10.2174/138161209787846766 · Cited by 342 · see citing works

COMP Acts as a Catalyst in Collagen Fibrillogenesis

Halász, K., Kassner, A., Mörgelin, M., & Heinegård, D. K. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m705735200 · Cited by 328 · see citing works

Fell‐Muir Lecture: Proteoglycans and more – from molecules to biology

Heinegård, D. K. (2009) · International Journal of Experimental Pathology · doi:10.1111/j.1365-2613.2009.00695.x · Cited by 311 · see citing works

Diverse Cell Signaling Events Modulated by Perlecan

Whitelock, J. M., Melrose, J., & Iozzo, R. V. (2008) · Biochemistry · doi:10.1021/bi8013938 · Cited by 270 · see citing works

Basement membrane components are key players in specialized extracellular matrices

Kruegel, J., & Miosge, N. (2010) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-010-0367-x · Cited by 254 · see citing works

Collagen Diversity, Synthesis and Assembly

HULMES, D. J. S. (2008) · Springer eBooks · doi:10.1007/978-0-387-73906-9_2 · Cited by 201 · see citing works

Basement membranes and human disease

Agtmael, T. V., & Bruckner‐Tuderman, L. (2009) · Cell and Tissue Research · doi:10.1007/s00441-009-0866-y · Cited by 141 · see citing works

Sec24D-Dependent Transport of Extracellular Matrix Proteins Is Required for Zebrafish Skeletal Morphogenesis

Sarmah, S., Barrallo‐Gimeno, A., Melville, D. B., Topczewski, J., Solnica‐Krezel, L., & Knapik, E. W. (2010) · PLoS ONE · doi:10.1371/journal.pone.0010367 · Cited by 141 · see citing works

The role of vascular-derived perlecan in modulating cell adhesion, proliferation and growth factor signaling

Lord, M. S., Chuang, C. Y., Melrose, J., Davies, M. J., Iozzo, R. V., & Whitelock, J. M. (2014) · Matrix Biology · doi:10.1016/j.matbio.2014.01.016 · Cited by 130 · see citing works

Granulin epithelin precursor: a bone morphogenic protein 2‐inducible growth factor that activates Erk1/2 signaling and JunB transcription factor in chondrogenesis

Feng, J. Q., Guo, F., Jiang, B., Zhang, Y., Frenkel, S. R., Wang, D., Tang, W., Xie, Y., & Liu, C.-J. (2010) · The FASEB Journal · doi:10.1096/fj.09-144659 · Cited by 120 · see citing works

Oversulfated chondroitin sulfate‐E binds to BMP‐4 and enhances osteoblast differentiation

Miyazaki, T., Miyauchi, S., Tawada, A., Anada, T., Matsuzaka, S., & Suzuki, O. (2008) · Journal of Cellular Physiology · doi:10.1002/jcp.21557 · Cited by 118 · see citing works

ADAMTS-7, a Direct Target of PTHrP, Adversely Regulates Endochondral Bone Growth by Associating with and Inactivating GEP Growth Factor

Bai, X.-H., Wang, D., Kong, L., Zhang, Y., Luan, Y., Kobayashi, T., Kronenberg, H. M., Yu, X., & Liu, C.-J. (2009) · Molecular and Cellular Biology · doi:10.1128/mcb.00056-09 · Cited by 111 · see citing works

Survey of the year 2006 commercial optical biosensor literature

Rich, R. L., & Myszka, D. G. (2007) · Journal of Molecular Recognition · doi:10.1002/jmr.862 · Cited by 111 · see citing works

Chondroitin Sulfate Sulfation Motifs as Putative Biomarkers for Isolation of Articular Cartilage Progenitor Cells

Hayes, A. J., Tudor, D., Nowell, M. A., Caterson, B., & Hughes, C. (2007) · Journal of Histochemistry & Cytochemistry · doi:10.1369/jhc.7a7320.2007 · Cited by 99 · see citing works

The cartilage extracellular matrix as a transient developmental scaffold for growth plate maturation

Melrose, J., Shu, C., Whitelock, J. M., & Lord, M. S. (2016) · Matrix Biology · doi:10.1016/j.matbio.2016.01.008 · Cited by 96 · see citing works

The Decorin Sequence SYIRIADTNIT Binds Collagen Type I

Kalamajski, S., Aspberg, A., & Oldberg, Å. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m700073200 · Cited by 90 · see citing works

Synovial perlecan is required for osteophyte formation in knee osteoarthritis

Kaneko, H., Ishijima, M., Futami, I., Tomikawa-Ichikawa, N., Kosaki, K., SADATSUKI, R., Yamada, Y., Kurosawa, H., Kaneko, K., & Arikawa‐Hirasawa, E. (2013) · Matrix Biology · doi:10.1016/j.matbio.2013.01.004 · Cited by 88 · see citing works

Perlecan modulates VEGF signaling and is essential for vascularization in endochondral bone formation

Ishijima, M., Suzuki, N., Hozumi, K., Matsunobu, T., Kosaki, K., Kaneko, H., Hassell, J. R., Arikawa‐Hirasawa, E., & Yamada, Y. (2012) · Matrix Biology · doi:10.1016/j.matbio.2012.02.006 · Cited by 81 · see citing works

Perlecan, the “jack of all trades” proteoglycan of cartilaginous weight‐bearing connective tissues

Melrose, J., Hayes, A. J., Whitelock, J. M., & Little, C. B. (2008) · BioEssays · doi:10.1002/bies.20748 · Cited by 82 · see citing works

Perlecan and vascular endothelial growth factor-encoding DNA-loaded chitosan scaffolds promote angiogenesis and wound healing

Lord, M. S., Ellis, A. L., Farrugia, B. L., Whitelock, J. M., Grenett, H. E., Li, C., O’Grady, R. L., & DeCarlo, A. A. (2017) · Journal of Controlled Release · doi:10.1016/j.jconrel.2017.02.009 · Cited by 82 · see citing works

Sulfated Glycosaminoglycans Control the Extracellular Trafficking and the Activity of the Metalloprotease Inhibitor TIMP-3

Troeberg, L., Lazenbatt, C., Anower-E-Khuda, M. F., Freeman, C. G., Federov, O., Habuchi, H., Habuchi, O., Kimata, K., & Nagase, H. (2014) · Chemistry & Biology · doi:10.1016/j.chembiol.2014.07.014 · Cited by 79 · see citing works

Heparan and chondroitin sulfate on growth plate perlecan mediate binding and delivery of FGF-2 to FGF receptors

Smith, S. M.-L., West, L. A., Govindraj, P., Zhang, X., Ornitz, D. M., & Hassell, J. R. (2006) · Matrix Biology · doi:10.1016/j.matbio.2006.10.012 · Cited by 79 · see citing works

Heparan sulfate proteoglycans: A GAGgle of skeletal‐hematopoietic regulators

Bungartz, K. D., Antonio, J. D. S., & Jacenko, O. (2008) · Developmental Dynamics · doi:10.1002/dvdy.21593 · Cited by 78 · see citing works

Glycosaminoglycans: Sweet as Sugar Targets for Topical Skin Anti-Aging

Wang, S. T., Neo, B. H., & Betts, R. J. (2021) · Clinical Cosmetic and Investigational Dermatology · doi:10.2147/ccid.s328671 · Cited by 74 · see citing works

Role of Proopiomelanocortin-Derived Peptides and Their Receptors in the Osteoarticular System: From Basic to Translational Research

Böhm, M., & Grässel, S. (2012) · Endocrine Reviews · doi:10.1210/er.2011-1016 · Cited by 73 · see citing works

Reduced perlecan in mice results in chondrodysplasia resembling Schwartz–Jampel syndrome

Bungartz, K. D., Sasaki, T., Aszódi, A., & Jacenko, O. (2007) · Human Molecular Genetics · doi:10.1093/hmg/ddl484 · Cited by 72 · see citing works

Glycosaminoglycan and Proteoglycan‐Based Biomaterials: Current Trends and Future Perspectives

Rnjak‐Kovacina, J., Tang, F., Whitelock, J. M., & Lord, M. S. (2017) · Advanced Healthcare Materials · doi:10.1002/adhm.201701042 · Cited by 72 · see citing works

Perlecan, a modular instructive proteoglycan with diverse functional properties

Melrose, J. (2020) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2020.105849 · Cited by 69 · see citing works

The multifaceted roles of perlecan in fibrosis

Lord, M. S., Tang, F., Rnjak‐Kovacina, J., Smith, J. G. W., Melrose, J., & Whitelock, J. M. (2018) · Matrix Biology · doi:10.1016/j.matbio.2018.02.013 · Cited by 63 · see citing works

The proteoglycan Trol controls the architecture of the extracellular matrix and balances proliferation and differentiation of blood progenitors in the Drosophila lymph gland

Grigorian, M., Liu, T., Banerjee, U. K., & Hartenstein, V. (2013) · Developmental Biology · doi:10.1016/j.ydbio.2013.03.007 · Cited by 63 · see citing works

Structure and function of ECM-inspired composite collagen type I scaffolds

Stamov, D. R., & Pompe, W. (2012) · Soft Matter · doi:10.1039/c2sm26134k · Cited by 62 · see citing works

Osteomodulin regulates diameter and alters shape of collagen fibrils

Tashima, T., Nagatoishi, S., Sagara, H., Ohnuma, S., & Tsumoto, K. (2015) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2015.05.053 · Cited by 57 · see citing works

Knockdown of the pericellular matrix molecule perlecan lowers in situ cell and matrix stiffness in developing cartilage

Xu, X., Li, Z., Leng, Y., Neu, C. P., & Calve, S. (2016) · Developmental Biology · doi:10.1016/j.ydbio.2016.08.029 · Cited by 55 · see citing works

Biodiversity of CS–proteoglycan sulphation motifs: chemical messenger recognition modules with roles in information transfer, control of cellular behaviour and tissue morphogenesis

Hayes, A. J., Sugahara, K., Farrugia, B. L., Whitelock, J. M., Caterson, B., & Melrose, J. (2018) · Biochemical Journal · doi:10.1042/bcj20170820 · Cited by 52 · see citing works

Extracellular Matrix and Developing Growth Plate

Myllyharju, J. (2014) · Current Osteoporosis Reports · doi:10.1007/s11914-014-0232-1 · Cited by 50 · see citing works

Alteration of proteoglycan sulfation affects bone growth and remodeling

Gualeni, B., de Vernejoul, M. C., Morieux, C., Leonardis, F. D., Franchi, M., Monti, L., Forlino, A., Houillier, P., Rossi, A., & Geoffroy, V. (2013) · Bone · doi:10.1016/j.bone.2013.01.036 · Cited by 48 · see citing works

Genome‐wide SNP association–based localization of a dwarfism gene in Friesian dwarf horses

Orr, N., Back, W., Gu, J., Leegwater, P. A. J., Govindarajan, P., Conroy, J., Ducro, B. J., van Arendonk, J. A. M., MacHugh, D. E., Ennis, S., et al. (2010) · Animal Genetics · doi:10.1111/j.1365-2052.2010.02091.x · Cited by 48 · see citing works

Molecular composition of GAG-collagen I multilayers affects remodeling of terminal layers and osteogenic differentiation of adipose-derived stem cells

Zhao, M., Altankov, G., Hohmann, U., Bennett, M., Salmerón‐Sánchez, M., Dehghani, F., & Groth, T. (2016) · Acta Biomaterialia · doi:10.1016/j.actbio.2016.05.023 · Cited by 47 · see citing works

The molecular structure of human tissue type XV presents a unique conformation among the collagens

Myers, J. C., Amenta, P. S., Dion, A. S., Sciancalepore, J. P., Nagaswami, C., Weisel, J. W., & Yurchenco, P. D. (2007) · Biochemical Journal · doi:10.1042/bj20070201 · Cited by 46 · see citing works

Transcriptome analysis of skin fibroblasts with dominant negative COL3A1 mutations provides molecular insights into the etiopathology of vascular Ehlers-Danlos syndrome

Chiarelli, N., Carini, G., Zoppi, N., Ritelli, M., & Colombi, M. (2018) · PLOS ONE · doi:10.1371/journal.pone.0191220 · Cited by 45 · see citing works

Phase 1 Clinical Study of siRNA Targeting Carbohydrate Sulphotransferase 15 in Crohn’s Disease Patients with Active Mucosal Lesions

Suzuki, K., Yokoyama, J., Kawauchi, Y., Honda, Y., Sato, H., Aoyagi, Y., Terai, S., Okazaki, K., Suzuki, Y., Sameshima, Y., et al. (2016) · Journal of Crohn s and Colitis · doi:10.1093/ecco-jcc/jjw143 · Cited by 43 · see citing works

The binding capacity of α1β1-, α2β1- and α10β1-integrins depends on non-collagenous surface macromolecules rather than the collagens in cartilage fibrils

Woltersdorf, C., Bonk, M., Leitinger, B., Huhtala, M. T., Käpylä, J., Heino, J., Girol, C. G., Niland, S., Eble, J. A., Brückner, P., et al. (2017) · Matrix Biology · doi:10.1016/j.matbio.2017.02.001 · Cited by 40 · see citing works

Novel Sulfated Octa- and Decasaccharides from Squid Cartilage Chondroitin Sulfate E: Sequencing and Application for Determination of the Epitope Structure of the Monoclonal Antibody MO-225

Deepa, S. S., Kalayanamitra, K., Ito, Y., Kongtawelert, P., Fukui, S., Yamada, S., Mikami, T., & Sugahara, K. (2007) · Biochemistry · doi:10.1021/bi602374m · Cited by 40 · see citing works

Insights in the etiopathology of galactosyltransferase II (GalT-II) deficiency from transcriptome-wide expression profiling of skin fibroblasts of two sisters with compound heterozygosity for two novel B3GALT6 mutations

Ritelli, M., Chiarelli, N., Zoppi, N., Dordoni, C., Quinzani, S., Traversa, M., Venturini, M., Calzavara-Pinton, P., & Colombi, M. (2015) · Molecular Genetics and Metabolism Reports · doi:10.1016/j.ymgmr.2014.11.005 · Cited by 37 · see citing works

Heparan sulfate proteoglycans in healthy and diseased systems

Whitelock, J. M., & Melrose, J. (2011) · WIREs Systems Biology and Medicine · doi:10.1002/wsbm.149 · Cited by 35 · see citing works

The Tyrosine Sulfate Domain of Fibromodulin Binds Collagen and Enhances Fibril Formation

Tillgren, V., Mörgelin, M., Önnerfjord, P., Kalamajski, S., & Aspberg, A. (2016) · Journal of Biological Chemistry · doi:10.1074/jbc.m116.730325 · Cited by 33 · see citing works

The localisation of inflammatory cells and expression of associated proteoglycans in response to implanted chitosan

Farrugia, B. L., Whitelock, J. M., Jung, M., McGrath, B., O’Grady, R. L., McCarthy, S. J., & Lord, M. S. (2013) · Biomaterials · doi:10.1016/j.biomaterials.2013.10.068 · Cited by 32 · see citing works

HS, an Ancient Molecular Recognition and Information Storage Glycosaminoglycan, Equips HS-Proteoglycans with Diverse Matrix and Cell-Interactive Properties Operative in Tissue Development and Tissue Function in Health and Disease

Hayes, A. J., & Melrose, J. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24021148 · Cited by 31 · see citing works

N-acetylcysteine treatment ameliorates the skeletal phenotype of a mouse model of diastrophic dysplasia

Monti, L., Paganini, C., Lecci, S., Leonardis, F. D., Haÿ, E., Cohen-Solal, M. E., Villani, S., Superti‐Furga, A., Tenni, R., Forlino, A., et al. (2015) · Human Molecular Genetics · doi:10.1093/hmg/ddv289 · Cited by 29 · see citing works

Synthesis of thiolated glycosaminoglycans and grafting to solid surfaces

Köwitsch, A., Abreu, M. J., Chhalotre, A., Hielscher, M., Fischer, S., Mäder, K., & Groth, T. (2014) · Carbohydrate Polymers · doi:10.1016/j.carbpol.2014.08.027 · Cited by 29 · see citing works

Chemical synthesis of human syndecan-4 glycopeptide bearing O-, N-sulfation and multiple aspartic acids for probing impacts of the glycan chain and the core peptide on biological functions

Yang, W., Eken, Y., Zhang, J., Cole, L., Ramadan, S., Xu, Y., Zhang, Z., Liu, J., Wilson, A. K., & Huang, X. (2020) · Chemical Science · doi:10.1039/d0sc01140a · Cited by 29 · see citing works

Chondroitin sulfate cluster of epiphycan from salmon nasal cartilage defines binding specificity to collagens

Tatara, Y., Kakizaki, I., Suto, S., Ishioka, H., Negishi, M., & Endo, M. (2014) · Glycobiology · doi:10.1093/glycob/cwu186 · Cited by 29 · see citing works

Regulation of FGF-2, FGF-18 and Transcription Factor Activity by Perlecan in the Maturational Development of Transitional Rudiment and Growth Plate Cartilages and in the Maintenance of Permanent Cartilage Homeostasis

Hayes, A. J., Whitelock, J. M., & Melrose, J. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23041934 · Cited by 27 · see citing works

Chondroitin Sulfate, Dermatan Sulfate, and Hyaluronic Acid Differentially Modify the Biophysical Properties of Collagen-Based Hydrogels

Cortes-Medina, M. G., Bushman, A., Beshay, P. E., Adorno, J. J., Menyhert, M. M., Hildebrand, R. M., Agarwal, S., Avendano, A., Friedman, A. K., & Song, J. W. (2023) · Acta Biomaterialia · doi:10.1016/j.actbio.2023.12.018 · Cited by 26 · see citing works

Recombinant Extracellular Matrix Protein Fragments Support Human Embryonic Stem Cell Chondrogenesis

Cheng, A., Cain, S. A., Tian, P., Baldwin, A. K., Uppanan, P., Kielty, C. M., & Kimber, S. J. (2017) · Tissue Engineering Part A · doi:10.1089/ten.tea.2017.0285 · Cited by 26 · see citing works

Aggrecan governs intervertebral discs development by providing critical mechanical cues of the extracellular matrix

Empere, M., Wang, X., Prein, C., Aspberg, A., Moser, M., Oohashi, T., Clausen‐Schaumann, H., Aszódi, A., & Alberton, P. (2023) · Frontiers in Bioengineering and Biotechnology · doi:10.3389/fbioe.2023.1128587 · Cited by 25 · see citing works

Concise Review: Stem/Progenitor Cell Proteoglycans Decorated with 7-D-4, 4-C-3, and 3-B-3(-) Chondroitin Sulfate Motifs Are Morphogenetic Markers of Tissue Development

Hayes, A. J., Smith, S. M., Caterson, B., & Melrose, J. (2018) · Stem Cells · doi:10.1002/stem.2860 · Cited by 25 · see citing works

Novel roles of glycosaminoglycans in the degradation of type I collagen by cathepsin K

Tatara, Y., Suto, S., & Itoh, K. (2017) · Glycobiology · doi:10.1093/glycob/cwx083 · Cited by 24 · see citing works

Physicochemical characterization and self-assembly of human amniotic membrane and umbilical cord collagen: A comparative study

Gunasekaran, D., Thada, R., Jeyakumar, G. F. S., Manimegalai, N. P., Shanmugam, G., & Sivagnanam, U. T. (2020) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2020.10.107 · Cited by 22 · see citing works

Perlecan Knockdown Significantly Alters Extracellular Matrix Composition and Organization During Cartilage Development

Ocken, A. R., Ku, M., Kinzer‐Ursem, T. L., & Calve, S. (2020) · Molecular & Cellular Proteomics · doi:10.1074/mcp.ra120.001998 · Cited by 22 · see citing works

Regulation of the collagen IV network by the basement membrane protein perlecan is crucial for squamous epithelial cell morphogenesis and organ architecture

Bonche, R., Smolen, P., Chessel, A., Boisivon, S., Pisano, S., Voigt, A., Schaub, S., Thérond, P. P., & Pizette, S. (2022) · Matrix Biology · doi:10.1016/j.matbio.2022.10.004 · Cited by 20 · see citing works

Impact of perlecan, a core component of basement membrane, on regeneration of cartilaginous tissues

Gao, G., Chen, S., Pei, Y. A., & Pei, M. (2021) · Acta Biomaterialia · doi:10.1016/j.actbio.2021.08.032 · Cited by 20 · see citing works

Sulfation Patterns and the Amounts of Chondroitin Sulfate in the Diamond Squid,Thysanoteuthis rhombus

Tamura, J., ARIMA, K., IMAZU, A., Tsutsumishita-Nakai, N., FUJITA, H., Yamane, M., & Matsumi, Y. (2009) · Bioscience Biotechnology and Biochemistry · doi:10.1271/bbb.90037 · Cited by 19 · see citing works

The cartilage matrix molecule components produced by human foetal cartilage rudiment cells within scaffolds and the role of exogenous growth factors

Chuang, C. Y., Shahin, K., Lord, M. S., Melrose, J., Doran, P. M., & Whitelock, J. M. (2012) · Biomaterials · doi:10.1016/j.biomaterials.2012.02.032 · Cited by 17 · see citing works

Effect of microenvironment on adhesion and differentiation of murine C3H10T1/2 cells cultured on multilayers containing collagen I and glycosaminoglycans

Zhao, M., Anouz, R., & Groth, T. (2020) · Journal of Tissue Engineering · doi:10.1177/2041731420940560 · Cited by 16 · see citing works

3D distribution of perlecan within intervertebral disc chondrons suggests novel regulatory roles for this multifunctional modular heparan sulphate proteoglycan

Hayes, A. J., & Melrose, J. (2021) · European Cells and Materials · doi:10.22203/ecm.v041a06 · Cited by 16 · see citing works

New endoscopic approach of anti-fibrotic therapy for inflammatory bowel disease

Suzuki, K., & Yoneyama, H. (2017) · Annals of Translational Medicine · doi:10.21037/atm.2017.03.65 · Cited by 14 · see citing works

Studies on the molecular significance in the interaction of bilirubin with collagen

Nagarajan, U., Jayakumar, G. C., Chandrasekaran, B., Jonnalagadda, R. R., Nair, B. U., & Kohsaku, K. (2013) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2013.08.001 · Cited by 12 · see citing works

Sil1-deficient fibroblasts generate an aberrant extracellular matrix leading to tendon disorganisation in Marinesco-Sjögren syndrome

Amodei, L., Ruggieri, A. G., Potenza, F., Viele, M., Dufrusine, B., Franciotti, R., Pietrangelo, L., Ardini, M., Stuppia, L., Federici, L., et al. (2024) · Journal of Translational Medicine · doi:10.1186/s12967-024-05582-0 · Cited by 11 · see citing works

Cardinal acuity on the extraction and characterization of soluble collagen from the underutilized abattoir junks for clinical demands

Manimegalai, N. P., Ramanathan, G., Gunasekaran, D., Jeyakumar, G. F. S., & Sivagnanam, U. T. (2022) · Process Biochemistry · doi:10.1016/j.procbio.2022.08.011 · Cited by 9 · see citing works

Second harmonic generation imaging reveals a distinct organization of collagen fibrils in locations associated with cartilage growth

Finnøy, A., Olstad, K., & Lilledahl, M. B. (2016) · Connective Tissue Research · doi:10.1080/03008207.2016.1190348 · Cited by 9 · see citing works

Diverse and multifunctional roles for perlecan (HSPG2) in repair of the intervertebral disc

Melrose, J., & Guilak, F. (2024) · JOR Spine · doi:10.1002/jsp2.1362 · Cited by 7 · see citing works

Probing the influence of SIBLING proteins on collagen-I fibrillogenesis and denaturation

Jiang, C., Zurick, K. M., Qin, C., & Bernards, M. T. (2017) · Connective Tissue Research · doi:10.1080/03008207.2017.1379514 · Cited by 7 · see citing works

Articular cartilage

Heinegård, D. K., Lorenzo, P., Önnerfjord, P., & Saxne, T. (2011) · Elsevier eBooks · doi:10.1016/b978-0-323-06551-1.00008-7 · Cited by 6 · see citing works

Different architectures of collagen fibrils enforce different fibrillogenesis mechanisms

Raspanti, M. (2010) · Journal of Biomedical Science and Engineering · doi:10.4236/jbise.2010.312152 · Cited by 5 · see citing works

Submucosal Injection of the RNA Oligonucleotide GUT-1 in Active Ulcerative Colitis Patients: A Randomized, Double-Blind, Placebo-Controlled Phase 2a Induction Trial

Atreya, R. N., Kühbacher, T., Waldner, M. J., Hirschmann, S., Drvarov, O., Hashem, R. A., Maaser, C., Kucharzik, T. F., Dinter, J., Mertens, J., et al. (2023) · Journal of Crohn s and Colitis · doi:10.1093/ecco-jcc/jjad162 · Cited by 4 · see citing works

Changes in Endocan and Dermatan Sulfate Are Associated with Biomechanical Properties of Abdominal Aortic Wall during Aneurysm Expansion and Rupture

Metschl, S., Bruder, L., Paloschi, V., Jakob, K., Reutersberg, B., Reeps, C., Mäegdefessel, L., Gee, M. W., Eckstein, H., & Pelisek, J. (2022) · Thrombosis and Haemostasis · doi:10.1055/a-1772-0574 · Cited by 3 · see citing works

Properties of Monoclonal Antibodies Recognizing Chondroitin Sulfate E

Watanabe, I. (2022) · Trends in Glycoscience and Glycotechnology · doi:10.4052/tigg.2120.1j · Cited by 3 · see citing works

GELATIN–CHONDROITIN–HYALURONAN TRI-COPOLYMER SCAFFOLD SEEDED WITH DENTAL BUD CELLS FOR ODONTOGENESIS: ANEX VIVOSTUDY ON NUDE MICE

Kuo, T., Lin, H.-C., Hung, A.-T., Yang, K., Lin, H.-F., Tanng, T.-K., Chen, S.-T., & Wang, A. H. ‐. (2010) · Biomedical Engineering Applications Basis and Communications · doi:10.4015/s1016237210002274 · Cited by 2 · see citing works

Review Cartilage homeostasis in health and rheumatic diseases

Goldring, M. B., & Marcu, K. B. (2009) · Cited by 2 · see citing works

Certain bioactive effects of complexes rich in glycosaminoglycans obtained from small sea fish

Ene, M. D., & Olariu, L. (2010) · Cited by 2 · see citing works

Intrinsically Cross‐Linked ECM‐Like Multilayers for BMP‐2 Delivery Promote Osteogenic Differentiation of Cells

Anouz, R., Selekere, T., Hautmann, A., Husteden, C., Menzel, M., Wölk, C., Schmelzer, C. E. H., & Groth, T. (2023) · Advanced Materials Interfaces · doi:10.1002/admi.202201596 · Cited by 2 · see citing works

Add-on multiple submucosal injections of the RNA oligonucleotide GUT-1 to anti-TNF antibody treatment in patients with moderate-to-severe ulcerative colitis: an open-label, proof-of concept study

Suzuki, K., Sameshima, Y., Yokoyama, J., Terai, S., Yoneyama, H., Atreya, R. N., Neurath, M. F., Hibi∥, T., & Asakura, H. (2024) · Inflammation and Regeneration · doi:10.1186/s41232-024-00332-7 · Cited by 2 · see citing works

Use of Chondroitin Sulphate to Aid In Vitro Stem Cell Differentiation

Farrugia, B. L., Hayes, A. J., & Melrose, J. (2021) · Biology of extracellular matrix · doi:10.1007/978-3-030-73453-4_4 · Cited by 2 · see citing works

Chondrodysplasia of Texel sheep.

Sa, P. (2008) · Europe PMC (PubMed Central) · Cited by 2 · see citing works

Properties of Monoclonal Antibodies Recognizing Chondroitin Sulfate E

Watanabe, I. (2022) · Trends in Glycoscience and Glycotechnology · doi:10.4052/tigg.2120.1e · Cited by 1 · see citing works

The proteoglycan perlecan regulates long bone growth through interactions with developmental proteins in the growth plate

Smith, S. M.-L. (2007) · Digital Commons - University of South Florida (University of South Florida)

Do Proteoglycans Mediate Chronic Photoaging?

Oh, J., & Chung, J. H. (2019) · Royal Society of Chemistry eBooks · doi:10.1039/9781788015981-00231

Activation of Discoidin Domain Receptors by collagen VI and collagen I fibrils

Gavriilidou, D. (2017) · Spiral (Imperial College London) · doi:10.25560/72245

Tailoring the Microenvironment of Cells Towards Osteogenic Differentiation Using Multilayers of Glycosaminoglycans and Growth Factor Immobilization

Anouz, R., Zhao, M., Gong, F., & Groth, T. (2023) · Engineering materials · doi:10.1007/978-3-031-17269-4_1

Additional file 4 of Sil1-deficient fibroblasts generate an aberrant extracellular matrix leading to tendon disorganisation in Marinesco-Sjögren syndrome

Amodei, L., Ruggieri, A. G., Potenza, F., Viele, M., Dufrusine, B., Franciotti, R., Pietrangelo, L., Ardini, M., Stuppia, L., Federici, L., et al. (2024) · Figshare · doi:10.6084/m9.figshare.26942757

Additional file 3 of Sil1-deficient fibroblasts generate an aberrant extracellular matrix leading to tendon disorganisation in Marinesco-Sjögren syndrome

Amodei, L., Ruggieri, A. G., Potenza, F., Viele, M., Dufrusine, B., Franciotti, R., Pietrangelo, L., Ardini, M., Stuppia, L., Federici, L., et al. (2024) · Figshare · doi:10.6084/m9.figshare.26942754

Additional file 7 of Sil1-deficient fibroblasts generate an aberrant extracellular matrix leading to tendon disorganisation in Marinesco-Sjögren syndrome

Amodei, L., Ruggieri, A. G., Potenza, F., Viele, M., Dufrusine, B., Franciotti, R., Pietrangelo, L., Ardini, M., Stuppia, L., Federici, L., et al. (2024) · Figshare · doi:10.6084/m9.figshare.26942766

Additional file 5 of Sil1-deficient fibroblasts generate an aberrant extracellular matrix leading to tendon disorganisation in Marinesco-Sjögren syndrome

Amodei, L., Ruggieri, A. G., Potenza, F., Viele, M., Dufrusine, B., Franciotti, R., Pietrangelo, L., Ardini, M., Stuppia, L., Federici, L., et al. (2024) · Figshare · doi:10.6084/m9.figshare.26942760

Chondroitin sulfate perlecan enhances collagen fibril formation - Implications for perlecan chondrodysplasias

Kvist, A., Johnson, A. E., Morgelin, M., Gustafsson, E., Bengtsson, E., Lindblom, K., Aszodi, A., Fässler, R., Sasaki, T., Timpl, R., et al. (2006) · Max Planck Institute for Plasma Physics

Cartilage homeostasis: Modulation of cells and extracelllar matrix assembly

Johnson, A. E. (2004) · Lund University Publications (Lund University)

Role of Collagen Type II and Perlecan in Skeletal Development

Gustafsson, E., Aszódi, A., Ortéga, N., Hunziker, E. B., Denker, H., Werb, Z., & Fässler, R. (2003) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.2003.tb03217.x · Cited by 56 · see citing works

Perlecan Knockdown Significantly Alters Extracellular Matrix Composition and Organization During Cartilage Development

Ocken, A. R., Ku, M., Kinzer‐Ursem, T. L., & Calve, S. (2020) · Molecular & Cellular Proteomics · doi:10.1074/mcp.ra120.001998 · Cited by 22 · see citing works

Basement membrane components in the chondrocyte extracellular matrix

Kvist, A. J. (2007) · Lund University Publications (Lund University)