Genetic diseases of connective tissues: cellular and extracellular effects of ECM mutations

Signal integration in the endoplasmic reticulum unfolded protein response

Ron, D., & Walter, P. (2007) · Nature reviews. Molecular cell biology · doi:10.1038/nrm2199 · Cited by 6,499 · see citing works

Losartan, an AT1 Antagonist, Prevents Aortic Aneurysm in a Mouse Model of Marfan Syndrome

Habashi, J. P., Judge, D. P., Holm, T. M., Cohn, R. D., Loeys, B. L., Cooper, T. K., Myers, L., Klein, E. C., Liu, G., Calvi, C., et al. (2006) · Science · doi:10.1126/science.1124287 · Cited by 1,794 · see citing works

A Selective Inhibitor of eIF2α Dephosphorylation Protects Cells from ER Stress

Boyce, M., Bryant, K. F., Jousse, C., Long, K., Harding, H. P., Scheuner, D. L., Kaufman, R. J., Ma, D., Coen, D. M., Ron, D., et al. (2005) · Science · doi:10.1126/science.1101902 · Cited by 1,403 · see citing works

ERAD: the long road to destruction

Meusser, B., Hirsch, C., Jarosch, E., & Sommer, T. (2005) · Nature Cell Biology · doi:10.1038/ncb0805-766 · Cited by 1,221 · see citing works

Collagens, modifying enzymes and their mutations in humans, flies and worms

Myllyharju, J. (2003) · Trends in Genetics · doi:10.1016/j.tig.2003.11.004 · Cited by 1,179 · see citing works

Of Extracellular Matrix, Scaffolds, and Signaling: Tissue Architecture Regulates Development, Homeostasis, and Cancer

Nelson, C. M., & Bissell, M. J. (2006) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev.cellbio.22.010305.104315 · Cited by 1,121 · see citing works

Potential therapeutic applications of autophagy

Rubinsztein, D. C., Gestwicki, J. E., Murphy, L. O., & Klionsky, D. J. (2007) · Nature Reviews Drug Discovery · doi:10.1038/nrd2272 · Cited by 1,004 · see citing works

Nonsense-mediated mRNA decayin health and disease

Frischmeyer, P. A. (1999) · Human Molecular Genetics · doi:10.1093/hmg/8.10.1893 · Cited by 991 · see citing works

The endoplasmic reticulum and the unfolded protein response

Malhotra, J. D., & Kaufman, R. J. (2007) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2007.09.003 · Cited by 984 · see citing works

Endoplasmic Reticulum Stress Signaling in Disease

Marciniak, S. J., & Ron, D. (2006) · Physiological Reviews · doi:10.1152/physrev.00015.2006 · Cited by 948 · see citing works

Connective Tissue and Its Heritable Disorders

Heinegård, D., Aspberg, A., Franzén, A., & Lorenzo, P. (2002) · Wiley eBooks · doi:10.1002/0471221929 · Cited by 946 · see citing works

Collagens at a glance

Kadler, K., Baldock, C., Bella, J., & Boot-Handford, R. (2007) · Journal of Cell Science · doi:10.1242/jcs.03453 · Cited by 903 · see citing works

Angiotensin II Blockade and Aortic-Root Dilation in Marfan's Syndrome

Brooke, B. S., Habashi, J. P., Judge, D. P., Patel, N. D., Loeys, B., & Dietz, H. C. (2008) · New England Journal of Medicine · doi:10.1056/nejmoa0706585 · Cited by 840 · see citing works

Endoplasmic reticulum stress in disease pathogenesis.

Lin, J. H., Walter, P., & Yen, T. S. B. (2008) · Annual Review of Pathology · doi:10.1146/annurev.pathmechdis.3.121806.151434 · Cited by 830 · see citing works

Novel targets for Huntington's disease in an mTOR-independent autophagy pathway

Williams, A., Sarkar, S., Cuddon, P., Ttofi, E. K., Saiki, S., Siddiqi, F. H., Jahreiss, L., Fleming, A., Pask, D., Goldsmith, P., et al. (2008) · Nature Chemical Biology · doi:10.1038/nchembio.79 · Cited by 800 · see citing works

Therapeutic approaches to protein-misfolding diseases

Cohen, F. E., & Kelly, J. W. (2003) · Nature · doi:10.1038/nature02265 · Cited by 792 · see citing works

Extracellular control of TGFβ signalling in vascular development and disease

ten Dijke, P., & Arthur, H. M. (2007) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2262 · Cited by 777 · see citing works

Consortium for osteogenesis imperfecta mutations in the helical domain of type I collagen: regions rich in lethal mutations align with collagen binding sites for integrins and proteoglycans

Marini, J. C., Forlino, A., Cabral, W. A., Barnes, A. M., Antonio, J. D. S., Milgrom, S. A., Hyland, J. C., Körkkö, J., Prockop, D. J., Paepe, A. D., et al. (2006) · Human Mutation · doi:10.1002/humu.20429 · Cited by 764 · see citing works

Procollagen trafficking, processing and fibrillogenesis

Canty, E. G., & Kadler, K. (2005) · Journal of Cell Science · doi:10.1242/jcs.01731 · Cited by 759 · see citing works

Endoplasmic Reticulum Chaperone Protein GRP78 Protects Cells from Apoptosis Induced by Topoisomerase Inhibitors

Reddy, R. K., Mao, C., Baumeister, P., Austin, R. C., Kaufman, R. J., & Lee, A. S. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m212328200 · Cited by 695 · see citing works

The Biology of the Small Leucine-rich Proteoglycans

Iozzo, R. V. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.27.18843 · Cited by 646 · see citing works

Small molecules enhance autophagy and reduce toxicity in Huntington's disease models

Sarkar, S., Perlstein, E. O., Imarisio, S., Pineau, S., Cordenier, A., Maglathlin, R. L., Webster, J. A., Lewis, T. A., O’Kane, C. J., Schreiber, S. L., et al. (2007) · Nature Chemical Biology · doi:10.1038/nchembio883 · Cited by 596 · see citing works

Quality control of eukaryotic mRNA: safeguarding cells from abnormal mRNA functionPreprint

Isken, O., & Maquat, L. E. (2007) · Genes & Development · doi:10.1101/gad.1566807 · Cited by 584 · see citing works

The unfolded protein response

Zhang, K., & Kaufman, R. J. (2006) · Neurology · doi:10.1212/01.wnl.0000192306.98198.ec · Cited by 580 · see citing works

Intracellular Signaling by the Unfolded Protein Response

Bernales, S., Papa, F. R., & Walter, P. (2006) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev.cellbio.21.122303.120200 · Cited by 543 · see citing works

CRTAP is required for prolyl 3- hydroxylation and mutations cause recessive osteogenesis imperfecta.

Morello, R., Bertin, T., Chen, Y., Hicks, J., Tonachini, L., Monticone, M., Castagnola, P., Rauch, F., Glorieux, F., Vranka, J., et al. (2006) · Cell · doi:10.1016/j.cell.2006.08.039 · Cited by 519 · see citing works

Mitochondrial dysfunction and apoptosis in myopathic mice with collagen VI deficiency

Irwin, W., Bergamin, N., Sabatelli, P., Reggiani, C., Megighian, A., Merlini, L., Braghetta, P., Columbaro, M., Volpin, D., Bressan, G. M., et al. (2003) · Nature Genetics · doi:10.1038/ng1270 · Cited by 509 · see citing works

Clinical and molecular genetics of Stickler syndrome

Snead, M. P., & Yates, J. R. W. (1999) · Journal of Medical Genetics · doi:10.1136/jmg.36.5.353 · Cited by 448 · see citing works

Connective tissue and its heritable disorders : molecular, genetic, and medical aspects

Royce, P. M., & Steinmann, B. (1993) · Cited by 440 · see citing works

Endoplasmic reticulum stress in health and disease

Zhao, L., & Ackerman, S. L. (2006) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2006.06.005 · Cited by 440 · see citing works

The collagen family members as cell adhesion proteins

Heino, J. (2007) · BioEssays · doi:10.1002/bies.20636 · Cited by 439 · see citing works

The molecular genetics of Marfan syndrome and related disorders

Robinson, P. N., Arteaga‐Solis, E., Baldock, C., Collod‐Béroud, G., Booms, P., Paepe, A. D., Dietz, H. C., Guo, G., Handford, P. A., Judge, D. P., et al. (2006) · Journal of Medical Genetics · doi:10.1136/jmg.2005.039669 · Cited by 430 · see citing works

Nonsense-mediated mRNA decay modulates clinical outcome of genetic disease

Khajavi, M., Inoue, K., & Lupski, J. R. (2006) · European Journal of Human Genetics · doi:10.1038/sj.ejhg.5201649 · Cited by 420 · see citing works

That which does not kill me makes me stronger: adapting to chronic ER stress

Rutkowski, D. T., & Kaufman, R. J. (2007) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2007.09.003 · Cited by 398 · see citing works

Sorting, recognition and activation of the misfolded protein degradation pathways through macroautophagy and the proteasome

Ding, W., & Yin, X.-M. (2008) · Autophagy · doi:10.4161/auto.5190 · Cited by 383 · see citing works

Defective pro alpha 2(I) collagen synthesis in a recessive mutation in mice: a model of human osteogenesis imperfecta.

Chipman, S. D., Sweet, H. O., McBride, D. J., Davisson, M. T., Marks, S. C., Shuldiner, A. R., WENSTRUP, R. J., Rowe, D. W., & Shapiro, J. R. (1993) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.90.5.1701 · Cited by 344 · see citing works

Integrins in regulation of tissue development and function

Danen, E. H. J., & Sonnenberg, A. (2003) · The Journal of Pathology · doi:10.1002/path.1416 · Cited by 318 · see citing works

The human type I collagen mutation database

Dalgleish, R. (1997) · Nucleic Acids Research · doi:10.1093/nar/25.1.181 · Cited by 315 · see citing works

Pseudoachondroplasia and multiple epiphyseal dysplasia: Mutation review, molecular interactions, and genotype to phenotype correlations

Briggs, M. D., & Chapman, K. L. (2002) · Human Mutation · doi:10.1002/humu.10066 · Cited by 290 · 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

Matricellular proteins: Extracellular modulators of bone development, remodeling, and regeneration

Alford, A. I., & Hankenson, K. D. (2006) · Bone · doi:10.1016/j.bone.2005.11.017 · Cited by 265 · see citing works

Pharmacologic Rescue of Conformationally‐Defective Proteins: Implications for the Treatment of Human Disease

Ulloa‐Aguirre, A., Janovick, J. A., Brothers, S. P., & Conn, P. M. (2004) · Traffic · doi:10.1111/j.1600-0854.2004.00232.x · Cited by 252 · see citing works

A molecular chaperone inducer protects neurons from ER stress

Kudo, T., Kanemoto, S., Hara, H., Morimoto, N., Morihara, T., Kimura, R., Tabira, T., Imaizumi, K., & Takeda, M. (2008) · Cell Death & Differentiation · doi:10.1038/sj.cdd.4402276 · Cited by 250 · see citing works

Chemical Chaperones: A Pharmacological Strategy for Disorders of Protein Folding and Trafficking

Perlmutter, D. H. (2002) · Pediatric Research · doi:10.1203/00006450-200212000-00004 · Cited by 250 · see citing works

Cartilage Oligomeric Matrix Protein Interacts with Type IX Collagen, and Disruptions to These Interactions Identify a Pathogenetic Mechanism in a Bone Dysplasia Family

Holden, P. K., Meadows, R. S., Chapman, K. L., Grant, M. E., Kadler, K. E., & Briggs, M. D. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m009507200 · Cited by 222 · see citing works

Collagens and Cartilage Matrix Homeostasis

Eyre, D. R. (2004) · Clinical Orthopaedics and Related Research · doi:10.1097/01.blo.0000144855.48640.b9 · Cited by 222 · see citing works

Endoplasmic Reticulum Stress: A New Pathway to Induce Autophagy

Yorimitsu, T., & Klionsky, D. J. (2007) · Autophagy · doi:10.4161/auto.3653 · Cited by 215 · see citing works

Versatility of the Endoplasmic Reticulum Protein Folding Factory

van Anken, E., & Braakman, I. (2005) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.1080/10409230591008161 · Cited by 214 · see citing works

CRTAPandLEPRE1mutations in recessive osteogenesis imperfecta

Baldridge, D., Schwarze, U., Morello, R., Lennington, J., Bertin, T., Pace, J. M., Pepin, M. G., Weis, M., Eyre, D. R., Walsh, J., et al. (2008) · Human Mutation · doi:10.1002/humu.20799 · Cited by 208 · see citing works

Cyclosporin A corrects mitochondrial dysfunction and muscle apoptosis in patients with collagen VI myopathies

Merlini, L., Angelin, A., Tiepolo, T., Braghetta, P., Sabatelli, P., Zamparelli, A., Ferlini, A., Maraldi, N. M., Bonaldo, P., & Bernardi, P. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0800962105 · Cited by 207 · see citing works

Molecular Recognition in the Assembly of Collagens: Terminal Noncollagenous Domains Are Key Recognition Modules in the Formation of Triple Helical Protomers

Khoshnoodi, J., Cartailler, J., Alvares, K., Veis, A., & Hudson, B. G. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.r600025200 · Cited by 205 · see citing works

Prolyl 3-Hydroxylase 1, Enzyme Characterization and Identification of a Novel Family of Enzymes

Vranka, J. A., Sakai, L. Y., & Bächinger, H. P. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m312807200 · Cited by 200 · see citing works

Abnormal Compartmentalization of Cartilage Matrix Components in Mice Lacking Collagen X: Implications for Function

Kwan, K. M., Pang, M. K. M., Zhou, S. X., Cowan, S., Kong, R. Y. C., Pfordte, T., Olsen, B. R., Sillence, D. O., Tam, P., & Cheah, K. S. E. (1997) · The Journal of Cell Biology · doi:10.1083/jcb.136.2.459 · Cited by 200 · see citing works

Connective tissue and its heritable disorders. Molecular, genetic and medical aspects

Olavesen, A. H. (1993) · FEBS Letters · doi:10.1016/0014-5793(93)80460-c · Cited by 198 · see citing works

Erratum: Integrins in regulation of tissue development and function. J Pathol ; 200: 471–480

Danen, E. H. J., & Sonnenberg, A. (2003) · The Journal of Pathology · doi:10.1002/path.1472 · Cited by 193 · see citing works

Surviving Endoplasmic Reticulum Stress Is Coupled to Altered Chondrocyte Differentiation and Function

Tsang, K. Y., Chan, D. T.-M., Cheslett, D., Chan, W. C. W., So, C. L., Melhado, I. G., Chan, T. W. Y., Kwan, K. M., Hunziker, E. B., Yamada, Y., et al. (2007) · PLoS Biology · doi:10.1371/journal.pbio.0050044 · Cited by 188 · see citing works

Phenotypic and molecular characterization of Bruck syndrome (osteogenesis imperfecta with contractures of the large joints) caused by a recessive mutation in PLOD2

Leuchter, R. H., Alanay, Y., Bank, R. A., Campos‐Xavier, B., Zankl, A., Superti‐Furga, A., & Bonafé, L. (2004) · American Journal of Medical Genetics Part A · doi:10.1002/ajmg.a.30231 · Cited by 185 · see citing works

What Mouse Mutants Teach Us About Extracellular Matrix Function

Aszódi, A., Legate, K. R., Nakchbandi, I. A., & Fässler, R. (2006) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev.cellbio.22.010305.104258 · Cited by 184 · see citing works

Dominant collagen VI mutations are a common cause of Ullrich congenital muscular dystrophy

Baker, N. L. (2004) · Human Molecular Genetics · doi:10.1093/hmg/ddi025 · Cited by 182 · see citing works

Type I Collagen in Hsp47-null Cells Is Aggregated in Endoplasmic Reticulum and Deficient in N-Propeptide Processing and Fibrillogenesis

Ishida, Y., KUBOTA, H. Y., Yamamoto, A., Kitamura, A., Bächinger, H. P., & Nagata, K. (2006) · Molecular Biology of the Cell · doi:10.1091/mbc.e05-11-1065 · Cited by 176 · see citing works

ER Stress-Mediated Apoptosis in a New Mouse Model of Osteogenesis imperfecta

Lisse, T. S., Thiele, F., Fuchs, H., Hans, W., Przemeck, G. K. H., Abe, K., Rathkolb, B., Quintanilla‐Martinez, L., Hoelzlwimmer, G., Helfrich, M., et al. (2008) · PLoS Genetics · doi:10.1371/journal.pgen.0040007 · Cited by 166 · see citing works

Characterization of 18 New Mutations in COL7A1 in Recessive Dystrophic Epidermolysis Bullosa Provides Evidence for Distinct Molecular Mechanisms Underlying Defective Anchoring Fibril Formation

Hovnanian, A., Rochat, A., Bodemer, C., Petit, É., Rivers, C. A., Prost‐Squarcioni, C., Fraitag, S., Christiano, A. M., Uitto, J., Lathrop, M. G., et al. (1997) · The American Journal of Human Genetics · doi:10.1086/515495 · Cited by 165 · see citing works

Small molecule pharmacological chaperones: From thermodynamic stabilization to pharmaceutical drugs

Arakawa, T., Ejima, D., Kita, Y. A., & Tsumoto, K. (2006) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2006.08.012 · Cited by 164 · see citing works

BiP binds type I procollagen pro alpha chains with mutations in the carboxyl-terminal propeptide synthesized by cells from patients with osteogenesis imperfecta.

Chessler, S. D., & Byers, P. H. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)46834-7 · Cited by 155 · see citing works

Mechanotransduction from the ECM to the genome: Are the pieces now in place?

Gieni, R. S., & Hendzel, M. J. (2007) · Journal of Cellular Biochemistry · doi:10.1002/jcb.21364 · Cited by 143 · see citing works

Novel Types of Mutation Responsible for the Dermatosparactic Type of Ehlers–Danlos Syndrome (Type VIIC) and Common Polymorphisms in the ADAMTS2 Gene

Colige, A., Nuytinck, L., Hausser, I., van Essen, A. J., Thiry, M., Herens, C., Adès, L. C., Malfait, F., Paepe, A. D., Franck, P., et al. (2004) · Journal of Investigative Dermatology · doi:10.1111/j.0022-202x.2004.23406.x · Cited by 139 · see citing works

Tissue-specific RNA surveillance? Nonsense-mediated mRNA decay causes collagen X haploinsufficiency in Schmid metaphyseal chondrodysplasia cartilage

Bateman, J. F. (2003) · Human Molecular Genetics · doi:10.1093/hmg/ddg054 · Cited by 139 · see citing works

Osteogenesis imperfecta type I: molecular heterogeneity for COL1A1 null alleles of type I collagen.

Willing, M. C., Deschenes, S. P., Scott, D. A., Byers, P. H., Slayton, R. L., Pitts, S. H. J., Arikat, H., & Roberts, E. J. (1994) · PubMed Central · Cited by 138 · see citing works

Endoplasmic Reticulum-mediated Quality Control of Type I Collagen Production by Cells from Osteogenesis Imperfecta Patients with Mutations in the proα1(I) Chain Carboxyl-terminal Propeptide which Impair Subunit Assembly

Lamandé, S. R., Chessler, S. D., Golub, S. B., Byers, P. H., Chan, C., Cole, W. G., Sillence, D. O., & Bateman, J. F. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.15.8642 · Cited by 135 · see citing works

A Connective Tissue Disorder Caused by Mutations of the Lysyl Hydroxylase 3 Gene

Salo, A. M., Cox, H., Farndon, P. A., Moss, C., Grindulis, H., Risteli, M., Robins, S. P., & Myllylä, R. (2008) · The American Journal of Human Genetics · doi:10.1016/j.ajhg.2008.09.004 · Cited by 135 · see citing works

Potential of mesenchymal stem cell therapy

Dazzi, F., & Horwood, N. J. (2007) · Current Opinion in Oncology · doi:10.1097/cco.0b013e3282f0e116 · Cited by 120 · see citing works

Novel therapeutic strategies for the treatment of protein-misfolding diseases

Rochet, J. (2007) · Expert Reviews in Molecular Medicine · doi:10.1017/s1462399407000385 · Cited by 118 · see citing works

Insight into Schmid Metaphyseal Chondrodysplasia from the Crystal Structure of the Collagen X NC1 Domain Trimer

Bogin, O., Kvansakul, M., Rom, E., Singer, J., Yayon, A., & Hohenester, E. (2002) · Structure · doi:10.1016/s0969-2126(02)00697-4 · Cited by 114 · see citing works

Reduced collagen VI causes Bethlem myopathy: a heterozygous COL6A1 nonsense mutation results in mRNA decay and functional haploinsufficiency

Lamandé, S. R. (1998) · Human Molecular Genetics · doi:10.1093/hmg/7.6.981 · Cited by 101 · see citing works

Proteoglycans: key partners in bone cell biology

Lamoureux, F., Baud’huin, M., Duplomb, L., Heymann, D., & Rédiní, F. (2007) · BioEssays · doi:10.1002/bies.20612 · Cited by 100 · see citing works

Reduced cell proliferation and increased apoptosis are significant pathological mechanisms in a murine model of mild pseudoachondroplasia resulting from a mutation in the C-terminal domain of COMP

Piróg, K. A., Meadows, R. S., Knowles, L., Heinegård, D. K., Thornton, D. J., Kadler, K. E., Boot-Handford, R., & Briggs, M. D. (2007) · Human Molecular Genetics · doi:10.1093/hmg/ddm155 · Cited by 97 · see citing works

Structural Heterogeneity of Type I Collagen Triple Helix and Its Role in Osteogenesis Imperfecta

Makareeva, E., Mertz, E. L., Kuznetsova, N. V., Sutter, M. B., DeRidder, A. M., Cabral, W. A., Barnes, A. M., McBride, D. J., Marini, J. C., & Leikin, S. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m705773200 · Cited by 94 · see citing works

Integration of splicing, transport and translation to achieve mRNA quality control by the nonsense-mediated decay pathway.

Schell, T., Kulozik, A. E., & Hentze, M. W. (2002) · Genome biology · doi:10.1186/gb-2002-3-3-reviews1006 · Cited by 93 · see citing works

Pathogenetics of the Human SLC26 Transporters

Dawson, P. A., & Markovich, D. (2005) · Current Medicinal Chemistry · doi:10.2174/0929867053363144 · Cited by 91 · see citing works

Messenger RNA Surveillance: Neutralizing Natural Nonsense

Weischenfeldt, J., Lykke‐Andersen, J., & Porse, B. T. (2005) · Current Biology · doi:10.1016/j.cub.2005.07.002 · Cited by 89 · see citing works

Calreticulin, PDI, Grp94 and BiP chaperone proteins are associated with retained COMP in pseudoachondroplasia chondrocytes

Hecht, J. T., Hayes, E., Snuggs, M. B., Decker, G. L., Montufar‐Solis, D., Doege, K. J., Mwalle, F., Poole, R., Stevens, J. W., & Duke, P. J. (2001) · Matrix Biology · doi:10.1016/s0945-053x(01)00136-6 · Cited by 89 · see citing works

Decreased chondrocyte proliferation and dysregulated apoptosis in the cartilage growth plate are key features of a murine model of epiphyseal dysplasia caused by a matn3 mutation

Leighton, M., Nundlall, S., Starborg, T., Meadows, R. S., Suleman, F. E., Knowles, L., Wagener, R., Thornton, D. J., Kadler, K. E., Boot-Handford, R., et al. (2007) · Human Molecular Genetics · doi:10.1093/hmg/ddm121 · Cited by 82 · see citing works

Macromolecular Specificity of Collagen Fibrillogenesis

Hansen, U. J., & Brückner, P. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m304325200 · Cited by 81 · see citing works

Proteasomal Degradation of Unassembled Mutant Type I Collagen Pro-α1(I) Chains

Fitzgerald, J., Lamandé, S. R., & Bateman, J. F. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.39.27392 · Cited by 81 · see citing works

Selective intracellular retention of extracellular matrix proteins and chaperones associated with pseudoachondroplasia

浅野, 弦., 矢野, 孝., 平尾, 和., 田中, 優., Corson, G., Sussman, M., Horton, W. A., Maddox, K., Sakai, L., & Bächinger, H. P. (2001) · Matrix Biology · doi:10.1016/s0945-053x(01)00148-2 · Cited by 79 · see citing works

Chondrocyte cell death and intracellular distribution of COMP and type IX collagen in the pseudoachondroplasia growth plate

Hecht, J. T., Mäkitie, O., Hayes, E., Haynes, R., Susic, M., Montufar‐Solis, D., Duke, P. J., & Cole, W. G. (2004) · Journal of Orthopaedic Research® · doi:10.1016/j.orthres.2003.11.010 · Cited by 79 · see citing works

Mutations ofCOL10A1 in Schmid metaphyseal chondrodysplasia

Bateman, J. F., Wilson, R., Freddi, S., Lamandé, S. R., & Savarirayan, R. (2005) · Human Mutation · doi:10.1002/humu.20183 · Cited by 79 · see citing works

COL10A1 nonsense and frame-shift mutations have a gain-of-function effect on the growth plate in human and mouse metaphyseal chondrodysplasia type Schmid

Ho, M. S. P., Tsang, K. Y., Lo, R. L. K., Susic, M., Mäkitie, O., Chan, T. W. Y., Ng, V. C. W., Sillence, D. O., Boot-Handford, R., GIBSON, G. J., et al. (2007) · Human Molecular Genetics · doi:10.1093/hmg/ddm067 · Cited by 73 · see citing works

High efficiency of mutation detection in type 1 stickler syndrome using a two-stage approach: vitreoretinal assessment coupled with exon sequencing for screening COL2A1

Richards, A. J., Laidlaw, M., Whittaker, J., Treacy, B., Rai, H., Bearcroft, P. W. P., Baguley, D., Poulson, A. V., Ang, A. J., Scott, J. D., et al. (2006) · Human Mutation · doi:10.1002/humu.20347 · Cited by 73 · see citing works

Collagen VI glycine mutations: Perturbed assembly and a spectrum of clinical severity

Pace, R. A., Peat, R. A., Baker, N. L., Zamurs, L. K., Mörgelin, M., Irving, M. D., Adams, N. E., Bateman, J. F., Mowat, D. R., Smith, N. J. C., et al. (2008) · Annals of Neurology · doi:10.1002/ana.21439 · Cited by 72 · see citing works

Mutation (D472Y) in the Type 3 Repeat Domain of Cartilage Oligomeric Matrix Protein Affects Its Early Vesicle Trafficking in Endoplasmic Reticulum and Induces Apoptosis

Hashimoto, Y., Tomiyama, T., Yamano, Y., & Mori, H. (2003) · American Journal Of Pathology · doi:10.1016/s0002-9440(10)63634-6 · Cited by 69 · see citing works

Pseudoachondroplasia is caused through both intra- and extracellular pathogenic pathways

Dinser, R., Zaucke, F., Kreppel, F., Hultenby, K. R., Kochanek, S., Paulsson, M., & Maurer, P. (2002) · Journal of Clinical Investigation · doi:10.1172/jci14386 · Cited by 69 · see citing works

Misfolding of Collagen X Chains Harboring Schmid Metaphyseal Chondrodysplasia Mutations Results in Aberrant Disulfide Bond Formation, Intracellular Retention, and Activation of the Unfolded Protein Response

Wilson, R., Freddi, S., Chan, D. T.-M., Cheah, K. S. E., & Bateman, J. F. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m410758200 · Cited by 69 · see citing works

Bethlem Myopathy and Engineered Collagen VI Triple Helical Deletions Prevent Intracellular Multimer Assembly and Protein Secretion

Lamandé, S. R., Shields, K. A., Kornberg, A. J., Shield, L. K., & Bateman, J. F. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.31.21817 · Cited by 68 · see citing works

Defective folding and stable association with protein disulfide isomerase/prolyl hydroxylase of type I procollagen with a deletion in the pro alpha 2(I) chain that preserves the Gly-X-Y repeat pattern.

Chessler, S. D., & Byers, P. H. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)42578-1 · Cited by 67 · see citing works

Unique Matrix Structure in the Rough Endoplasmic Reticulum Cisternae of Pseudoachondroplasia Chondrocytes

Merritt, T. M., Bick, R. J., Poindexter, B. J., Alcorn, J. L., & Hecht, J. T. (2007) · American Journal Of Pathology · doi:10.2353/ajpath.2007.060530 · Cited by 63 · see citing works

Premature Termination Codon Mutations in the Type VII Collagen Gene in Recessive Dystrophic Epidermolysis Bullosa Result in Nonsense-Mediated mRNA Decay and Absence of Functional Protein

Christiano, A. M., Amano, S., Eichenfield, L. F., Burgeson, R. E., & Uitto, J. (1997) · Journal of Investigative Dermatology · doi:10.1111/1523-1747.ep12336276 · Cited by 62 · see citing works

Selective retention and degradation of molecules with a single mutant α1(I) chain in the Brtl IV mouse model of OI

Forlino, A., Kuznetsova, N. V., Marini, J. C., & Leikin, S. (2007) · Matrix Biology · doi:10.1016/j.matbio.2007.06.005 · Cited by 60 · see citing works

X‐linked recessive chondrodysplasia punctata: Spectrum of arylsulfatase E gene mutations and expanded clinical variability

Brunetti‐Pierri, N., Andreucci, M. V., Tuzzi, M. R., Vega, G. R., Gray, G., McKeown, C., Ballabio, A., Andria, G., Meroni, G., & Parenti, G. (2002) · American Journal of Medical Genetics Part A · doi:10.1002/ajmg.a.10950 · Cited by 55 · see citing works

Deposition and selective degradation of structually-abnormal type I collagen in a collagen matrix produced by osteogenesis imperfecta fibroblasts in vitro

Bateman, J. F., & Golub, S. B. (1994) · Matrix Biology · doi:10.1016/0945-053x(94)90189-9 · Cited by 55 · see citing works

Pseudoachondroplasia is caused through both intra- and extracellular pathogenic pathways

Dinser, R., Zaucke, F., Kreppel, F., Hultenby, K. R., Kochanek, S., Paulsson, M., & Maurer, P. (2002) · Journal of Clinical Investigation · doi:10.1172/jci0214386 · Cited by 55 · see citing works

Differential expression of both extracellular and intracellular proteins is involved in the lethal or nonlethal phenotypic variation of BrtlIV, a murine model for osteogenesis imperfecta

Forlino, A., Tani, C., Rossi, A., Lupi, A., Campari, E., Gualeni, B., Bianchi, L., Armini, A., Cetta, G., Bini, L., et al. (2007) · PROTEOMICS · doi:10.1002/pmic.200600919 · Cited by 54 · see citing works

Collagen binding proteins

Svensson, L., Oldberg, Å., & Heinegård, D. K. (2001) · Osteoarthritis and Cartilage · doi:10.1053/joca.2001.0440 · Cited by 49 · see citing works

Transgenic mice expressing D469Δ mutated cartilage oligomeric matrix protein (COMP) show growth plate abnormalities and sternal malformations

Schmitz, M., Niehoff, A., Miosge, N., Smyth, N. R., Paulsson, M., & Zaucke, F. (2007) · Matrix Biology · doi:10.1016/j.matbio.2007.08.001 · Cited by 48 · see citing works

Emerging therapeutic approaches for osteogenesis imperfecta

Millington‐Ward, S., McMahon, H. P., & Farrar, G. J. (2005) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2005.04.006 · Cited by 41 · see citing works

Cyclosporine A treatment for Ullrich congenital muscular dystrophy: a cellular study of mitochondrial dysfunction and its rescue

Hicks, D., Lampe, A., Laval, S. H., Allamand, V., Jimenez-Mallebrera, C., Walter, M. C., Francesco Muntoni, A., Quijano-Roy, S., Richard, P., Straub, V. W., et al. (2008) · Brain · doi:10.1093/brain/awn289 · Cited by 40 · see citing works

Variable penetrance of COL6A1 null mutations: Implications for prenatal diagnosis and genetic counselling in Ullrich congenital muscular dystrophy families

Peat, R. A., Baker, N. L., Jones, K., North, K. N., & Lamandé, S. R. (2007) · Neuromuscular Disorders · doi:10.1016/j.nmd.2007.03.017 · Cited by 39 · see citing works

Thrombospondins: from structure to therapeutics

Posey, K. L., Yang, Y. M., Veerisetty, A. C., Sharan, S. K., & Hecht, J. T. (2008) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-007-7485-0 · Cited by 38 · see citing works

Cells expressing partially unfolded R789C/p.R989C type II procollagen mutant associated with spondyloepiphyseal dysplasia undergo apoptosis

Hintze, V., Steplewski, A., Ito, H., Jensen, D. A., Rodeck, U., & Fertala, A. (2008) · Human Mutation · doi:10.1002/humu.20736 · Cited by 35 · see citing works

Collagen X Chains Harboring Schmid Metaphyseal Chondrodysplasia NC1 Domain Mutations Are Selectively Retained and Degraded in Stably Transfected Cells

Wilson, R., Freddi, S., & Bateman, J. F. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m112044200 · Cited by 34 · see citing works

Competency for Nonsense-Mediated Reduction in Collagen X mRNA Is Specified by the 3′ UTR and Corresponds to the Position of Mutations in Schmid Metaphyseal Chondrodysplasia

Tan, J., Kremer, F., Freddi, S., Bell, K. M., Baker, N. L., Lamandé, S. R., & Bateman, J. F. (2008) · The American Journal of Human Genetics · doi:10.1016/j.ajhg.2008.01.006 · Cited by 33 · see citing works

A homozygous COL6A2 intron mutation causes in-frame triple-helical deletion and nonsense-mediated mRNA decay in a patient with Ullrich congenital muscular dystrophy

Lucarini, L., Giusti, B., Zhang, R.-Z., Pan, T., Jimenez-Mallebrera, C., Mercuri, E. M., Francesco Muntoni, A., Pepe, G., & Chu, M. (2005) · Human Genetics · doi:10.1007/s00439-005-1318-8 · Cited by 25 · see citing works

Protein consequences of the Col2a1 C-propeptide mutation in the chondrodysplastic Dmm mouse

Fernandes, R. J., Seegmiller, R. E., Nelson, W. R., & Eyre, D. R. (2003) · Matrix Biology · doi:10.1016/s0945-053x(03)00077-5 · Cited by 24 · see citing works

Expression of PSACH-associated mutant COMP in tendon fibroblasts leads to increased apoptotic cell death irrespective of the secretory characteristics of mutant COMP

Weirich, C., Keene, D. R., Kirsch, K., Heil, M., Neumann, E., & Dinser, R. (2007) · Matrix Biology · doi:10.1016/j.matbio.2007.01.004 · Cited by 14 · see citing works

Molecular Mechanisms of Stress-Responsive Changes in Collagen and Elastin Networks in Skin

Aziz, J., Shezali, H., Radzi, Z., Yahya, N. A., Abu Kassim, N. H., Czernuszka, J., & Rahman, M. T. (2016) · Skin Pharmacology and Physiology · doi:10.1159/000447017 · Cited by 7,323 · see citing works

Remodelling the extracellular matrix in development and disease

Bonnans, C., Chou, J., & Werb, Z. (2014) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3904 · Cited by 4,367 · see citing works

Wound repair and regeneration: Mechanisms, signaling, and translation

Eming, S. A., Martin, P., & Tomic-Canic, M. (2014) · Science Translational Medicine · doi:10.1126/scitranslmed.3009337 · Cited by 3,562 · see citing works

The Collagen Family

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

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

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

Overview of the Matrisome--An Inventory of Extracellular Matrix Constituents and Functions

Hynes, R. O., & Naba, A. (2012) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a004903 · Cited by 1,349 · see citing works

Engineering organoids

Hofer, M., & Lutolf, M. P. (2021) · Nature Reviews Materials · doi:10.1038/s41578-021-00279-y · Cited by 1,184 · see citing works

The extracellular matrix: tools and insights for the "omics" era

Naba, A., Clauser, K. R., Ding, H., Whittaker, C. A., Carr, S. A., & Hynes, R. O. (2016) · Matrix Biology · doi:10.1016/j.matbio.2015.06.003 · Cited by 1,037 · see citing works

Matrix Metalloproteinases: From Molecular Mechanisms to Physiology, Pathophysiology, and Pharmacology

de Almeida, L. G. N., Thode, H., Eslambolchi, Y., Chopra, S., Young, D. W., Gill, S. E., Devel, L., & Dufour, A. (2022) · Pharmacological Reviews · doi:10.1124/pharmrev.121.000349 · Cited by 555 · see citing works

The extracellular matrix in development

Walma, D. A. C., & Yamada, K. M. (2020) · Development · doi:10.1242/dev.175596 · Cited by 398 · see citing works

The role of matrix metalloproteinases in aging: Tissue remodeling and beyond

Freitas‐Rodríguez, S., Folgueras, A. R., & López-Otı́n, C. (2017) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2017.05.007 · Cited by 367 · see citing works

A selective ER‐phagy exerts procollagen quality control via a Calnexin‐FAM134B complex

Forrester, A., De Leonibus, C., Grumati, P., Fasana, E., Piemontese, M., Staiano, L., Fregno, I., Raimondi, A., Marazza, A., Bruno, G., et al. (2019) · The EMBO Journal · doi:10.15252/embj.201899847 · Cited by 259 · see citing works

Extracellular matrix: The driving force of mammalian diseases

Iozzo, R. V., & Gubbiotti, M. A. (2018) · Matrix Biology · doi:10.1016/j.matbio.2018.03.023 · Cited by 236 · see citing works

Ocular Features in Alport Syndrome

Savige, J., Sheth, S. J., LEYS, A. M., Nicholson, A., Mack, H. G., & Colville, D. J. (2015) · Clinical Journal of the American Society of Nephrology · doi:10.2215/cjn.10581014 · Cited by 228 · see citing works

The Role of Extracellular Matrix in Skin Wound Healing

Potekaev, N., Borzykh, O., Medvedev, G. V., Pushkin, D., Petrova, M., Petrov, A. V., Dmitrenko, D., Karpova, E. I., Demina, O., & Shnayder, N. (2021) · Journal of Clinical Medicine · doi:10.3390/jcm10245947 · Cited by 189 · see citing works

A molecular ensemble in the rER for procollagen maturation

Ishikawa, Y., & Bächinger, H. P. (2013) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2013.04.008 · Cited by 176 · see citing works

Fibronectin splice variants: understanding their multiple roles in health and disease using engineered mouse models

White, E. S., & Muro, A. F. (2011) · IUBMB Life · doi:10.1002/iub.493 · Cited by 174 · see citing works

Defining the extracellular matrix using proteomics

Byron, A., Humphries, J. D., & Humphries, M. J. (2013) · International Journal of Experimental Pathology · doi:10.1111/iep.12011 · Cited by 171 · see citing works

Hsp47 as a Collagen-Specific Molecular Chaperone

Ishida, Y., & Nagata, K. (2011) · Methods in Enzymology · doi:10.1016/b978-0-12-386471-0.00009-2 · Cited by 159 · see citing works

Stickler syndrome and the vitreous phenotype: mutations in COL2A1 and COL11A1

Richards, A. J., McNinch, A. M., Martin, H., Oakhill, K., Rai, H., Waller, S. J., Treacy, B., Whittaker, J., Meredith, S. P., Poulson, A. V., et al. (2010) · Human Mutation · doi:10.1002/humu.21257 · Cited by 154 · see citing works

ER remodeling via ER-phagy

Gubaš, A., & Đikić, I. (2022) · Molecular Cell · doi:10.1016/j.molcel.2022.02.018 · Cited by 142 · see citing works

Genetic causes and mechanisms of Osteogenesis Imperfecta

Lim, J., Grafe, I., Alexander, S., & Lee, B. (2017) · Bone · doi:10.1016/j.bone.2017.02.004 · Cited by 144 · see citing works

The unfolded protein response and its relevance to connective tissue diseases

Boot-Handford, R. P., & Briggs, M. D. (2010) · Cell and Tissue Research · doi:10.1007/s00441-009-0877-8 · Cited by 143 · 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

Targeted Induction of Endoplasmic Reticulum Stress Induces Cartilage Pathology

Rajpar, M. H., McDermott, B., Kung, L. H. W., Eardley, R., Knowles, L., Heeran, M. C., Thornton, D. J., Wilson, R., Bateman, J. F., Poulsom, R., et al. (2009) · PLoS Genetics · doi:10.1371/journal.pgen.1000691 · Cited by 136 · see citing works

Thrombospondin-2 and extracellular matrix assembly

Calabro, N. E., Kristofik, N. J., & Kyriakides, T. R. (2014) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2014.01.013 · Cited by 136 · see citing works

MatrixDB, the extracellular matrix interaction database

Chautard, É., Fatoux-Ardore, M., Ballut, L., Thierry‐Mieg, N., & Ricard‐Blum, S. (2010) · Nucleic Acids Research · doi:10.1093/nar/gkq830 · Cited by 134 · see citing works

Skeletal muscle fibroblasts in health and disease

Chapman, M., Meza, R. C., & Lieber, R. L. (2016) · Differentiation · doi:10.1016/j.diff.2016.05.007 · Cited by 134 · see citing works

Decorin Antagonizes Met Receptor Activity and Down-regulates β-Catenin and Myc Levels

Buraschi, S., Pal, N., Tyler-Rubinstein, N., Owens, R. T., Neill, T., & Iozzo, R. V. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.172841 · Cited by 130 · see citing works

HIF1α is a central regulator of collagen hydroxylation and secretion under hypoxia during bone development

Bentovim, L., Amarilio, R., & Zelzer, E. (2012) · Development · doi:10.1242/dev.083881 · Cited by 122 · see citing works

Osteogenesis imperfecta and therapeutics

Morello, R. (2018) · Matrix Biology · doi:10.1016/j.matbio.2018.03.010 · Cited by 121 · see citing works

Intracellular mechanisms of molecular recognition and sorting for transport of large extracellular matrix molecules

Ishikawa, Y., Ito, S., Nagata, K., Sakai, L. Y., & Bächinger, H. P. (2016) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1609571113 · Cited by 119 · see citing works

Matrikines as mediators of tissue remodelling

Jariwala, N., Ozols, M., Bell, M., Bradley, E., Gilmore, A. P., Debelle, L., & Sherratt, M. J. (2022) · Advanced Drug Delivery Reviews · doi:10.1016/j.addr.2022.114240 · Cited by 123 · see citing works

TGF-β Family Signaling in Connective Tissue and Skeletal DiseasesPreprint

MacFarlane, E. G., Haupt, J., Dietz, H. C., & Shore, E. M. (2017) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a022269 · Cited by 119 · see citing works

The renin–angiotensin system and its involvement in vascular disease

van Thiel, B. S., van der Pluijm, I., Riet, L. T., Essers, J., & Danser, A. H. J. (2015) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2015.03.090 · Cited by 115 · see citing works

Reciprocal Interplay Between Fibrillar Collagens and Collagen‐Binding Integrins: Implications in Cancer Progression and Metastasis

Bourgot, I., Primac, I., Louis, T., Noël, A., & Maquoi, E. (2020) · Frontiers in Oncology · doi:10.3389/fonc.2020.01488 · Cited by 113 · see citing works

Changes in the Chondrocyte and Extracellular Matrix Proteome during Post-natal Mouse Cartilage Development*

Wilson, R., Norris, E. L., Brachvogel, B., Angelucci, C., Živković, S., Gordon, L., Bernardo, B., Stermann, J., Sekiguchi, K., Gorman, J., et al. (2011) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m111.014159 · Cited by 103 · see citing works

Into the Tissues: Extracellular Matrix and Its Artificial Substitutes: Cell Signalling Mechanisms

Bandzerewicz, A., & Gadomska‐Gajadhur, A. (2022) · Cells · doi:10.3390/cells11050914 · Cited by 114 · see citing works

ColVI myopathies: where do we stand, where do we go?

Allamand, V., Briñas, L., Richard, P., Stojkovic, T., Quijano-Roy, S., & Bonne, G. (2011) · Skeletal Muscle · doi:10.1186/2044-5040-1-30 · Cited by 108 · see citing works

The extracellular matrix of the dermis: flexible structures with dynamic functions

Krieg, T. M., & Aumailley, M. (2011) · Experimental Dermatology · doi:10.1111/j.1600-0625.2011.01313.x · Cited by 107 · see citing works

Genetic Disorders of the Extracellular Matrix

Lamandé, S. R., & Bateman, J. F. (2019) · The Anatomical Record · doi:10.1002/ar.24086 · Cited by 105 · see citing works

Overgrowth syndromes — clinical and molecular aspects and tumour risk

Brioude, F., Toutain, A., Giabicani, É., Cottereau, E., Cormier‐Daire, V., & Netchine, I. (2019) · Nature Reviews Endocrinology · doi:10.1038/s41574-019-0180-z · Cited by 104 · see citing works

Dissecting the role of hyaluronan synthases in the tumor microenvironment

Passi, A. G., Vigetti, D., Buraschi, S., & Iozzo, R. V. (2019) · FEBS Journal · doi:10.1111/febs.14847 · Cited by 106 · see citing works

Structural basis of fibrillar collagen trimerization and related genetic disorders

Bourhis, J., Mariano, N., Zhao, Y., Harlos, K., Exposito, J., Jones, E. Y., Moali, C., Aghajari, N., & HULMES, D. J. S. (2012) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.2389 · Cited by 102 · see citing works

Exploring the extracellular matrix in health and disease using proteomics

Taha, I. N., & Naba, A. (2019) · Essays in Biochemistry · doi:10.1042/ebc20190001 · Cited by 100 · see citing works

RIN2 Deficiency Results in Macrocephaly, Alopecia, Cutis Laxa, and Scoliosis: MACS Syndrome

Basel‐Vanagaite, L., Sarig, O., Hershkovitz, D., Fuchs‐Telem, D., Rapaport, D., Gat, A., Isman, G., Shirazi, I., Shohat, M., Enk, C. D., et al. (2009) · The American Journal of Human Genetics · doi:10.1016/j.ajhg.2009.07.001 · Cited by 97 · see citing works

Cartilage Intermediate Layer Protein 2 (CILP-2) Is Expressed in Articular and Meniscal Cartilage and Down-regulated in Experimental Osteoarthritis

Bernardo, B. C., Belluoccio, D., Rowley, L., Little, C. B., Hansen, U. J., & Bateman, J. F. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.248039 · Cited by 97 · see citing works

mTORC1 hyperactivation arrests bone growth in lysosomal storage disorders by suppressing autophagy

Bartolomeo, R., Cinque, L., Leonibus, C. D., Forrester, A. R., Salzano, A. C., Monfregola, J., Gennaro, E. D., Nusco, E., Azario, I., Lanzara, C., et al. (2017) · Journal of Clinical Investigation · doi:10.1172/jci94130 · Cited by 93 · see citing works

Clinical phenotypes associated with type II collagen mutations

Kannus, P., Bateman, J. F., & Savarirayan, R. (2011) · Journal of Paediatrics and Child Health · doi:10.1111/j.1440-1754.2010.01979.x · Cited by 96 · see citing works

Wound healing: a paradigm for regeneration.

Wong, V. W., Gurtner, G., & Longaker, M. (2013) · Mayo Clinic proceedings · doi:10.1016/j.mayocp.2013.04.012 · Cited by 94 · see citing works

E3 Ubiquitin Ligase Synoviolin Is Involved in Liver Fibrogenesis

Hasegawa, D., Fujii, R., Yagishita, N., Matsumoto, N., Aratani, S., Izumi, T., Azakami, K., Nakazawa, M., Fujita, H., Sato, T., et al. (2010) · PLoS ONE · doi:10.1371/journal.pone.0013590 · Cited by 93 · see citing works

Biomechanical Rigidity and Quantitative Proteomics Analysis of Segmental Regions of the Trabecular Meshwork at Physiologic and Elevated Pressures

Vranka, J. A., Staverosky, J. A., Reddy, A. P., Wilmarth, P. A., David, L. L., Acott, T. S., Russell, P., & Raghunathan, V. K. (2018) · Investigative Ophthalmology & Visual Science · doi:10.1167/iovs.17-22759 · Cited by 91 · see citing works

Charting the unexplored extracellular matrix in cancer

Filipe, E. C., Chitty, J. L., & Cox, T. R. (2018) · International Journal of Experimental Pathology · doi:10.1111/iep.12269 · Cited by 91 · see citing works

Application of biomaterials to advance induced pluripotent stem cell research and therapy

Tong, Z.-X., Solanki, A., Hamilos, A. E., Levy, O., Wen, K., Yin, X., & Karp, J. (2015) · EMBO Journal · doi:10.15252/embj.201490756 · Cited by 97 · see citing works

Protein localization as a principal feature of the etiology and comorbidity of genetic diseases

Park, S., Yang, J., Shin, Y., Park, J. M., Jang, S. K., & Kim, S. (2011) · Molecular Systems Biology · doi:10.1038/msb.2011.29 · Cited by 89 · see citing works

Type IV Collagens and Basement Membrane Diseases

Mao, M., Alavi, M. V., Labelle‐Dumais, C., & Gould, D. B. (2015) · Current topics in membranes · doi:10.1016/bs.ctm.2015.09.002 · Cited by 89 · see citing works

SWATH mass spectrometry as a tool for quantitative profiling of the matrisome

Krásný, L., Bland, P. J., Kogata, N., Wai, P. T., Howard, B. A., Natrajan, R., & Huang, P. H. (2018) · Journal of Proteomics · doi:10.1016/j.jprot.2018.02.026 · Cited by 89 · see citing works

Companion Blood Cells Control Ovarian Stem Cell Niche Microenvironment and Homeostasis.

Bor, V. V. D., Zimniak, G., Papone, L., Cerezo, D., Malbouyres, M., Juan, T., Ruggiero, F., & Noselli, S. (2015) · Cell Reports · doi:10.1016/j.celrep.2015.09.008 · Cited by 83 · see citing works

Molecular mechanisms of phenotypic variability in junctional epidermolysis bullosa

Kiritsi, D., Kern, J. S., Schumann, H., Kohlhase, J., Has, C., & Bruckner‐Tuderman, L. (2011) · Journal of Medical Genetics · doi:10.1136/jmg.2010.086751 · Cited by 86 · see citing works

An unfolded protein response is the initial cellular response to the expression of mutant matrilin-3 in a mouse model of multiple epiphyseal dysplasia

Nundlall, S., Rajpar, M. H., Bell, P. A., Clowes, C., Zeeff, L. A. H., Gardner, B., Thornton, D. J., Boot-Handford, R., & Briggs, M. D. (2010) · Cell Stress and Chaperones · doi:10.1007/s12192-010-0193-y · Cited by 85 · see citing works

Forty-two novel COL7A1 mutations and the role of a frequent single nucleotide polymorphism in the MMP1 promoter in modulation of disease severity in a large European dystrophic epidermolysis bullosa cohort

Kern, J. S., Grüninger, G., Imsak, R., Müller, M. L., Schumann, H., Kiritsi, D., Emmert, S., Borozdin, W., Kohlhase, J., Bruckner‐Tuderman, L., et al. (2009) · British Journal of Dermatology · doi:10.1111/j.1365-2133.2009.09333.x · Cited by 84 · see citing works

The proteostasis boundary in misfolding diseases of membrane traffic

Hutt, D. M., Powers, E. T., & Balch, W. E. (2009) · FEBS Letters · doi:10.1016/j.febslet.2009.07.014 · Cited by 85 · see citing works

The profibrotic role of endothelin-1: Is the door still open for the treatment of fibrotic diseases?

Rodríguez‐Pascual, F., Busnadiego, Ó., & González, J. (2014) · Life Sciences · doi:10.1016/j.lfs.2013.12.024 · Cited by 83 · see citing works

Cellular and Molecular Mechanisms in the Pathogenesis of Classical, Vascular, and Hypermobile Ehlers‒Danlos Syndromes

Chiarelli, N., Ritelli, M., Zoppi, N., & Colombi, M. (2019) · Genes · doi:10.3390/genes10080609 · Cited by 82 · see citing works

Chemical chaperone treatment reduces intracellular accumulation of mutant collagen IV and ameliorates the cellular phenotype of a COL4A2 mutation that causes haemorrhagic stroke

Murray, L. S., Lu, Y., Taggart, A., Regemorter, N. V., Vilain, C. N., Abramowicz, M. J., Kadler, K. E., & Agtmael, T. V. (2013) · Human Molecular Genetics · doi:10.1093/hmg/ddt418 · Cited by 80 · see citing works

Pan-cancer analysis connects tumor matrisome to immune response

Lim, S. B., Chua, M. L. K., Yeong, J. P.-S., Tan, S. J., Lim, W., & Lim, C. T. (2019) · npj Precision Oncology · doi:10.1038/s41698-019-0087-0 · Cited by 79 · see citing works

Three distinct cell populations express extracellular matrix proteins and increase in number during skeletal muscle fibrosis

Chapman, M., Mukund, K., Subramaniam, S., Brenner, D. A., & Lieber, R. L. (2016) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00226.2016 · Cited by 77 · see citing works

Mutations in COL27A1 cause Steel syndrome and suggest a founder mutation effect in the Puerto Rican population

Gonzaga-Jauregui, C. G., Gamble, C., Yuan, B., Penney, S., Jhangiani, S. N., Muzny, D. M., Gibbs, R. A., Lupski, J. R., & Hecht, J. T. (2014) · European Journal of Human Genetics · doi:10.1038/ejhg.2014.107 · Cited by 76 · see citing works

Armet/Manf and Creld2 are components of a specialized ER stress response provoked by inappropriate formation of disulphide bonds: implications for genetic skeletal diseases

Hartley, C. L., Edwards, S. M., Mullan, L., Bell, P. A., Fresquet, M., Boot-Handford, R., & Briggs, M. D. (2013) · Human Molecular Genetics · doi:10.1093/hmg/ddt383 · Cited by 76 · see citing works

Chaperoning osteogenesis: new protein-folding disease paradigms

Makareeva, E., Aviles, N. A., & Leikin, S. (2010) · Trends in Cell Biology · doi:10.1016/j.tcb.2010.11.007 · Cited by 75 · see citing works

Impaired lymphoid extracellular matrix impedes antibacterial immunity in epidermolysis bullosa

Nyström, A., Bornert, O., Kühl, T., Gretzmeier, C., Thriene, K., Dengjel, J., Pfister‐Wartha, A., Kiritsi, D., & Bruckner‐Tuderman, L. (2018) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1709111115 · Cited by 74 · see citing works

Fibronectin matrix as a scaffold for procollagen proteinase binding and collagen processing

Saunders, J. T., & Schwarzbauer, J. E. (2019) · Molecular Biology of the Cell · doi:10.1091/mbc.e19-03-0140 · Cited by 72 · see citing works

Frequency of COL4A3/COL4A4 Mutations amongst Families Segregating Glomerular Microscopic Hematuria and Evidence for Activation of the Unfolded Protein Response. Focal and Segmental Glomerulosclerosis Is a Frequent Development during Ageing

Papazachariou, L., Demosthenous, P., Pieri, M., Papagregoriou, G., Savva, I., Stavrou, C., Zavros, M., Athanasiou, Y., Ioannou, K. I., Patsias, C., et al. (2014) · PLoS ONE · doi:10.1371/journal.pone.0115015 · Cited by 72 · see citing works

From Spheroids to Organoids: The Next Generation of Model Systems of Human Cardiac Regeneration in a Dish

Scalise, M., Marino, F., Salerno, L., Cianflone, E., Molinaro, C., Salerno, N., Angelis, A. D., Viglietto, G., Urbanek, K., & Torella, D. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms222413180 · Cited by 67 · see citing works

Biomechanical relationships between the corneal endothelium and Descemet's membrane

Ali, M., Raghunathan, V. K., Li, J. Y., Murphy, C. J., & Thomasy, S. M. (2016) · Experimental Eye Research · doi:10.1016/j.exer.2016.09.004 · Cited by 69 · see citing works

Severe Extracellular Matrix Abnormalities and Chondrodysplasia in Mice Lacking Collagen Prolyl 4-Hydroxylase Isoenzyme II in Combination with a Reduced Amount of Isoenzyme I

Aro, E., Salo, A. M., Khatri, R., Finnilä, M., Miinalainen, I., Sormunen, R. T., Pakkanen, O., Holster, T., Soininen, R., Prein, C., et al. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m115.662635 · Cited by 69 · see citing works

Digenic Alport Syndrome

Savige, J., Renieri, A., Ars, E., Daga, S., Pinto, A. M., Rothe, H. M., Gale, D. P., Евгеньевна, А. М., Čerkauskaitė, A., Bielska, O., et al. (2022) · Clinical Journal of the American Society of Nephrology · doi:10.2215/cjn.03120322 · Cited by 69 · see citing works

Human Recombinant Type I Collagen Produced in Plants

Shoseyov, O., Posen, Y., & Grynspan, F. (2012) · Tissue Engineering Part A · doi:10.1089/ten.tea.2012.0347 · Cited by 68 · see citing works

Short Stature, Onychodysplasia, Facial Dysmorphism, and Hypotrichosis Syndrome Is Caused by a POC1A Mutation

Sarig, O., Nahum, S., Rapaport, D., Ishida‐Yamamoto, A., Fuchs‐Telem, D., Li, Q., Cohen‐Katsenelson, K., Spiegel, R., Nousbeck, J., Israeli, S., et al. (2012) · The American Journal of Human Genetics · doi:10.1016/j.ajhg.2012.06.003 · Cited by 66 · see citing works

Blood-testis barrier: a review on regulators in maintaining cell junction integrity between Sertoli cells

Wanjari, U. R., & Gopalakrishnan, A. V. (2024) · Cell and Tissue Research · doi:10.1007/s00441-024-03894-7 · Cited by 65 · see citing works

A cysteine-based molecular code informs collagen C-propeptide assembly

DiChiara, A. S., Li, R. C., Suen, P., Hosseini, A. S., Taylor, R. J., Weickhardt, A. F., Malhotra, D., McCaslin, D. R., & Shoulders, M. D. (2018) · Nature Communications · doi:10.1038/s41467-018-06185-2 · Cited by 62 · see citing works

Genotype-Phenotype Correlations for Pathogenic COL4A3–COL4A5 Variants in X-Linked, Autosomal Recessive, and Autosomal Dominant Alport Syndrome

Savige, J., Huang, M., Dabrera, M. S. C., Shukla, K., & Gibson, J. T. (2022) · Frontiers in Medicine · doi:10.3389/fmed.2022.865034 · Cited by 62 · see citing works

Alport syndrome: its effects on the glomerular filtration barrier and implications for future treatment

Savige, J. (2014) · The Journal of Physiology · doi:10.1113/jphysiol.2014.274449 · Cited by 62 · see citing works

Development of the Mechanical Properties of Engineered Skin Substitutes After Grafting to Full-Thickness Wounds

Sander, E. A., Lynch, K. A., & Boyce, S. T. (2014) · Journal of Biomechanical Engineering · doi:10.1115/1.4026290 · Cited by 62 · see citing works

Transcriptional Profiling of Chondrodysplasia Growth Plate Cartilage Reveals Adaptive ER-Stress Networks That Allow Survival but Disrupt Hypertrophy

Cameron, T. L., Bell, K. M., Tatarczuch, L., Mackie, E. J., Rajpar, M. H., McDermott, B., Boot-Handford, R., & Bateman, J. F. (2011) · PLoS ONE · doi:10.1371/journal.pone.0024600 · Cited by 61 · see citing works

Heterozygous Pathogenic COL4A3 and COL4A4 Variants (Autosomal Dominant Alport Syndrome) Are Common, and Not Typically Associated With End-Stage Kidney Failure, Hearing Loss, or Ocular Abnormalities

Savige, J. (2022) · Kidney International Reports · doi:10.1016/j.ekir.2022.06.001 · Cited by 59 · see citing works

Type IX collagen gene mutations can result in multiple epiphyseal dysplasia that is associated with osteochondritis dissecans and a mild myopathy

Jackson, G. C., Marcus‐Soekarman, D., Stolte‐Dijkstra, I., Verrips, A., Taylor, J. A., & Briggs, M. D. (2010) · American Journal of Medical Genetics Part A · doi:10.1002/ajmg.a.33240 · Cited by 59 · see citing works

Emerging lysosomal pathways for quality control at the endoplasmic reticulum

Leonibus, C. D., Cinque, L., & Settembre, C. (2019) · FEBS Letters · doi:10.1002/1873-3468.13571 · Cited by 57 · see citing works

Extracellular matrix in cancer progression and therapy

He, X., Lee, B., & Jiang, Y. (2022) · Medical Review · doi:10.1515/mr-2021-0028 · Cited by 56 · see citing works

Collagen XXVII Organises the Pericellular Matrix in the Growth Plate

Plumb, D. A., Ferrara, L., Torbica, T., Knowles, L., Mironov, A., Kadler, K. E., Briggs, M. D., & Boot-Handford, R. (2011) · PLoS ONE · doi:10.1371/journal.pone.0029422 · Cited by 56 · see citing works

Antibodies and methods for immunohistochemistry of extracellular matrix proteins

Rickelt, S., & Hynes, R. O. (2018) · Matrix Biology · doi:10.1016/j.matbio.2018.04.011 · Cited by 51 · see citing works

Matrix Stiffening Facilitates the Collective Invasion of Breast Cancer through the Periostin-Integrin Mechanotransduction Pathway.

Wu, T., Xiong, S., Chen, M., Tam, B. T., Chen, W., Dong, K., Ma, Z., Wang, Z., & Ouyang, G. (2023) · Matrix Biology · doi:10.1016/j.matbio.2023.05.006 · Cited by 55 · see citing works

Comparative proteomic assessment of matrisome enrichment methodologies

Krásný, L., Paul, A., Wai, P. T., Howard, B. A., Natrajan, R., & Huang, P. H. (2016) · Biochemical Journal · doi:10.1042/bcj20160686 · Cited by 53 · see citing works

A substrate preference for the rough endoplasmic reticulum resident protein FKBP22 during collagen biosynthesis

Ishikawa, Y., & Bächinger, H. P. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.561944 · Cited by 52 · see citing works

Diagnostic Exome Sequencing Identifies a Novel Gene,EMILIN1, Associated with Autosomal‐Dominant Hereditary Connective Tissue Disease

Capuano, A., Bucciotti, F., Hagman, K. D. F., Davis, B. T., Mroske, C., Hulick, P. J., Weissman, S. M., Gao, Q., Spessotto, P., Colombatti, A., et al. (2015) · Human Mutation · doi:10.1002/humu.22920 · Cited by 52 · see citing works

Identification of novel and known KRT5 and KRT14 mutations in 53 patients with epidermolysis bullosa simplex: correlation between genotype and phenotype

Arin, M. J., Grimberg, G., Schumann, H., de Almeida, H., Chang, Y.-R., Tadini, G., Kohlhase, J., Krieg, T. M., Bruckner‐Tuderman, L., & Has, C. (2010) · British Journal of Dermatology · doi:10.1111/j.1365-2133.2010.09657.x · Cited by 51 · see citing works

ER stress and basement membrane defects combine to cause glomerular and tubular renal disease resulting from Col4a1 mutations in mice

Jones, F. E., Bailey, M. A., Murray, L. S., Lu, Y., McNeilly, S., Schlötzer-Schrehardt, U. M., Lennon, R., Sado, Y., Brownstein, D. G., Mullins, J. J., et al. (2016) · Disease Models & Mechanisms · doi:10.1242/dmm.021741 · Cited by 51 · see citing works

Molecular alterations in the extracellular matrix in the brains of newborns with congenital Zika syndrome

Aguiar, R. S., Pohl, F. B., de Morais, G. L., Nogueira, F. C. S., de Carvalho, J. B., Guida, L. D. C., Arge, L. W. P., Melo, A., Moreira, M. E. L., Cunha, D. P., et al. (2020) · Science Signaling · doi:10.1126/scisignal.aay6736 · Cited by 51 · see citing works

Anoikis in cell fate, physiopathology, and therapeutic interventions

Mei, J., Jiang, X., Tian, H., Rong, D., Song, J., Wang, L., Chen, Y., Wong, R. C. B., Guo, C., Wang, L., et al. (2024) · MedComm · doi:10.1002/mco2.718 · Cited by 52 · see citing works

Molecular mechanisms and clinical manifestations of rare genetic disorders associated with type I collagen

Lu, Y., Zhang, S., Wang, Y., Ren, X., & Han, J. (2019) · Intractable & Rare Diseases Research · doi:10.5582/irdr.2019.01064 · Cited by 50 · see citing works

Genetic Disorders of the Extracellular Matrix

Lamandé, S. R., & Bateman, J. F. (2019) · The Anatomical Record · doi:10.1002/ar.24086 · Cited by 105 · 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

The Extracellular Matrix Across States: From Homeostasis to Dysfunction in Rare Connective Tissue Disorders

Diana, R., Gulberti, S., & Bui, C. (2026) · Proteoglycan Research · doi:10.1002/pgr2.70047

Inherited Connective Tissue Disorders of Collagens: Lessons from Targeted Mutagenesis

Bonod‐Bidaud, C., & Ruggiero, F. (2013) · InTech eBooks · doi:10.5772/50858 · Cited by 7 · see citing works

Genetic diseases of the extracellular matrix: more than just connective tissue disorders

Bruckner‐Tuderman, L., & Brückner, P. (1998) · Journal of Molecular Medicine · doi:10.1007/s001090050213 · Cited by 42 · see citing works