Brain Dysfunction in LAMA2-Related Congenital Muscular Dystrophy: Lessons From Human Case Reports and Mouse Models

Principles of diffusion tensor imaging and its applications to basic neuroscience research

Mori, S., & Zhang, J. (2006) · Neuron · doi:10.1016/j.neuron.2006.08.012 · Cited by 1,708 · see citing works

Ventral tegmental area: cellular heterogeneity, connectivity and behaviour

Morales, M., & Margolis, E. B. (2017) · Nature reviews. Neuroscience · doi:10.1038/nrn.2016.165 · Cited by 1,108 · see citing works

A specialized vascular niche for adult neural stem cells

Tavazoie, M., Van der Veken, L., Silva-Vargas, V., Louissaint, M., Colonna, L., Zaidi, B., Garcia-Verdugo, J. M., & Doetsch, F. (2008) · Cell stem cell · doi:10.1016/j.stem.2008.07.025 · Cited by 1,033 · see citing works

Adult SVZ stem cells lie in a vascular niche: a quantitative analysis of niche cell-cell interactions

Shen, Q., Wang, Y., Kokovay, E., Lin, G., Chuang, S.-M., Goderie, S. K., Roysam, B., & Temple, S. (2008) · Cell stem cell · doi:10.1016/j.stem.2008.07.026 · Cited by 1,027 · see citing works

Mutations in the Fukutin-Related Protein Gene (FKRP) Cause a Form of Congenital Muscular Dystrophy with Secondary Laminin α2 Deficiency and Abnormal Glycosylation of α-Dystroglycan

Brockington, M., Blake, D. J., Prandini, P., Brown, S., Torelli, S., Benson, M. A., Ponting, C. P., Estournet, B., Romero, N. B., Mercuri, E. M., et al. (2001) · The American Journal of Human Genetics · doi:10.1086/324412 · Cited by 600 · see citing works

G Protein-Coupled Receptor-Dependent Development of Human Frontal Cortex

Piao, X., Hill, R. S., Bodell, A., Chang, B. S., Basel-Vanagaite, L., Straussberg, R., Dobyns, W. B., Qasrawi, B., Winter, R. M., Innes, A. M., et al. (2004) · Science · doi:10.1126/science.1092780 · Cited by 517 · see citing works

Endothelial Cell Laminin Isoforms, Laminins 8 and 10, Play Decisive Roles in T Cell Recruitment across the Blood–Brain Barrier in Experimental Autoimmune Encephalomyelitis

Sixt, M., Engelhardt, B., Pausch, F., Hallmann, R., Wendler, O., & Sorokin, L. M. (2001) · The Journal of Cell Biology · doi:10.1083/jcb.153.5.933 · Cited by 504 · see citing works

Laminins

Durbeej, M. (2009) · Cell and Tissue Research · doi:10.1007/s00441-009-0838-2 · Cited by 500 · see citing works

Diagnostic criteria for Walker‐Warburg syndrome

Dobyns, W. B., Pagon, R. A., Armstrong, D. L., Curry, C. J., Greenberg, F., Grix, A., Holmes, L. B., Laxová, R., Michels, V. V., Robinow, M., et al. (1989) · American Journal of Medical Genetics · doi:10.1002/ajmg.1320320213 · Cited by 445 · see citing works

Distribution and Function of Laminins in the Neuromuscular System of Developing, Adult, and Mutant Mice

Patton, B. L., Miner, J. H., Chiu, A. Y., & Sanes, J. R. (1997) · The Journal of Cell Biology · doi:10.1083/jcb.139.6.1507 · Cited by 436 · see citing works

Mutations in the human LARGE gene cause MDC1D, a novel form of congenital muscular dystrophy with severe mental retardation and abnormal glycosylation of -dystroglycan

Longman, C. (2003) · Human Molecular Genetics · doi:10.1093/hmg/ddg307 · Cited by 416 · see citing works

Merosin, a tissue-specific basement membrane protein, is a laminin-like protein.

Ehrig, K., Leivo, I. V. V., Argraves, W. S., Ruoslahti, E. I., & Engvall, E. (1990) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.87.9.3264 · Cited by 392 · see citing works

N-cadherin and integrins: Two receptor systems that mediate neuronal process outgrowth on astrocyte surfaces

Tomaselli, K. J., Neugebauer, K. M., Bixby, J. L., Lilien, J. E., & Reichard, L. F. (1988) · Neuron · doi:10.1016/0896-6273(88)90207-3 · Cited by 371 · see citing works

Astrocytic laminin regulates pericyte differentiation and maintains blood brain barrier integrity

Yao, Y., Chen, Z.-L., Norris, E. H., & Strickland, S. (2014) · Nature Communications · doi:10.1038/ncomms4413 · Cited by 357 · see citing works

Murine muscular dystrophy caused by a mutation in the laminin α2 (Lama2) gene

Xu, H. W., Wu, X., Wewer, U. M., & Engvall, E. (1994) · Nature Genetics · doi:10.1038/ng1194-297 · Cited by 341 · see citing works

Diagnostic approach to the congenital muscular dystrophies

Bönnemann, C. G., Wang, C. H., Quijano-Roy, S., Deconinck, N., Bertini, E., Ferreiro, A., Francesco Muntoni, A., Sewry, C. A., Béroud, C., Mathews, K. D., et al. (2014) · Neuromuscular Disorders · doi:10.1016/j.nmd.2013.12.011 · Cited by 341 · see citing works

Dystrophia Muscularis: A HEREDITARY PRIMARY MYOPATHY IN THE HOUSE MOUSE

Michelson, A. M., Russell, E. S., & Harman, P. J. (1955) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.41.12.1079 · Cited by 333 · see citing works

Neurodevelopmental, emotional, and behavioural problems in Duchenne muscular dystrophy in relation to underlying dystrophin gene mutations

Ricotti, V., Mandy, W., Scoto, M., Pane, M., Deconinck, N., Messina, S., Mercuri, E. M., Skuse, D., & Francesco Muntoni, A. (2015) · Developmental Medicine & Child Neurology · doi:10.1111/dmcn.12922 · Cited by 332 · see citing works

β1 integrins activate a MAPK signalling pathway in neural stem cells that contributes to their maintenance

Campos, L. S., Leone, D. P., Relvas, J. B., Brakebusch, C., Fässler, R., Suter, U., & ffrench‐Constant, C. (2004) · Development · doi:10.1242/dev.01199 · Cited by 313 · see citing works

Origin and dynamics of oligodendrocytes in the developing brain: Implications for perinatal white matter injury

van Tilborg, E., de Theije, C. G. M., van Hal, M., Wagenaar, N., de Vries, L. S., Benders, M. J. N. L., Rowitch, D. H., & Nijboer, C. H. A. (2017) · Glia · doi:10.1002/glia.23256 · Cited by 292 · see citing works

Cellular signaling by neural cell adhesion molecules of the immunoglobulin superfamily

Crossin, K. L., & Krushel, L. A. (2000) · Developmental Dynamics · doi:10.1002/(sici)1097-0177(200006)218:2 · Cited by 283 · see citing works

The Adhesion GPCR GPR126 Has Distinct, Domain-Dependent Functions in Schwann Cell Development Mediated by Interaction with Laminin-211

Petersen, S. C., Luo, R., Liebscher, I., Giera, S., Jeong, S., Mogha, A., Ghidinelli, M., Feltri, M. L., Schöneberg, T., Piao, X., et al. (2015) · Neuron · doi:10.1016/j.neuron.2014.12.057 · Cited by 283 · see citing works

Sticky Signaling—Adhesion Class G Protein–Coupled Receptors Take the Stage

Langenhan, T., Aust, G., & Hamann, J. (2013) · Science Signaling · doi:10.1126/scisignal.2003825 · Cited by 267 · see citing works

Laminin α2 chain‐null mutant mice by targeted disruption of the Lama2 gene: a new model of merosin (laminin 2)‐deficient congenital muscular dystrophy

Miyagoe, Y., Hanaoka, K., Nonaka, I., Hayasaka, M., Nabeshima, Y., Arahata, K., Nabeshima, Y.-I., & Takeda, S. (1997) · FEBS Letters · doi:10.1016/s0014-5793(97)01007-7 · Cited by 262 · see citing works

Human laminin M chain (merosin): complete primary structure, chromosomal assignment, and expression of the M and A chain in human fetal tissues

Vuolteenaho, R., Nissinen, M., Sainio, K., Byers, M. G., Eddy, R. L., Hirvonen, H., Shows, T. B., Sariola, H. V., Engvall, E., & Tryggvason, K. (1994) · The Journal of Cell Biology · doi:10.1083/jcb.124.3.381 · Cited by 258 · see citing works

Laminin isoforms in endothelial and perivascular basement membranes

Yousif, L. F., Russo, J. D., & Sorokin, L. M. (2013) · Cell Adhesion & Migration · doi:10.4161/cam.22680 · Cited by 249 · see citing works

CNS integrins switch growth factor signalling to promote target-dependent survival

Colognato, H., Baron, W., Avellana‐Adalid, V., Relvas, J. B., Evercooren, A. B., Georges‐Labouesse, E., & ffrench‐Constant, C. (2002) · Nature Cell Biology · doi:10.1038/ncb865 · Cited by 246 · see citing works

GPR56 Regulates Pial Basement Membrane Integrity and Cortical Lamination

Li, S., Jin, Z., Koirala, S., Bu, L., Xu, L., Hynes, R. O., Walsh, C. A., Corfas, G., & Piao, X. (2008) · The Journal of Neuroscience · doi:10.1523/jneurosci.0853-08.2008 · Cited by 241 · see citing works

Muscle-eye-brain disease (MEB)

Santavuori, P., Somer, H., Sainio, K., Rapola, J., Kruus, S., Nikitin, T., Ketonen, L., & Leisti, J. (1989) · Brain and Development · doi:10.1016/s0387-7604(89)80088-9 · Cited by 238 · see citing works

The Extracellular Matrix Protein Laminin α2 Regulates the Maturation and Function of the Blood–Brain Barrier

Menezes, M. J., McClenahan, F. K., Leiton, C. V., Aranmolate, A., Shan, X., & Colognato, H. (2014) · The Journal of Neuroscience · doi:10.1523/jneurosci.3678-13.2014 · Cited by 226 · see citing works

Identification of a Post-translational Modification with Ribitol-Phosphate and Its Defect in Muscular Dystrophy

Kanagawa, M., Kobayashi, K., Tajiri, M., Manya, H., Kuga, A., Yamaguchi, Y., Akasaka‐Manya, K., Furukawa, J., Mizuno, M., Kawakami, H., et al. (2016) · Cell Reports · doi:10.1016/j.celrep.2016.02.017 · Cited by 226 · see citing works

Laminin-2/integrin interactions enhance myelin membrane formation by oligodendrocytes.

Buttery, P., & ffrench-Constant, C. (1999) · Molecular and cellular neurosciences · doi:10.1006/mcne.1999.0781 · Cited by 217 · see citing works

A developmental analysis of oligodendroglial integrins in primary cells: changes in αv-associated β subunits during differentiation

Milner, R., & ffrench‐Constant, C. (1994) · Development · doi:10.1242/dev.120.12.3497 · Cited by 210 · see citing works

Molecular characterization of perivascular drainage pathways in the murine brain

Hannocks, M.-J., Pizzo, M. E., Huppert, J., Deshpande, T., Abbott, N. J., Thorne, R. G., & Sorokin, L. (2018) · Journal of Cerebral Blood Flow & Metabolism · doi:10.1177/0271678x17749689 · Cited by 201 · see citing works

The Dystroglycan Complex Is Necessary for Stabilization of Acetylcholine Receptor Clusters at Neuromuscular Junctions and Formation of the Synaptic Basement Membrane

Jacobson, C., Côté, P. D., Rossi, S. G., Rotundo, R. L., & Carbonetto, S. (2001) · The Journal of Cell Biology · doi:10.1083/jcb.152.3.435 · Cited by 199 · see citing works

Genotype–phenotype correlation in a large population of muscular dystrophy patients with LAMA2 mutations

Geranmayeh, F., Clement, E. M., Feng, L., Sewry, C. A., Pagan, J. G., Mein, R., Abbs, S. J., Brueton, L. A., Childs, A., Jungbluth, H., et al. (2010) · Neuromuscular Disorders · doi:10.1016/j.nmd.2010.02.001 · Cited by 198 · see citing works

Merosin-deficient congenital muscular dystrophy. Partial genetic correction in two mouse models.

Kuang, W., Xu, H. W., Vachon, P. H., Liu, L., Loechel, F., Wewer, U. M., & Engvall, E. (1998) · Journal of Clinical Investigation · doi:10.1172/jci3705 · Cited by 188 · see citing works

β1 Integrin Maintains Integrity of the Embryonic Neocortical Stem Cell Niche

Loulier, K., Lathia, J. D., Marthiens, V., Relucio, J. L. V., Mughal, M. R., Tang, S., Coksaygan, T., Hall, P. E., Chigurupati, S., Patton, B. L., et al. (2009) · PLoS Biology · doi:10.1371/journal.pbio.1000176 · Cited by 184 · see citing works

Integrin-linked kinase is required for laminin-2–induced oligodendrocyte cell spreading and CNS myelination

Chun, S. J., Rasband, M. N., Sidman, R. L., Habib, A. A., & Vartanian, T. (2003) · The Journal of Cell Biology · doi:10.1083/jcb.200304154 · Cited by 170 · see citing works

Muscle—eye—brain disease: A neuropathological study

Haltia, M., Leivo, I. V. V., Somer, H., Pihko, H. S., Paetau, A. E., Kivelä, T., Tarkkanen, A. H. A., Tomé, F. M. S., Engvall, E., & Santavuori, P. (1997) · Annals of Neurology · doi:10.1002/ana.410410208 · Cited by 166 · see citing works

Basal lamina strengthens cell membrane integrity via the laminin G domain-binding motif of α-dystroglycan

Han, R., Kanagawa, M., Yoshida‐Moriguchi, T., Rader, E. P., Ng, R. A., Michele, D. E., Muirhead, D. E., Kunz, S., Moore, S. A., Iannaccone, S. T., et al. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0906545106 · Cited by 157 · see citing works

Purification and Characterization of Human Laminin-8

Fujiwara, H., Kikkawa, Y., Sanzen, N., & Sekiguchi, K. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m010155200 · Cited by 157 · see citing works

Genetic and Molecular Regulation of Extrasynaptic GABA-A Receptors in the Brain: Therapeutic Insights for Epilepsy

Chuang, S.-H., & Reddy, D. S. (2017) · Journal of Pharmacology and Experimental Therapeutics · doi:10.1124/jpet.117.244673 · Cited by 149 · see citing works

Electron microscopic evidence for a mucin‐like region in chick muscle α‐dystroglycan

Brancaccio, A., Schulthess, T., Gesemann, M., & Engel, J. (1995) · FEBS Letters · doi:10.1016/0014-5793(95)00628-m · Cited by 145 · see citing works

GPR56-related bilateral frontoparietal polymicrogyria: further evidence for an overlap with the cobblestone complex

Bahi-Buisson, N., Poirier, K., Boddaert, N., Fallet-Bianco, C., Specchio, N., Bertini, E., Caglayan, O., Lascelles, K., Elie, C., Rambaud, J., et al. (2010) · Brain · doi:10.1093/brain/awq259 · Cited by 144 · see citing works

The role of pericytic laminin in blood brain barrier integrity maintenance

Gautam, J., Zhang, X., & Yao, Y. (2016) · Scientific Reports · doi:10.1038/srep36450 · Cited by 139 · see citing works

Congenital muscular dystrophy: molecular and cellular aspects

Jimenez-Mallebrera, C., Brown, S., Sewry, C. A., & Francesco Muntoni, A. (2005) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-004-4510-4 · Cited by 137 · see citing works

Patterns of laminins and integrins in the embryonic ventricular zone of the CNS

Lathia, J. D., Patton, B. L., Eckley, D. M., Magnus, T., Mughal, M. R., Sasaki, T., Caldwell, M. A., Rao, M. S., Mattson, M. P., & ffrench‐Constant, C. (2007) · The Journal of Comparative Neurology · doi:10.1002/cne.21520 · Cited by 135 · see citing works

Laminins promote postsynaptic maturation by an autocrine mechanism at the neuromuscular junction

Nishimune, H., Valdez, G., Jarad, G., Moulson, C. L., Müller, U., Miner, J. H., & Sanes, J. R. (2008) · The Journal of Cell Biology · doi:10.1083/jcb.200805095 · Cited by 131 · see citing works

Pericytes Stimulate Oligodendrocyte Progenitor Cell Differentiation during CNS Remyelination

de la Fuente, A. G., Lange, S., Silva, M. E., González, G. A., Tempfer, H., van Wijngaarden, P., Zhao, C., Canio, L. D., Trost, A., Bieler, L., et al. (2017) · Cell Reports · doi:10.1016/j.celrep.2017.08.007 · Cited by 129 · see citing works

Merosin‐negative congenital muscular dystrophy associated with extensive brain abnormalities

Sunada, Y., Edgar, T. S., Lotz, B. P., Rust, R. S., & Campbell, K. P. (1995) · Neurology · doi:10.1212/wnl.45.11.2084 · Cited by 126 · see citing works

Congenital muscular dystrophies in the UK population: Clinical and molecular spectrum of a large cohort diagnosed over a 12-year period

Sframeli, M., Sárközy, A., Bértoli, M., Astrea, G., Hudson, J. A., Scoto, M., Mein, R., Yau, M., Phadke, R., Feng, L., et al. (2017) · Neuromuscular Disorders · doi:10.1016/j.nmd.2017.06.008 · Cited by 123 · see citing works

Muscular dystrophy in the mouse caused by an allele at the -locus

Meier, H., & Southard, J. L. (1970) · Life Sciences · doi:10.1016/0024-3205(70)90306-1 · Cited by 122 · see citing works

Merosin-deficient congenital muscular dystrophy: the spectrum of brain involvement on magnetic resonance imaging

Philpot, J., Cowan, F. M., Pennock, J. M., Sewry, C. A., Dubowitz, V., Bydder, G. M., & Francesco Muntoni, A. (1999) · Neuromuscular Disorders · doi:10.1016/s0960-8966(98)00110-2 · Cited by 122 · see citing works

Mild Congenital Muscular Dystrophy in Two Patients with an Internally Deleted Laminin 2-Chain

Allamand, V., Sunada, Y., Salih, M. A. M., Straub, V. W., Ozo, O., Al-Turaiki, M. H. S., Akbar, M., Kolo, T., Colognato, H., Zhang, X., et al. (1997) · Human Molecular Genetics · doi:10.1093/hmg/6.5.747 · Cited by 121 · see citing works

Expression and Distribution of Laminin α1 and α2 Chains in Embryonic and Adult Mouse Tissues: An Immunochemical Approach

Sasaki, T., Giltay, R., Talts, U., Timpl, R., & Talts, J. F. (2002) · Experimental Cell Research · doi:10.1006/excr.2002.5499 · Cited by 120 · see citing works

Laminin-deficient muscular dystrophy: Molecular pathogenesis and structural repair strategies

Yurchenco, P. D., McKee, K. K., Reinhard, J. R., & Rüegg, M. A. (2017) · Matrix Biology · doi:10.1016/j.matbio.2017.11.009 · Cited by 119 · see citing works

Both Laminin and Schwann Cell Dystroglycan Are Necessary for Proper Clustering of Sodium Channels at Nodes of Ranvier

Occhi, S., Zambroni, D., Carro, U. D., Amadio, S., Sirkowski, E. E., Scherer, S. S., Campbell, K. P., Moore, S. A., Chen, Z.-L., Strickland, S., et al. (2005) · Journal of Neuroscience · doi:10.1523/jneurosci.2068-05.2005 · Cited by 116 · see citing works

Dystroglycan on Radial Glia End Feet Is Required for Pial Basement Membrane Integrity and Columnar Organization of the Developing Cerebral Cortex

Myshrall, T. D., Moore, S. A., Ostendorf, A. P., Satz, J. S., Kowalczyk, T., Nguyen, H., Daza, R. A. M., Lau, C., Campbell, K. P., & Hevner, R. F. (2012) · Journal of Neuropathology & Experimental Neurology · doi:10.1097/nen.0b013e318274a128 · Cited by 102 · see citing works

Dystroglycan mediates homeostatic synaptic plasticity at GABAergic synapses

Pribiag, H., Peng, H., Shah, W. A., Stellwagen, D., & Carbonetto, S. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1321774111 · Cited by 97 · see citing works

Protein binding and cell adhesion properties of two laminin isoforms (amb1eb2e, amb1sb2e) from human placenta

Brown, J. C., Wiedemann, H., & Timpl, R. (1994) · Journal of Cell Science · doi:10.1242/jcs.107.1.329 · Cited by 95 · see citing works

Glia unglued: How signals from the extracellular matrix regulate the development of myelinating glia

Colognato, H., & Tzvetanova, I. D. (2011) · Developmental Neurobiology · doi:10.1002/dneu.20966 · Cited by 90 · see citing works

Linker proteins restore basement membrane and correct LAMA2 -related muscular dystrophy in mice

Reinhard, J. R., Lin, S., McKee, K. K., Meinen, S., Crosson, S. C., Sury, M., Hobbs, S., Maier, G., Yurchenco, P. D., & Rüegg, M. A. (2017) · Science Translational Medicine · doi:10.1126/scitranslmed.aal4649 · Cited by 90 · see citing works

beta1 Integrin and alpha-dystroglycan binding sites are localized to different laminin-G-domain-like (LG) modules within the laminin alpha5 chain G domain

Hao, Y. U., & Talts, J. F. (2003) · Biochemical Journal · doi:10.1042/bj20021500 · Cited by 89 · see citing works

Laminins of the adult mammalian CNS; laminin-α2 (merosin M-) chain immunoreactivity is associated with neuronal processes

Hagg, T., Portera‐Cailliau, C., Jucker, M., & Engvall, E. (1997) · Brain Research · doi:10.1016/s0006-8993(97)00419-8 · Cited by 88 · see citing works

β1 integrins are required for normal CNS myelination and promote AKT-dependent myelin outgrowth

Barros, C. S., Nguyen, T., Spencer, K. S. R., Nishiyama, A., Colognato, H., & Müller, U. (2009) · Development · doi:10.1242/dev.038679 · Cited by 87 · see citing works

Laminin regulates postnatal oligodendrocyte production by promoting oligodendrocyte progenitor survival in the subventricular zone

Relucio, J. L. V., Menezes, M. J., Miyagoe‐Suzuki, Y., Takeda, S., & Colognato, H. (2012) · Glia · doi:10.1002/glia.22365 · Cited by 87 · see citing works

Analysis of Gpr126 function defines distinct mechanisms controlling the initiation and maturation of myelin

Glenn, T. D., & Talbot, W. S. (2013) · Development · doi:10.1242/dev.093401 · Cited by 87 · see citing works

The laminin α2 expressed by dystrophic dy2J mice is defective in its ability to form polymers

Colognato, H., & Yurchenco, P. D. (1999) · Current Biology · doi:10.1016/s0960-9822(00)80056-1 · Cited by 78 · see citing works

Absence of Glial α-Dystrobrevin Causes Abnormalities of the Blood-Brain Barrier and Progressive Brain Edema

Lien, C. F., Mohanta, S. K., Frontczak‐Baniewicz, M., Swinny, J. D., Zabłocka, B., & Górecki, D. C. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.400044 · Cited by 76 · see citing works

Laminin Alters Fyn Regulatory Mechanisms and Promotes Oligodendrocyte Development

Relucio, J. L. V., Tzvetanova, I. D., Ao, W., Lindquist, S., & Colognato, H. (2009) · Journal of Neuroscience · doi:10.1523/jneurosci.0888-09.2009 · Cited by 75 · see citing works

Functionally distinct PI 3-kinase pathways regulate myelination in the peripheral nervous system

Heller, B. A., Ghidinelli, M., Voelkl, J. G. J., Einheber, S., Smith, R., Grund, E. M., Morahan, G., Chandler, D., Kalaydjieva, L. V., Giancotti, F. G., et al. (2014) · The Journal of Cell Biology · doi:10.1083/jcb.201307057 · Cited by 75 · see citing works

Laminins and human disease

McGowan, K. A., & Marinkovich, M. P. (2000) · Microscopy Research and Technique · doi:10.1002/1097-0029(20001101)51:3 · Cited by 75 · see citing works

Laminin and Integrin in LAMA2-Related Congenital Muscular Dystrophy: From Disease to Therapeutics

Barraza‐Flores, P., Bates, C. R., Oliveira‐Santos, A., & Burkin, D. J. (2020) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2020.00001 · Cited by 75 · see citing works

Laminin alpha 2 chain (M chain) is found within the pathway of avian and murine retinal projections

Morissette, N., & Carbonetto, S. (1995) · Journal of Neuroscience · doi:10.1523/jneurosci.15-12-08067.1995 · Cited by 75 · see citing works

Differential effects of laminin and merosin on neurite outgrowth by developing retinal ganglion cells

Cohen, J., & Johnson, A. R. (1991) · Journal of Cell Science · doi:10.1242/jcs.1991.supplement_15.1 · Cited by 73 · see citing works

Congenital muscular dystrophy with laminin α2 chain deficiency: Identification of a new intermediate phenotype and correlation of clinical findings to muscle immunohistochemistry

Herrmann, R., Straub, V. W., Meyer, K. L., Kahn, T., Wagner, M., & Voït, T. (1996) · European Journal of Pediatrics · doi:10.1007/bf02282889 · Cited by 71 · see citing works

A Laminin-2, Dystroglycan, Utrophin Axis Is Required for Compartmentalization and Elongation of Myelin Segments

Court, F. A., Hewitt, J., Davies, K. E., Patton, B. L., Uncini, A., Wrabetz, L. G., & Feltri, M. L. (2009) · Journal of Neuroscience · doi:10.1523/jneurosci.5672-08.2009 · Cited by 68 · see citing works

Targeting Dystroglycan in the Brain

Montanaro, F., & Carbonetto, S. (2003) · Neuron · doi:10.1016/s0896-6273(03)00032-1 · Cited by 66 · see citing works

Avian neural crest cell migration on laminin: interaction of the α1β1 integrin with distinct laminin-1 domains mediates different adhesive responses

Desban, N., & Duband, J. (1997) · Journal of Cell Science · doi:10.1242/jcs.110.21.2729 · Cited by 66 · see citing works

Laminin α2 chain-deficient congenital muscular dystrophy

Cohn, R. D., Herrmann, R., Sorokin, L. M., Wewer, U. M., & Voït, T. (1998) · Neurology · doi:10.1212/wnl.51.1.94 · Cited by 66 · see citing works

Clinical and molecular characterization of limb‐girdle muscular dystrophy due to LAMA2 mutations

Gavassini, B. F., Carboni, N., Nielsen, J. E., Danielsen, E. R., Thomsen, C. E., Svenstrup, K., Bello, L., Maioli, M. A., Marrosu, G., Ticca, A. F., et al. (2011) · Muscle & Nerve · doi:10.1002/mus.22132 · Cited by 64 · see citing works

Laminin-α2 chain-like antigens in CNS dendritic spines

Tian, M., Hagg, T., Denisova, N., Knüsel, B., Engvall, E., & Jucker, M. (1997) · Brain Research · doi:10.1016/s0006-8993(97)00420-4 · Cited by 63 · see citing works

Merosin-negative congenital muscular dystrophy, occipital epilepsy with periodic spasms and focal cortical dysplasia. Report of three Italian cases in two families

Pini, A., Merlini, L., Tomé, F. M. S., Chevallay, M., & Gobbi, G. (1996) · Brain and Development · doi:10.1016/0387-7604(96)00028-9 · Cited by 62 · see citing works

Fractone Bulbs Derive from Ependymal Cells and Their Laminin Composition Influence the Stem Cell Niche in the Subventricular Zone

Nascimento, M. A., Sorokin, L. M., & Coelho‐Sampaio, T. (2018) · Journal of Neuroscience · doi:10.1523/jneurosci.3064-17.2018 · Cited by 61 · see citing works

Vascular laminins in physiology and pathology

Russo, J. D., Hannocks, M., Luik, A., Song, J., Zhang, X., Yousif, L. F., Aspite, G., Hallmann, R., & Sorokin, L. M. (2016) · Matrix Biology · doi:10.1016/j.matbio.2016.06.008 · Cited by 61 · see citing works

Schwann cell myelination occurred without basal lamina formation in laminin α2 chain‐null mutant (dy3K/dy3K) mice

Nakagawa, M. M., Miyagoe‐Suzuki, Y., Ikezoe, K., Miyata, Y., Nonaka, I., Harii, K., & Takeda, S. (2001) · Glia · doi:10.1002/glia.1075 · Cited by 59 · see citing works

A single point mutation in the LN domain of LAMA2 causes muscular dystrophy and peripheral amyelination

Patton, B. L., Wang, B., Tarumi, Y. S., Seburn, K. L., & Burgess, R. W. (2008) · Journal of Cell Science · doi:10.1242/jcs.015354 · Cited by 57 · see citing works

Detection of variants in dystroglycanopathy-associated genes through the application of targeted whole-exome sequencing analysis to a large cohort of patients with unexplained limb-girdle muscle weakness

Johnson, K., Bértoli, M., Phillips, L. C., Töpf, A., den Bergh, P. Y. K. V., Vissing, J., Witting, N., Nafissi, S., Jamal-Omidi, S., Łusakowska, A., et al. (2018) · Skeletal Muscle · doi:10.1186/s13395-018-0170-1 · Cited by 56 · see citing works

Laminin 211 inhibits protein kinase A in Schwann cells to modulate neuregulin 1 type III-driven myelination

Ghidinelli, M., Poitelon, Y., Shin, Y. K., Ameroso, D., Williamson, C., Ferri, C., Pellegatta, M., Espino, K., Mogha, A., Monk, K. R., et al. (2017) · PLoS Biology · doi:10.1371/journal.pbio.2001408 · Cited by 53 · see citing works

Neurons and glial cells of the embryonic human brain and spinal cord express multiple and distinct isoforms of laminin

Liesi, P., Fried, G., & Stewart, R. R. (2001) · Journal of Neuroscience Research · doi:10.1002/jnr.1061 · Cited by 52 · see citing works

The inside and out of dystroglycan post-translational modification

Moore, C. J., & Winder, S. J. (2012) · Neuromuscular Disorders · doi:10.1016/j.nmd.2012.05.016 · Cited by 52 · see citing works

Myelinated nerve fibre counts in the nerves of normal and dystrophic mouse muscle

Harris, J. B., Wallace, C., & Wing, J. (1972) · Journal of the Neurological Sciences · doi:10.1016/0022-510x(72)90067-6 · Cited by 51 · see citing works

Reduced postsynaptic GABAA receptor number and enhanced gaboxadol induced change in holding currents in Purkinje cells of the dystrophin-deficient mdx mouse

Kueh, S. L. L., Dempster, J., Head, S. I., & Morley, J. W. (2011) · Neurobiology of Disease · doi:10.1016/j.nbd.2011.05.002 · Cited by 48 · see citing works

Hypermyelinating neuropathy, mental retardation and epilepsy in a case of merosin deficiency

Deodato, F., Sabatelli, M., Ricci, E., Mercuri, E. M., Francesco Muntoni, A., Sewry, C. A., Naom, I., Tonali, P., & Guzzetta, F. (2002) · Neuromuscular Disorders · doi:10.1016/s0960-8966(01)00312-1 · Cited by 48 · see citing works

Congenital muscular dystrophy: use of brain MR imaging findings to predict merosin deficiency.

Lamer, S., Carlier, R., Pinard, J.-M., Mompoint, D. M., Bagard, C., Burdairon, E., Estournet, B., Barois, A., & Vallée, C. A. (1998) · Radiology · doi:10.1148/radiology.206.3.9494506 · Cited by 46 · see citing works

Congenital muscular dystrophies in China

Lin, G., Zhang, C., Wang, Z., Chan, H. S., Zhu, W., Han, C., Zhang, X., Zheng, H. X., Wu, L., Jin, B., et al. (2019) · Clinical Genetics · doi:10.1111/cge.13560 · Cited by 46 · see citing works

Dystroglycan promotes filopodial formation and process branching in differentiating oligodendroglia

Eyermann, C. E., Czaplinski, K., & Colognato, H. (2011) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2011.07600.x · Cited by 45 · see citing works

Localization of laminin α2 chain in normal human central nervous system: an immunofluorescence and ultrastructural study

Villanova, M., Malandrini, A., Sabatelli, P., Sewry, C. A., Toti, P., Torelli, S., Six, J., Scarfò, G. B., Palma, L., Francesco Muntoni, A., et al. (1997) · Acta Neuropathologica · doi:10.1007/s004010050751 · Cited by 45 · see citing works

Mesenchymal Stem Cell Conditioning Promotes Rat Oligodendroglial Cell Maturation

Jadasz, J. J., Kremer, D., Göttle, P., Tzekova, N., Domke, J., Rivera, F. J., Adjaye, J., Hartung, H., Aigner, L., & Küry, P. (2013) · PLoS ONE · doi:10.1371/journal.pone.0071814 · Cited by 44 · see citing works

Localization of merosin in the normal human brain: implications for congenital muscular dystrophy with merosin deficiency.

Villanova, M., Malandrini, A., Toti, P., Salvestroni, R., Six, J., Jj, M., & Gc, G. (1996) · PubMed · Cited by 43 · see citing works

A Family of Laminin α2 Chain-Deficient Mouse Mutants: Advancing the Research on LAMA2-CMD

Gawlik, K. I., & Durbeej, M. (2020) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2020.00059 · Cited by 39 · see citing works

LAMA2 stop-codon mutation: Merosin-deficient congenital muscular dystrophy with occipital polymicrogyria, epilepsy and psychomotor regression

Vigliano, P., Dassi, P., Blasi, C. D., Mora, M., & Jarre, L. (2008) · European Journal of Paediatric Neurology · doi:10.1016/j.ejpn.2008.01.010 · Cited by 38 · see citing works

LAMA2 Neuropathies: Human Findings and Pathomechanisms From Mouse Models

Previtali, S. C., & Zambon, A. A. (2020) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2020.00060 · Cited by 36 · see citing works

Atypical phenotype in two patients with LAMA2 mutations

Marques, J., Duarte, S. T., Costa, S., Jacinto, S. H., Oliveira, J., Oliveira, M. E., Santos, R., Bronze-da-Rocha, E., Silvestre, A. R., Calado, E., et al. (2014) · Neuromuscular Disorders · doi:10.1016/j.nmd.2014.01.004 · Cited by 36 · see citing works

Ventricular–subventricular zone fractones are speckled basement membranes that function as a neural stem cell niche

Sato, Y., Kiyozumi, D., Futaki, S., Nakano, I., Shimono, C., Kaneko, N., Ikawa, M., Okabe, M., Sawamoto, K., & Sekiguchi, K. (2018) · Molecular Biology of the Cell · doi:10.1091/mbc.e18-05-0286 · Cited by 35 · see citing works

Epilepsy in LAMA2‐related muscular dystrophy: An electro‐clinico‐radiological characterization

Benito, D. N., Muchart, J., Itzep, D., Ortez, C., González‐Quereda, L., Gallano, P., Ramírez-Camacho, A., Aparicio, J., Domínguez‐Carral, J., Carrera‐García, L., et al. (2020) · Epilepsia · doi:10.1111/epi.16493 · Cited by 35 · see citing works

Integrin-Linked Kinase Regulates Process Extension in Oligodendrocytes via Control of Actin Cytoskeletal Dynamics

O’Meara, R. W., Michalski, J., Anderson, C., Bhanot, K., Rippstein, P. U., & Kothary, R. (2013) · Journal of Neuroscience · doi:10.1523/jneurosci.5582-12.2013 · Cited by 33 · see citing works

Fibrogenesis in LAMA2-Related Muscular Dystrophy Is a Central Tenet of Disease Etiology

Accorsi, A., Cramer, M. L., & Girgenrath, M. (2020) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2020.00003 · Cited by 29 · see citing works

Essential role for InSyn1 in dystroglycan complex integrity and cognitive behaviors in mice

Uezu, A., Hisey, E. E., Kobayashi, Y., Gao, Y., Bradshaw, T. W., Devlin, P., Rodriguiz, R. M., Tata, P. R., & Soderling, S. H. (2019) · eLife · doi:10.7554/elife.50712 · Cited by 29 · see citing works

Pericytes Favor Oligodendrocyte Fate Choice in Adult Neural Stem Cells

Silva, M. E., Lange, S., Hinrichsen, B., Philp, A. R., Reyes, C. R., Halabí, D., Mansilla, J. B., Rotheneichner, P., de la Fuente, A. G., Couillard‐Després, S., et al. (2019) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2019.00085 · Cited by 26 · see citing works

Merosin-deficient congenital muscular dystrophy and cortical dysplasia

Brett, F. M., Costigan, D. A., Farrell, M., Heaphy, P., Thornton, J., & King, M. (1998) · European Journal of Paediatric Neurology · doi:10.1016/s1090-3798(98)80045-7 · Cited by 25 · see citing works

Activation of c-Raf-1 Kinase Signal Transduction Pathway in α7 Integrin-deficient Mice

Saher, G., & Hildt, E. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.39.27651 · Cited by 25 · see citing works

An early onset muscular dystrophy with diaphragmatic involvement, early respiratory failure and secondary α2 laminin deficiency unlinked to the LAMA2 locus on 6q22

Francesco Muntoni, A., Taylor, J., Sewry, C. A., Naom, I., & Dubowitz, V. (1998) · European Journal of Paediatric Neurology · doi:10.1016/1090-3798(98)01001-9 · Cited by 24 · see citing works

Ocular findings in Fukuyama type congenital muscular dystrophy

Tsutsumi, A., Uchida, Y., Ōsawa, M., & Fukuyama, Y. (1989) · Brain and Development · doi:10.1016/s0387-7604(89)80026-9 · Cited by 24 · see citing works

Hearing loss in the laminin-deficient dy mouse model of congenital muscular dystrophy

Pillers, D.-A. M., Kempton, J. B., Duncan, N. M., Pang, J., Dwinnell, S. J., & Trune, D. R. (2002) · Molecular Genetics and Metabolism · doi:10.1016/s1096-7192(02)00039-2 · Cited by 24 · see citing works

Clinical, Radiological, and Genetic Survey of Patients With Muscle-Eye-Brain Disease Caused by Mutations in POMGNT1

Yiş, U., Uyanık, G., Morris-Rosendahl, D. J., Çarman, K. B., Bayram, E., Heise, M., Cömertpay, G., & Kurul, S. H. (2014) · Pediatric Neurology · doi:10.1016/j.pediatrneurol.2014.01.008 · Cited by 23 · see citing works

GPR56 -Related Polymicrogyria

Desai, N. A., & Udani, V. P. (2015) · Journal of Child Neurology · doi:10.1177/0883073815583335 · Cited by 20 · see citing works

Congenital Muscular Dystrophy, White-Matter Abnormalities, and Neuronal Migration Disorders: The Expanding Concept

Mackay, M. T., Kornberg, A. J., Shield, L. K., Phelan, E., Kean, M. J., Coleman, L. T., & Dennett, X. (1998) · Journal of Child Neurology · doi:10.1177/088307389801301003 · Cited by 20 · see citing works

Expression of autoimmune disease-related antigens by cells of the immune system

Mor, F., Boccaccio, G. L., & Unger, T. (1998) · Journal of Neuroscience Research · doi:10.1002/(sici)1097-4547(19981015)54:2 · Cited by 19 · see citing works

Identification of Candidate Protein Markers in Skeletal Muscle of Laminin-211-Deficient CMD Type 1A-Patients

Kölbel, H., Hathazi, D., Jennings, M. J., Horváth, R., Roos, A., & Schara, U. (2019) · Frontiers in Neurology · doi:10.3389/fneur.2019.00470 · Cited by 19 · see citing works

Early human brain development: insights into macroscale connectome wiring

Keunen, K., van der Burgh, H. K., de Reus, M. A., Moeskops, P., Schmidt, R., Stolwijk, L. J., de Lange, S. C., Išgum, I., de Vries, L. S., Benders, M. J. N. L., et al. (2018) · Pediatric Research · doi:10.1038/s41390-018-0138-1 · Cited by 18 · see citing works

Integrin‐linked kinase regulates oligodendrocyte cytoskeleton, growth cone, and adhesion dynamics

Michalski, J., Cummings, S. E., O’Meara, R. W., & Kothary, R. (2015) · Journal of Neurochemistry · doi:10.1111/jnc.13446 · Cited by 17 · see citing works

Laminin α2 controls mouse and human stem cell behaviour during midbrain dopaminergic neuron development

Ahmed, M., Marziali, L. N., Arenas, E., Feltri, M. L., & ffrench‐Constant, C. (2019) · Development · doi:10.1242/dev.172668 · Cited by 16 · see citing works

Peripheral nerve pathology, including aberrant Schwann cell differentiation, is ameliorated by doxycycline in a laminin- 2-deficient mouse model of congenital muscular dystrophy

Homma, S. T., Beermann, M. L., & Miller, J. B. (2011) · Human Molecular Genetics · doi:10.1093/hmg/ddr168 · Cited by 16 · see citing works

GPR126: A novel candidate gene implicated in autosomal recessive intellectual disability

Hosseini, M., Fattahi, Z., Abedini, S. S., Hu, H., Ropers, H., Kalscheuer, V. M., Najmabadi, H., & Kahrizi, K. (2018) · American Journal of Medical Genetics Part A · doi:10.1002/ajmg.a.40531 · Cited by 15 · see citing works

Synaptic plasticity in the dy2J mouse model of laminin α2-deficient congenital muscular dystrophy

Anderson, J. L., Head, S. I., & Morley, J. W. (2005) · Brain Research · doi:10.1016/j.brainres.2005.02.001 · Cited by 13 · see citing works

Improving Reproducibility of Phenotypic Assessments in the DyW Mouse Model of Laminin-α2 Related Congenital Muscular Dystrophy

Willmann, R., Gordish‐Dressman, H., Meinen, S., Rüegg, M. A., Yu, Q., Nagaraju, K., Kumar, A., Girgenrath, M., Coffey, C. B. M., Cruz, V., et al. (2017) · Journal of Neuromuscular Diseases · doi:10.3233/jnd-170217 · Cited by 11 · see citing works

MR spectroscopy and diffusion tensor imaging of the brain in congenital muscular dystrophy with merosin deficiency: Metabolite level decreases, fractional anisotropy decreases, and apparent diffusion coefficient increases in the white matter

Sijens, P. E., Fock, J. M., Meiners, L. C., Potze, J.-H., Irwan, R., & Oudkerk, M. (2006) · Brain and Development · doi:10.1016/j.braindev.2006.10.004 · Cited by 10 · see citing works

Localization of laminin chains in the human retina: possible implications for congenital muscular dystrophy associated with α2-chain of laminin deficiency

Toti, P., Felice, C. D., Malandrini, A., Megha, T., Cardone, C., & Villanova, M. (1997) · Neuromuscular Disorders · doi:10.1016/s0960-8966(96)00399-9 · Cited by 8 · see citing works

Kinetic analysis of regulated myosin ATPase activity using single and limited turnover assays

Ankrett, R. J., Walmsley, A. R., & Bagshaw, C. R. (1991) · Journal of Cell Science · doi:10.1242/jcs.1991.supplement_14.1 · Cited by 8 · see citing works

The reciprocal change of neurotrophin-4 and glial cell line-derived neurotrophic factor protein in the muscles, spinal cord and cerebellum of the dy mouse

Sakuma, K., Watanabe, K., Totsuka, T., Sano, M., Nakano, H., Nakao, R., Nishikawa, J., Sorimachi, Y., Yoshimoto, K., & Yasuhara, M. (2002) · Acta Neuropathologica · doi:10.1007/s00401-002-0576-y · Cited by 7 · see citing works

Merosin-Deficient Congenital Muscular Dystrophy (MDCMD): A Case Report with MRI, MRS and DTI Findings

Ip, J., Hui, P. K. T., & Lam, W. W. M. (2012) · Journal of Radiology Case Reports · doi:10.3941/jrcr.v6i8.997 · Cited by 5 · see citing works

Challenges and progress in the diagnosis of Congenital Muscular Dystrophies

Angelini, C. I. (2016) · Expert Opinion on Orphan Drugs · doi:10.1517/21678707.2016.1145587 · Cited by 4 · see citing works

A guide to the composition and functions of the extracellular matrix

Karamanos, N. K., Theocharis, A. D., Piperigkou, Z., Manou, D., Passi, A. G., Skandalis, S. S., Vynios, D. H., Orian‐Rousseau, V., Ricard‐Blum, S., Schmelzer, C. E. H., et al. (2021) · FEBS Journal · doi:10.1111/febs.15776 · Cited by 1,100 · see citing works

Congenital muscular dystrophies: What is new?

Zambon, A. A., & Francesco Muntoni, A. (2021) · Neuromuscular Disorders · doi:10.1016/j.nmd.2021.07.009 · Cited by 65 · see citing works

Circumventing the packaging limit of AAV-mediated gene replacement therapy for neurological disorders

Marrone, L., Marchi, P. M., & Azzouz, M. (2022) · Expert Opinion on Biological Therapy · doi:10.1080/14712598.2022.2012148 · Cited by 56 · see citing works

The molecular regulation of oligodendrocyte development and CNS myelination by ECM proteins

Yamada, M., Iwase, M., Sasaki, B., & Suzuki, N. (2022) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2022.952135 · Cited by 24 · see citing works

The alpha7 integrin subunit in astrocytes promotes endothelial blood–brain barrier integrity

Chen, Z., Kelly, J. R., Morales, J. E., Sun, R. C., De, A., Burkin, D. J., & McCarty, J. H. (2023) · Development · doi:10.1242/dev.201356 · Cited by 24 · see citing works

Brain MRI Abnormalities, Epilepsy and Intellectual Disability in LAMA2 Related Dystrophy – a Genotype/Phenotype Correlation

Camelo, C. G., Artilheiro, M. C., Moreno, C. A. M., Ferraciolli, S. F., da Silva, A. M. S., Fernandes, T. R., Lucato, L. T., Rocha, A. J., Reed, U. C., & Zanoteli, E. (2023) · Journal of Neuromuscular Diseases · doi:10.3233/jnd-221638 · Cited by 21 · see citing works

Epilepsy in LAMA2-related muscular dystrophy: A systematic review of the literature

Salvati, A., Bonaventura, E., Sesso, G., Pasquariello, R., & Sicca, F. (2021) · Seizure · doi:10.1016/j.seizure.2021.07.020 · Cited by 17 · see citing works

Pharmacotherapeutic Approaches to Treatment of Muscular Dystrophies

Rawls, A., Diviak, B. K., Smith, C. I., Severson, G. W., Acosta, S. A., & Wilson‐Rawls, J. (2023) · Biomolecules · doi:10.3390/biom13101536 · Cited by 20 · see citing works

Unique genotype-phenotype correlations within LAMA2-related limb girdle muscular dystrophy in Chinese patients

Huang, X., Tan, D., Zhang, Z., Lin, G., Liu, J., Ding, J., Yang, H., Wei, C., Chang, X., Yuan, Y., et al. (2023) · Frontiers in Neurology · doi:10.3389/fneur.2023.1158094 · Cited by 11 · see citing works

Microfluidics for brain endothelial cell-astrocyte interactions

Sanapathi, J., Vipparthi, P., Mishra, S., Sosnik, A., & Kumarasamy, M. (2023) · Organs-on-a-Chip · doi:10.1016/j.ooc.2023.100033 · Cited by 11 · see citing works

Laminin-dystroglycan mediated ferroptosis in hemorrhagic shock and reperfusion induced-cognitive impairment through AMPK/Nrf2

Xu, A., Yuan, K., Xue, S., Lü, W., Wu, X., Liu, W., Xue, Q., Liu, L., Hu, J., Guo, L., et al. (2025) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2025.01.046 · Cited by 9 · see citing works

Whole exome sequencing identified a novel LAMA2 frameshift variant causing merosin-deficient congenital muscular dystrophy in a patient with cardiomyopathy, and autism-like behavior

Nouri, Z. H. M., Sarmadi, A., Narrei, S., Sehhati, M., & Tabatabaiefar, M. A. (2022) · Neuromuscular Disorders · doi:10.1016/j.nmd.2022.07.400 · Cited by 7 · see citing works

RNA-binding proteins potentially regulate the alternative splicing of apoptotic genes during knee osteoarthritis progression

Zhang, Z., Dong, L., Tao, H., Dong, Y., Xiang, W., Tao, F., & Zhao, Y. (2024) · BMC Genomics · doi:10.1186/s12864-024-10181-w · Cited by 7 · see citing works

Extension of the Clinicoradiologic Spectrum of Newly Described End-Truncating LAMB1 Variations

Morel, H., Bailly, L., Urbanczyk, C., Hervé, D., Berroir, S., Bouc, R. L., Lévy, R., Meyer, M., Aloui, C., Tournier‐Lasserve, E., et al. (2023) · Neurology Genetics · doi:10.1212/nxg.0000000000200069 · Cited by 6 · see citing works

Faster progression to multiple sclerosis disability is linked to neuronal pathways associated with neurodegeneration: An ethnicity study

Harari, G., Gurevich, M., Dolev, M., Falb, R., & Achiron, A. (2023) · PLoS ONE · doi:10.1371/journal.pone.0280515 · Cited by 4 · see citing works

Bioinformatics analysis of potential key genes and mechanisms in type 2 diabetes mellitusPreprint

Vastrad, B. M., & Vastrad, C. M. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.03.28.437386 · Cited by 3 · see citing works

Neuromuscular disorders with evidence of both neuropathic and myopathic phenotype

Laurini, C., Bosco, L., Zambon, A. A., Sorrenti, B., Falzone, Y., & Previtali, S. C. (2025) · Brain · doi:10.1093/brain/awaf399 · Cited by 2 · see citing works

The landscape of pediatric genetic white matter disorders at a tertiary referral hospital in Upper Egypt and the report of 31 novel variants

Noureldeen, M. M., Zaki, M. S., Rafat, K., Abdel‐Hamid, M. S., & Salem, A. M. S. (2025) · The Italian Journal of Pediatrics/Italian journal of pediatrics · doi:10.1186/s13052-025-02031-6 · Cited by 2 · see citing works

A Novel Mouse Model for LAMA2-Related Muscular Dystrophy: Analysis of Molecular Pathogenesis and Clinical PhenotypePreprint

Tan, D., Liu, Y., Luo, H., Shen, Q., Long, X., Xu, L., Liu, J., Zhong, N. A., Zhang, H., & Xiong, H. (2024) · eLife · doi:10.7554/elife.94288.1 · Cited by 2 · see citing works

A novel mouse model for LAMA2-related muscular dystrophy with analysis of molecular pathogenesis and clinical phenotypePreprint

Tan, D., Liu, Y., Luo, H., Shen, Q., Long, X., Xu, L., Liu, J., Zhong, N. A., Zhang, H., & Xiong, H. (2024) · eLife · doi:10.7554/elife.94288 · Cited by 2 · see citing works

LAMA2-related muscular dystrophy mimicking multiple sclerosis

Koshorek, J., Sobreira, N. L. D. M., & Saidha, S. (2022) · BMJ Case Reports · doi:10.1136/bcr-2022-249061 · Cited by 1 · see citing works

A novel mouse model for LAMA2-related muscular dystrophy with analysis of molecular pathogenesis and clinical phenotype

Tan, D., Liu, Y., Luo, H., Shen, Q., Long, X., Xu, L., Liu, J., Zhong, N. A., Zhang, H., & Xiong, H. (2025) · eLife · doi:10.7554/elife.94288.4 · Cited by 1 · see citing works

Epilepsy, epileptiform discharges and features of brain magnetic resonance imaging in merosin-deficient muscular dystrophy

Monakhova, А. V., Белоусова, Е. Д., & Казбулатовна, Г. З. (2025) · Epilepsy and Paroxysmal Conditions · doi:10.17749/2077-8333/epi.par.con.2025.213 · Cited by 1 · see citing works

283rd ENMC international workshop: Establishing expert care recommendations for LAMA2-RD: A prototype for the development of congenital muscular dystrophy subtype-specific care guidelines. Hoofddorp, The Netherlands, January 17th-19th 2025

Zambon, A. A., Klein, A., Sárközy, A., Foley, A. R., Alfano, L., Bönnemann, C., Camelo, C. G., Cicala, G., Chiusolo, F., de Laat, I., et al. (2025) · Neuromuscular Disorders · doi:10.1016/j.nmd.2025.106220 · Cited by 1 · see citing works

Roles and therapeutic prospects of the laminin family in disorders of the nervous system

Zhang, X., Li, X., Gao, L., Qiao, Y., Lv, B., Zhang, Q. D., Zhang, M., Yu, J., Li, H., Bi, H., et al. (2026) · Journal of Translational Medicine · doi:10.1186/s12967-026-08410-9 · Cited by 2 · see citing works

LAMA2 -Related Muscular Dystrophy: The Importance of Accurate Phenotyping and Brain Imaging in the Diagnosis of LGMD

Stojkovic, T., Masingue, M., Métay, C., Romero, N. B., Eymard, B., Yaou, R. B., Rialland, L., Drunat, S., Gartioux, C., Nelson, I. P., et al. (2022) · Journal of Neuromuscular Diseases · doi:10.3233/jnd-221555 · Cited by 1 · see citing works

Muscular Dystrophy: Underlying Cellular and Molecular Mechanisms and Various Nanotherapeutic Approaches for Muscular Dystrophy

Syed, D. S., Khan, M. S., Afnan, U., Dar, M. J., & Maqbool, T. (2024) · Springer eBooks · doi:10.1007/978-981-99-9404-5_7 · Cited by 1 · see citing works

A Novel Mouse Model for LAMA2-Related Muscular Dystrophy: Analysis of Molecular Pathogenesis and Clinical PhenotypePreprint

Tan, D., Liu, Y., Luo, H., Shen, Q., Long, X., Xu, L., Liu, J., Zhong, N. A., Zhang, H., & Xiong, H. (2024) · eLife · doi:10.7554/elife.94288.2 · Cited by 1 · see citing works

Estudo clínico e molecular de pacientes com distrofia muscular relacionada ao gene LAMA2

Camelo, C. G. (2023) · doi:10.11606/t.5.2023.tde-26052023-153344

Atypical Presentation of Congenital Muscular Dystrophy: A LAMA2 Related Muscular Dystrophy

Oswald, S., Finch, M., & Schwaede, A. (2025) · Journal of Child Neurology · doi:10.1177/08830738251333467

A Novel Mouse Model for LAMA2-Related Muscular Dystrophy: Analysis of Molecular Pathogenesis and Clinical PhenotypePreprint

Tan, D., Liu, Y., Luo, H., Shen, Q., Long, X., Xu, L., Liu, J., Zhong, N. A., Zhang, H., & Xiong, H. (2025) · eLife · doi:10.7554/elife.94288.3

Additional file 1 of RNA-binding proteins potentially regulate the alternative splicing of apoptotic genes during knee osteoarthritis progression

Zhang, Z., Dong, L., Tao, H., Dong, Y., Xiang, W., Tao, F., & Zhao, Y. (2024) · Figshare · doi:10.6084/m9.figshare.25440872

Additional file 2 of RNA-binding proteins potentially regulate the alternative splicing of apoptotic genes during knee osteoarthritis progression

Zhang, Z., Dong, L., Tao, H., Dong, Y., Xiang, W., Tao, F., & Zhao, Y. (2024) · Figshare · doi:10.6084/m9.figshare.25441026

Additional file 5 of RNA-binding proteins potentially regulate the alternative splicing of apoptotic genes during knee osteoarthritis progression

Zhang, Z., Dong, L., Tao, H., Dong, Y., Xiang, W., Tao, F., & Zhao, Y. (2024) · Figshare · doi:10.6084/m9.figshare.26695308

Additional file 4 of RNA-binding proteins potentially regulate the alternative splicing of apoptotic genes during knee osteoarthritis progression

Zhang, Z., Dong, L., Tao, H., Dong, Y., Xiang, W., Tao, F., & Zhao, Y. (2024) · Figshare · doi:10.6084/m9.figshare.26695302

Additional file 3 of RNA-binding proteins potentially regulate the alternative splicing of apoptotic genes during knee osteoarthritis progression

Zhang, Z., Dong, L., Tao, H., Dong, Y., Xiang, W., Tao, F., & Zhao, Y. (2024) · Figshare · doi:10.6084/m9.figshare.26695299

Central T3 deprivation disturbs cortical cilia formation, oligodendrocyte lineage and neuronal cell-cell-communication in a MCT8/OATP1C1 deficient Allan-Herndon-Dudley Syndrome mouse modelPreprint

Molenaar, A., Pathak, E., Bernecker, M., Mallet, N., Gutiérrez‐Aguilar, R., Castillejo, C. M., Lutter, D., Angelis, M. D., Maity‐Kumar, G., Kuehnen, P., et al. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2025.12.23.696195

Central Thyroid Hormone Deprivation Disrupts Cortical Cilia and Oligodendrocyte Lineage in an Allan–Herndon–Dudley Syndrome Mouse Model

Molenaar, A., Pathak, E., Bernecker, M., Mallet, N., Gutiérrez‐Aguilar, R., Castillejo, C. M., Lutter, D., Angelis, M. D., Maity‐Kumar, G., Kühnen, P., et al. (2026) · Thyroid · doi:10.1177/10507256261475205

Laminin-α2 deficiency is associated with altered multiorgan redox signatures

Martins, S. G., Pita, M., Naidu, S. D., Ribeiro, V., Lameirão-Ferreira, H., Gravato, C., Dinkova‐Kostova, A. T., Þorsteinsdóttir, S., & Carlos, A. R. (2026) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2026.10.042

The evolving spectrum of LAMA2 related congenital muscular dystrophy (MDC1)-Case series and review of literature

Sinha, R. J., Singh, S., Tiwari, M., Luhar, Z., Meena, A. K., Wander, A., & Soneji, D. (2025) · Brain Disorders · doi:10.1016/j.dscb.2025.100181 · Cited by 3 · see citing works

Central nervous system involvement and the genotype-phenotype correlation in CMD-LAMA2

Camelo, C. G., Artilheiro, M. C., Moreno, C. A. M., Ferraciolli, S. F., da Silva, A. M. S., Lucato, L. T., Rocha, A. J., Reed, U. C., & Zanoteli, E. (2023) · Arquivos de Neuro-Psiquiatria · doi:10.1055/s-0043-1774420

Cobblestone Malformation in LAMA2 Congenital Muscular Dystrophy (MDC1A)

Jayakody, H., Zarei, S., Nguyen, H., Dalton, J. C., Chen, K. S., Hudgins, L., Day, J., Withrow, K., Pandya, A., Teasley, J., et al. (2020) · Journal of Neuropathology & Experimental Neurology · doi:10.1093/jnen/nlaa062 · Cited by 20 · see citing works

C.P.2.13 Widening the LAMA2 mutation spectrum in MDC1A patients: New mutations including gross deletions

Oliveira, J., Soares‐Silva, I., Jorge, P., Vieira, E., Oliveira, M. E., & Santos, R. (2007) · Neuromuscular Disorders · doi:10.1016/j.nmd.2007.06.289

CONGENITAL MUSCULAR DYSTROPHIES WITH STRUCTURAL BRAIN INVOLVEMENT: THE ROLE OF BRAIN MRI

Vajsar, J. (2006) · Neuropediatrics · doi:10.1055/s-2006-943553