Defective membrane repair in dysferlin-deficient muscular dystrophy

Dystrophin protects the sarcolemma from stresses developed during muscle contraction

Petrof, B. J., Shrager, J. B., Stedman, H. H., Kelly, A. M., & Sweeney, H. L. (1993) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.90.8.3710 · Cited by 1,526

Plasma Membrane Repair Is Mediated by Ca2+-Regulated Exocytosis of Lysosomes

Reddy, A. J., Caler, E. V., & Andrews, N. W. (2001) · Cell · doi:10.1016/s0092-8674(01)00421-4 · Cited by 1,043

Deficiency of a glycoprotein component of the dystrophin complex in dystrophic muscle

Ervasti, J. M., Ohlendieck, K., Kahl, S. D., Gaver, M. G., & Campbell, K. P. (1990) · Nature · doi:10.1038/345315a0 · Cited by 1,033

Dysferlin, a novel skeletal muscle gene, is mutated in Miyoshi myopathy and limb girdle muscular dystrophy

Liu, J., Aoki, M., Illa, I., Wu, C., Fardeau, M., Angelini, C. I., Serrano, C., Urtizberea, J. A., Hentati, F., Hamida, M. B., et al. (1998) · Nature Genetics · doi:10.1038/1682 · Cited by 919

A gene related to Caenorhabditis elegans spermatogenesis factor fer-1 is mutated in limb-girdle muscular dystrophy type 2B

Bashir, R., Britton, S., Strachan, T., Keers, S. M., Vafiadaki, E., Lako, M., Richard, I., Marchand, S., Bourg, N., Argov, Z., et al. (1998) · Nature Genetics · doi:10.1038/1689 · Cited by 685

The Laminin α Chains: Expression, Developmental Transitions, and Chromosomal Locations of α1-5, Identification of Heterotrimeric Laminins 8–11, and Cloning of a Novel α3 Isoform

Miner, J. H., Patton, B. L., Lentz, S. I., Gilbert, D. J., Snider, W. D., Jenkins, N. A., Copeland, N. G., & Sanes, J. R. (1997) · The Journal of Cell Biology · doi:10.1083/jcb.137.3.685 · Cited by 650

Molecular basis of muscular dystrophies

Cohn, R. D., & Campbell, K. P. (2000) · Muscle & Nerve · doi:10.1002/1097-4598(200010)23:10 · Cited by 538

Cell Membrane Resealing by a Vesicular Mechanism Similar to Neurotransmitter Release

Steinhardt, R. A., Bi, G., & Alderton, J. M. (1994) · Science · doi:10.1126/science.7904084 · Cited by 530

Animal models for muscular dystrophy show different patterns of sarcolemmal disruption

Straub, V., Rafael, J. A., Chamberlain, J. S., & Campbell, K. P. (1997) · The Journal of Cell Biology · doi:10.1083/jcb.139.2.375 · Cited by 488

Muscular dystrophies involving the dystrophin–glycoprotein complex: an overview of current mouse models

Durbeej, M., & Campbell, K. P. (2002) · Current Opinion in Genetics & Development · doi:10.1016/s0959-437x(02)00309-x · Cited by 434

Dysferlin Forms a Dimer Mediated by the C2 Domains and the Transmembrane Domain In Vitro and in Living Cells

Xu, L. M., Pallikkuth, S., Hou, Z., Mignery, G. A., Robia, S. L., & Han, R. (2011) · PLoS ONE · doi:10.1371/journal.pone.0027884 · Cited by 36

Myofiber Damage Precedes Macrophage Infiltration after in Vivo Injury in Dysferlin-Deficient A/J Mouse Skeletal Muscle

Roche, J. A., Tulapurkar, M. E., Mueller, A. L., van Rooijen, N., Hasday, J. D., Lovering, R. M., & Bloch, R. J. (2015) · American Journal Of Pathology · doi:10.1016/j.ajpath.2015.02.020 · Cited by 36

Dysferlin mutations and mitochondrial dysfunction

Vincent, A. E., Rosa, H. S., Alston, C. L., Grady, J. P., Rygiel, K. A., Rocha, M. C., Barresi, R., Taylor, R. W., & Turnbull, D. M. (2016) · Neuromuscular Disorders · doi:10.1016/j.nmd.2016.08.008 · Cited by 36

Coupling of excitation to Ca2+release is modulated by dysferlin

Lukyanenko, V. I., Muriel, J. M., & Bloch, R. J. (2017) · The Journal of Physiology · doi:10.1113/jp274515 · Cited by 36

Cardiac Muscle Membrane Stabilization in Myocardial Reperfusion Injury

Houang, E. M., Bartos, J. A., Hackel, B. J., Lodge, T. P., Yannopoulos, D., Bates, F. S., & Metzger, J. M. (2019) · JACC Basic to Translational Science · doi:10.1016/j.jacbts.2019.01.009 · Cited by 36

Defective membrane repair machinery impairs survival of invasive cancer cells

Bouvet, F., Ros, M., Bonedeau, E., Croissant, C., Frelin, L., Saltel, F., Moreau, V., & Bouter, A. (2020) · Scientific Reports · doi:10.1038/s41598-020-77902-5 · Cited by 36

The muscle protein dysferlin accumulates in the Alzheimer brain

Galvin, J. E., Palamand, D., Strider, J., Milone, M., & Pestronk, A. (2006) · Acta Neuropathologica · doi:10.1007/s00401-006-0147-8 · Cited by 36

Dysferlinopathy: Spectrum of pathological changes in skeletal muscle tissue

Gayathri, N., Alefia, R., Nalini, A., Yasha, T. C., Anita, M., Santosh, V., & Shankar, S. (2011) · Indian Journal of Pathology and Microbiology · doi:10.4103/0377-4929.81636 · Cited by 36

Dysferlin‐deficient muscular dystrophy and innate immune activation

Mariano, A. T., Henning, A., & Han, R. (2013) · FEBS Journal · doi:10.1111/febs.12261 · Cited by 36

Myoferlin gene silencing decreases Tie-2 expression in vitro and angiogenesis in vivo

Yu, C., Sharma, A., Trane, A., Utokaparch, S., Leung, C., & Bernatchez, P. N. (2011) · Vascular Pharmacology · doi:10.1016/j.vph.2011.04.001 · Cited by 36

Two-photon absorption of metal–organic DNA-probes

Hańczyc, P., Nordén, B., & Samoc, M. J. (2012) · Dalton Transactions · doi:10.1039/c2dt12264b · Cited by 35

Fam65b is important for formation of the HDAC6‐dysferlin protein complex during myogenic cell differentiation

Balasubramanian, A., Kawahara, G., Gupta, V., Rozkalne, A., Beauvais, A., Kunkel, L. M., & Gussoni, E. (2014) · The FASEB Journal · doi:10.1096/fj.13-246470 · Cited by 35

The ties that bind: functional clusters in limb-girdle muscular dystrophy

Barton, E. R., Pacak, C. A., Stoppel, W. L., & Kang, P. B. (2020) · Skeletal Muscle · doi:10.1186/s13395-020-00240-7 · Cited by 35

Skeletal muscle explants: ex-vivo models to study cellular behavior in a complex tissue environment

Smith, L., & Meyer, G. A. (2019) · Connective Tissue Research · doi:10.1080/03008207.2019.1662409 · Cited by 37

Testis-enriched ferlin, FER1L5, is required for Ca 2+ -activated acrosome reaction and male fertility

Morohoshi, A., Miyata, H., Tokuhiro, K., Iida‐Norita, R., Noda, T., Fujihara, Y., & Ikawa, M. (2023) · Science Advances · doi:10.1126/sciadv.ade7607 · Cited by 34

A Plasma Membrane Wound Proteome

Mellgren, R. L. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.110015 · Cited by 34

While Dysferlin and Myoferlin Are Coexpressed in the Human Placenta, Only Dysferlin Expression Is Responsive to Trophoblast Fusion in Model Systems1

Robinson, J. M., Ackerman, W. E., Behrendt, N. J., & Vandré, D. D. (2009) · Biology of Reproduction · doi:10.1095/biolreprod.108.074591 · Cited by 34

Self-assembly behaviours of primitive and modern lipid membrane solutions: a coarse-grained molecular simulation study

Arai, N., Yoshimoto, Y., Yasuoka, K., & Ebisuzaki, T. (2016) · Physical Chemistry Chemical Physics · doi:10.1039/c6cp02380k · Cited by 34

Phenotypic Drug Screening for Dysferlinopathy Using Patient-Derived Induced Pluripotent Stem Cells

Kokubu, Y., Nagino, T., Sasa, K., Oikawa, T., Miyake, K., Kume, A., Fukuda, M., Fuse, H., Tozawa, R., & Sakurai, H. (2019) · Stem Cells Translational Medicine · doi:10.1002/sctm.18-0280 · Cited by 34

Annexin-A6 in Membrane Repair of Human Skeletal Muscle Cell: A Role in the Cap Subdomain

Croissant, C., Gounou, C., Bouvet, F., Tan, S., & Bouter, A. (2020) · Cells · doi:10.3390/cells9071742 · Cited by 33

Secreted acid sphingomyelinase as a potential gene therapy for limb girdle muscular dystrophy 2B

Bittel, D. C., Sreetama, S. C., Chandra, G., Ziegler, R. J., Nagaraju, K., der Meulen, J. H. V., & Jaiswal, J. K. (2022) · Journal of Clinical Investigation · doi:10.1172/jci141295 · Cited by 33

Fetuin A Stabilizes m-Calpain and Facilitates Plasma Membrane Repair

Mellgren, R. L., & Huang, X. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m706929200 · Cited by 33

"Sr stress" in mixed hindlimb muscles of aging Male rats

Russ, D. W., Krause, J., Wills, A., & Arreguin, R. (2012) · Biogerontology · doi:10.1007/s10522-012-9399-y · Cited by 32

Reverse Engineering Gene Network Identifies New Dysferlin-interacting Proteins

Cacciottolo, M., Belcastro, V., Laval, S., Bushby, K. M. D., di Bernardo, D., & Nigro, V. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.173559 · Cited by 32

Stretch-Induced Membrane Damage in Muscle: Comparison of Wild-Type and mdx Mice

Allen, D. G., Zhang, B., & Whitehead, N. P. (2010) · Advances in experimental medicine and biology · doi:10.1007/978-1-4419-6366-6_17 · Cited by 32

Anaesthesia and the sex-linked dystrophies: between a rock and a hard place

Hopkins, P. M. (2010) · British Journal of Anaesthesia · doi:10.1093/bja/aeq036 · Cited by 32

Hip region muscular dystrophy and emergence of motor deficits in dysferlin‐deficient Bla/J mice

Nagy, N., Nonneman, R. J., Llanga, T., Dial, C. F., Riddick, N. V., Hampton, T. G., Moy, S. S., Lehtimäki, K. K., Ahtoniemi, T., Puoliväli, J. T., et al. (2017) · Physiological Reports · doi:10.14814/phy2.13173 · Cited by 32

FerA is a Membrane-Associating Four-Helix Bundle Domain in the Ferlin Family of Membrane-Fusion Proteins

Harsini, F. M., Chebrolu, S., Fuson, K. L., White, M. A., Rice, A. M., & Sutton, R. B. (2018) · Scientific Reports · doi:10.1038/s41598-018-29184-1 · Cited by 32

Actin Polymerization and ESCRT Trigger Recruitment of the Fusogens Syntaxin-2 and EFF-1 to Promote Membrane Repair in C. elegans

Meng, X., Yang, Q., Yu, X., Zhou, J., Ren, X., Zhou, Y., & Xu, S. (2020) · Developmental Cell · doi:10.1016/j.devcel.2020.06.027 · Cited by 32

Sarcolemma wounding activates dynamin‐dependent endocytosis in striated muscle

McDade, J. R., Naylor, M. T., & Michele, D. E. (2021) · The FEBS Journal · doi:10.1111/febs.15556 · Cited by 32

Loss of dysferlin or myoferlin results in differential defects in excitation–contraction coupling in mouse skeletal muscle

Barefield, D. Y., Sell, J. J., Tahtah, I., Kearns, S. D., McNally, E. M., & Demonbreun, A. R. (2021) · Scientific Reports · doi:10.1038/s41598-021-95378-9 · Cited by 32

Cell wounding activates phospholipase D in primary mouse keratinocytes

Arun, S. N., Xie, D., Howard, A. C., Zhong, Q., Zhong, X., McNeil, P. L., & Bollag, W. B. (2013) · Journal of Lipid Research · doi:10.1194/jlr.m027060 · Cited by 32

GRAF1 promotes ferlin-dependent myoblast fusion

Lenhart, K. C., Becherer, A. L., Li, J., Xiao, X., McNally, E. M., Mack, C. P., & Taylor, J. M. (2014) · Developmental Biology · doi:10.1016/j.ydbio.2014.06.025 · Cited by 31

Enhanced Muscular Dystrophy from Loss of Dysferlin Is Accompanied by Impaired Annexin A6 Translocation after Sarcolemmal Disruption

Demonbreun, A. R., Allen, M. V., Warner, J. L., Barefield, D. Y., Krishnan, S., Swanson, K. E., Earley, J. U., & McNally, E. M. (2016) · American Journal Of Pathology · doi:10.1016/j.ajpath.2016.02.005 · Cited by 31

Muscular dystrophy modeling in zebrafish

Li, M., Hromowyk, K. J., Amacher, S. L., & Currie, P. D. (2016) · Methods in cell biology · doi:10.1016/bs.mcb.2016.11.004 · Cited by 31

Whole exome sequencing identifies novel predisposing genes in neural tube defects

Lemay, P., Marco, P. D., Traverso, M., Merello, E., Dionne‐Laporte, A., Spiegelman, D., Henrion, É., Diallo, O., Audibert, F., Michaud, J. L., et al. (2018) · Molecular Genetics & Genomic Medicine · doi:10.1002/mgg3.467 · Cited by 31

Myoferlin, a Membrane Protein with Emerging Oncogenic Roles

Dong, Y., Kang, H., Liu, H., Wang, J., Guo, Q., Song, C., Sun, Y., Zhang, Y., Zhang, H., Zhang, Z., et al. (2019) · BioMed Research International · doi:10.1155/2019/7365913 · Cited by 31

Surface-associated antigen induces permeabilization of primary mouse B-cells and lysosome exocytosis facilitating antigen uptake and presentation to T-cells

Maeda, F. Y., van Haaren, J. J., Langley, D. B., Christ, D., Andrews, N. W., & Song, W. (2021) · eLife · doi:10.7554/elife.66984 · Cited by 31

Mechanism of action and therapeutic route for a muscular dystrophy caused by a genetic defect in lipid metabolism

Tavasoli, M., Lahire, S., Sokolenko, S., Novorolsky, R. J., Reid, S. A., Lefsay, A., Otley, M. O. C., Uaesoontrachoon, K., Rowsell, J., Srinivassane, S., et al. (2022) · Nature Communications · doi:10.1038/s41467-022-29270-z · Cited by 31

Proteomics of the Human Placenta: Promises and Realities

Robinson, J. M., Ackerman, W. E., Kniss, D. A., Takizawa, T., & Vandré, D. D. (2008) · Placenta · doi:10.1016/j.placenta.2007.12.005 · Cited by 31

Actuated tissue engineered muscle grafts restore functional mobility after volumetric muscle loss

Rousseau, E. B., Raman, R., Tamir, T. Y., Bu, A., Srinivasan, S. S., Lynch, N., Langer, R., White, F. M., & Cima, M. J. (2023) · Biomaterials · doi:10.1016/j.biomaterials.2023.122317 · Cited by 30

Genetic silencing of Nrf2 enhances X-ROS in dysferlin-deficient muscle

Kombairaju, P., Kerr, J. P., Roche, J. A., Pratt, S. J. P., Lovering, R. M., Sussan, T. E., Kim, J., Shi, G., Biswal, S. S., & Ward, C. W. (2014) · Frontiers in Physiology · doi:10.3389/fphys.2014.00057 · Cited by 30

Full-length Dysferlin Transfer by the Hyperactive Sleeping Beauty Transposase Restores Dysferlin-deficient Muscle

Escobar, H., Schoewel, V., Spuler, S., Marg, A., & Izsvák, Z. (2016) · Molecular Therapy — Nucleic Acids · doi:10.1038/mtna.2015.52 · Cited by 30

Cardiomyocyte damage control in heart failure and the role of the sarcolemma

Kitmitto, A., Baudoin, F., & Cartwright, E. J. (2019) · Journal of Muscle Research and Cell Motility · doi:10.1007/s10974-019-09539-5 · Cited by 30

Multiple poloxamers increase plasma membrane repair capacity in muscle and nonmuscle cells

Kwiatkowski, T. A., Rose, A., Jung, R., Capati, A., Hallak, D., Yan, R., & Weisleder, N. L. (2019) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00321.2019 · Cited by 30

A placental sub-proteome: The apical plasma membrane of the syncytiotrophoblast

Vandré, D. D., Ackerman, W. E., Tewari, A., Kniss, D. A., & Robinson, J. M. (2012) · Placenta · doi:10.1016/j.placenta.2011.12.010 · Cited by 30

Variations in gene expression among different types of human skeletal muscle

Kang, P. B., Kho, A. T., Sanoudou, D., Haslett, J. N., Dow, C. P., Han, M., Blasko, J., Lidov, H. G. W., Beggs, A. H., & Kunkel, L. M. (2005) · Muscle & Nerve · doi:10.1002/mus.20356 · Cited by 30

Pex24 and Pex32 are required to tether peroxisomes to the ER for organelle biogenesis, positioning and segregation in yeast

Wu, F., de Boer, R., Krikken, A. M., Akşit, A., Bordin, N., Devos, D. P., & van der Klei, I. J. (2020) · Journal of Cell Science · doi:10.1242/jcs.246983 · Cited by 31

AHNAK1 and AHNAK2 are costameric proteins: AHNAK1 affects transverse skeletal muscle fiber stiffness

Marg, A., Haase, H., Neumann, T., Kouno, M., & Morano, I. L. (2010) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2010.09.030 · Cited by 30

Muscle protein analysis in the detection of heterozygotes for recessive limb girdle muscular dystrophy type 2B and 2E

Fanin, M., Nascimbeni, A. C., & Angelini, C. I. (2006) · Neuromuscular Disorders · doi:10.1016/j.nmd.2006.06.010 · Cited by 30

Absence of T and B lymphocytes modulates dystrophic features in dysferlin deficient animal model

Farini, A., Sitzia, C., Navarro, C. L., D’Antona, G., Belicchi, M., Parolini, D., Fraro, G. D., Razini, P., Bottinelli, R., Meregalli, M., et al. (2012) · Experimental Cell Research · doi:10.1016/j.yexcr.2012.03.010 · Cited by 31

The C2 domains of dysferlin: roles in membrane localization, Ca2+ signalling and sarcolemmal repair

Muriel, J. M., Lukyanenko, V. I., Kwiatkowski, T., Bhattacharya, S., Garman, D., Weisleder, N. L., & Bloch, R. J. (2022) · The Journal of Physiology · doi:10.1113/jp282648 · Cited by 29

Chapter 5 Spatiotemporal Dynamics of the ER‐derived Peroxisomal Endomembrane System

Titorenko, V. I., & Rachubinski, R. A. (2008) · International review of cytology · doi:10.1016/s1937-6448(08)01605-5 · Cited by 29

Identification of Splicing Defects Caused by Mutations in the Dysferlin Gene

Kergourlay, V., Raï, G., Blandin, G., Salgado, D., Béroud, C., Lévy, N., Krahn, M., & Bartoli, M. (2014) · Human Mutation · doi:10.1002/humu.22710 · Cited by 29

Diaphragm displays early and progressive functional deficits in dysferlin‐deficient mice

Barton, E. R., Wang, B. J., Brisson, B. K., & Sweeney, H. L. (2010) · Muscle & Nerve · doi:10.1002/mus.21645 · Cited by 29

Dysferlinopathy: mitochondrial abnormalities in human skeletal muscle

Liu, F., Lou, J., Zhao, D., Li, W., Zhao, Y., Sun, X., & Yan, C. (2015) · International Journal of Neuroscience · doi:10.3109/00207454.2015.1034801 · Cited by 29

Multiple C2 domains transmembrane protein 1 is expressed in CNS neurons and possibly regulates cellular vesicle retrieval and oxidative stress

Qiu, L., Yu, H., & Liang, F. (2015) · Journal of Neurochemistry · doi:10.1111/jnc.13251 · Cited by 29

Loss of calpains-1 and -2 prevents repair of plasma membrane scrape injuries, but not small pores, and induces a severe muscular dystrophy

Piper, A., Sophocleous, R. A., Ross, S. E., Evesson, F. J., Saleh, O., Bournazos, A., Yasa, J., Reed, C. E., Woolger, N., Sluyter, R., et al. (2020) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00408.2019 · Cited by 28

S1P lyase in skeletal muscle regeneration and satellite cell activation: Exposing the hidden lyase

Saba, J. D., & de la Garza-Rodea, A. S. (2012) · Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids · doi:10.1016/j.bbalip.2012.06.009 · Cited by 28

Nitric oxide donors improve prednisone effects on muscular dystrophy in the mdx mouse diaphragm

Mizunoya, W., Upadhaya, R., Burczynski, F. J., Wang, G., & Anderson, J. E. (2011) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00482.2010 · Cited by 28

Lipid raft–dependent plasma membrane repair interferes with the activation of B lymphocytes

Miller, H. E., Castro‐Gomes, T., Corrotte, M., Tam, C. C., Maugel, T. K., Andrews, N. W., & Song, W. (2015) · The Journal of Cell Biology · doi:10.1083/jcb.201505030 · Cited by 28

Dual function of MG53 in membrane repair and insulin signaling

Tan, T., Ko, Y., & Ma, J. (2016) · BMB Reports · doi:10.5483/bmbrep.2016.49.8.079 · Cited by 28

Dysferlin Gene Mutation Spectrum in a Large Cohort of Chinese Patients with Dysferlinopathy

Jin, S., Yu, M., Zhang, W. Y., Lyu, H., Yuan, Y., & Wang, Z. (2016) · Chinese Medical Journal · doi:10.4103/0366-6999.190671 · Cited by 28

Changes in skeletal muscle expression of AQP1 and AQP4 in dystrophinopathy and dysferlinopathy patients

Au, C. G., Butler, T. L., Egan, J. R., Cooper, S. T., Lo, H. P., Compton, A. G., North, K. N., & Winlaw, D. S. (2008) · Acta Neuropathologica · doi:10.1007/s00401-008-0369-z · Cited by 28

Proteomic investigation of the molecular pathophysiology of dysferlinopathy

Palma, S. D., Morandi, L. O., Mariani, E., Begum, S., Cerretelli, P., Wait, R., & Gelfi, C. (2005) · PROTEOMICS · doi:10.1002/pmic.200500098 · Cited by 28

Titin splicing regulates cardiotoxicity associated with calpain 3 gene therapy for limb-girdle muscular dystrophy type 2A

Lostal, W., Roudaut, C., Faivre, M., Charton, K., Suel, L., Bourg, N., Best, H. A., Smith, J. E., Gohlke, J., Corre, G., et al. (2019) · Science Translational Medicine · doi:10.1126/scitranslmed.aat6072 · Cited by 27

The effects of MyD88 deficiency on disease phenotype in dysferlin‐deficient A/J mice: role of endogenous TLR ligands

Uaesoontrachoon, K., Cha, H., Ampong, B., Sali, A., Vandermeulen, J., Wei, B. P. C., Creeden, B., Huynh, T., Quinn, J., Tatem, K. S., et al. (2013) · The Journal of Pathology · doi:10.1002/path.4207 · Cited by 27

Characterization of zebrafish dysferlin by morpholino knockdown

Kawahara, G., Serafini, P. R., Myers, J. A., Alexander, M. S., & Kunkel, L. M. (2011) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2011.08.105 · Cited by 27

Therapy Insight: cardiovascular complications associated with muscular dystrophies

McNally, E. M., & MacLeod, H. M. (2005) · Nature Clinical Practice Cardiovascular Medicine · doi:10.1038/ncpcardio0213 · Cited by 27

DNA Electroporation, Isolation and Imaging of Myofibers

Demonbreun, A. R., & McNally, E. M. (2015) · Journal of Visualized Experiments · doi:10.3791/53551 · Cited by 27

Inflammation in Skeletal Muscle Regeneration

Tidball, J. G. (2008) · Springer eBooks · doi:10.1007/978-1-4020-6768-6_12 · Cited by 27

Ferlin Overview: From Membrane to Cancer Biology

Peulen, O., Rademaker, G., Anania, S., Turtoï, A., Bellahcène, A., & Castronovo, V. (2019) · Cells · doi:10.3390/cells8090954 · Cited by 27

PTEN Inhibition Ameliorates Muscle Degeneration and Improves Muscle Function in a Mouse Model of Duchenne Muscular Dystrophy

Yue, F., Song, C., Huang, D., Narayanan, N., Qiu, J., Jia, Z., Yuan, Z., Oprescu, S. N., Roseguini, B. T., Deng, M., et al. (2020) · Molecular Therapy · doi:10.1016/j.ymthe.2020.09.029 · Cited by 28

Genetic modifiers of muscular dystrophy: Implications for therapy

Heydemann, A., Doherty, K. R., & McNally, E. M. (2006) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2006.06.013 · Cited by 28

Proteomic identification of dysferlin-interacting protein complexes in human vascular endothelium

Leung, C., Utokaparch, S., Sharma, A., Yu, C., Abraham, T., Borchers, C. H., & Bernatchez, P. N. (2011) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2011.10.031 · Cited by 26

Abnormal Excitation-Contraction Coupling and Calcium Homeostasis in Myopathies and Cardiomyopathies

Schartner, V., Laporte, J., & Böhm, J. (2019) · Journal of Neuromuscular Diseases · doi:10.3233/jnd-180314 · Cited by 29

Ahnak1 abnormally localizes in muscular dystrophies and contributes to muscle vesicle release

Zacharias, U., Purfürst, B., Schoewel, V., Morano, I. L., Spuler, S., & Haase, H. (2011) · Journal of Muscle Research and Cell Motility · doi:10.1007/s10974-011-9271-8 · Cited by 26

Heterogeneous Characteristics of Korean Patients with Dysferlinopathy

Park, H. J., Hong, J., Suh, G. I., Shin, H. Y., Kim, S. M., Sunwoo, I. N., Suh, B. C., & Choi, Y. (2012) · Journal of Korean Medical Science · doi:10.3346/jkms.2012.27.4.423 · Cited by 26

Genetic profile for suspected dysferlinopathy identified by targeted next-generation sequencing

Izumi, R., Niihori, T., Takahashi, T., Suzuki, N., Tateyama, M., Watanabe, C., Sugie, K., Nakanishi, H., Sobue, G., Kato, M., et al. (2015) · Neurology Genetics · doi:10.1212/nxg.0000000000000036 · Cited by 26

Early ultrastructural events of skeletal muscle damage following cardiotoxin-induced injury and glycerol-induced injury

Mahdy, M. A. A., Warita, K., & Hosaka, Y. Z. (2016) · Micron · doi:10.1016/j.micron.2016.09.009 · Cited by 26

A study of wound repair in Dictyostelium cells by using novel laserporation

Pervin, M. S., Itoh, G., Talukder, M. S. U., Fujimoto, K., Morimoto, Y. V., Tanaka, M., Ueda, M., & Yumura, S. (2018) · Scientific Reports · doi:10.1038/s41598-018-26337-0 · Cited by 26

Painful enlargement of the calf muscles in limb girdle muscular dystrophy type 2B (LGMD2B) with a novel compound heterozygous mutation in DYSF

Diers, A., Carl, M., Stoltenburg, G., Vorgerd, M., & Spuler, S. (2006) · Neuromuscular Disorders · doi:10.1016/j.nmd.2006.09.015 · Cited by 26

Developmental and tissue‐specific regulation of a novel dysferlin isoform

Salani, S., Lucchiari, S., Fortunato, F., Crimi, M., Corti, S. P., Locatelli, F., Bossolasco, P., Bresolin, N., & Comi, G. P. (2004) · Muscle & Nerve · doi:10.1002/mus.20106 · Cited by 26

Rapid Increase in Plasma Membrane Chloride Permeability during Wound Resealing in Starfish Oocytes

Fein, A., & Terasaki, M. (2005) · The Journal of General Physiology · doi:10.1085/jgp.200509294 · Cited by 26

Dysferlin rescue by spliceosome-mediated pre-mRNA trans-splicing targeting introns harbouring weakly defined 3′ splice sites

Philippi, S., Lorain, S., Beley, C., Peccate, C., Précigout, G., Spuler, S., & Garcı́a, L. (2015) · Human Molecular Genetics · doi:10.1093/hmg/ddv141 · Cited by 25

Otoferlin as a multirole Ca2+ signaling protein: from inner ear synapses to cancer pathways

Leclere, J.-C., & Dulon, D. (2023) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2023.1197611 · Cited by 25

Endoplasmic reticulum maintains ion homeostasis required for plasma membrane repair

Chandra, G., Sreetama, S. C., Mázala, D. A. G., Charton, K., Vandermeulen, J., Richard, I., & Jaiswal, J. K. (2021) · The Journal of Cell Biology · doi:10.1083/jcb.202006035 · Cited by 25

Direct Evidence That Mutations within Dysferlin’s C2A Domain Inhibit Lipid Clustering

Golbek, T. W., Otto, S. C., Roeters, S. J., Weidner, T., Johnson, C. P., & Baio, J. E. (2020) · The Journal of Physical Chemistry B · doi:10.1021/acs.jpcb.0c07143 · Cited by 24

Muscle is a stage, and cells and factors are merely players

Roman, W., & Muñoz‐Cánoves, P. (2022) · Trends in Cell Biology · doi:10.1016/j.tcb.2022.03.001 · Cited by 25

Childhood Onset of Limb-Girdle Muscular Dystrophy

Rosales, X. Q., & Tsao, C. (2011) · Pediatric Neurology · doi:10.1016/j.pediatrneurol.2011.08.014 · Cited by 24

Emerging role of polymerase-1 and transcript release factor (PTRF/ Cavin-1) in health and disease

Low, J., & Nicholson, H. D. (2014) · Cell and Tissue Research · doi:10.1007/s00441-014-1964-z · Cited by 24

Dual Effects of Exercise in Dysferlinopathy

Biondi, O., Villemeur, M., Marchand, A., Chrétien, F. C., Bourg, N., Gherardi, R. K., Richard, I., & Authier, F. (2013) · American Journal Of Pathology · doi:10.1016/j.ajpath.2013.02.045 · Cited by 24

The absence of dysferlin induces the expression of functional connexin-based hemichannels in human myotubes

Cea, L. A., Bevilacqua, J. A., Arriagada, C., Cárdenas, A. M., Bigot, A., Mouly, V., Sáez, J. C., & Caviedes, P. A. (2016) · BMC Cell Biology · doi:10.1186/s12860-016-0096-6 · Cited by 24

Nerve damage induced skeletal muscle atrophy is associated with increased accumulation of intramuscular glucose and polyol pathway intermediates

Langer, H. T., Afzal, S., Kempa, S., & Spuler, S. (2020) · Scientific Reports · doi:10.1038/s41598-020-58213-1 · Cited by 27

Muscle enzyme and fiber type‐specific sarcomere protein increases in serum after inertial concentric‐eccentric exercise

Carmona, G., Guerrero, M., Cussó, R., Padullés, J. M., Moras, G., Lloret, M., Bedini, J. L., & Cadefau, J. A. (2014) · Scandinavian Journal of Medicine and Science in Sports · doi:10.1111/sms.12363 · Cited by 24

Surface wound healing: a new, general function of eukaryotic cells

Meldolesi, J. (2003) · Journal of Cellular and Molecular Medicine · doi:10.1111/j.1582-4934.2003.tb00220.x · Cited by 24

Redefining the architecture of ferlin proteins: Insights into multi-domain protein structure and function

Dominguez, M. J., McCord, J. J., & Sutton, R. B. (2022) · PLOS ONE · doi:10.1371/journal.pone.0270188 · Cited by 24

Genetic Defects in Muscular Dystrophy

Chandrasekharan, K., & Martin, P. T. (2010) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(10)79017-0 · Cited by 23

Wrecking Repair

(2003) · Science · doi:10.1126/science.300.5624.1343a

Patching Things Up

(2003) · Science Signaling · doi:10.1126/scisignal.1822003tw184 · Cited by 1

Repairing the tears: dysferlin in muscle membrane repair.

Doherty, K. R., & McNally, E. (2003) · Trends in Molecular Medicine · doi:10.1016/s1471-4914(03)00136-9 · Cited by 81

Dysferlin and the plasma membrane repair in muscular dystrophy

Bansal, D., & Campbell, K. P. (2004) · Trends in Cell Biology · doi:10.1016/j.tcb.2004.03.001 · Cited by 333

Dysferlin in Membrane Trafficking and Patch Repair

Glover, L. E., & Brown, R. H. (2007) · Traffic · doi:10.1111/j.1600-0854.2007.00573.x · Cited by 170