Identification of KLHL41 Mutations Implicates BTB-Kelch-Mediated Ubiquitination as an Alternate Pathway to Myofibrillar Disruption in Nemaline Myopathy

Fast and accurate short read alignment with Burrows-Wheeler transform

Li, H., & Durbin, R. (2009) · Bioinformatics · doi:10.1093/bioinformatics/btp324 · Cited by 58,607 · see citing works

ANNOVAR: functional annotation of genetic variants from high-throughput sequencing data

Wang, K., Li, M., & Hakonarson, H. H. (2010) · Nucleic Acids Research · doi:10.1093/nar/gkq603 · Cited by 14,380 · see citing works

Predicting Changes in the Stability of Proteins and Protein Complexes: A Study of More Than 1000 Mutations

Guerois, R., Nielsen, J. E., & Serrano, L. (2002) · Journal of Molecular Biology · doi:10.1016/s0022-2836(02)00442-4 · Cited by 1,728 · see citing works

The kelch repeat superfamily of proteins: propellers of cell function

Adams, J. C., Kelso, R., & Cooley, L. (2000) · Trends in Cell Biology · doi:10.1016/s0962-8924(99)01673-6 · Cited by 603 · see citing works

Mutations in the skeletal muscle α-actin gene in patients with actin myopathy and nemaline myopathy

Nowak, K. J., Wattanasirichaigoon, D., Goebel, H. H., Wilce, M. C. J., Pelin, K., Donner, K. M., Jacob, R. L., Hübner, C., Oexle, K., Anderson, J. R., et al. (1999) · Nature Genetics · doi:10.1038/13837 · Cited by 408 · see citing works

A mutation in the α tropomyosin gene TPM3 associated with autosomal dominant nemaline myopathy

Laing, N. G., Wilton, S. D., Akkari, P. A., Dorosz, S. M., Boundy, K. L., Kneebone, C., Blumbergs, P. C., White, S. J., Watkins, H. C., Love, D. R., et al. (1995) · Nature Genetics · doi:10.1038/ng0195-75 · Cited by 356 · see citing works

Mutations in the nebulin gene associated with autosomal recessive nemaline myopathy

Pelin, K., Hotulainen, P., Donner, K. M., Sewry, C. A., Akkari, P. A., Wilton, S. D., Wattanasirichaigoon, D., Bang, M., Centner, T., Hanefeld, F. A., et al. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.5.2305 · Cited by 336 · see citing works

A Novel Nemaline Myopathy in the Amish Caused by a Mutation in Troponin T1

Johnston, J. J., Kelley, R. I., Crawford, T. O., Morton, D. H., Agarwala, R., Koch, T., Schäffer, A. A., Francomano, C. A., & Biesecker, L. G. (2000) · The American Journal of Human Genetics · doi:10.1086/303089 · Cited by 328 · see citing works

Ubiquitination of Keap1, a BTB-Kelch Substrate Adaptor Protein for Cul3, Targets Keap1 for Degradation by a Proteasome-independent Pathway

Zhang, D. D., Lo, S., Sun, Z., Habib, G. M., Lieberman, M. W., & Hannink, M. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m501279200 · Cited by 299 · see citing works

Structural basis for Cul3 protein assembly with the BTB-Kelch family of E3 ubiquitin ligases

Canning, P., Cooper, C. D. O., Krojer, T., Murray, J. W., Pike, A. C. W., Chaikuad, A., Keates, T., Thangaratnarajah, C., Hojzan, V., Marsden, B. D., et al. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.437996 · Cited by 284 · see citing works

Nemaline myopathy: A clinical study of 143 cases

Ryan, M. M., Schnell, C., Strickland, C. D., Shield, L. K., Morgan, G., Iannaccone, S. T., Laing, N. G., Beggs, A. H., & North, K. N. (2001) · Annals of Neurology · doi:10.1002/ana.1080 · Cited by 278 · see citing works

Update on the Kelch-like (KLHL) gene family

Dhanoa, B. S., Cogliati, T., Satish, A. G., Bruford, E. A., & Friedman, J. S. (2013) · Human Genomics · doi:10.1186/1479-7364-7-13 · Cited by 260 · see citing works

Nemaline Myopathy with Minicores Caused by Mutation of the CFL2 Gene Encoding the Skeletal Muscle Actin–Binding Protein, Cofilin-2

Agrawal, P. B., Greenleaf, R. S., Tomczak, K. K., Lehtokari, V., Wallgren‐Pettersson, C., Wallefeld, W., Laing, N. G., Darras, B. T., Maciver, S. K., Dormitzer, P. R., et al. (2006) · The American Journal of Human Genetics · doi:10.1086/510402 · Cited by 239 · see citing works

Loss of Myotubularin Function Results in T-Tubule Disorganization in Zebrafish and Human Myotubular Myopathy

Dowling, J. J., Vreede, A. P., Low, S. E., Gibbs, E. M., Kuwada, J. Y., Bönnemann, C. G., & Feldman, E. L. (2009) · PLoS Genetics · doi:10.1371/journal.pgen.1000372 · Cited by 235 · see citing works

Mutations in KLHL40 Are a Frequent Cause of Severe Autosomal-Recessive Nemaline Myopathy

Ravenscroft, G., Miyatake, S., Lehtokari, V., Todd, E. J., Vornanen, P., Yau, K. S., Hayashi, Y. K., Miyake, N., Tsurusaki, Y., Doi, H., et al. (2013) · The American Journal of Human Genetics · doi:10.1016/j.ajhg.2013.05.004 · Cited by 226 · see citing works

Dominant Mutations in KBTBD13, a Member of the BTB/Kelch Family, Cause Nemaline Myopathy with Cores

Sambuughin, N., Yau, K. S., Olivé, M., Duff, R. M., Bayarsaikhan, M., Lu, S., González, L., Sivadorai, P., Nowak, K. J., Ravenscroft, G., et al. (2010) · The American Journal of Human Genetics · doi:10.1016/j.ajhg.2010.10.020 · Cited by 163 · see citing works

Nemaline Myopathies

Wallgren‐Pettersson, C., Sewry, C. A., Nowak, K. J., & Laing, N. G. (2011) · Seminars in Pediatric Neurology · doi:10.1016/j.spen.2011.10.004 · Cited by 157 · see citing works

A Splice Site Mutation in Laminin-α2 Results in a Severe Muscular Dystrophy and Growth Abnormalities in Zebrafish

Gupta, V., Kawahara, G., Myers, J. A., Chen, A. T., Hall, T. E., Manzini, M. C., Currie, P. D., Zhou, Y., Zon, L. I., Kunkel, L. M., et al. (2012) · PLoS ONE · doi:10.1371/journal.pone.0043794 · Cited by 111 · see citing works

Discovery of Rare Homozygous Mutations from Studies of Consanguineous Pedigrees

Alkuraya, F. S. (2012) · Current Protocols in Human Genetics · doi:10.1002/0471142905.hg0612s75 · Cited by 106 · see citing works

Congenital Myopathy With Nemaline Rods and Cap Structures Caused by a Mutation in the β-Tropomyosin Gene (TPM2)

Tajsharghi, H., Ohlsson, M., Lindberg, C., & Oldfors, A. (2007) · Archives of Neurology · doi:10.1001/archneur.64.9.1334 · Cited by 102 · see citing works

Analysis of Skeletal Muscle Defects in Larval Zebrafish by Birefringence and Touch-evoke Escape Response Assays

Smith, L. L., Beggs, A. H., & Gupta, V. (2013) · Journal of Visualized Experiments · doi:10.3791/50925 · Cited by 94 · see citing works

New N-RAP-binding partners α-actinin, filamin and Krp1 detected by yeast two-hybrid screening: implications for myofibril assembly

Lu, S., Carroll, S. L., Herrera, A. H., Ozanne, B. W., & Horowits, R. (2003) · Journal of Cell Science · doi:10.1242/jcs.00425 · Cited by 60 · see citing works

Distribution of the endoplasmic reticulum and its relationship with the sarcoplasmic reticulum in skeletal myofibers

Kaisto, T. (2003) · Experimental Cell Research · doi:10.1016/s0014-4827(03)00231-3 · Cited by 59 · see citing works

Autosomal dominant nemaline myopathy with intranuclear rods due to mutation of the skeletal muscle ACTA1 gene: Clinical and pathological variability within a kindred

Hutchinson, D. O., Charlton, A., Laing, N. G., Ilkovski, B., & North, K. N. (2006) · Neuromuscular Disorders · doi:10.1016/j.nmd.2005.11.004 · Cited by 56 · see citing works

Krp1, a novel kelch related protein that is involved in pseudopod elongation in transformed cells

Spence, H. J., Johnston, I., Ewart, K., Buchanan, S. J., FitzGerald, U., & Ozanne, B. W. (2000) · Oncogene · doi:10.1038/sj.onc.1203433 · Cited by 50 · see citing works

Pathological defects in congenital myopathies

Sewry, C. A. (2008) · Journal of Muscle Research and Cell Motility · doi:10.1007/s10974-008-9155-8 · Cited by 50 · see citing works

Myotubularin-Deficient Myoblasts Display Increased Apoptosis, Delayed Proliferation, and Poor Cell Engraftment

Lawlor, M. W., Alexander, M. S., Viola, M. G., Meng, H., Joubert, R., Gupta, V., Motohashi, N., Manfready, R. A., Hsu, C. P., Huang, P. C., et al. (2012) · American Journal Of Pathology · doi:10.1016/j.ajpath.2012.05.016 · Cited by 44 · see citing works

α‐Actinin‐2 deficiency results in sarcomeric defects in zebrafish that cannot be rescued by α‐actinin‐3 revealing functional differences between sarcomeric isoforms

Gupta, V., Discenza, M. N., Guyon, J. R., Kunkel, L. M., & Beggs, A. H. (2012) · The FASEB Journal · doi:10.1096/fj.11-194548 · Cited by 43 · see citing works

AP-1 Differentially Expressed Proteins Krp1 and Fibronectin Cooperatively Enhance Rho-ROCK-Independent Mesenchymal Invasion by Altering the Function, Localization, and Activity of Nondifferentially Expressed Proteins

Spence, H. J., McGarry, L., Chew, C. S., Carragher, N. O., Carragher, L., Yuan, Z., Croft, D. R., Olson, M. F., Frame, M. C., & Ozanne, B. W. (2006) · Molecular and Cellular Biology · doi:10.1128/mcb.26.4.1480-1495.2006 · Cited by 39 · see citing works

Krp1 (Sarcosin) promotes lateral fusion of myofibril assembly intermediates in cultured mouse cardiomyocytes

Greenberg, C. C., Connelly, P. S., Daniels, M. P., & Horowits, R. (2007) · Experimental Cell Research · doi:10.1016/j.yexcr.2007.12.009 · Cited by 31 · see citing works

Novel β-Propeller of the BTB-Kelch Protein Krp1 Provides a Binding Site for Lasp-1 That Is Necessary for Pseudopodial Extension

Gray, C. H., McGarry, L., Spence, H. J., Riboldi‐Tunnicliffe, A., & Ozanne, B. W. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.023259 · Cited by 29 · see citing works

Analysis of Skeletal Muscle Defects in Larval Zebrafish by Birefringence and Touch-evoke Escape Response Assays

Smith, L. L., Beggs, A. H., & Gupta, V. (2013) · Journal of Visualized Experiments · doi:10.3791/50925-v · Cited by 28 · see citing works

BTB-Kelch protein Krp1 regulates proliferation and differentiation of myoblasts

Paxton, C. W., Cosgrove, R. A., Drozd, A. C., Wiggins, E. L., Woodhouse, S., Watson, R. A., Spence, H. J., Ozanne, B. W., & Pell, J. M. (2011) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00321.2010 · Cited by 22 · see citing works

Nemaline and myotubular myopathies

Wallgren‐Pettersson, C. (2002) · Seminars in Pediatric Neurology · doi:10.1053/spen.2002.33804 · Cited by 18 · see citing works

Sarcosin (Krp1) in skeletal muscle differentiation: gene expression profiling and knockdown experiments

du Puy, L., Beqqali, A., van Tol, H. T. A., Monshouwer‐Kloots, J., Passier, R. C., Haagsman, H. P., & Roelen, B. A. J. (2012) · The International Journal of Developmental Biology · doi:10.1387/ijdb.113327lp · Cited by 18 · see citing works

PROTAC targeted protein degraders: the past is prologue

Békés, M., Langley, D. R., & Crews, C. M. (2022) · Nature Reviews Drug Discovery · doi:10.1038/s41573-021-00371-6 · Cited by 3,395 · see citing works

Congenital myopathies: disorders of excitation–contraction coupling and muscle contraction

Jungbluth, H., Treves, S., Zorzato, F., Sárközy, A., Ochala, J., Sewry, C. A., Phadke, R., Gautel, M., & Francesco Muntoni, A. (2018) · Nature Reviews Neurology · doi:10.1038/nrneurol.2017.191 · Cited by 282 · see citing works

Ubiquitin ligases: guardians of mammalian development

Walma, D. A. C., Chen, Z., Bullock, A. N., & Yamada, K. M. (2022) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-021-00448-5 · Cited by 212 · see citing works

Leiomodin-3 dysfunction results in thin filament disorganization and nemaline myopathy

Yuen, M., Sandaradura, S. A., Dowling, J. J., Kostyukova, A. S., Moroz, N., Quinlan, K. G. R., Lehtokari, V., Ravenscroft, G., Todd, E. J., Ceyhan‐Birsoy, O., et al. (2014) · Journal of Clinical Investigation · doi:10.1172/jci75199 · Cited by 209 · see citing works

The Ubiquitin–Proteasome System in Regulation of the Skeletal Muscle Homeostasis and Atrophy: From Basic Science to Disorders

Kitajima, Y., Yoshioka, K., & Suzuki, N. (2020) · The Journal of Physiological Sciences · doi:10.1186/s12576-020-00768-9 · Cited by 171 · see citing works

Kelch proteins: emerging roles in skeletal muscle development and diseases

Gupta, V., & Beggs, A. H. (2014) · Skeletal Muscle · doi:10.1186/2044-5040-4-11 · Cited by 154 · see citing works

Rapid Targeted Genomics in Critically Ill Newborns

van Diemen, C. C., Kerstjens‐Frederikse, W. S., Bergman, K. A., de Koning, T. J., Sikkema‐Raddatz, B., van der Velde, J. K., Abbott, K. M., Herkert, J. C., Löhner, K., Rump, P., et al. (2017) · PEDIATRICS · doi:10.1542/peds.2016-2854 · Cited by 148 · see citing works

Mutation Update: The Spectra of Nebulin Variants and Associated Myopathies

Lehtokari, V., Kiiski, K., Sandaradura, S. A., Laporte, J., Repo, P. E., Frey, J. A., Donner, K. M., Marttila, M. M., Saunders, C., Barth, P. G., et al. (2014) · Human Mutation · doi:10.1002/humu.22693 · Cited by 145 · see citing works

Congenital myopathies: clinical phenotypes and new diagnostic tools

the Italian Network on Congenital Myopathies, Cassandrini, D., Trovato, R., Rubegni, A., Lenzi, S., Fiorillo, C., Baldacci, J., Minetti, C., Astrea, G., Bruno, C., et al. (2017) · The Italian Journal of Pediatrics/Italian journal of pediatrics · doi:10.1186/s13052-017-0419-z · Cited by 136 · see citing works

KLHL40 deficiency destabilizes thin filament proteins and promotes nemaline myopathy

Garg, A., O’Rourke, J., Long, C., Doering, J., Ravenscroft, G., Bezprozvannaya, S., Nelson, B. R., Beetz, N., Li, L., Chen, S., et al. (2014) · Journal of Clinical Investigation · doi:10.1172/jci74994 · Cited by 127 · see citing works

Next generation sequencing in a large cohort of patients presenting with neuromuscular disease before or at birth

Todd, E. J., Yau, K. S., Ong, R., Slee, J., McGillivray, G., Barnett, C., Haliloğlu, G., Talim, B., Akçören, Z., Kariminejad, A., et al. (2015) · Orphanet Journal of Rare Diseases · doi:10.1186/s13023-015-0364-0 · Cited by 118 · see citing works

Mutations of GPR126 Are Responsible for Severe Arthrogryposis Multiplex Congenita

Ravenscroft, G., Nolent, F., Rajagopalan, S., Meireles, A. M., Paavola, K. J., Gaillard, D. A., Alanio, E., Buckland, M. E., Arbuckle, S. M., Krivanek, M., et al. (2015) · The American Journal of Human Genetics · doi:10.1016/j.ajhg.2015.04.014 · Cited by 116 · see citing works

Molecular and cellular basis of genetically inherited skeletal muscle disorders

Dowling, J. J., Weihl, C. C., & Spencer, M. J. (2021) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-021-00389-z · Cited by 106 · see citing works

A Premature Stop Codon in MYO18B is Associated with Severe Nemaline Myopathy with Cardiomyopathy

Malfatti, E., Böhm, J., Lacène, E., Beuvin, M., Brochier, G., Romero, N. B., & Laporte, J. (2015) · Journal of Neuromuscular Diseases · doi:10.3233/jnd-150085 · Cited by 105 · see citing works

Recent advances in nemaline myopathy

Laitila, J. M., & Wallgren‐Pettersson, C. (2021) · Neuromuscular Disorders · doi:10.1016/j.nmd.2021.07.012 · Cited by 93 · see citing works

Genetics and genomic medicine in Saudi Arabia

Alkuraya, F. S. (2014) · Molecular Genetics & Genomic Medicine · doi:10.1002/mgg3.97 · Cited by 93 · see citing works

Pathophysiological concepts in the congenital myopathies: blurring the boundaries, sharpening the focus

Ravenscroft, G., Laing, N. G., & Bönnemann, C. G. (2014) · Brain · doi:10.1093/brain/awu368 · Cited by 89 · see citing works

Muscle histopathology in nebulin-related nemaline myopathy: ultrastrastructural findings correlated to disease severity and genotype

Malfatti, E., Lehtokari, V., Böhm, J., de Winter, J. M., Schaeffer, U., Estournet, B., Quijano-Roy, S., Monges, S., Lubieniecki, F. J., Bellance, R., et al. (2014) · Acta Neuropathologica Communications · doi:10.1186/2051-5960-2-44 · Cited by 89 · see citing works

Kelch-like proteins: Physiological functions and relationships with diseases

Shi, X., Xiang, S., Cao, J., Zhu, H., Yang, B., He, Q., & Ying, M. (2019) · Pharmacological Research · doi:10.1016/j.phrs.2019.104404 · Cited by 88 · see citing works

Biallelic Mutations in MYPN , Encoding Myopalladin, Are Associated with Childhood-Onset, Slowly Progressive Nemaline Myopathy

Miyatake, S., Mitsuhashi, S., Hayashi, Y. K., Purevjav, E., Nishikawa, A., Koshimizu, E., Suzuki, M., Yatabe, K., Tanaka, Y., Ogata, K., et al. (2016) · The American Journal of Human Genetics · doi:10.1016/j.ajhg.2016.11.017 · Cited by 81 · see citing works

The genetics of congenital myopathies

Gonorazky, H. D., Bönnemann, C. G., & Dowling, J. J. (2018) · Handbook of clinical neurology · doi:10.1016/b978-0-444-64076-5.00036-3 · Cited by 79 · see citing works

Myopathology in congenital myopathies

Sewry, C. A., & Wallgren‐Pettersson, C. (2016) · Neuropathology and Applied Neurobiology · doi:10.1111/nan.12369 · Cited by 75 · see citing works

Mutation‐specific effects on thin filament length in thin filament myopathy

de Winter, J. M., Joureau, B., Lee, E., Kiss, B., Yuen, M., Gupta, V., Pappas, C. T., Gregorio, C. C., Stienen, G. J. M., Edvardson, S., et al. (2016) · Annals of Neurology · doi:10.1002/ana.24654 · Cited by 71 · see citing works

Sarcomere Dysfunction in Nemaline Myopathy

de Winter, J. M., & Ottenheijm, C. A. C. (2017) · Journal of Neuromuscular Diseases · doi:10.3233/jnd-160200 · Cited by 70 · see citing works

Nemaline myopathies: State of the art

Malfatti, E., & Romero, N. B. (2016) · Revue Neurologique · doi:10.1016/j.neurol.2016.08.004 · Cited by 66 · see citing works

KLHL41 stabilizes skeletal muscle sarcomeres by nonproteolytic ubiquitination

Ramirez-Martinez, A., Cenik, B. K., Bezprozvannaya, S., Chen, B., Bassel‐Duby, R., Liu, N., & Olson, E. N. (2017) · eLife · doi:10.7554/elife.26439 · Cited by 66 · see citing works

Congenital Muscular Dystrophies and Myopathies: An Overview and Update

Kirschner, J., Bönnemann, C. G., & Schorling, D. (2017) · Neuropediatrics · doi:10.1055/s-0037-1604154 · Cited by 57 · see citing works

Zebrafish models for nemaline myopathy reveal a spectrum of nemaline bodies contributing to reduced muscle function

Sztal, T. E., Zhao, M., Williams, C., Oorschot, V. M. J., Parslow, A. C., Giousoh, A., Yuen, M., Hall, T. E., Costin, A. J., Ramm, G., et al. (2015) · Acta Neuropathologica · doi:10.1007/s00401-015-1430-3 · Cited by 55 · see citing works

Dominantly inherited distal nemaline/cap myopathy caused by a large deletion in the nebulin gene

Kiiski, K., Lehtokari, V., Vihola, A., Laitila, J. M., Huovinen, S., Sagath, L., Evilä, A., Paetau, A. E., Sewry, C. A., Hackman, P., et al. (2018) · Neuromuscular Disorders · doi:10.1016/j.nmd.2018.12.007 · Cited by 51 · see citing works

Nebulin interactions with actin and tropomyosin are altered by disease-causing mutations

Marttila, M. M., Hanif, M., Lemola, E., Nowak, K. J., Laitila, J. M., Grönholm, M., Wallgren‐Pettersson, C., & Pelin, K. (2014) · Skeletal Muscle · doi:10.1186/2044-5040-4-15 · Cited by 49 · see citing works

A Cross-Sectional Study of Nemaline Myopathy

Amburgey, K., Acker, M., Saeed, S., Amin, R., Beggs, A. H., Bönnemann, C. G., Brudno, M., Constantinescu, A., Dastgir, J., Diallo, M., et al. (2021) · Neurology · doi:10.1212/wnl.0000000000011458 · Cited by 49 · see citing works

Mutation of the mitochondrial carrier SLC25A42 causes a novel form of mitochondrial myopathy in humans

Shamseldin, H. E., Smith, L. L., Kentab, A. Y., Alkhalidi, H., Summers, B. J., Alsedairy, H., Xiong, Y., Gupta, V., & Alkuraya, F. S. (2015) · Human Genetics · doi:10.1007/s00439-015-1608-8 · Cited by 47 · see citing works

RNA helicase, DDX27 regulates skeletal muscle growth and regeneration by modulation of translational processes

Bennett, A. H., O’Donohue, M.-F., Gundry, S. R., Chan, A. T., Widrick, J. J., Draper, I., Chakraborty, A., Zhou, Y., Zon, L. I., Gleizes, P., et al. (2018) · PLoS Genetics · doi:10.1371/journal.pgen.1007226 · Cited by 47 · see citing works

Dysregulation of NRAP degradation by KLHL41 contributes to pathophysiology in nemaline myopathy

Jirka, C., Pak, J. H., Grosgogeat, C. A., Marchetii, M. M., & Gupta, V. (2019) · Human Molecular Genetics · doi:10.1093/hmg/ddz078 · Cited by 47 · see citing works

Nemaline body myopathy caused by a novel mutation in troponin T1 (TNNT1)

Abdulhaq, U. N., Daana, M., Dor, T., Fellig, Y., Eylon, S., Schuelke, M., Shaag, A., Elpeleg, O. N., & Edvardson, S. (2015) · Muscle & Nerve · doi:10.1002/mus.24885 · Cited by 46 · see citing works

Genetics of neuromuscular fetal akinesia in the genomics era

Beecroft, S. J., Lombard, M., Mowat, D. R., McLean, C., Cairns, A. G., Davis, M. R., Laing, N. G., & Ravenscroft, G. (2018) · Journal of Medical Genetics · doi:10.1136/jmedgenet-2018-105266 · Cited by 43 · see citing works

KBTBD13 is an actin-binding protein that modulates muscle kinetics

de Winter, J. M., Molenaar, J. P. F., Yuen, M., van der Pijl, R. J., Shen, S., Conijn, S., van de Locht, M., van Willigenburg, M., Bogaards, S. J. P., van Kleef, E. S. B., et al. (2019) · Journal of Clinical Investigation · doi:10.1172/jci124000 · Cited by 42 · see citing works

Expanding the Phenotype Associated With theNEFLMutation

Agrawal, P. B., Joshi, M., Marinakis, N. S., Schmitz‐Abe, K., Ciarlini, P. D. S. C., Sargent, J. C., Markianos, K., Girolami, U. D., Chad, D. A., & Beggs, A. H. (2014) · JAMA Neurology · doi:10.1001/jamaneurol.2014.1432 · Cited by 42 · see citing works

Deficiency in Kelch protein Klhl31 causes congenital myopathy in mice

Papizan, J. B., Garry, G. A., Brezprozvannaya, S., McAnally, J., Bassel‐Duby, R., Liu, N., & Olson, E. N. (2017) · Journal of Clinical Investigation · doi:10.1172/jci93445 · Cited by 41 · see citing works

Update on the Genetics of Congenital Myopathies

Pelin, K., & Wallgren‐Pettersson, C. (2019) · Seminars in Pediatric Neurology · doi:10.1016/j.spen.2019.01.005 · Cited by 39 · see citing works

Dysfunctional sarcomere contractility contributes to muscle weakness in ACTA1‐related nemaline myopathy (NEM3)

Joureau, B., de Winter, J. M., Conijn, S., Bogaards, S. J. P., Kovačević, I., Kalganov, A., Persson, M., Lindqvist, J., Stienen, G. J. M., Irving, T. C., et al. (2018) · Annals of Neurology · doi:10.1002/ana.25144 · Cited by 38 · see citing works

Loss of Tropomodulin4 in the zebrafish mutant träge causes cytoplasmic rod formation and muscle weakness reminiscent of nemaline myopathy

Berger, J., Tarakci, H., Berger, S., Li, M., Hall, T. E., Arner, A., & Currie, P. D. (2014) · Disease Models & Mechanisms · doi:10.1242/dmm.017376 · Cited by 37 · see citing works

KBTBD11, a novel BTB-Kelch protein, is a negative regulator of osteoclastogenesis through controlling Cullin3-mediated ubiquitination of NFATc1

Narahara, S., Sakai, E., Kadowaki, T., Yamaguchi, Y., Narahara, H., Okamoto, K., Asahina, I., & Tsukuba, T. (2019) · Scientific Reports · doi:10.1038/s41598-019-40240-2 · Cited by 36 · see citing works

Leiomodin-3-deficient mice display nemaline myopathy with fast-myofiber atrophy

Tian, L., Ding, S., You, Y., Li, T.-R., Liu, Y., Wu, X., Sun, L. V., & Xu, T. (2015) · Disease Models & Mechanisms · doi:10.1242/dmm.019430 · Cited by 34 · see citing works

“Muscling” Throughout Life

Goody, M. F., Carter, E. V., Kilroy, E. A., Maves, L., & Henry, C. A. (2016) · Current topics in developmental biology/Current Topics in Developmental Biology · doi:10.1016/bs.ctdb.2016.11.002 · Cited by 34 · see citing works

Identification of a novel nemaline myopathy‐Causing mutation in the troponin T1 (TNNT1) gene: A case outside of the old order amish

Marra, J. D., Engelstad, K., Ankala, A., Tanji, K., Dastgir, J., Vivo, D. C. D., Coffee, B. W., & Chiriboga, C. A. (2014) · Muscle & Nerve · doi:10.1002/mus.24528 · Cited by 34 · see citing works

Modular UBE2H-CTLH E2-E3 complexes regulate erythroid maturation

Sherpa, D., Mueller, J., Karayel, Ö., Xu, P., Yao, Y., Chrustowicz, J., Gottemukkala, K. V., Baumann, C., Groß, A., Czarnecki, O., et al. (2022) · eLife · doi:10.7554/elife.77937 · Cited by 31 · see citing works

New era in genetics of early-onset muscle disease: Breakthroughs and challenges

Ravenscroft, G., Davis, M. R., Lamont, P. J., Forrest, A. R. R., & Laing, N. G. (2016) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2016.08.002 · Cited by 33 · see citing works

Novel autosomal dominant TNNT 1 mutation causing nemaline myopathy

Konersman, C. G., Freyermuth, F., Winder, T. L., Lawlor, M. W., Lagier‐Tourenne, C., & Patel, S. B. (2017) · Molecular Genetics & Genomic Medicine · doi:10.1002/mgg3.325 · Cited by 33 · see citing works

Myostatin inhibition using mRK35 produces skeletal muscle growth and tubular aggregate formation in wild type and TgACTA1D286G nemaline myopathy mice

Tinklenberg, J. A., Siebers, E. M., Beatka, M. J., Meng, H., Yang, L., Zhang, Z., Ross, J. A., Ochala, J., Morris, C. A., Owens, J. M., et al. (2017) · Human Molecular Genetics · doi:10.1093/hmg/ddx431 · Cited by 33 · see citing works

Cullin-3–RING ubiquitin ligase activity is required for striated muscle function in mice

Papizan, J. B., Vidal, A., Bezprozvannaya, S., Bassel‐Duby, R., & Olson, E. N. (2018) · Journal of Biological Chemistry · doi:10.1074/jbc.ra118.002104 · Cited by 34 · see citing works

ZBTB42 mutation defines a novel lethal congenital contracture syndrome (LCCS6)

Patel, N., Smith, L. L., Faqeih, E., Mohamed, J. Y., Gupta, V., & Alkuraya, F. S. (2014) · Human Molecular Genetics · doi:10.1093/hmg/ddu384 · Cited by 30 · see citing works

Discovery of Novel Therapeutics for Muscular Dystrophies using Zebrafish Phenotypic Screens

Widrick, J. J., Kawahara, G., Alexander, M. S., Beggs, A. H., & Kunkel, L. M. (2019) · Journal of Neuromuscular Diseases · doi:10.3233/jnd-190389 · Cited by 30 · see citing works

Novel cofilin-2 (CFL2) four base pair deletion causing nemaline myopathy

Ong, R., Alsaman, A., Selcen, D., Arabshahi, A., Yau, K. S., Ravenscroft, G., Duff, R. M., Atkinson, V. J., Allcock, R. J. N., & Laing, N. G. (2014) · Journal of Neurology Neurosurgery & Psychiatry · doi:10.1136/jnnp-2014-307608 · Cited by 29 · see citing works

The Challenge of Next Generation Sequencing in the Context of Neuromuscular Diseases

Lek, M., & MacArthur, D. G. (2014) · Journal of Neuromuscular Diseases · doi:10.3233/jnd-140032 · Cited by 29 · see citing works

Prenatal diagnosis of congenital myopathies and muscular dystrophies

Massalska, D., Zimowski, J. G., Bijok, J., Kucińska‐Chahwan, A., Łusakowska, A., Jakiel, G., & Roszkowski, T. (2016) · Clinical Genetics · doi:10.1111/cge.12801 · Cited by 28 · see citing works

Shaping Striated Muscles with Ubiquitin Proteasome System in Health and Disease

Hnia, K., Clausen, T., & Moog‐Lutz, C. (2019) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2019.05.008 · Cited by 28 · see citing works

Treatment with ActRIIB-mFc Produces Myofiber Growth and Improves Lifespan in the Acta1 H40Y Murine Model of Nemaline Myopathy

Tinklenberg, J. A., Meng, H., Yang, L., Liu, F., Hoffmann, R. G., Dasgupta, M., Allen, K. P., Beggs, A. H., Hardeman, E. C., Pearsall, R. S., et al. (2016) · American Journal Of Pathology · doi:10.1016/j.ajpath.2016.02.008 · Cited by 27 · see citing works

The Role of Cullin-RING Ligases in Striated Muscle Development, Function, and Disease

Blondelle, J., Biju, A., & Lange, S. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21217936 · Cited by 27 · see citing works

Myoblast deactivation within engineered human skeletal muscle creates a transcriptionally heterogeneous population of quiescent satellite-like cells

Wang, J. T., Broer, T., Chavez, T., Zhou, C. J., Tran, S., Xiang, Y., Khodabukus, A., Diao, Y., & Bursac, N. (2022) · Biomaterials · doi:10.1016/j.biomaterials.2022.121508 · Cited by 25 · see citing works

Effect of levosimendan on the contractility of muscle fibers from nemaline myopathy patients with mutations in the nebulin gene

de Winter, J. M., Joureau, B., Sequeira, V., Clarke, N. F., van der Velden, J., Stienen, G. J. M., Granzier, H. L. M., Beggs, A. H., & Ottenheijm, C. A. C. (2015) · Skeletal Muscle · doi:10.1186/s13395-015-0037-7 · Cited by 27 · see citing works

Novel Recessive TNNT1 Congenital Core‐Rod Myopathy in French Canadians

Pellerin, D., Aykanat, A., Ellezam, B., Troiano, E. C., Karamchandani, J., Dicaire, M., Petitclerc, M., Robertson, R., Allard‐Chamard, X., Brunet, D., et al. (2020) · Annals of Neurology · doi:10.1002/ana.25685 · Cited by 27 · see citing works

Cullin-3–dependent deregulation of ACTN1 represents a pathogenic mechanism in nemaline myopathy

Blondelle, J., Tallapaka, K., Seto, J. T., Ghassemian, M., Clark, M., Laitila, J. M., Bournazos, A., Singer, J. D., & Lange, S. (2019) · JCI Insight · doi:10.1172/jci.insight.125665 · Cited by 26 · see citing works

Pathogenic variants in TNNC2 cause congenital myopathy due to an impaired force response to calcium

van de Locht, M., Donkervoort, S. C., de Winter, J. M., Conijn, S., Begthel, L. P. L., Küsters, B., Mohassel, P., Hu, Y., Medne, L., Quinn, C. C., et al. (2021) · Journal of Clinical Investigation · doi:10.1172/jci145700 · Cited by 26 · see citing works

Testing of therapies in a novel nebulin nemaline myopathy model demonstrate a lack of efficacy

Sztal, T. E., McKaige, E. A., Williams, C., Oorschot, V. M. J., Ramm, G., & Bryson‐Richardson, R. J. (2018) · Acta Neuropathologica Communications · doi:10.1186/s40478-018-0546-9 · Cited by 26 · see citing works

Quantitative proteomic analysis of skeletal muscles from wild-type and transgenic mice carrying recessive Ryr1 mutations linked to congenital myopathies

Eckhardt, J., Ruiz, A., Koenig, S., Frieden, M., Meier, H., Schmidt, A., Treves, S., & Zorzato, F. (2023) · eLife · doi:10.7554/elife.83618 · Cited by 21 · see citing works

Update on Congenital Myopathies in Adulthood

Papadimas, G. K., Xirou, S., Kararizou, E. G., & Papadopoulos, C. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21103694 · Cited by 23 · see citing works

Muscle magnetic resonance imaging and histopathology in ACTA1‐ related congenital nemaline myopathy

Claudia Castiglioni, T., Cassandrini, D., Fattori, F., Bellacchio, E., D’Amico, A., Álvarez, K., Gejman, R., Díaz, J., Santorelli, F. M., Romero, N. B., et al. (2014) · Muscle & Nerve · doi:10.1002/mus.24353 · Cited by 21 · see citing works

Internal and external morphology of adults of the appendicularian, Oikopleura dioica: an SEM study

Onuma, T. A., Isobe, M., & Nishida, H. (2016) · Cell and Tissue Research · doi:10.1007/s00441-016-2524-5 · Cited by 21 · see citing works

Massive parallel sequencing identifies RAPSN and PDHA1 mutations causing fetal akinesia deformation sequence

Winters, L., Hoof, E. V., Catte, L. D., Bogaert, K. V. D., de Ravel, T. J. L., Waele, L. D., Corveleyn, A., & Breckpot, J. (2017) · European Journal of Paediatric Neurology · doi:10.1016/j.ejpn.2017.04.641 · Cited by 21 · see citing works

Acute and chronic tirasemtiv treatment improves in vivo and in vitro muscle performance in actin-based nemaline myopathy mice

de Winter, J. M., Gineste, C., Minardi, E., Brocca, L., Rossi, M., Borsboom, T. C., Beggs, A. H., Bernard, M., Bendahan, D., Hwee, D. T., et al. (2021) · Human Molecular Genetics · doi:10.1093/hmg/ddab112 · Cited by 20 · see citing works

Neonatal fractures as a presenting feature of LMOD3‐associated congenital myopathy

Abbott, M., Jain, M., Pferdehirt, R. E., Chen, Y., Tran, A. A., Düz, M. B., Seven, M., Gibbs, R. A., Muzny, D. M., Lee, B., et al. (2017) · American Journal of Medical Genetics Part A · doi:10.1002/ajmg.a.38383 · Cited by 20 · see citing works

Dynamic Regulation of Inter-Organelle Communication by Ubiquitylation Controls Skeletal Muscle Development and Disease Onset

Mansur, A., Joseph, R., Kim, E. S., Beltran, P. M. J., Udeshi, N. D., Pearce, C., Jiang, H., Iwase, R., Milev, M. P., Almousa, H. A., et al. (2022) · eLife · doi:10.7554/elife.81966 · Cited by 19 · see citing works

New massive parallel sequencing approach improves the genetic characterization of congenital myopathies

Oliveira, J., Gonçalves, A., Taipa, R. J. F., Pires, M. M., Oliveira, M. E., Costa, J. L., Machado, J. C., Medeiros, E., Coelho, T., Santos, M., et al. (2016) · Journal of Human Genetics · doi:10.1038/jhg.2016.2 · Cited by 19 · see citing works

Mild clinical presentation in KLHL40-related nemaline myopathy (NEM 8)

Seferian, A., Malfatti, E., Bosson, C., Pelletier, L., Taytard, J., Forin, V., Gidaro, T., Gargaun, E., Carlier, P. G., Fauré, J., et al. (2016) · Neuromuscular Disorders · doi:10.1016/j.nmd.2016.07.011 · Cited by 19 · see citing works

Mutational and clinical spectrum in a cohort of Chinese patients with hereditary nemaline myopathy

Wang, Q., Hu, Z., Chang, X., Yu, M., Xie, Z., Lv, H., Zhang, W. Y., Xiong, H., Yuan, Y., & Wang, Z. (2020) · Clinical Genetics · doi:10.1111/cge.13745 · Cited by 19 · see citing works

Kelch Repeat and BTB Domain Containing Protein 5 (Kbtbd5) Regulates Skeletal Muscle Myogenesis through the E2F1-DP1 Complex

Gong, W., Gohla, R. M., Bowlin, K. M., Koyano‐Nakagawa, N., Garry, D. J., & Shi, X. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.629956 · Cited by 19 · see citing works

Respiratory muscle function in patients with nemaline myopathy

van Kleef, E. S. B., van Doorn, J. L. M., Gaytant, M. A., de Weerd, W., Vosse, B. A. H., Wallgren‐Pettersson, C., van Engelen, B. G. M., Ottenheijm, C. A. C., Voermans, N. C., & Doorduin, J. (2022) · Neuromuscular Disorders · doi:10.1016/j.nmd.2022.06.009 · Cited by 18 · see citing works

New Mutations in NEB Gene Discovered by Targeted Next-Generation Sequencing in Nemaline Myopathy Italian Patients

Piga, D., Magri, F., Ronchi, D., Corti, S. P., Cassandrini, D., Mercuri, E. M., Tasca, G. A., Bertini, E., Fattori, F., Toscano, A., et al. (2016) · Journal of Molecular Neuroscience · doi:10.1007/s12031-016-0739-2 · Cited by 18 · see citing works

Therapeutic Aspects in Congenital Myopathies

Jungbluth, H., & Francesco Muntoni, A. (2019) · Seminars in Pediatric Neurology · doi:10.1016/j.spen.2019.01.004 · Cited by 17 · see citing works

Deep sequencing detects very-low-grade somatic mosaicism in the unaffected mother of siblings with nemaline myopathy

Miyatake, S., Koshimizu, E., Hayashi, Y. K., Miya, K., Shiina, M., Nakashima, M., Tsurusaki, Y., Miyake, N., Saitsu, H., Ogata, K., et al. (2014) · Neuromuscular Disorders · doi:10.1016/j.nmd.2014.04.002 · Cited by 16 · see citing works

Novel KLHL26 variant associated with a familial case of Ebstein’s anomaly and left ventricular noncompaction

Thareja, S. K., North, L. M., Stamm, K., Earing, M. G., Frommelt, M. A., Willes, R. J., Tripathi, S., Dsouza, N. R., Zimmermann, M. T., Mahnke, D. K., et al. (2020) · Molecular Genetics & Genomic Medicine · doi:10.1002/mgg3.1152 · Cited by 16 · see citing works

Long-term follow-up and characteristic pathological findings in severe nemaline myopathy due to LMOD3 mutations

Michael, E., Hedberg‐Oldfors, C., Wilmar, P., Visuttijai, K., Oldfors, A., & Darín, N. (2018) · Neuromuscular Disorders · doi:10.1016/j.nmd.2018.12.009 · Cited by 16 · see citing works

Weighted Single-Step GWAS Identifies Genes Influencing Fillet Color in Rainbow Trout

Ahmed, R. O., Ali, A., Al-Tobasei, R., Leeds, T. D., Kenney, B., & Salem, M. (2022) · Genes · doi:10.3390/genes13081331 · Cited by 15 · see citing works

Targeting kelch-like (KLHL) proteins: achievements, challenges and perspectives

Zhou, Y., Zhang, Q., Zhao, Z., Hu, X., You, Q., & Jiang, Z. (2024) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2024.116270 · Cited by 14 · see citing works

Deleting nebulin's C-terminus reveals its importance to sarcomeric structure and function and is sufficient to invoke nemaline myopathy

Li, F. W., Barton, E. R., & Granzier, H. L. M. (2019) · Human Molecular Genetics · doi:10.1093/hmg/ddz016 · Cited by 15 · see citing works

‘Amish Nemaline Myopathy’ in 2 Italian siblings harbouring a novel homozygous mutation in Troponin-I gene

D’Amico, A., Fattori, F., Fiorillo, C., Paglietti, M. G., Testa, M. B. C., Verardo, M., Catteruccia, M., Bruno, C., & Bertini, E. (2019) · Neuromuscular Disorders · doi:10.1016/j.nmd.2019.09.005 · Cited by 15 · see citing works

Expanding the histopathological spectrum of CFL2‐related myopathies

Fattori, F., Fiorillo, C., Rodolico, C., Tasca, G. A., Verardo, M., Bellacchio, E., Pizzi, S., Ciolfi, A., Fagiolari, G., Lupica, A., et al. (2018) · Clinical Genetics · doi:10.1111/cge.13240 · Cited by 15 · see citing works

NRAP reduction rescues sarcomere defects in nebulin-related nemaline myopathy

Casey, J. G., Kim, E. S., Joseph, R., Li, F. W., Granzier, H. L. M., & Gupta, V. (2023) · Human Molecular Genetics · doi:10.1093/hmg/ddad011 · Cited by 14 · see citing works

Control of craniofacial and brain development by Cullin3-RING ubiquitin ligases: Lessons from human disease genetics

Asmar, A. J., Beck, D. B., & Werner, A. A. (2020) · Experimental Cell Research · doi:10.1016/j.yexcr.2020.112300 · Cited by 13 · see citing works

Clinical massively parallel sequencing for the diagnosis of myopathies

Gorokhova, S., Biancalana, V., Lévy, N., Laporte, J., Bartoli, M., & Krahn, M. (2015) · Revue Neurologique · doi:10.1016/j.neurol.2015.02.019 · Cited by 14 · see citing works

Clinical and genetic diversity of nemaline myopathy from a single neuromuscular center in Korea

Lee, J., Lim, J. G., Shin, J., Park, Y.-E., & Kim, D. (2017) · Journal of the Neurological Sciences · doi:10.1016/j.jns.2017.10.020 · Cited by 14 · see citing works

Identification of Potentially Relevant Genes for Excessive Exercise-Induced Pathological Cardiac Hypertrophy in Zebrafish

Zhou, Z., Zheng, L., Tang, C., Chen, Z., Zhu, R., Peng, X., Wu, X., & Zhu, P. (2020) · Frontiers in Physiology · doi:10.3389/fphys.2020.565307 · Cited by 13 · see citing works

Beta2‐Adrenergic Stimulation Induces Resistance Training‐Like Adaptations in Human Skeletal Muscle: Potential Role of KLHL41

Jessen, S., Quesada, J. P., Credico, A. D., Moreno‐Justicia, R., Wilson, R., Jacobson, G. A., Bangsbo, J., Deshmukh, A. S., & Hostrup, M. (2024) · Scandinavian Journal of Medicine and Science in Sports · doi:10.1111/sms.14736 · Cited by 13 · see citing works

Clinical utility gene card for: Nemaline myopathy – update 2015

Nowak, K. J., Davis, M. R., Wallgren‐Pettersson, C., Lamont, P. J., & Laing, N. G. (2015) · European Journal of Human Genetics · doi:10.1038/ejhg.2015.12 · Cited by 13 · see citing works

Clinico-pathological features and mutational spectrum of 16 nemaline myopathy patients from a Chinese neuromuscular center

Yin, X., Pu, C., Wang, Z., Li, K., & Wang, H. (2021) · Acta Neurologica Belgica · doi:10.1007/s13760-020-01542-9 · Cited by 14 · see citing works

The widening genetic and myopathologic spectrum of congenital myopathies (CMYOs): a narrative review

Onnée, M., & Malfatti, E. (2025) · Neuromuscular Disorders · doi:10.1016/j.nmd.2025.105338 · Cited by 12 · see citing works

NEM6, KBTBD13-Related Congenital Myopathy: Myopathological Analysis in 18 Dutch Patients Reveals Ring Rods Fibers, Cores, Nuclear Clumps, and Granulo-Filamentous Protein Material

Bouman, K., Küsters, B., de Winter, J. M., Gillet, C., van Kleef, E. S. B., Eshuis, L., Brochier, G., Madelaine, A., Labasse, C., Boulogne, C., et al. (2021) · Journal of Neuropathology & Experimental Neurology · doi:10.1093/jnen/nlab012 · Cited by 12 · see citing works

Muscle weakness in respiratory and peripheral skeletal muscles in a mouse model for nebulin-based nemaline myopathy

Joureau, B., de Winter, J. M., Stam, K., Granzier, H. L. M., & Ottenheijm, C. A. C. (2016) · Neuromuscular Disorders · doi:10.1016/j.nmd.2016.10.004 · Cited by 12 · see citing works

A novel long non-coding RNA, lncKBTBD10, involved in bovine skeletal muscle myogenesis

Chen, M., Li, X., Zhang, X., Li, Y., Zhang, J., Liu, M., Zhang, L., Ding, X., Liu, X., & Guo, H. (2018) · In Vitro Cellular & Developmental Biology - Animal · doi:10.1007/s11626-018-0306-y · Cited by 12 · see citing works

Understanding the role of KLHL41 interactors in nemaline myopathy

Jirka, C. (2016) · OpenBU (Boston University)

Dysregulation of NRAP degradation by KLHL41 contributes to pathophysiology in nemaline myopathy

Jirka, C., Pak, J. H., Grosgogeat, C. A., Marchetii, M. M., & Gupta, V. (2019) · Human Molecular Genetics · doi:10.1093/hmg/ddz078 · Cited by 47 · see citing works

KLHL40 deficiency destabilizes thin filament proteins and promotes nemaline myopathy

Garg, A., O’Rourke, J., Long, C., Doering, J., Ravenscroft, G., Bezprozvannaya, S., Nelson, B. R., Beetz, N., Li, L., Chen, S., et al. (2014) · Journal of Clinical Investigation · doi:10.1172/jci74994 · Cited by 127 · see citing works

Mutations in KLHL40 Are a Frequent Cause of Severe Autosomal-Recessive Nemaline Myopathy

Ravenscroft, G., Miyatake, S., Lehtokari, V., Todd, E. J., Vornanen, P., Yau, K. S., Hayashi, Y. K., Miyake, N., Tsurusaki, Y., Doi, H., et al. (2013) · The American Journal of Human Genetics · doi:10.1016/j.ajhg.2013.05.004 · Cited by 226 · see citing works

[A case of KLHL40 mutation related nemaline myopathy].

Song, D., Ji, T., & Bao, X. (2016) · PubMed · doi:10.3760/cma.j.issn.0578-1310.2016.10.015 · Cited by 2 · see citing works