The DOI matches its Crossref record; 35 of the 35 references it cites were found in a registry or an index.
Identification of KLHL41 Mutations Implicates BTB-Kelch-Mediated Ubiquitination as an Alternate Pathway to Myofibrillar Disruption in Nemaline Myopathy
Open accessAbstract
Nemaline myopathy (NM) is a rare congenital muscle disorder primarily affecting skeletal muscles that results in neonatal death in severe cases as a result of associated respiratory insufficiency. NM is thought to be a disease of sarcomeric thin filaments as six of eight known genes whose mutation can cause NM encode components of that structure, however, recent discoveries of mutations in non-thin filament genes has called this model in question. We performed whole-exome sequencing and have identified recessive small deletions and missense changes in the Kelch-like family member 41 gene (KLHL41) in four individuals from unrelated NM families. Sanger sequencing of 116 unrelated individuals with NM identified compound heterozygous changes in KLHL41 in a fifth family. Mutations in KLHL41 showed a clear phenotype-genotype correlation: Frameshift mutations resulted in severe phenotypes with neonatal death, whereas missense changes resulted in impaired motor function with survival into late childhood and/or early adulthood. Functional studies in zebrafish showed that loss of Klhl41 results in highly diminished motor function and myofibrillar disorganization, with nemaline body formation, the pathological hallmark of NM. These studies expand the genetic heterogeneity of NM and implicate a critical role of BTB-Kelch family members in maintenance of sarcomeric integrity in NM.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
In the citing paper
“which have a documented role in the biology of nemaline myopathy146,147.”
From PROTAC targeted protein degraders: the past is prologue (2022) · cites this paper as [146]
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
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
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 14,724
Guerois, R., Nielsen, J. E., & Serrano, L. (2002) · Journal of Molecular Biology · doi:10.1016/s0022-2836(02)00442-4 · Cited by 1,728
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
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
Self-citationA 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
Self-citationMutations 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
Self-citationA 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
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
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
Cited by
Sorted by citations
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
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., & Muntoni, F. (2018) · Nature Reviews Neurology · doi:10.1038/nrneurol.2017.191 · Cited by 292
Self-citationUbiquitin 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 220
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
Self-citationKitajima, Y., Yoshioka, K., & Suzuki, N. (2020) · The Journal of Physiological Sciences · doi:10.1186/s12576-020-00768-9 · Cited by 171
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 160
Self-citationRapid 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
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
Self-citationCongenital 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
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
Self-citationTodd, 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 121
Self-citationMutations 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
Self-citationMolecular 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 107
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 104
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
Self-citationGenetics and genomic medicine in Saudi Arabia
Alkuraya, F. S. (2014) · Molecular Genetics & Genomic Medicine · doi:10.1002/mgg3.97 · Cited by 93
Self-citationRavenscroft, G., Laing, N. G., & Bönnemann, C. G. (2014) · Brain · doi:10.1093/brain/awu368 · Cited by 94
Self-citationMalfatti, 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
Self-citationKelch-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 92
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
Self-citationThe 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 82
Myopathology in congenital myopathies
Sewry, C. A., & Wallgren‐Pettersson, C. (2016) · Neuropathology and Applied Neurobiology · doi:10.1111/nan.12369 · Cited by 75
Self-citationMutation‐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
Self-citationSarcomere 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
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
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 67
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 58
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
Self-citationDominantly 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
Self-citationNebulin 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
Self-citationA 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 51
Self-citationShamseldin, 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
Self-citationBennett, 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 45
Self-citationDysregulation 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 44
Self-citationNemaline 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
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 44
Self-citationKBTBD13 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
Self-citationExpanding 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
Self-citationDeficiency 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
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 42
Self-citationJoureau, 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
Self-citationBerger, 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
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 38
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 33
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
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
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 32
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 31
Self-citationNovel 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
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
Self-citationCullin-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
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
Self-citationDiscovery 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
Self-citationNovel 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 28
Self-citationThe 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
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 29
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 30
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
Self-citationThe 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
Wang, J., 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 28
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
Self-citationNovel 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
Self-citationCullin-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
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
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
Eckhardt, J., Ruiz, A., Koenig, S., Frieden, M., Meier, H., Schmidt, A., Treves, S., & Zorzato, F. (2022) · bioRxiv · doi:10.7554/elife.83618 · Cited by 16
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 25
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
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
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
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
Self-citationNeonatal 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
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
Self-citationOliveira, 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
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
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
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
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
Self-citationPiga, 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
Therapeutic Aspects in Congenital Myopathies
Jungbluth, H., & Muntoni, F. (2019) · Seminars in Pediatric Neurology · doi:10.1016/j.spen.2019.01.004 · Cited by 17
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
Self-citationThareja, 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
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
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
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 15
Li, F. W., Barton, E. R., & Granzier, H. L. M. (2019) · Human Molecular Genetics · doi:10.1093/hmg/ddz016 · Cited by 15
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
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
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
Self-citationAsmar, A. J., Beck, D. B., & Werner, A. A. (2020) · Experimental Cell Research · doi:10.1016/j.yexcr.2020.112300 · Cited by 13
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 16
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
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
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
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
Self-citationYin, X., Pu, C., Wang, Z., Li, K., & Wang, H. (2021) · Acta Neurologica Belgica · doi:10.1007/s13760-020-01542-9 · Cited by 14
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
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
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
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
Metadata
- Authors
- Gupta, V. A., Ravenscroft, G., Shaheen, R., Todd, E. J., Swanson, L. C., Shiina, M., Ogata, K., Hsu, C., Clarke, N. F., Darras, B. T., Farrar, M. A., Hashem, A., Manton, N. D., Muntoni, F., North, K. N., Sandaradura, S. A., Nishino, I., Hayashi, Y. K., Sewry, C. A., Thompson, E. M., Yau, K. S., Brownstein, C. A., Yu, T. W., Allcock, R. J. N., Davis, M. R., Wallgren-Pettersson, C., Matsumoto, N., Alkuraya, F. S., Laing, N. G., & Beggs, A. H.
- Affiliations
- Boston Children's Hospital (US)
- The University of Western Australia (AU)
- King Faisal Specialist Hospital & Research Centre (SA)
- Yokohama City University (JP)
- The University of Sydney (AU)
- Sydney Children's Hospital (AU)
- South Australia Pathology (AU)
- Royal Children's Hospital (AU)
- National Center of Neurology and Psychiatry (JP)
- Great Ormond Street Hospital (GB)
- Royal Perth Hospital (AU)
- Corresponding author
- Beggs, Alan H.
- ORCID
- Gupta, Vandana A.
- Ravenscroft, Gianina
- Shaheen, Ranad
- Shiina, Masaaki
- Ogata, Kazuhiro
- Darras, Basil T.
- Farrar, Michelle A.
- North, Kathryn N.
- Sandaradura, Sarah A.
- Nishino, Ichizo
- Hayashi, Yukiko K.
- Sewry, Caroline A.
- Brownstein, Catherine A.
- Yu, Timothy W.
- Davis, Mark R.
- Matsumoto, Naomichi
- Alkuraya, Fowzan S.
- Laing, Nigel G.
- Beggs, Alan H.
- Venue
- The American Journal of Human Genetics
- Publisher
- Elsevier BV
- Published
- 2013-12
- Volume
- 93
- Issue
- 6
- Pages
- 1108-1117
- ISSN
- 0002-9297 (ISSN-L)
- PMC
- PMC3852928
- OpenAlex
- W1973202003
- Cited by
- 168
- References
- 35
- Citations by year
- 2026: 6 · 2025: 8 · 2024: 12 · 2023: 8 · 2022: 9 · 2021: 10 · 2020: 11 · 2019: 15 · 2018: 22 · 2017: 12 · 2016: 16 · 2015: 16 · 2014: 23
- FWCI
- 8.22
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- The American Journal of Human Genetics (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- UWA Profiles and Research Repository (UWA) (submittedVersion, other-oa)
- Adelaide Research & Scholarship (AR&S) (University of Adelaide) (submittedVersion)
- UCL Discovery (University College London) (submittedVersion)
- Funders
- Muscular Dystrophy Association (MDA 201302)
- Rosetrees Trust
- Great Ormond Street Hospital Charity
- National Institutes of Health (HD18655)
- Medical Research Council (MR/K000608/1)
- National Health and Medical Research Council (1022707, 1002147, 1035955)
- Japan Society for the Promotion of Science (24118005, 24249019)
- National Heart, Lung, and Blood Institute
- National Institute of Arthritis and Musculoskeletal and Skin Diseases (K01AR062601, R01AR044345)
- Eunice Kennedy Shriver National Institute of Child Health and Human Development (P30HD018655, P30HD-18655)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Muscle Physiology and Disorders
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Genomics and Rare Diseases
- Health Sciences › Medicine › Cardiology and Cardiovascular Medicine › Cardiomyopathy and Myosin Studies
- Keywords
- nemaline myopathy, ubiquitination, myofibrillar disorganization, nemaline bodies, genetic heterogeneity, compound heterozygosity, frameshift mutation, missense mutations, zebrafish model, motor function, congenital muscle disease
- MeSH terms
- Adolescent, Animals, Child, Child, Preschool, Cytoskeletal Proteins, Female, Humans, Infant, Infant, Newborn, Male, Models, Molecular, Mutation, Myofibrils, Protein Conformation, Proteins, Zebrafish, Signal Transduction, Gene Expression, Myopathies, Nemaline, Fatal Outcome, Muscle, Skeletal, Gene Order, Protein Interaction Domains and Motifs, Ubiquitination, Genetic Association Studies
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
