A Lethal Defect of Mitochondrial and Peroxisomal Fission

Waterham, Hans R.; Koster, Janet; van Roermund, Carlo W.T.; Mooyer, Petra A.W.; Wanders, Ronald J.A.; Leonard, James V.

doi:10.1056/nejmoa064436

Cited by 749Mitochondrial Function and PathologyMetabolism and Genetic DisordersAutophagy in Disease and Therapy

A Lethal Defect of Mitochondrial and Peroxisomal Fission

Waterham, Hans R., Koster, Janet, van Roermund, Carlo W.T., Mooyer, Petra A.W., Wanders, Ronald J.A., Leonard, James V.·2007·New England Journal of Medicine

DOI 10.1056/nejmoa064436

Open this paper in CoChat — free account

Abstract

We report on a newborn girl with microcephaly, abnormal brain development, optic atrophy and hypoplasia, persistent lactic acidemia, and a mildly elevated plasma concentration of very-long-chain fatty acids. We found a defect of the fission of both mitochondria and peroxisomes, as well as a heterozygous, dominant-negative mutation in the dynamin-like protein 1 gene (DLP1). The DLP1 protein has previously been implicated, in vitro, in the fission of both these organelles. Overexpression of the mutant DLP1 in control cells reproduced the fission defect. Our findings are representative of a class of disease characterized by defects in both mitochondria and peroxisomes.

Integrity signals

Registry

Crossref · 10.1056/nejmoa064436

Cites

25 of 25 references verified0 citation errors · 0 not checkable

Statistics

Recomputing p-values needs the paper’s full text.

Claims the paper makes

This paper’s full text isn’t openly available, so its claims and self-check weren’t run. The registry and citation checks still apply.

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?

Mutations in DRP1 lead to a severe neurological syndrome with microencephaly, hypotonia, alterations in brain development, and metabolism that cause neonatal lethality due to multi-system damage.
“Mutations in DRP1 lead to a severe neurological syndrome with microencephaly, hypotonia, alterations in brain development, and metabolism that cause neonatal lethality due to multi-system damage [201–203].”
From The connection between the dynamic remodeling of the mitochondrial network and the regulation of muscle mass (2021) · cites this paper as [201]

Dynamin-related Protein Drp1 Is Required for Mitochondrial Division in Mammalian Cells
Smirnova, E., Griparić, L., Shurland, D., & van der Bliek, A. M. (2001) · Molecular Biology of the Cell · doi:10.1091/mbc.12.8.2245 · Cited by 1,938 · see citing works
Mutations in the mitochondrial GTPase mitofusin 2 cause Charcot-Marie-Tooth neuropathy type 2A
Züchner, S., Mersiyanova, I. V., Muglia, M., Bissar-Tadmouri, N., Rochelle, J., Dadali, E. L., Zappia, M., Nelis, E., Patitucci, A., Senderek, J., et al. (2004) · Nature Genetics · doi:10.1038/ng1341 · Cited by 1,572 · see citing works
The dynamin superfamily: universal membrane tubulation and fission molecules?
Praefcke, G. J. K., & McMahon, H. T. (2004) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1313 · Cited by 1,380 · see citing works
OPA1, encoding a dynamin-related GTPase, is mutated in autosomal dominant optic atrophy linked to chromosome 3q28
Alexander, C., Votruba, M., Pesch, U. E. A., Thiselton, D. L., Mayer, S., Moore, A., Rodriguez, M., Kellner, U., Leo-Kottler, B., Auburger, G., et al. (2000) · Nature Genetics · doi:10.1038/79944 · Cited by 1,330 · see citing works
The Mitochondrial Protein hFis1 Regulates Mitochondrial Fission in Mammalian Cells through an Interaction with the Dynamin-Like Protein DLP1
Yoon, Y., Krueger, E. W., Oswald, B. J., & McNiven, M. A. (2003) · Molecular and Cellular Biology · doi:10.1128/mcb.23.15.5409-5420.2003 · Cited by 820 · see citing works
Mitochondrial Morphology and Dynamics in Yeast and Multicellular Eukaryotes
Okamoto, K., & Shaw, J. M. (2005) · Annual Review of Genetics · doi:10.1146/annurev.genet.38.072902.093019 · Cited by 737 · see citing works
hFis1, a Novel Component of the Mammalian Mitochondrial Fission Machinery
James, D. I., Parone, P. A., Mattenberger, Y., & Martinou, J. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m303758200 · Cited by 653 · see citing works
Emerging functions of mammalian mitochondrial fusion and fission
Chen, H., & Chan, D. C. (2005) · Human Molecular Genetics · doi:10.1093/hmg/ddi270 · Cited by 538 · see citing works
Dynamin-like protein 1 is involved in peroxisomal fission
Koch, A., Thiemann, M., Grabenbauer, M., Yoon, Y., McNiven, M. A., & Schrader, M. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m211761200 · Cited by 374 · see citing works
Mutations in the pleckstrin homology domain of dynamin 2 cause dominant intermediate Charcot-Marie-Tooth disease
Zuchner, S. L., Noureddine, M., Kennerson, M. L., Verhoeven, K., Claeys, K. G., Jonghe, P. D., Merory, J. R., Oliveira, S. A., Speer, M. C., Stenger, J. E., et al. (2005) · Nature Genetics · doi:10.1038/ng1514 · Cited by 363 · see citing works
The Dynamin-like Protein DLP1 Is Essential for Normal Distribution and Morphology of the Endoplasmic Reticulum and Mitochondria in Mammalian Cells
Pitts, K. R., Yoon, Y., Krueger, E. W., & McNiven, M. A. (1999) · Molecular Biology of the Cell · doi:10.1091/mbc.10.12.4403 · Cited by 311 · see citing works
A role for Fis1 in both mitochondrial and peroxisomal fission in mammalian cells
Koch, A., Yoon, Y., Bonekamp, N. A., McNiven, M. A., & Schrader, M. (2005) · Molecular Biology of the Cell · doi:10.1091/mbc.e05-02-0159 · Cited by 308 · see citing works
Mammalian Dynamin-like Protein DLP1 Tubulates Membranes
Yoon, Y., Pitts, K. R., & McNiven, M. A. (2001) · Molecular Biology of the Cell · doi:10.1091/mbc.12.9.2894 · Cited by 285 · see citing works
Intra- and Intermolecular Domain Interactions of the C-terminal GTPase Effector Domain of the Multimeric Dynamin-like GTPase Drp1
Zhu, P.-P., Patterson, A. D., Stadler, J., Seeburg, D. P., Sheng, M., & Blackstone, C. D. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m404105200 · Cited by 221 · see citing works
The Dynamin-like GTPase DLP1 Is Essential for Peroxisome Division and Is Recruited to Peroxisomes in Part by PEX11
Li, X., & Gould, S. J. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m212031200 · Cited by 215 · see citing works
Shared components of mitochondrial and peroxisomal division
Schrader, M. (2006) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2006.01.004 · Cited by 134 · see citing works
Peroxisomal Bifunctional Protein Deficiency Revisited: Resolution of Its True Enzymatic and Molecular Basis
van Grunsven, E. G., van Berkel, E., Mooijer, P. A. W., Watkins, P. A., Moser, H. W., Suzuki, Y., Jiang, L., Hashimoto, T., Höefler, G., Adamski, J., et al. (1999) · The American Journal of Human Genetics · doi:10.1086/302180 · Cited by 108 · see citing works
Self-citation
Rapid stable isotope dilution analysis of very-long-chain fatty acids, pristanic acid and phytanic acid using gas chromatography–electron impact mass spectrometry
Vreken, P., van Lint, A. E. M., Bootsma, A. H., Overmars, H., Wanders, R. J. A., & Gennip, A. H. (1998) · Journal of Chromatography B Biomedical Sciences and Applications · doi:10.1016/s0378-4347(98)00186-8 · Cited by 99 · see citing works
Self-citation
Measurement of peroxisomal fatty acid β‐oxidation in cultured human skin fibroblasts
Wanders, R. J. A., Denis, S. W., Ruiter, J. P. N., Schutgens, R. B. H., van Roermund, C. W. T., & Jacobs, B. S. (1995) · Journal of Inherited Metabolic Disease · doi:10.1007/bf00711434 · Cited by 95 · see citing works
Self-citation
Studies on mitochondrial oxidative phosphorylation in permeabilized human skin fibroblasts: application to mitochondrial encephalomyopathies
Wanders, R. J. A., Ruiter, J. P. N., & Wijburg, F. A. (1993) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/0925-4439(93)90024-u · Cited by 66 · see citing works
Self-citation
Peroxisome division is impaired in a CHO cell mutant with an inactivating point-mutation in dynamin-like protein 1 gene
Tanaka, A., Kobayashi, S., & Fujiki, Y. (2006) · Experimental Cell Research · doi:10.1016/j.yexcr.2006.01.028 · Cited by 62 · see citing works
The expanding phenotype of mitochondrial myopathy
DiMauro, S., & Gurgel‐Giannetti, J. (2005) · Current Opinion in Neurology · doi:10.1097/01.wco.0000179761.63486.1a · Cited by 42 · see citing works
Diagnostic Value of Succinate Ubiquinone Reductase Activity in the Identification of Patients with Mitochondrial DNA Depletion
Hargreaves, I. P., Rahman, S., Guthrie, P., et al. (2002) · Journal of Inherited Metabolic Disease · doi:10.1023/a:1015104910239 · Cited by 30 · see citing works
Genomic organization, alternative splicing, and promoter analysis of human dynamin-like protein gene
Howng, S., Sy, W.-D., Cheng, T.-S., et al. (2004) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2003.12.172 · Cited by 18 · see citing works
Erratum: Corrigendum: Mutations in the mitochondrial GTPase mitofusin 2 cause Charcot-Marie-Tooth neuropathy type 2A
Zuchner, S. L., Mersiyanova, I., Muglia, M., et al. (2004) · Nature Genetics · doi:10.1038/ng0604-660 · Cited by 14 · see citing works

Flagged first, then by citations

Sorted by citations

Mitochondria: In Sickness and in Health
Nunnari, J., & Suomalainen, A. (2012) · Cell · doi:10.1016/j.cell.2012.02.035 · Cited by 3,479 · see citing works
Mitochondrial fusion and fission in cell life and death
Westermann, B. (2010) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3013 · Cited by 2,002 · see citing works
The cell biology of mitochondrial membrane dynamics
Giacomello, M., Pyakurel, A., Glytsou, C., & Scorrano, L. (2020) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-020-0210-7 · Cited by 1,550 · see citing works
Mitochondrial Dynamics and Its Involvement in Disease
Chan, D. C. (2020) · Annual Review of Pathology: Mechanisms of Disease · doi:10.1146/annurev-pathmechdis-012419-032711 · Cited by 1,416 · see citing works
Functions and dysfunctions of mitochondrial dynamics
Detmer, S. A., & Chan, D. C. (2007) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2275 · Cited by 1,369 · see citing works
Mitochondrial Dynamics in the Regulation of Nutrient Utilization and Energy Expenditure
Liesa, M., & Shirihai, O. S. (2013) · Cell Metabolism · doi:10.1016/j.cmet.2013.03.002 · Cited by 1,341 · see citing works
Mitochondrial dynamics and apoptosis
Suen, D.-F., Norris, K. L., & Youle, R. J. (2008) · Genes & Development · doi:10.1101/gad.1658508 · Cited by 1,270 · see citing works
Fusion and fission: interlinked processes critical for mitochondrial health
Chan, D. C. (2012) · Annual Review of Genetics · doi:10.1146/annurev-genet-110410-132529 · Cited by 1,196 · see citing works
Mff is an essential factor for mitochondrial recruitment of Drp1 during mitochondrial fission in mammalian cells
Otera, H., Wang, C., Cleland, M. M., Setoguchi, K., Yokota, S., Youle, R. J., & Mihara, K. (2010) · Journal of Cell Biology · doi:10.1083/jcb.201007152 · Cited by 1,110 · see citing works
Mitochondrial fission factor Drp1 is essential for embryonic development and synapse formation in mice
Ishihara, N., Nomura, M., Jofuku, A., Kato, H., Suzuki, S. O., Masuda, K., Otera, H., Nakanishi, Y., Nonaka, I., Goto, Y.-I., et al. (2009) · Nature Cell Biology · doi:10.1038/ncb1907 · Cited by 1,066 · see citing works
Mitochondrial Dynamics in Mammalian Health and Disease
Liesa, M., Palacín, M., & Zorzano, A. (2009) · Physiological Reviews · doi:10.1152/physrev.00030.2008 · Cited by 953 · see citing works
Regulation of mitochondrial dynamics in acute kidney injury in cell culture and rodent models
Brooks, C., Wei, Q., Cho, S.-G., & Dong, Z. (2009) · Journal of Clinical Investigation · doi:10.1172/jci37829 · Cited by 735 · see citing works
The dynamin-related GTPase Drp1 is required for embryonic and brain development in mice
Wakabayashi, J., Zhang, Z., Wakabayashi, N., Tamura, Y., Fukaya, M., Kensler, T. W., Iijima, M., & Sesaki, H. (2009) · Journal of Cell Biology · doi:10.1083/jcb.200903065 · Cited by 667 · see citing works
Mitochondrial optic neuropathies—Disease mechanisms and therapeutic strategies
Yu-Wai-Man, P., Griffiths, P. G., & Chinnery, P. F. (2011) · Progress in Retinal and Eye Research · doi:10.1016/j.preteyeres.2010.11.002 · Cited by 633 · see citing works
OPA1 mutations induce mitochondrial DNA instability and optic atrophy 'plus' phenotypes
Amati-Bonneau, P., Valentino, M. L., Reynier, P., Gallardo, M. E., Bornstein, B., Boissiere, A., Campos, Y., Rivera, H., de la Aleja, J. G., Carroccia, R., et al. (2008) · Brain · doi:10.1093/brain/awm298 · Cited by 520 · see citing works
Mitochondrial quality control and muscle mass maintenance.
Romanello, V., & Sandri, M. (2016) · Frontiers in Physiology · doi:10.3389/fphys.2015.00422 · Cited by 434 · see citing works
Mutation of OPA1 causes dominant optic atrophy with external ophthalmoplegia, ataxia, deafness and multiple mitochondrial DNA deletions: a novel disorder of mtDNA maintenance
Hudson, G., Amati-Bonneau, P., Blakely, E. L., Stewart, J. D., He, L., Schaefer, A. M., Griffiths, P. G., Ahlqvist, K., Suomalainen, A., Reynier, P., et al. (2008) · Brain · doi:10.1093/brain/awm272 · Cited by 428 · see citing works
Pharmacological approaches to restore mitochondrial function
Andreux, P. A., Houtkooper, R. H., & Auwerx, J. (2013) · Nature Reviews Drug Discovery · doi:10.1038/nrd4023 · Cited by 383 · see citing works
Tau Promotes Neurodegeneration via DRP1 Mislocalization In Vivo
DuBoff, B., Götz, J., & Feany, M. B. (2012) · Neuron · doi:10.1016/j.neuron.2012.06.026 · Cited by 377 · see citing works
The Peroxisome-Mitochondria Connection: How and Why?
Fransen, M., Lismont, C., & Walton, P. (2017) · International Journal of Molecular Sciences · doi:10.3390/ijms18061126 · Cited by 351 · see citing works
“For example, defects in DNM1L have been associated with the autosomal dominant disorder encephalopathy due to defective mitochondrial and peroxisomal fission (EMPF), a lethal disorder characterized by cerebral dysgenesis, optic atrophy and hypoplasia, and seizures [167]; infantile encephalopathy [168]; and refractory…”
Background
Repairing mitochondrial dysfunction in disease
Sorrentino, V., Menzies, K. J., & Auwerx, J. (2018) · Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev-pharmtox-010716-104908 · Cited by 337 · see citing works
Adaptor Proteins MiD49 and MiD51 Can Act Independently of Mff and Fis1 in Drp1 Recruitment and Are Specific for Mitochondrial Fission
Palmer, C. S., Elgass, K. D., Parton, R. G., Osellame, L. D., Stojanovski, D., & Ryan, M. T. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.479873 · Cited by 301 · see citing works
Total Skeletal Muscle PGC-1 Deficiency Uncouples Mitochondrial Derangements from Fiber Type Determination and Insulin Sensitivity
Zechner, C., Lai, L., Zechner, J. F., Geng, T., Yan, Z., Rumsey, J. W., Collia, D., Chen, Z., Wozniak, D. F., Leone, T. C., et al. (2010) · Cell Metabolism · doi:10.1016/j.cmet.2010.11.008 · Cited by 274 · see citing works
“This latter function has been ascribed to the ongoing dynamics of fusion and fission, which serve to maintain mitochondrial quality control (Chen et al., 2005; Waterham et al., 2007; Zhang and Chan, 2007).”
Background
Local translation of extranuclear lamin B promotes axon maintenance
Yoon, B. C., Jung, H., Dwivedy, A., O'Hare, C. M., Zivraj, K. H., & Holt, C. E. (2012) · Cell · doi:10.1016/j.cell.2011.11.064 · Cited by 263 · see citing works
The constriction and scission machineries involved in mitochondrial fission
Kraus, F., & Ryan, M. T. (2017) · Journal of Cell Science · doi:10.1242/jcs.199562 · Cited by 244 · see citing works
Loss of MARCH5 mitochondrial E3 ubiquitin ligase induces cellular senescence through dynamin-related protein 1 and mitofusin 1
Park, Y.-Y., Lee, S., Karbowski, M., Neutzner, A., Youle, R. J., & Cho, H. (2010) · Journal of Cell Science · doi:10.1242/jcs.061481 · Cited by 244 · see citing works
Skeletal muscle mitochondria as a target to prevent or treat type 2 diabetes mellitus
Hesselink, M. K. C., Schrauwen-Hinderling, V., & Schrauwen, P. (2016) · Nature Reviews Endocrinology · doi:10.1038/nrendo.2016.104 · Cited by 242 · see citing works
Dynamics of nucleoid structure regulated by mitochondrial fission contributes to cristae reformation and release of cytochrome <i>c</i>
Ban-Ishihara, R., Ishihara, T., Sasaki, N., Mihara, K., & Ishihara, N. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1301951110 · Cited by 231 · see citing works
Mitochondrial Translation and Beyond: Processes Implicated in Combined Oxidative Phosphorylation Deficiencies
Smits, P., Smeitink, J., & van den Heuvel, L. (2010) · Journal of Biomedicine and Biotechnology · doi:10.1155/2010/737385 · Cited by 202 · see citing works
The connection between the dynamic remodeling of the mitochondrial network and the regulation of muscle mass
Romanello, V., & Sandri, M. (2021) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-020-03662-0 · Cited by 197 · see citing works
Fission and proliferation of peroxisomes
Schrader, M., Bonekamp, N. A., & Islinger, M. (2012) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2011.12.014 · Cited by 189 · see citing works
Genomic analysis of mitochondrial diseases in a consanguineous population reveals novel candidate disease genes
Shamseldin, H. E., Alshammari, M., Al-Sheddi, T., Salih, M. A., Alkhalidi, H., Kentab, A., Repetto, G. M., Hashem, M., & Alkuraya, F. S. (2012) · Journal of Medical Genetics · doi:10.1136/jmedgenet-2012-100836 · Cited by 182 · see citing works
A neurodegenerative perspective on mitochondrial optic neuropathies
Yu-Wai-Man, P., Votruba, M., Burté, F., La Morgia, C., Barboni, P., & Carelli, V. (2016) · Acta Neuropathologica · doi:10.1007/s00401-016-1625-2 · Cited by 176 · see citing works
Titration of mitochondrial fusion rescues <i>Mff</i> -deficient cardiomyopathy
Chen, H., Ren, S., Clish, C., Jain, M., Mootha, V., McCaffery, J. M., & Chan, D. C. (2015) · Journal of Cell Biology · doi:10.1083/jcb.201507035 · Cited by 168 · see citing works
Organelle interplay-peroxisome interactions in health and disease.
Schrader, M., Kamoshita, M., & Islinger, M. (2020) · Journal of Inherited Metabolic Disease · doi:10.1002/jimd.12083 · Cited by 149 · see citing works
Muscle-specific Drp1 overexpression impairs skeletal muscle growth via translational attenuation
Touvier, T., De Palma, C., Rigamonti, E., Scagliola, A., Incerti, E., Mazelin, L., Thomas, J.-L., D'Antonio, M., Politi, L., Schaeffer, L., et al. (2015) · Cell Death & Disease · doi:10.1038/cddis.2014.595 · Cited by 140 · see citing works
DNM1L-related mitochondrial fission defect presenting as refractory epilepsy
Care4Rare Consortium, Vanstone, J. R., Smith, A. M., McBride, S., Naas, T., Holcik, M., Antoun, G., Harper, M.-E., Michaud, J., Sell, E., et al. (2016) · European Journal of Human Genetics · doi:10.1038/ejhg.2015.243 · Cited by 135 · see citing works
Disturbed mitochondrial and peroxisomal dynamics due to loss of MFF causes Leigh-like encephalopathy, optic atrophy and peripheral neuropathy
Koch, J., Feichtinger, R. G., Freisinger, P., Pies, M., Schrödl, F., Iuso, A., Sperl, W., Mayr, J. A., Prokisch, H., & Haack, T. B. (2016) · Journal of Medical Genetics · doi:10.1136/jmedgenet-2015-103500 · Cited by 127 · see citing works
Simultaneous impairment of mitochondrial fission and fusion reduces mitophagy and shortens replicative lifespan
Bernhardt, D., Müller, M., Reichert, A. S., & Osiewacz, H. D. (2015) · Scientific Reports · doi:10.1038/srep07885 · Cited by 125 · see citing works
The Interplay between Mitochondrial Morphology and Myomitokines in Aging Sarcopenia
Romanello, V. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms22010091 · Cited by 101 · see citing works
Downregulation of dynamin-related protein 1 contributes to impaired autophagic flux and angiogenic function in senescent endothelial cells
Lin, J.-R., Shen, W.-L., Yan, C., & Gao, P.-J. (2015) · Arteriosclerosis Thrombosis and Vascular Biology · doi:10.1161/atvbaha.115.305706 · Cited by 97 · see citing works
Lethal Disorder of Mitochondrial Fission Caused by Mutations in DNM1L
Yoon, G., Malam, Z., Paton, T., Marshall, C. R., Hyatt, E., Ivakine, Z., Scherer, S. W., Lee, K.-S., Hawkins, C., Cohn, R. D., et al. (2016) · The Journal of Pediatrics · doi:10.1016/j.jpeds.2015.12.060 · Cited by 78 · see citing works
A novel mechanism causing imbalance of mitochondrial fusion and fission in human myopathies
Bartsakoulia, M., Pyle, A., Troncoso-Chandía, D., Vial-Brizzi, J., Paz-Fiblas, M. V., Duff, J., Griffin, H., Boczonadi, V., Lochmüller, H., Kleinle, S., et al. (2018) · Human Molecular Genetics · doi:10.1093/hmg/ddy033 · Cited by 68 · see citing works
Resistance of Dynamin-related Protein 1 Oligomers to Disassembly Impairs Mitophagy, Resulting in Myocardial Inflammation and Heart Failure
Cahill, T. J., Leo, V., Kelly, M., Stockenhuber, A., Kennedy, N. W., Bao, L., Cereghetti, G., Harper, A. R., Czibik, G., Lao, C., et al. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m115.665695 · Cited by 66 · see citing works
Glucose Stimulation Induces Dynamic Change of Mitochondrial Morphology to Promote Insulin Secretion in the Insulinoma Cell Line INS-1E
Jhun, B. S., Lee, H., Jin, Z.-G., & Yoon, Y. (2013) · PLoS ONE · doi:10.1371/journal.pone.0060810 · Cited by 49 · see citing works
Mitochondrial dynamics in aging and disease
Bereiter-Hahn, J. (2014) · Progress in molecular biology and translational science · doi:10.1016/b978-0-12-394625-6.00004-0 · Cited by 48 · see citing works
Self-Interaction of Human Pex11pβ during Peroxisomal Growth and Division
Bonekamp, N. A., Grille, S., Cardoso, M. J., Almeida, M., Aroso, M., Gomes, S., Magalhaes, A. C., Ribeiro, D., Islinger, M., & Schrader, M. (2013) · PLoS ONE · doi:10.1371/journal.pone.0053424 · Cited by 29 · see citing works
Resistance of dynamin-related protein 1 oligomers to disassembly impairs mitophagy, resulting in myocardial inflammation and heart failure
Cahill, T. J., Leo, V., Kelly, M., Stockenhuber, A., Kennedy, N. W., Bao, L., Cereghetti, G. M., Harper, A. R., Czibik, G., Liao, C., et al. (2016) · Journal of Biological Chemistry · doi:10.1074/jbc.a115.665695 · Cited by 14 · see citing works
“Mitochondria in Drp1 C452F MEFs Are Morphologically and Functionally Abnormal—Assessment of mitochondrial fissionfusion in the heart is challenging, possibly because of relative low event frequency or constraints on mitochondrial morphology imposed by the “sardine tin” architecture of the cardiomyocyte (11, 18, 19).”
Background

Authors: Waterham, H. R., Koster, J., van Roermund, C. W. T., Mooyer, P. A. W., Wanders, R. J. A., & Leonard, J. V.
Affiliations: Amsterdam UMC Location University of Amsterdam (NL)
University College London (GB)
ORCID: Waterham, Hans R.
Wanders, Ronald J.A.
Venue: New England Journal of Medicine
Publisher: Massachusetts Medical Society
Published: 2007-04-26
Volume: 356
Issue: 17
Pages: 1736-1741
ISSN: 0028-4793 (ISSN-L)
1533-4406
DOI: 10.1056/nejmoa064436
OpenAlex: W1978268445
Cited by: 749
References: 25
Citations by year: 2026: 16 · 2025: 30 · 2024: 30 · 2023: 16 · 2022: 31 · 2021: 48 · 2020: 45 · 2019: 49 · 2018: 40 · 2017: 53 · 2016: 50 · 2015: 46 · 2014: 38 · 2013: 46 · 2012: 64
FWCI: 14.75
Type: journal article
Language: en
Open access: closed
Locations: New England Journal of Medicine (publishedVersion)
PubMed (publishedVersion)
Pure Amsterdam UMC (publishedVersion)
Data Archiving and Networked Services (DANS) (submittedVersion)
UCL Discovery (University College London) (submittedVersion)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
Life Sciences › Biochemistry, Genetics and Molecular Biology › Clinical Biochemistry › Metabolism and Genetic Disorders
Health Sciences › Medicine › Epidemiology › Autophagy in Disease and Therapy
Keywords: mitochondrial fission, Drp1, dominant negative mutation, microcephaly, optic atrophy, lactic acidemia, very long chain fatty acids
MeSH terms: Abnormalities, Multiple, Acidosis, Lactic, Eye Abnormalities, Fatty Acids, Female, Fibroblasts, Humans, Infant, Newborn, Male, Microcephaly, Microtubule-Associated Proteins, Mitochondria, Muscle Hypotonia, Mutation, Open Reading Frames, Sequence Analysis, DNA, Fatal Outcome, GTP Phosphohydrolases, Peroxisomes, Mitochondrial Proteins, Dynamins

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

A Lethal Defect of Mitochondrial and Peroxisomal Fission

Abstract

Integrity signals

Claims the paper makes

Claims other papers make about this one

Cites

Cited by

Related

Record

About these checks