ELOVL1 production of C24 acyl-CoAs is linked to C24 sphingolipid synthesis

Fatty acid composition of adipose tissue and blood in humans and its use as a biomarker of dietary intake

Hodson, L., Skeaff, C. M., & Fielding, B. A. (2008) · Progress in Lipid Research · doi:10.1016/j.plipres.2008.03.003 · Cited by 1,315 · see citing works

Global analysis of the yeast lipidome by quantitative shotgun mass spectrometry

Ejsing, C. S., Sampaio, J. L., Surendranath, V., Duchoslav, E., Ekroos, K., Klemm, R. W., Simons, K., & Shevchenko, A. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0811700106 · Cited by 1,053 · see citing works

Fatty acid elongases in mammals: their regulation and roles in metabolism

JAKOBSSON, A., WESTERBERG, R., & JACOBSSON, A. (2006) · Progress in Lipid Research · doi:10.1016/j.plipres.2006.01.004 · Cited by 936 · see citing works

Sphingolipidomics: High-throughput, structure-specific, and quantitative analysis of sphingolipids by liquid chromatography tandem mass spectrometry

Merrill, A. H., Sullards, M. C., Allegood, J. C., Kelly, S. L., & Wang, E. L. (2005) · Methods · doi:10.1016/j.ymeth.2005.01.009 · Cited by 594 · see citing works

Elongation of long-chain fatty acids

Leonard, A. E., Pereira, S. L., Sprecher, H. W., & Huang, Y. S. (2003) · Progress in Lipid Research · doi:10.1016/s0163-7827(03)00040-7 · Cited by 584 · see citing works

Crucial role of a long-chain fatty acid elongase, Elovl6, in obesity-induced insulin resistance

Matsuzaka, T., Shimano, H., Yahagi, N., Kato, T., Atsumi, A., Yamamoto, T., Inoue, N., Ishikawa, M., Okada, S., Ishigaki, N., et al. (2007) · Nature Medicine · doi:10.1038/nm1662 · Cited by 546 · see citing works

Thematic Review Series: Proteomics. An integrated omics analysis of eicosanoid biology

Buczynski, M. W., Dumlao, D. S., & Dennis, E. A. (2009) · Journal of Lipid Research · doi:10.1194/jlr.r900004-jlr200 · Cited by 535 · see citing works

ELO2 and ELO3, Homologues of theSaccharomyces cerevisiae ELO1 Gene, Function in Fatty Acid Elongation and Are Required for Sphingolipid Formation

Oh, C.-S., Toke, D. A., MANDALA, S. M., & Martin, C. E. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.28.17376 · Cited by 487 · see citing works

Mammalian Long-Chain Acyl-CoA Synthetases

Soupène, E., & Kuypers, F. A. (2008) · Experimental Biology and Medicine · doi:10.3181/0710-mr-287 · Cited by 465 · see citing works

Mammalian Lass6 and its related family members regulate synthesis of specific ceramides

Mizutani, Y., Kihara, A., & Igarashi, Y. (2005) · Biochemical Journal · doi:10.1042/bj20050291 · Cited by 376 · see citing works

Identification of a Mammalian Long Chain Fatty Acyl Elongase Regulated by Sterol Regulatory Element-binding Proteins

Moon, Y.-A., Shah, N. A., Mohapatra, S., Warrington, J. A., & Horton, J. D. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m108413200 · Cited by 353 · see citing works

Adult ceramide synthase 2 (CERS2)-deficient mice exhibit myelin sheath defects, cerebellar degeneration, and hepatocarcinomas

Imgrund, S., Hartmann, D., Farwanah, H., Eckhardt, M., Sandhoff, R., Degen, J., Gieselmann, V., Sandhoff, K., & Willecke, K. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.031971 · Cited by 299 · see citing works

A Molecular Caliper Mechanism for Determining Very Long-Chain Fatty Acid Length

Denic, V., & Weissman, J. S. (2007) · Cell · doi:10.1016/j.cell.2007.06.031 · Cited by 279 · see citing works

A Critical Role for Ceramide Synthase 2 in Liver Homeostasis

Pewzner‐Jung, Y., Park, H. J., Laviad, E. L., Silva, L. C., Lahiri, S., Stiban, J., Erez-Roman, R., Brügger, B., Sachsenheimer, T., Wieland, F., et al. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.077594 · Cited by 263 · see citing works

Ceramide biosynthesis in keratinocyte and its role in skin function

Mizutani, Y., Mitsutake, S., Tsuji, K., Kihara, A., & Igarashi, Y. (2009) · Biochimie · doi:10.1016/j.biochi.2009.04.001 · Cited by 254 · see citing works

A Critical Role for Ceramide Synthase 2 in Liver Homeostasis

Pewzner‐Jung, Y., Brenner, O. J., Braun, S., Laviad, E. L., Ben‐Dor, S., Feldmesser, E., Horn‐Saban, S., Amann‐Zalcenstein, D., Raanan, C., Berkutzki, T., et al. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.077610 · Cited by 230 · see citing works

Cloning of a human cDNA encoding a novel enzyme involved in the elongation of long-chain polyunsaturated fatty acids

Leonard, A. E., BOBIK, E. G., DORADO, J., Kroeger, P. E., Chuang, L., Thurmond, J. M., PARKER-BARNES, J. M., Das, T., Huang, Y. S., & Mukerji, P. (2000) · Biochemical Journal · doi:10.1042/bj3500765 · Cited by 220 · see citing works

Role of a New Mammalian Gene Family in the Biosynthesis of Very Long Chain Fatty Acids and Sphingolipids

Tvrdík, P., Westerberg, R., Silve, S., Asadi, A., Jakobsson, A., Cannon, B., Loison, G., & Jacobsson, A. (2000) · The Journal of Cell Biology · doi:10.1083/jcb.149.3.707 · Cited by 218 · see citing works

Identification and expression of mammalian long‐chain PUFA elongation enzymes

Leonard, A. E., Kelder, B., Bobik, E. G., Chuang, L., Lewis, C. J., Kopchick, J. J., Mukerji, P., & Huang, Y. (2002) · Lipids · doi:10.1007/s11745-002-0955-6 · Cited by 209 · see citing works

Role for ELOVL3 and Fatty Acid Chain Length in Development of Hair and Skin Function

Westerberg, R., Tvrdík, P., Undén, A.-B., Månsson, J.-E., Norlen, L. P. O., Jakobsson, A., Holleran, W. H., Elias, P. M., Asadi, A., Flodby, P., et al. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m310529200 · Cited by 196 · see citing works

A shotgun tandem mass spectrometric analysis of phospholipids with normal‐phase and/or reverse‐phase liquid chromatography/electrospray ionization mass spectrometry

Houjou, T., Yamatani, K., Imagawa, M., Shimizu, T., & Taguchi, R. (2005) · Rapid Communications in Mass Spectrometry · doi:10.1002/rcm.1836 · Cited by 191 · see citing works

ELOVL3 Is an Important Component for Early Onset of Lipid Recruitment in Brown Adipose Tissue

Westerberg, R., Månsson, J.-E., Golozoubova, V., Shabalina, I. G., Backlund, E. C., Tvrdík, P., Retterstøl, K., Capecchi, M. R., & Jacobsson, A. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m511588200 · Cited by 149 · see citing works

Characterization of four mammalian 3‐hydroxyacyl‐CoA dehydratases involved in very long‐chain fatty acid synthesis

Ikeda, M., Kanao, Y., Yamanaka, M., Sakuraba, H., Mizutani, Y., Igarashi, Y., & Kihara, A. (2008) · FEBS Letters · doi:10.1016/j.febslet.2008.06.007 · Cited by 132 · see citing works

Involvement of very long fatty acid-containing lactosylceramide in lactosylceramide-mediated superoxide generation and migration in neutrophils

Iwabuchi, K., Prinetti, A., Sonnino, S., Mauri, L., Kobayashi, T., Ishii, K., Kaga, N., Murayama, K., Kurihara, H., Nakayama, H., et al. (2007) · Glycoconjugate Journal · doi:10.1007/s10719-007-9084-6 · Cited by 108 · see citing works

Cig30, a Mouse Member of a Novel Membrane Protein Gene Family, Is Involved in the Recruitment of Brown Adipose Tissue

Tvrdík, P., Asadi, A., Kozak, L. P., Nedergaard, J., Cannon, B., & Jacobsson, A. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.50.31738 · Cited by 106 · see citing works

2-Hydroxy-ceramide synthesis by ceramide synthase family: enzymatic basis for the preference of FA chain length

Mizutani, Y., Kihara, A., Chiba, H., Tojo, H., & Igarashi, Y. (2008) · Journal of Lipid Research · doi:10.1194/jlr.m800158-jlr200 · Cited by 106 · see citing works

Identification and Expression of a Rat Fatty Acid Elongase Involved in the Biosynthesis of C18 Fatty Acids

Inagaki, K., Aki, T., FUKUDA, Y., Kawamoto, S., Shigeta, S., Ono, K., & Suzuki, O. (2002) · Bioscience Biotechnology and Biochemistry · doi:10.1271/bbb.66.613 · Cited by 86 · see citing works

n-3 Fatty acids and cardiovascular disease: Actions and molecular mechanisms

Torrejón, C., Jung, U. J., & Deckelbaum, R. J. (2007) · Prostaglandins Leukotrienes and Essential Fatty Acids · doi:10.1016/j.plefa.2007.10.014 · Cited by 77 · see citing works

The Immunosuppressant SR 31747 Blocks Cell Proliferation by Inhibiting a Steroid Isomerase in Saccharomyces cerevisiae

Silve, S., Leplatois, P., Josse, A., Dupuy, P.-H., Lanau, C., Kaghad, M., Dhers, C., Picard, C., Rahier, A., Taton, M., et al. (1996) · Molecular and Cellular Biology · doi:10.1128/mcb.16.6.2719 · Cited by 72 · see citing works

Characterization of a new gene family developing pleiotropic phenotypes upon mutation inSaccharomyces cerevisiae

Revardel, E., Bonneau, M., Durrens, P., & Aigle, M. (1995) · Biochimica et Biophysica Acta (BBA) - Gene Structure and Expression · doi:10.1016/0167-4781(95)00124-y · Cited by 62 · see citing works

Role of very long fatty acid-containing glycosphingolipids in membrane organization and cell signaling: the model of lactosylceramide in neutrophils

Sonnino, S., Prinetti, A., Nakayama, H., Yangida, M., Ogawa, H., & Iwabuchi, K. (2008) · Glycoconjugate Journal · doi:10.1007/s10719-008-9215-8 · Cited by 61 · see citing works

Membrane Topology and Essential Amino Acid Residues of Phs1, a 3-Hydroxyacyl-CoA Dehydratase Involved in Very Long-chain Fatty Acid Elongation*

Kihara, A., Sakuraba, H., Ikeda, M., Denpoh, A., & Igarashi, Y. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m708993200 · Cited by 59 · see citing works

Fatty acid and long‐chain base composition of gangliosides isolated from adult human brain

Ando, S., & Yu, R. K. (1984) · Journal of Neuroscience Research · doi:10.1002/jnr.490120208 · Cited by 49 · see citing works

5,5-Dimethyl-3-(5-methyl-3-oxo-2-phenyl-2,3-dihydro-1H-pyrazol-4-yl)-1-phenyl-3-(trifluoromethyl)-3,5,6,7-tetrahydro-1H-indole-2,4-dione, a Potent Inhibitor for Mammalian Elongase of Long-Chain Fatty Acids Family 6: Examination of Its Potential Utility as a Pharmacological Tool

Shimamura, K., Kitazawa, H., Miyamoto, Y., Kanesaka, M., Nagumo, A., Yoshimoto, R., Aragane, K., Morita, N., Ohe, T., Takahashi, T., et al. (2009) · Journal of Pharmacology and Experimental Therapeutics · doi:10.1124/jpet.109.150854 · Cited by 16 · see citing works

Sphingolipid and Glycosphingolipid Metabolic Pathways in the Era of Sphingolipidomics

Merrill, A. H. (2011) · Chemical Reviews · doi:10.1021/cr2002917 · Cited by 781 · see citing works

The important role of stratum corneum lipids for the cutaneous barrier function

van Smeden, J., Janssens, M., Gooris, G. S., & Bouwstra, J. A. (2014) · Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids · doi:10.1016/j.bbalip.2013.11.006 · Cited by 549 · see citing works

Increase in short-chain ceramides correlates with an altered lipid organization and decreased barrier function in atopic eczema patients

Janssens, M., van Smeden, J., Gooris, G. S., Bras, W., Portale, G., Caspers, P. J., Vreeken, R. J., Hankemeier, T., Kezic, S., Wolterbeek, R., et al. (2012) · Journal of Lipid Research · doi:10.1194/jlr.p030338 · Cited by 488 · see citing works

Very long-chain fatty acids: elongation, physiology and related disorders

Kihara, A. (2012) · The Journal of Biochemistry · doi:10.1093/jb/mvs105 · Cited by 441 · see citing works

TNF-α and Th2 Cytokines Induce Atopic Dermatitis–Like Features on Epidermal Differentiation Proteins and Stratum Corneum Lipids in Human Skin Equivalents

Danso, M. O., van Drongelen, V., Mulder, A. A., van Esch, J., Scott, H. C., van Smeden, J., Ghalbzouri, A. E., & Bouwstra, J. A. (2014) · Journal of Investigative Dermatology · doi:10.1038/jid.2014.83 · Cited by 333 · see citing works

Metabolism of Very Long-Chain Fatty Acids: Genes and Pathophysiology

Sassa, T., & Kihara, A. (2014) · Biomolecules & Therapeutics · doi:10.4062/biomolther.2014.017 · Cited by 302 · see citing works

The importance of free fatty acid chain length for the skin barrier function in atopic eczema patients

van Smeden, J., Janssens, M., Kaye, E., Caspers, P. J., Lavrijsen, A. P. M., Vreeken, R. J., & Bouwstra, J. A. (2013) · Experimental Dermatology · doi:10.1111/exd.12293 · Cited by 271 · see citing works

Ceramide synthesis in the epidermis

Rabionet, M., Gorgas, K., & Sandhoff, R. (2013) · Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids · doi:10.1016/j.bbalip.2013.08.011 · Cited by 256 · see citing works

Omega-3 fatty acid supplementation and cardiovascular disease

Jump, D. Β., Depner, C. M., & Tripathy, S. (2012) · Journal of Lipid Research · doi:10.1194/jlr.r027904 · Cited by 243 · see citing works

Synthesis and degradation pathways, functions, and pathology of ceramides and epidermal acylceramides

Kihara, A. (2016) · Progress in Lipid Research · doi:10.1016/j.plipres.2016.04.001 · Cited by 238 · see citing works

Ceramide synthases as potential targets for therapeutic intervention in human diseases

Park, J., Park, W., & Futerman, A. H. (2013) · Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids · doi:10.1016/j.bbalip.2013.08.019 · Cited by 231 · see citing works

Sphingolipids and Plant Defense/Disease: The “Death” Connection and Beyond

Berkey, R., Bendigeri, D., & Xiao, S. (2012) · Frontiers in Plant Science · doi:10.3389/fpls.2012.00068 · Cited by 213 · see citing works

X‐linked adrenoleukodystrophy: Pathology, pathophysiology, diagnostic testing, newborn screening and therapies

Turk, B. R., Theda, C., Fatemi, A. S., & Moser, A. B. (2020) · International Journal of Developmental Neuroscience · doi:10.1002/jdn.10003 · Cited by 206 · see citing works

Long chain ceramides and very long chain ceramides have opposite effects on human breast and colon cancer cell growth

Hartmann, D., Lucks, J., Fuchs, S., Schiffmann, S., Schreiber, Y., Ferreirós, N., Merkens, J., Marschalek, R., Geißlinger, G., & Grösch, S. (2012) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2011.12.019 · Cited by 209 · see citing works

Genome-wide DNA methylation profiling in the superior temporal gyrus reveals epigenetic signatures associated with Alzheimer’s disease

Watson, C. T., Roussos, P., Garg, P., Ho, D. J., Azam, N., Katsel, P. L., Haroutunian, V., & Sharp, A. J. (2016) · Genome Medicine · doi:10.1186/s13073-015-0258-8 · Cited by 201 · see citing works

Regulation of long-chain polyunsaturated fatty acid biosynthesis in teleost fish

Xie, D., Chen, C., Dong, Y., You, C., Wang, S., Monroig, Ó., Tocher, D. R., & Li, Y. (2021) · Progress in Lipid Research · doi:10.1016/j.plipres.2021.101095 · Cited by 195 · see citing works

Peroxisomes in brain development and function

Berger, J., Dorninger, F., Forss-Petter, S., & Kunze, M. (2016) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2015.12.005 · Cited by 194 · see citing works

Dynamic Modification of Sphingomyelin in Lipid Microdomains Controls Development of Obesity, Fatty Liver, and Type 2 Diabetes

Mitsutake, S., Zama, K., Yokota, H., Yoshida, T., Tanaka, M., Mitsui, M., Ikawa, M., Okabe, M., Tanaka, Y., Yamashita, T., et al. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.255646 · Cited by 190 · see citing works

Desaturase and elongase-limiting endogenous long-chain polyunsaturated fatty acid biosynthesis

Zhang, J. Y., Kothapalli, K. S. D., & Brenna, J. T. (2016) · Current Opinion in Clinical Nutrition & Metabolic Care · doi:10.1097/mco.0000000000000254 · Cited by 186 · see citing works

The skin barrier: An extraordinary interface with an exceptional lipid organization

Bouwstra, J. A., Nădăban, A., Bras, W., McCabe, C., Bunge, A. L., & Gooris, G. S. (2023) · Progress in Lipid Research · doi:10.1016/j.plipres.2023.101252 · Cited by 184 · see citing works

The role of sphingolipid metabolism in cutaneous permeabilitybarrier formation

Breiden, B., & Sandhoff, K. (2013) · Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids · doi:10.1016/j.bbalip.2013.08.010 · Cited by 176 · see citing works

Oxylipin biosynthesis reinforces cellular senescence and allows detection of senolysis

Wiley, C. D., Sharma, R., Davis, S. S., Lopez-Dominguez, J. A., Mitchell, K. P., Wiley, S., Alimirah, F., Kim, D. E., Payne, T., Rosko, A., et al. (2021) · Cell Metabolism · doi:10.1016/j.cmet.2021.03.008 · Cited by 173 · see citing works

Essential role of the cytochrome P450 CYP4F22 in the production of acylceramide, the key lipid for skin permeability barrier formation

Ohno, Y., Nakamichi, S., Ohkuni, A., Kamiyama, N., Naoe, A., Tsujimura, H., Yokose, U., Sugiura, K., Ishikawa, J., Akiyama, M., et al. (2015) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1503491112 · Cited by 168 · see citing works

Impaired Epidermal Permeability Barrier in Mice Lacking Elovl1 , the Gene Responsible for Very-Long-Chain Fatty Acid Production

Sassa, T., Ohno, Y., Suzuki, S., Nomura, T., Nishioka, C., Kashiwagi, T., Hirayama, T., Akiyama, M., Taguchi, R., Shimizu, H., et al. (2013) · Molecular and Cellular Biology · doi:10.1128/mcb.00192-13 · Cited by 167 · see citing works

Loss-or gain-of-function mutations in ACOX1 cause axonal loss via different mechanisms

Chung, H.-L., Wangler, M. F., Marcogliese, P. C., Jo, J., Ravenscroft, T. A., Zuo, Z., Duraine, L., Sadeghzadeh, S., Li-Kroeger, D., Schmidt, R. E., et al. (2020) · Neuron · doi:10.1016/j.neuron.2020.02.021 · Cited by 154 · see citing works

Elovl2 ablation demonstrates that systemic DHA is endogenously produced and is essential for lipid homeostasis in mice

Pauter, A. M., Olsson, P., Asadi, A., Herslöf, B. G., Csikasz, R. I., Zadravec, D., & Jacobsson, A. (2014) · Journal of Lipid Research · doi:10.1194/jlr.m046151 · Cited by 152 · see citing works

Docosahexaenoic Acid Attenuates Hepatic Inflammation, Oxidative Stress, and Fibrosis without Decreasing Hepatosteatosis in a Ldlr Mouse Model of Western Diet-Induced Nonalcoholic Steatohepatitis

Depner, C. M., Philbrick, K. A., & Jump, D. Β. (2013) · Journal of Nutrition · doi:10.3945/jn.112.171322 · Cited by 145 · see citing works

Altered expression of epidermal lipid bio-synthesis enzymes in atopic dermatitis skin is accompanied by changes in stratum corneum lipid composition

Danso, M. O., Boiten, W. A., van Drongelen, V., Meijling, K. A. G., Gooris, G. S., Ghalbzouri, A. E., Absalah, S., Vreeken, R. J., Kežić, S., van Smeden, J., et al. (2017) · Journal of Dermatological Science · doi:10.1016/j.jdermsci.2017.05.005 · Cited by 140 · see citing works

Interferon-γ Decreases Ceramides with Long-Chain Fatty Acids: Possible Involvement in Atopic Dermatitis and Psoriasis

Tawada, C., Kanoh, H., Nakamura, M., Mizutani, Y., Fujisawa, T., Banno, Y., & Seishima, M. (2013) · Journal of Investigative Dermatology · doi:10.1038/jid.2013.364 · Cited by 138 · see citing works

Ceramides in Skin Health and Disease: An Update

Uchida, Y., & Park, K. (2021) · American Journal of Clinical Dermatology · doi:10.1007/s40257-021-00619-2 · Cited by 138 · see citing works

The enigma of ceramide synthase regulation in mammalian cells

Wegner, M.-S., Schiffmann, S., Parnham, M. J., Geißlinger, G., & Grösch, S. (2016) · Progress in Lipid Research · doi:10.1016/j.plipres.2016.03.006 · Cited by 130 · see citing works

Cold-induced lipid dynamics and transcriptional programs in white adipose tissue

Xu, Z., You, W., Zhou, Y., Chen, W., Wang, Y., & Shan, T. (2019) · BMC Biology · doi:10.1186/s12915-019-0693-x · Cited by 127 · see citing works

PNPLA1 is a transacylase essential for the generation of the skin barrier lipid ω-O-acylceramide

Ohno, Y., Kamiyama, N., Nakamichi, S., & Kihara, A. (2017) · Nature Communications · doi:10.1038/ncomms14610 · Cited by 121 · see citing works

Plasma phospholipid very-long-chain saturated fatty acids and incident diabetes in older adults: the Cardiovascular Health Study

Lemaitre, R. N., Fretts, A. M., Sitlani, C. M., Biggs, M. L., Mukamal, K., King, I. B., Song, X., Djoussé, L., Siscovick, D. S., McKnight, B., et al. (2015) · The American Journal of Clinical Nutrition · doi:10.3945/ajcn.114.101857 · Cited by 117 · see citing works

Novel Cellular Functions of Very Long Chain-Fatty Acids: Insight From ELOVL4 Mutations

Deák, F., Anderson, R. E., Fessler, J. L., & Sherry, D. M. (2019) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2019.00428 · Cited by 110 · see citing works

Biochemical characterization of the very long-chain fatty acid elongase ELOVL7

Naganuma, T., Sato, Y. Z., Sassa, T., Ohno, Y., & Kihara, A. (2011) · FEBS Letters · doi:10.1016/j.febslet.2011.09.024 · Cited by 107 · see citing works

Fatty Acid Elongase 7 Catalyzes Lipidome Remodeling Essential for Human Cytomegalovirus Replication

Purdy, J. G., Shenk, T., & Rabinowitz, J. D. (2015) · Cell Reports · doi:10.1016/j.celrep.2015.02.003 · Cited by 103 · see citing works

A shift in sphingolipid composition from C24 to C16 increases susceptibility to apoptosis in HeLa cells

Sassa, T., Suto, S., Okayasu, Y., & Kihara, A. (2012) · Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids · doi:10.1016/j.bbalip.2012.04.008 · Cited by 102 · see citing works

Glucocerebrosidase: Functions in and Beyond the Lysosome

Boer, D. E. C., van Smeden, J., Bouwstra, J. A., & Aerts, J. M. F. G. (2020) · Journal of Clinical Medicine · doi:10.3390/jcm9030736 · Cited by 101 · see citing works

The structural basis of fatty acid elongation by the ELOVL elongases

Nie, L., Pascoa, T. C., Pike, A. C. W., Bushell, S. R., Quigley, A., Ruda, G. F., Chu, A., Cole, V., Speedman, D., Moreira, T., et al. (2021) · Nature Structural & Molecular Biology · doi:10.1038/s41594-021-00605-6 · Cited by 94 · see citing works

Very long-chain saturated fatty acids and diabetes and cardiovascular disease

Lemaître, R. N., & King, I. B. (2021) · Current Opinion in Lipidology · doi:10.1097/mol.0000000000000806 · Cited by 90 · see citing works

Complex lipid metabolic remodeling is required for efficient hepatitis C virus replication

Hofmann, S., Krajewski, M. P., Scherer, C., Scholz, V., Mordhorst, V., Truschow, P., Schöbel, A., Reimer, R., Schwudke, D., & Herker, E. (2018) · Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids · doi:10.1016/j.bbalip.2018.06.002 · Cited by 90 · see citing works

The Wnt Effector Transcription Factor 7-Like 2 Positively Regulates Oligodendrocyte Differentiation in a Manner Independent of Wnt/β-Catenin Signaling

Hammond, E., Lang, J., Maeda, Y., Pleasure, D., Angus-Hill, M. L., Xu, J., Horiuchi, M., Deng, W., & Guo, F. (2015) · Journal of Neuroscience · doi:10.1523/jneurosci.4787-14.2015 · Cited by 91 · see citing works

Lipid metabolism of the oleaginous yeast Lipomyces starkeyi

Takaku, H., Matsuzawa, T., Yaoi, K., & Yamazaki, H. (2020) · Applied Microbiology and Biotechnology · doi:10.1007/s00253-020-10695-9 · Cited by 89 · see citing works

Identification of genes and pathways involved in the synthesis of Mead acid (20:3n − 9), an indicator of essential fatty acid deficiency

Ichi, I., Kono, N., Arita, Y., Haga, S., Arisawa, K., Yamano, M., Nagase, M., Fujiwara, Y., & Arai, H. (2013) · Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids · doi:10.1016/j.bbalip.2013.10.013 · Cited by 88 · see citing works

Regulation of glucose homeostasis and insulin action by ceramide acyl-chain length: A beneficial role for very long-chain sphingolipid species

Montgomery, M. K., Brown, S. H. J., Lim, X. Y., Fiveash, C. E., Osborne, B., Bentley, N. L., Braude, J. P., Mitchell, T. W., Coster, A. C. F., Don, A. S., et al. (2016) · Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids · doi:10.1016/j.bbalip.2016.08.016 · Cited by 88 · see citing works

Sphingolipid homeostasis in the web of metabolic routes

Aguilera-Romero, A., Gehin, C., & Riezman, H. (2013) · Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids · doi:10.1016/j.bbalip.2013.10.014 · Cited by 87 · see citing works

A comprehensive review of the family of very-long-chain fatty acid elongases: structure, function, and implications in physiology and pathology

Wang, X., Yu, H., Gao, R., Liu, M., & Xie, W. (2023) · European journal of medical research · doi:10.1186/s40001-023-01523-7 · Cited by 87 · see citing works

The equilibrium between long and very long chain ceramides is important for the fate of the cell and can be influenced by co-expression of CerS

Hartmann, D., Wegner, M.-S., Wanger, R. A., Ferreirós, N., Schreiber, Y., Lucks, J., Schiffmann, S., Geißlinger, G., & Grösch, S. (2013) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2013.03.012 · Cited by 85 · see citing works

Enzyme Activities of the Ceramide Synthases CERS2–6 Are Regulated by Phosphorylation in the C-terminal Region

Sassa, T., Hirayama, T., & Kihara, A. (2016) · Journal of Biological Chemistry · doi:10.1074/jbc.m115.695858 · Cited by 84 · see citing works

Very Long Chain Fatty Acids Are Functionally Involved in Necroptosis

Parisi, L. R., Li, N., & Atilla‐Gokcumen, G. E. (2017) · Cell chemical biology · doi:10.1016/j.chembiol.2017.08.026 · Cited by 82 · see citing works

Impairment of systemic DHA synthesis affects macrophage plasticity and polarization: implications for DHA supplementation during inflammation

Talamonti, E., Pauter, A. M., Asadi, A., Fischer, A. W., Chiurchiù, V., & Jacobsson, A. (2017) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-017-2498-9 · Cited by 81 · see citing works

CardioNet: A human metabolic network suited for the study of cardiomyocyte metabolism

Karlstaedt, A., Fliegner, D., Kararigas, G., Ruderisch, H. S., Regitz‐Zagrosek, V., & Holzhütter, H. (2012) · BMC Systems Biology · doi:10.1186/1752-0509-6-114 · Cited by 80 · see citing works

Multi-omics analysis reveals the glycolipid metabolism response mechanism in the liver of genetically improved farmed Tilapia (GIFT, Oreochromis niloticus) under hypoxia stress

Ma, J., Qiang, J., Tao, Y., Bao, J., Zhu, H., Li, L.-G., & Xu, P. (2021) · BMC Genomics · doi:10.1186/s12864-021-07410-x · Cited by 79 · see citing works

Invited review: Sphingolipid biology in the dairy cow: The emerging role of ceramide

McFadden, J. W., & Rico, J. E. (2019) · Journal of Dairy Science · doi:10.3168/jds.2018-16095 · Cited by 80 · see citing works

Staphylococcus aureus causes aberrant epidermal lipid composition and skin barrier dysfunction

Kim, J., Kim, B. E., Berdyshev, E. V., Bronova, I. A., Bin, L., Bae, J., Kim, S., Kim, H., Lee, U. H., Kim, M. S., et al. (2023) · Allergy · doi:10.1111/all.15640 · Cited by 79 · see citing works

Epidermal BarriersPreprint

Natsuga, K. (2014) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a018218 · Cited by 81 · see citing works

Brown Adipose Tissue Thermogenic Capacity Is Regulated by Elovl6

Tan, C. Y., Virtue, S., Bidault, G., Dale, M., Hagen, R., Griffin, J. L., & Vidal‐Puig, A. (2015) · Cell Reports · doi:10.1016/j.celrep.2015.11.004 · Cited by 76 · see citing works

De novo mutation in ELOVL1 causes ichthyosis, acanthosis nigricans, hypomyelination, spastic paraplegia, high frequency deafness and optic atrophy

Mueller, N., Sassa, T., Morales-Gonzalez, S., Schneider, J., Salchow, D. J., Seelow, D., Knierim, E., Stenzel, W., Kihara, A., & Schuelke, M. (2018) · Journal of Medical Genetics · doi:10.1136/jmedgenet-2018-105711 · Cited by 75 · see citing works

Inhibition of central de novo ceramide synthesis restores insulin signaling in hypothalamus and enhances β-cell function of obese Zucker rats

Campaña, M. B., Bellini, L., Rouch, C., Rachdi, L., Coant, N., Butin, N., Bandet, C. L., Philippe, E., Meneyrol, K., Kassis, N., et al. (2017) · Molecular Metabolism · doi:10.1016/j.molmet.2017.10.013 · Cited by 74 · see citing works

Circulating Very Long‐Chain Saturated Fatty Acids and Heart Failure: The Cardiovascular Health Study

Lemaître, R. N., McKnight, B., Sotoodehnia, N., Fretts, A. M., Qureshi, W., Song, X., King, I. B., Sitlani, C. M., Siscovick, D. S., Psaty, B. M., et al. (2018) · Journal of the American Heart Association · doi:10.1161/jaha.118.010019 · Cited by 74 · see citing works

Very-long-chain fatty acids induce glial-derived sphingosine-1-phosphate synthesis, secretion, and neuroinflammation

Chung, H.-L., Ye, Q., Park, Y.-J., Zuo, Z., Mok, J.-W., Kanca, O., Tattikota, S. G., Lu, S., Perrimon, N., Lee, H. K., et al. (2023) · Cell Metabolism · doi:10.1016/j.cmet.2023.03.022 · Cited by 70 · see citing works

Establishment of HeLa Cell Mutants Deficient in Sphingolipid-Related Genes Using TALENs

Yamaji, T., & Hanada, K. (2014) · PLoS ONE · doi:10.1371/journal.pone.0088124 · Cited by 70 · see citing works

Lorenzo's oil inhibits ELOVL1 and lowers the level of sphingomyelin with a saturated very long-chain fatty acid

Sassa, T., Wakashima, T., Ohno, Y., & Kihara, A. (2014) · Journal of Lipid Research · doi:10.1194/jlr.m044586 · Cited by 70 · see citing works

The 3-hydroxyacyl-CoA dehydratases HACD1 and HACD2 exhibit functional redundancy and are active in a wide range of fatty acid elongation pathways

Sawai, M., Uchida, Y., Ohno, Y., Miyamoto, M., Nishioka, C., Itohara, S., Sassa, T., & Kihara, A. (2017) · Journal of Biological Chemistry · doi:10.1074/jbc.m117.803171 · Cited by 69 · see citing works

Very long chain fatty acid-containing lipids: A decade of novel insights from the study of ELOVL4.

Yeboah, G. K., Lobanova, E. S., Brush, R. S., & Agbaga, M.-P. (2021) · Journal of Lipid Research · doi:10.1016/j.jlr.2021.100030 · Cited by 69 · see citing works

EGFR regulation of epidermal barrier function

Tran, Q. T., Kennedy, L. H., Carrion, S. L., Bodreddigari, S., Goodwin, S. B., Sutter, T. R., & Sutter, T. R. (2012) · Physiological Genomics · doi:10.1152/physiolgenomics.00176.2011 · Cited by 66 · see citing works

Very long‐chain tear film lipids produced by fatty acid elongase ELOVL1 prevent dry eye disease in mice

Sassa, T., Tadaki, M., Kiyonari, H., & Kihara, A. (2018) · The FASEB Journal · doi:10.1096/fj.201700947r · Cited by 65 · see citing works

Skin permeability barrier formation by the ichthyosis-causative gene FATP4 through formation of the barrier lipid ω- O -acylceramide

Yamamoto, H., Hattori, M., Chamulitrat, W., Ohno, Y., & Kihara, A. (2020) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1917525117 · Cited by 63 · see citing works

Endurance and Resistance Training Affect High Fat Diet-Induced Increase of Ceramides, Inflammasome Expression, and Systemic Inflammation in Mice

Mardare, C., Krüger, K., Liebisch, G., Seimetz, M., Couturier, A., Ringseis, R., Wilhelm, J., Weißmann, N., Eder, K., & Mooren, F. (2015) · Journal of Diabetes Research · doi:10.1155/2016/4536470 · Cited by 63 · see citing works

Elovl5 regulates the mTORC2-Akt-FOXO1 pathway by controlling hepatic cis-vaccenic acid synthesis in diet-induced obese mice

Tripathy, S., & Jump, D. Β. (2012) · Journal of Lipid Research · doi:10.1194/jlr.m028787 · Cited by 61 · see citing works

New insights into the organ-specific adverse effects of fumonisin B1: comparison between lung and liver

Loiseau, N., Polizzi, A., Dupuy, A., Therville, N., Rakotonirainy, M., Loy, J., Viadère, J.-L., Cossalter, A., Bailly, J., Puel, O., et al. (2014) · Archives of Toxicology · doi:10.1007/s00204-014-1323-6 · Cited by 60 · see citing works

Fatty acid elongase-5 (Elovl5) regulates hepatic triglyceride catabolism in obese C57BL/6J mice

Tripathy, S., Lytle, K. A., Stevens, R. D., Bain, J. R., Newgard, C. B., Greenberg, A. S., Huang, L., & Jump, D. Β. (2014) · Journal of Lipid Research · doi:10.1194/jlr.m050062 · Cited by 60 · see citing works

Direct interaction, instrumental for signaling processes, between LacCer and Lyn in the lipid rafts of neutrophil-like cells

Chiricozzi, E., Ciampa, M. G., Brasile, G., Compostella, F., Prinetti, A., Nakayama, H., Ekyalongo, R. C., Iwabuchi, K., Sonnino, S., & Mauri, L. (2014) · Journal of Lipid Research · doi:10.1194/jlr.m055319 · Cited by 60 · see citing works

Characterization of the fatty acyl elongase (elovl) gene family, and hepatic elovl and delta-6 fatty acyl desaturase transcript expression and fatty acid responses to diets containing camelina oil in Atlantic cod (Gadus morhua)

Xue, X., Feng, C. Y., Hixson, S. M., Kim, J., Anderson, D. M., Parrish, C. C., & Rise, M. L. (2014) · Comparative Biochemistry and Physiology Part B Biochemistry and Molecular Biology · doi:10.1016/j.cbpb.2014.06.005 · Cited by 59 · see citing works

Very-long-chain polyunsaturated fatty acids accumulate in phosphatidylcholine of fibroblasts from patients with Zellweger syndrome and acyl-CoA oxidase1 deficiency

Abe, Y., Honsho, M., Nakanishi, H., Taguchi, R., & Fujiki, Y. (2014) · Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids · doi:10.1016/j.bbalip.2014.01.001 · Cited by 59 · see citing works

Long-chain acyl-CoA synthetase 4 participates in the formation of highly unsaturated fatty acid-containing phospholipids in murine macrophages

Kuwata, H., Nakatani, E., Shimbara, S., Ishikawa, F., Shibanuma, M., Sasaki, Y., Yoda, E., Nakatani, Y., & Hara, S. (2019) · Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids · doi:10.1016/j.bbalip.2019.07.013 · Cited by 58 · see citing works

HACD1, a regulator of membrane composition and fluidity, promotes myoblast fusion and skeletal muscle growth

Blondelle, J., Ohno, Y., Gache, V., Guyot, S., Storck, S., Blanchard‐Gutton, N., Barthélémy, I., Walmsley, G., Rahier, A., Gadin, S., et al. (2015) · Journal of Molecular Cell Biology · doi:10.1093/jmcb/mjv049 · Cited by 58 · see citing works

ELOVL4 protein preferentially elongates 20:5n3 to very long chain PUFAs over 20:4n6 and 22:6n3

Yu, M., Benham, A., Logan, S., Brush, R. S., Mandal, M. N. A., Anderson, R. E., & Agbaga, M. (2011) · Journal of Lipid Research · doi:10.1194/jlr.m021386 · Cited by 57 · see citing works

Dominant ELOVL1 mutation causes neurological disorder with ichthyotic keratoderma, spasticity, hypomyelination and dysmorphic features

Kutkowska‐Kaźmierczak, A., Rydzanicz, M., Chlebowski, A., Kłosowska-Kosicka, K., Mika, A., Gruchota, J., Jurkiewicz, E., Kowaléwski, C., Pollak, A., Stradomska, T. J., et al. (2018) · Journal of Medical Genetics · doi:10.1136/jmedgenet-2017-105172 · Cited by 57 · see citing works

Interaction between hormone-sensitive lipase and ChREBP in fat cells controls insulin sensitivity

Morigny, P., Houssier, M., Mairal, A., Ghilain, C., Mouisel, É., Benhamed, F., Masri, B., Recazens, E., Denechaud, P., Tavernier, G., et al. (2018) · Nature Metabolism · doi:10.1038/s42255-018-0007-6 · Cited by 57 · see citing works

A Role for ELOVL4 in the Mouse Meibomian Gland and Sebocyte Cell Biology

McMahon, A., Lu, H., & Butovich, I. A. (2014) · Investigative Ophthalmology & Visual Science · doi:10.1167/iovs.13-13335 · Cited by 55 · see citing works

The diversity of ACBD proteins – From lipid binding to protein modulators and organelle tethers

Islinger, M., Costello, J. L., Kors, S., Soupène, E., Levine, T. P., Kuypers, F. A., & Schrader, M. (2020) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2020.118675 · Cited by 55 · see citing works

Very long-chain-fatty acids enhance adipogenesis through coregulation of Elovl3 and PPARγ in 3T3-L1 cells

Kobayashi, T., & Fujimori, K. (2012) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00623.2011 · Cited by 55 · see citing works

Transcriptomics in the wild: Hibernation physiology in free‐ranging dwarf lemurs

Faherty, S. L., Villanueva‐Cañas, J. L., Blanco, M. B., Albà, M. M., & Yoder, A. D. (2018) · Molecular Ecology · doi:10.1111/mec.14483 · Cited by 54 · see citing works

Lipid polarity gradient formed by ω-hydroxy lipids in tear film prevents dry eye disease

Miyamoto, M., Sassa, T., Sawai, M., & Kihara, A. (2020) · eLife · doi:10.7554/elife.53582 · Cited by 54 · see citing works

Molecular phenotyping of multiple mouse strains under metabolic challenge uncovers a role for Elovl2 in glucose-induced insulin secretion

Cruciani‐Guglielmacci, C., Bellini, L., Denom, J., Oshima, M., Fernandez, N., Normandie-Levi, P., Berney, X. P., Kassis, N., Rouch, C., Dairou, J., et al. (2017) · Molecular Metabolism · doi:10.1016/j.molmet.2017.01.009 · Cited by 53 · see citing works

IFN-γ Reduces Epidermal Barrier Function by Affecting Fatty Acid Composition of Ceramide in a Mouse Atopic Dermatitis Model

Kanoh, H., Ishitsuka, A., Fujine, E., Matsuhaba, S., Nakamura, M., Ito, H., Inagaki, N., Banno, Y., & Seishima, M. (2019) · Journal of Immunology Research · doi:10.1155/2019/3030268 · Cited by 53 · see citing works

The very-long-chain fatty acid elongase Elo2 rescues lethal defects associated with loss of the nuclear barrier function in fission yeast cells

Kinugasa, Y., Hirano, Y., Sawai, M., Ohno, Y., Shindo, T., Asakawa, H., Chikashige, Y., Shibata, S., Kihara, A., Haraguchi, T., et al. (2019) · Journal of Cell Science · doi:10.1242/jcs.229021 · Cited by 53 · see citing works

Membrane Disruption by Very Long Chain Fatty Acids during Necroptosis

Parisi, L. R., Sowlati‐Hashjin, S., Berhane, I. A., Galster, S. L., Carter, K. A., Lovell, J. F., Chemler, S. R., Karttunen, M., & Atilla‐Gokcumen, G. E. (2019) · ACS Chemical Biology · doi:10.1021/acschembio.9b00616 · Cited by 52 · see citing works

C24:0 avoids cold exposure-induced oxidative stress and fatty acid β-oxidation damage

Sun, S., Cao, X., & Gao, J. (2021) · iScience · doi:10.1016/j.isci.2021.103409 · Cited by 50 · see citing works

Global gene expression patterns of grass carp following compensatory growth

He, L., Pei, Y., Jiang, Y., Li, Y., Liao, L., Zhu, Z., & Wang, Y. (2015) · BMC Genomics · doi:10.1186/s12864-015-1427-2 · Cited by 49 · see citing works

Cooperative Synthesis of Ultra Long-Chain Fatty Acid and Ceramide during Keratinocyte Differentiation

Mizutani, Y., Sun, H., Ohno, Y., Sassa, T., Wakashima, T., Obara, M., Yuyama, K., Kihara, A., & Igarashi, Y. (2013) · PLoS ONE · doi:10.1371/journal.pone.0067317 · Cited by 49 · see citing works

ABCD 1 deletion‐induced mitochondrial dysfunction is corrected by SAHA : implication for adrenoleukodystrophy

Baarine, M., Beeson, C., Singh, A. K., & Singh, I. (2014) · Journal of Neurochemistry · doi:10.1111/jnc.12992 · Cited by 47 · see citing works

C26:0-Carnitine Is a New Biomarker for X-Linked Adrenoleukodystrophy in Mice and Man

van de Beek, M.-C., Dijkstra, I. M. E., van Lenthe, H., Ofman, R., Goldhaber-Pasillas, D., Schauer, N., Schackmann, M., Engelen-Lee, J.-Y., Vaz, F. M., Kulik, W., et al. (2016) · PLOS ONE · doi:10.1371/journal.pone.0154597 · Cited by 48 · see citing works

The Significance of Epidermal Lipid Metabolism in Whole-Body Physiology

Kruse, V., Neess, D., & Færgeman, N. J. (2017) · Trends in Endocrinology and Metabolism · doi:10.1016/j.tem.2017.06.001 · Cited by 50 · see citing works

Production of branched-chain very-long-chain fatty acids by fatty acid elongases and their tissue distribution in mammals

Tanno, H., Sassa, T., Sawai, M., & Kihara, A. (2020) · Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids · doi:10.1016/j.bbalip.2020.158842 · Cited by 47 · see citing works

Emerging roles and therapeutic potentials of sphingolipids in pathophysiology: emphasis on fatty acyl heterogeneity

Mu, J., Lam, S. M., & Shui, G. (2023) · Journal of genetics and genomics/Journal of Genetics and Genomics · doi:10.1016/j.jgg.2023.06.006 · Cited by 47 · see citing works

Transcriptome analysis of pigeon milk production – role of cornification and triglyceride synthesis genes

Gillespie, M. J., Crowley, T. M., Haring, V. R., Wilson, S. L., Harper, J. A., Payne, J., Green, D., Monaghan, P., Donald, J. A., Nicholas, K. R., et al. (2013) · BMC Genomics · doi:10.1186/1471-2164-14-169 · Cited by 47 · see citing works

A review on neuropharmacological role of erucic acid: an omega-9 fatty acid from edible oils

Kumar, J. B. S., & Sharma, B. (2020) · Nutritional Neuroscience · doi:10.1080/1028415x.2020.1831262 · Cited by 49 · see citing works

Fatty acid elongases in mammals: their regulation and roles in metabolism

JAKOBSSON, A., WESTERBERG, R., & JACOBSSON, A. (2006) · Progress in Lipid Research · doi:10.1016/j.plipres.2006.01.004 · Cited by 936 · see citing works

Very long-chain fatty acids: elongation, physiology and related disorders

Kihara, A. (2012) · The Journal of Biochemistry · doi:10.1093/jb/mvs105 · Cited by 441 · see citing works

Rom2-dependent Phosphorylation of Elo2 Controls the Abundance of Very Long-chain Fatty Acids

Olson, D. K., Fröhlich, F., Christiano, R., Hannibal‐Bach, H. K., Ejsing, C. S., & Walther, T. C. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.629279 · Cited by 32 · see citing works

Biochemical characterization of the very long-chain fatty acid elongase ELOVL7

Naganuma, T., Sato, Y. Z., Sassa, T., Ohno, Y., & Kihara, A. (2011) · FEBS Letters · doi:10.1016/j.febslet.2011.09.024 · Cited by 107 · see citing works

The structural basis of fatty acid elongation by the ELOVL elongases

Nie, L., Pascoa, T. C., Pike, A. C. W., Bushell, S. R., Quigley, A., Ruda, G. F., Chu, A., Cole, V., Speedman, D., Moreira, T., et al. (2021) · Nature Structural & Molecular Biology · doi:10.1038/s41594-021-00605-6 · Cited by 94 · see citing works