Identification and Characterization of a Sphingolipid Δ4-Desaturase Family

Gapped BLAST and PSI-BLAST: a new generation of protein database search programs

Altschul, S. (1997) · Nucleic Acids Research · doi:10.1093/nar/25.17.3389 · Cited by 73,302

The CLUSTAL_X windows interface: flexible strategies for multiple sequence alignment aided by quality analysis tools

Thompson, J. (1997) · Nucleic Acids Research · doi:10.1093/nar/25.24.4876 · Cited by 38,685

Current protocols in molecular biology

Sargent, T. (1988) · Analytical Biochemistry · doi:10.1016/0003-2697(88)90147-9 · Cited by 7,281

T-coffee: a novel method for fast and accurate multiple sequence alignment 1 1Edited by J. Thornton

Notredame, C., Higgins, D. G., & Heringa, J. (2000) · Journal of Molecular Biology · doi:10.1006/jmbi.2000.4042 · Cited by 6,964

The Transcriptional Program of Sporulation in Budding Yeast

Chu, S., DeRisi, J. L., Eisen, M. B., Mulholland, J., Botstein, D., Brown, P. O., & Herskowitz, I. (1998) · Science · doi:10.1126/science.282.5389.699 · Cited by 1,860

The I.M.A.G.E. Consortium: An Integrated Molecular Analysis of Genomes and Their Expression

Lennon, G., Auffray, C., Polymeropoulos, M. H., & Soares, M. B. (1996) · Genomics · doi:10.1006/geno.1996.0177 · Cited by 1,123

Nuclear localization of EGF receptor and its potential new role as a transcription factor

Lin, S., Makino, K., Xia, W., Matin, A., Wen, Y., Kwong, K. Y., Bourguignon, L., & Hung, M. (2001) · Nature Cell Biology · doi:10.1038/ncb0901-802 · Cited by 1,064

DESATURATION AND RELATED MODIFICATIONS OF FATTY ACIDS

Shanklin, J., & Cahoon, E. B. (1998) · Annual Review of Plant Physiology and Plant Molecular Biology · doi:10.1146/annurev.arplant.49.1.611 · Cited by 924

Eight Histidine Residues Are Catalytically Essential in a Membrane-Associated Iron Enzyme, Stearoyl-CoA Desaturase, and Are Conserved in Alkane Hydroxylase and Xylene Monooxygenase

Shanklin, J., Whittle, E. J., & Fox, B. G. (1994) · Biochemistry · doi:10.1021/bi00209a009 · Cited by 764

Sphingosine 1-phosphate signalling in mammalian cells

Pyne, S., & Pyne, N. J. (2000) · Biochemical Journal · doi:10.1042/0264-6021:3490385 · Cited by 737

Alkaline Ceramidase 3 Deficiency Results in Purkinje Cell Degeneration and Cerebellar Ataxia Due to Dyshomeostasis of Sphingolipids in the Brain

Wang, K., Xu, R., Schrandt, J., Shah, P. K., Gong, Y. Z., Preston, C., Wang, L., Yi, J. K., Lin, C., Sun, W., et al. (2015) · PLoS Genetics · doi:10.1371/journal.pgen.1005591 · Cited by 56

The Role of Sphingolipid Metabolism in Bone Remodeling

Tang, Q., Liao, L., & Tian, W. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.752540 · Cited by 59

Ceramides are fuel gauges on the drive to cardiometabolic disease

Wilkerson, J. L., Tatum, S. M., Holland, W. L., & Summers, S. A. (2024) · Physiological Reviews · doi:10.1152/physrev.00008.2023 · Cited by 65

FTY720 Induces Apoptosis of M2 Subtype Acute Myeloid Leukemia Cells by Targeting Sphingolipid Metabolism and Increasing Endogenous Ceramide Levels

Chen, L., Luo, L., Lu, J., Li, L., Liu, Y., Wang, J., Liu, H. S., Song, H., Jiang, H., Chen, S., et al. (2014) · PLoS ONE · doi:10.1371/journal.pone.0103033 · Cited by 54

The role of PNPLA1 in ω-O-acylceramide synthesis and skin barrier function

Hirabayashi, T., Murakami, M., & Kihara, A. (2018) · Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids · doi:10.1016/j.bbalip.2018.09.010 · Cited by 54

Sphingosine-1-Phosphate Phosphohydrolase Regulates Endoplasmic Reticulum-to-Golgi Trafficking of Ceramide

Giussani, P., Maceyka, M. W., Stunff, H. L., Mikami, A., Lépine, S., Wang, E. L., Kelly, S. L., Merrill, A. H., Milstien, S., & Spiegel, S. (2006) · Molecular and Cellular Biology · doi:10.1128/mcb.02107-05 · Cited by 53

Specificity of the Dihydroceramide Desaturase Inhibitor N-[(1R,2S)-2-Hydroxy-1-hydroxymethyl-2-(2-tridecyl-1-cyclopropenyl)ethyl]octanamide (GT11) in Primary Cultured Cerebellar Neurons

Triola, G., Fabriàs, G., Dragusin, M., Niederhausen, L., Broere, R., Llebaria, A., & van Echten‐Deckert, G. (2004) · Molecular Pharmacology · doi:10.1124/mol.104.003681 · Cited by 52

Biosynthesis of the anti‐lipid‐microdomain sphingoid base 4,14‐sphingadiene by the ceramide desaturase FADS3

Jojima, K., Edagawa, M., Sawai, M., Ohno, Y., & Kihara, A. (2020) · The FASEB Journal · doi:10.1096/fj.201902645r · Cited by 52

Myristic acid increases the activity of dihydroceramide Δ4-desaturase 1 through its N-terminal myristoylation

Beauchamp, E., Goenaga, D., Bloc’h, J. L., Catheline, D., Legrand, P., & Rioux, V. (2007) · Biochimie · doi:10.1016/j.biochi.2007.07.001 · Cited by 50

The yeast model system as a tool towards the understanding of apoptosis regulation by sphingolipids

Rego, A., Trindade, D., Chaves, S. R., Manon, S., Costa, V., Sousa, M. J., & Côrte‐Real, M. (2013) · FEMS Yeast Research · doi:10.1111/1567-1364.12096 · Cited by 50

Mammalian sphingoid bases: Biophysical, physiological and pathological properties

Carreira, A. C., Santos, T. C. B., Lone, M. A., Zupančič, E., Lloyd‐Evans, E., de Almeida, R. F. M., Hornemann, T., & Silva, L. C. (2019) · Progress in Lipid Research · doi:10.1016/j.plipres.2019.100988 · Cited by 49

Sphingolipids in neurodegenerative diseases

Pan, X., Dutta, D., Lu, S., & Bellen, H. J. (2023) · Frontiers in Neuroscience · doi:10.3389/fnins.2023.1137893 · Cited by 50

Targeted ablation of Arnt in mouse epidermis results in profound defects in desquamation and epidermal barrier function

Geng, S., Mezentsev, A., Kalachikov, S. M., Raith, K., Roop, D. R., & Panteleyev, A. A. (2006) · Journal of Cell Science · doi:10.1242/jcs.03282 · Cited by 49

Ceramide sensing by human SPT-ORMDL complex for establishing sphingolipid homeostasis

Xie, T., Liu, P., Wu, X., Dong, F., Zhang, Z., Yue, J., Mahawar, U., Farooq, F., Vohra, H., Fang, Q., et al. (2023) · Nature Communications · doi:10.1038/s41467-023-39274-y · Cited by 45

Unraveling the role of the Target of Rapamycin signaling in sphingolipid metabolism

Teixeira, V., & Costa, V. (2015) · Progress in Lipid Research · doi:10.1016/j.plipres.2015.11.001 · Cited by 46

Functional characterization of the A spergillus nidulans glucosylceramide pathway reveals that LCB Δ8‐desaturation and C9‐methylation are relevant to filamentous growth, lipid raft localization and Psd1 defensin activity

Fernandes, C. M., de Castro, P. A., Singh, A., Fonseca, F. L., Pereira, M. D., Vila, T. V. M., Atella, G. C., Rozental, S., Savoldi, M., Poeta, M. D., et al. (2016) · Molecular Microbiology · doi:10.1111/mmi.13474 · Cited by 42

The role of fatty acid elongation in epidermal structure and function

Uchida, Y. (2011) · Dermato-Endocrinology · doi:10.4161/derm.3.2.14662 · Cited by 43

CERT1 mutations perturb human development by disrupting sphingolipid homeostasis

Gehin, C. J. C., Lone, M. A., Lee, W., Capolupo, L., Ho, S., Adeyemi, A. M., Gerkes, E. H., Stegmann, A. P. A., Martín, E. L., Bermejo, E., et al. (2023) · Journal of Clinical Investigation · doi:10.1172/jci165019 · Cited by 38

Inhibitors of dihydroceramide desaturase 1: Therapeutic agents and pharmacological tools to decipher the role of dihydroceramides in cell biology

Casasampere, M., Ordóñez, Y. F., Pou, A., & Casas, J. (2015) · Chemistry and Physics of Lipids · doi:10.1016/j.chemphyslip.2015.07.025 · Cited by 42

N-Myristoylation targets dihydroceramide Δ4-desaturase 1 to mitochondria: Partial involvement in the apoptotic effect of myristic acid

Beauchamp, E., Tekpli, X., Marteil, G., Lagadic‐Gossmann, D., Legrand, P., & Rioux, V. (2009) · Biochimie · doi:10.1016/j.biochi.2009.07.014 · Cited by 42

Sphingolipid desaturase DEGS1 is essential for mitochondria-associated membrane integrity

Planas‐Serra, L., Launay, N., Goicoechea, L., Héron, B., Jou, C., Juliá‐Palacios, N., Ruíz, M., Fourcade, S., Casasnovas, C., de la Torre, C., et al. (2023) · Journal of Clinical Investigation · doi:10.1172/jci162957 · Cited by 41

Glycosphingolipids in Filamentous Fungi: Biological Roles and Potential Applications in Cosmetics and Health Foods

Jiang, C., Ge, J., He, B., & Zeng, B. (2021) · Frontiers in Microbiology · doi:10.3389/fmicb.2021.690211 · Cited by 40

Fatty Acid Desaturase 3 (Fads3) is a singular member of the Fads cluster

Blanchard, H. C., Legrand, P., & Pédrono, F. (2010) · Biochimie · doi:10.1016/j.biochi.2010.03.002 · Cited by 41

Biosynthesis of Sphingolipids in Plants (and Some of Their Functions)

Zäuner, S., Ternes, P., & Warnecke, D. C. (2010) · Advances in experimental medicine and biology · doi:10.1007/978-1-4419-6741-1_18 · Cited by 39

Sphingolipids in plant immunity

Zeng, H., & Yao, N. (2022) · Phytopathology Research · doi:10.1186/s42483-022-00125-1 · Cited by 38

Biosynthesis and Immunogenicity of Glucosylceramide inCryptococcus neoformansand Other Human Pathogens

Rhome, R. M., McQuiston, T. J., Kechichian, T. B., Bielawska, A. E., Hennig, M., Drago, M., Morace, G., Luberto, C., & Poeta, M. D. (2007) · Eukaryotic Cell · doi:10.1128/ec.00208-07 · Cited by 38

Fads1 and 2 are promoted to meet instant need for long-chain polyunsaturated fatty acids in goose fatty liver

Osman, R. H., Liu, L., Xia, L., Zhao, X., Wang, Q., Sun, X., Zhang, Y., Yang, B., Zheng, Y., Gong, D., et al. (2016) · Molecular and Cellular Biochemistry · doi:10.1007/s11010-016-2737-7 · Cited by 36

Producing human ceramide-NS by metabolic engineering using yeast Saccharomyces cerevisiae

Murakami, S., Shimamoto, T., Nagano, H., Tsuruno, M., Okuhara, H., Hatanaka, H., Tojo, H., Kodama, Y., & Funato, K. (2015) · Scientific Reports · doi:10.1038/srep16319 · Cited by 35

Fatty Acid Desaturases: Uncovering Their Involvement in Grapevine Defence against Downy Mildew

Laureano, G., Cavaco, A. R., Matos, A. R., & Figueiredo, A. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22115473 · Cited by 35

Queen Conch (Strombus gigas) Testis Regresses during the Reproductive Season at Nearshore Sites in the Florida Keys

Spade, D. J., Griffitt, R. J., Liu, L., Brown‐Peterson, N. J., Kroll, K. J., Feswick, A., Glazer, R. A., Barber, D. S., & Denslow, N. D. (2010) · PLoS ONE · doi:10.1371/journal.pone.0012737 · Cited by 34

Transcript profiling and lipidomic analysis of ceramide subspecies in mouse embryonic stem cells and embryoid bodies

Park, H. J., Haynes, C. A., Nairn, A. V., Kulik, M. J., Dalton, S., Moremen, K. W., & Merrill, A. H. (2009) · Journal of Lipid Research · doi:10.1194/jlr.m000984 · Cited by 34

Plant Sphingolipids Today ‐ Are They Still Enigmatic?

Spassieva, S. D., & Hille, J. (2003) · Plant Biology · doi:10.1055/s-2003-40726 · Cited by 34

Rescue of cell growth by sphingosine with disruption of lipid microdomain formation in Saccharomyces cerevisiae deficient in sphingolipid biosynthesis

Tani, M., Kihara, A., & Igarashi, Y. (2006) · Biochemical Journal · doi:10.1042/bj20051354 · Cited by 33

A possible role of sphingolipids in the aluminium resistance of yeast and maize

da Silva, A. L. S., Sperling, P., Horst, W. J., Franke, S., Ott, C., Becker, D., Staß, A., Lörz, H., & Heinz, E. (2005) · Journal of Plant Physiology · doi:10.1016/j.jplph.2005.03.009 · Cited by 33

Unravelling neuronal and glial differences in ceramide composition, synthesis, and sensitivity to toxicity

McInnis, J. J., Sood, D., Guo, L., Dufault, M. R., García, M. G., Passaro, R., Gao, G., Zhang, B., & Dodge, J. C. (2024) · Communications Biology · doi:10.1038/s42003-024-07231-0 · Cited by 33

Lipid metabolism in Rhodnius prolixus : Lessons from the genome

Majerowicz, D., Calderón‐Fernández, G. M., Alves‐Bezerra, M., Paula, I. F. D., Cardoso, L. S., Juárez, M. P., Atella, G. C., & Gondim, K. C. (2016) · Gene · doi:10.1016/j.gene.2016.09.045 · Cited by 32

Ceramide Transfer Protein (CERT): An Overlooked Molecular Player in Cancer

Chung, L. H., Liu, D., Liu, X. T., & Qi, Y. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms222413184 · Cited by 32

Decreased Skin Barrier Lipid Acylceramide and Differentiation-Dependent Gene Expression in Ichthyosis Gene Nipal4-Knockout Mice

Honda, Y., Kitamura, T., Naganuma, T., Takaya, A., Ohno, Y., Sassa, T., & Kihara, A. (2017) · Journal of Investigative Dermatology · doi:10.1016/j.jid.2017.11.008 · Cited by 31

Resolving Modifications on Sphingoid Base and N ‑Acyl Chain of Sphingomyelin Lipids in Complex Lipid Extracts

Zhao, X., Wu, G., Zhang, W., Dong, M., & Xia, Y. (2020) · Analytical Chemistry · doi:10.1021/acs.analchem.0c03502 · Cited by 31

The Role of the Trans Double Bond in Skin Barrier Sphingolipids: Permeability and Infrared Spectroscopic Study of Model Ceramide and Dihydroceramide Membranes

Školová, B., Jandovská, K., Pullmannová, P., Tesař, O., Roh, J., Hrabálek, A., & Vávrová, K. (2014) · Langmuir · doi:10.1021/la500622f · Cited by 30

Metabolic engineering of the non-conventional yeast Pichia ciferrii for production of rare sphingoid bases

Börgel, D., van den Berg, M. A., Hueller, T., Andrea, H., Liebisch, G., Boles, E., Schorsch, C., van der Pol, R., Arink, A. M., Boogers, I., et al. (2012) · Metabolic Engineering · doi:10.1016/j.ymben.2012.03.003 · Cited by 29

Stress-Induced Cell Death Is Mediated by Ceramide Synthesis in Neurospora crassa

Plesofsky, N. S., Levery, S. B., Castle, S. A., & Brambl, R. M. (2008) · Eukaryotic Cell · doi:10.1128/ec.00147-08 · Cited by 30

Analogs of the dihydroceramide desaturase inhibitor GT11 modified at the amide function: synthesis and biological activities

Bedia, C., Triola, G., Casas, J., Llebaria, A., & Fabriàs, G. (2005) · Organic & Biomolecular Chemistry · doi:10.1039/b510198k · Cited by 29

Dihydroceramide:sphinganine C-4-hydroxylation requires Des2 hydroxylase and the membrane form of cytochrome b5

Enomoto, A., Omae, F., Miyazaki, M., Kozutsumi, Y., Yubisui, T., & Suzuki, A. (2006) · Biochemical Journal · doi:10.1042/bj20051938 · Cited by 28

The Chemistry and Biology of 6‐Hydroxyceramide, the Youngest Member of the Human Sphingolipid Family

Kováčik, A., Roh, J., & Vávrová, K. (2014) · ChemBioChem · doi:10.1002/cbic.201402153 · Cited by 28

Sphingolipid management by an orchestra of lipid transfer proteins

Neumann, S., & Gerrit van, M. E. E. R. (2008) · Biological Chemistry · doi:10.1515/bc.2008.154 · Cited by 30

Lipid Polarization during Cytokinesis

Govind, K., Acharya, U. R., & Acharya, J. (2022) · Cells · doi:10.3390/cells11243977 · Cited by 27

The effect of long-term cigarette smoking on selected skin barrier proteins and lipids

Hergesell, K., Paraskevopoulou, A., Opálka, L., Velebný, V., Vávrová, K., & Dolečková, I. (2023) · Scientific Reports · doi:10.1038/s41598-023-38178-7 · Cited by 29

The Same or Not the Same: Lineage-Specific Gene Expansions and Homology Relationships in Multigene Families in Nematodes

Markov, G. V., Baskaran, P., & Sommer, R. J. (2014) · Journal of Molecular Evolution · doi:10.1007/s00239-014-9651-y · Cited by 23

Multiple actions of doxorubicin on the sphingolipid network revealed by flux analysis

Snider, J. M., Trayssac, M., Clarke, C. J., Schwartz, N. U., Snider, A. J., Obeid, L. M., Luberto, C., & Hannun, Y. A. (2018) · Journal of Lipid Research · doi:10.1194/jlr.m089714 · Cited by 26

A Novel Function of Sphingosine Kinase 2 in the Metabolism of Sphinga-4,14-Diene Lipids

Couttas, T. A., Rustam, Y. H., Song, H., Qi, Y., Teo, J. D., Chen, J., Reid, G. E., & Don, A. S. (2020) · Metabolites · doi:10.3390/metabo10060236 · Cited by 25

Identification of an essential sequence for dihydroceramide C‐4 hydroxylase activity of mouse DES2

Omae, F., Miyazaki, M., Enomoto, A., & Suzuki, A. (2004) · FEBS Letters · doi:10.1016/j.febslet.2004.08.060 · Cited by 26

Ceramide synthases: Reflections on the impact of Dr. Lina M. Obeid

Kim, J. L., Mestre, B., Shin, S.-H., & Futerman, A. H. (2021) · Cellular Signalling · doi:10.1016/j.cellsig.2021.109958 · Cited by 25

Structural basis of the mechanism and inhibition of a human ceramide synthase

Pascoa, T. C., Pike, A. C. W., Tautermann, C. S., Chi, G., Traub, M., Quigley, A., Chalk, R., Štefanić, S., Thamm, S., Pautsch, A., et al. (2025) · Nature Structural & Molecular Biology · doi:10.1038/s41594-024-01414-3 · Cited by 25

Stereochemistry of a bifunctional dihydroceramide Δ 4 -desaturase/hydroxylase from Candida albicans; a key enzyme of sphingolipid metabolism

Beckmann, C., Rattke, J., Sperling, P., Heinz, E., & Boland, W. (2003) · Organic & Biomolecular Chemistry · doi:10.1039/b303939k · Cited by 25

Conditional deletion of Des1 in the mouse retina does not impair the visual cycle in cones

Kiser, P. D., Kolesnikov, A. V., Kiser, J. Z., Dong, Z., Chaurasia, B., Wang, L., Summers, S. A., Hoang, T. V., Blackshaw, S., Peachey, N. S., et al. (2019) · The FASEB Journal · doi:10.1096/fj.201802493r · Cited by 24

Sphingosine in plants – more riddles from the Sphinx?

Islam, M. N., Jacquemot, M., Coursol, S., & Ng, C. K. ‐. (2011) · New Phytologist · doi:10.1111/j.1469-8137.2011.03963.x · Cited by 24

Sphingolipids from the human fungal pathogen Aspergillus fumigatus

Fontaine, T. (2017) · Biochimie · doi:10.1016/j.biochi.2017.06.012 · Cited by 23

Probing the role of ceramide hydroxylation in skin barrier lipid models by 2H solid-state NMR spectroscopy and X-ray powder diffraction

Kováčik, A., Vogel, A., Adler, J., Pullmannová, P., Vávrová, K., & Huster, D. (2018) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2018.02.003 · Cited by 23

The Desaturase Gene Family is Crucially Required for Fatty Acid Metabolism and Survival of the Brown Planthopper, Nilaparvata lugens

Zeng, J., Ye, W., Noman, A., Machado, R. A. R., & Lou, Y. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20061369 · Cited by 22

Dihydroceramide desaturase promotes the formation of intraluminal vesicles and inhibits autophagy to increase exosome production

Wu, C.-Y., Jhang, J.-G., Lin, W.-S., Chuang, P.-H., Lin, C.-W., Chu, L., Chiang, A., Ho, H., Chan, C., & Huang, S. (2021) · iScience · doi:10.1016/j.isci.2021.103437 · Cited by 22

Genome-Wide Identification of Membrane-Bound Fatty Acid Desaturase Genes in Three Peanut Species and Their Expression in Arachis hypogaea during Drought Stress

Gai, W., Sun, H., Hu, Y., Liu, C., Zhang, Y., Gai, S., & Yuan, Y. (2022) · Genes · doi:10.3390/genes13101718 · Cited by 22

Beyond membrane components: uncovering the intriguing world of fungal sphingolipid synthesis and regulation

Usmani, S. A., Kumar, M., Arya, K., Ali, B., Bhardwaj, N., Gaur, N. A., Prasad, R., & Singh, A. (2023) · Research in Microbiology · doi:10.1016/j.resmic.2023.104087 · Cited by 21

Developmental changes in glycolipids and synchronized expression of nutrient transporters in the mouse small intestine

Yoneshige, A., Sasaki, A., Miyazaki, M., Kojima, N., Suzuki, A., & Matsuda, J. (2009) · The Journal of Nutritional Biochemistry · doi:10.1016/j.jnutbio.2008.12.009 · Cited by 21

In Silico Analysis of Fatty Acid Desaturases Structures in Camelina sativa, and Functional Evaluation of Csafad7 and Csafad8 on Seed Oil Formation and Seed Morphology

Raboanatahiry, N. H., Yin, Y., Chen, K., He, J., Yu, L., & Li, M. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms221910857 · Cited by 21

Dietary fat modifies lipid metabolism in the adipose tissue of metabolic syndrome patients

Camargo, A., Meneses, M. E. P. D., Pérez‐Martínez, P., Delgado‐Lista, J., Rangel-Zúñiga, O. A., Marı́n, C., Almadén, Y., Yubero‐Serrano, E. M., González-Guardia, L., Fuentes, F. J., et al. (2014) · Genes & Nutrition · doi:10.1007/s12263-014-0409-3 · Cited by 21

Overexpression of Tisochrysis lutea Akd1 identifies a key cold-induced alkenone desaturase enzyme

Endo, H., Hanawa, Y., Araie, H., Suzuki, I., & Shiraiwa, Y. (2018) · Scientific Reports · doi:10.1038/s41598-018-29482-8 · Cited by 22

Bifunctional DEGS2 has higher hydroxylase activity toward substrates with very-long-chain fatty acids in the production of phytosphingosine ceramides

Ota, A., Morita, H., Naganuma, T., Miyamoto, M., Jojima, K., Nojiri, K., Matsuda, J., & Kihara, A. (2023) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2023.104603 · Cited by 23

Mysterious sphingolipids: metabolic interrelationships at the center of pathophysiology

Jamjoum, R., Majumder, S., Issleny, B. M., & Stiban, J. (2024) · Frontiers in Physiology · doi:10.3389/fphys.2023.1229108 · Cited by 26

Isolation and functional analysis of fatty acid desaturase genes from peanut (Arachis hypogaea L.)

Chi, X., Zhang, Z., Chen, N., Zhang, X., Wang, M., Chen, M., Wang, T., Pan, L., Chen, J., Yang, Z., et al. (2017) · PLoS ONE · doi:10.1371/journal.pone.0189759 · Cited by 20

The dihydroceramide desaturase is not essential for cell viability in Schizosaccharomyces pombe

Garton, S., Michaelson, L. V., Beaudoin, F., Beale, M. H., & Napier, J. A. (2003) · FEBS Letters · doi:10.1016/s0014-5793(03)00163-7 · Cited by 20

The Implication of Sphingolipids in Viral Infections

Thomas, S., Samuel, S. V., Hoch, A., Syphurs, C., & Diray‐Arce, J. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms242417303 · Cited by 20

A new class of lipid desaturase central to sphingolipid biosynthesis and signalling

Napier, J. A., Michaelson, L. V., & Dunn, T. M. (2002) · Trends in Plant Science · doi:10.1016/s1360-1385(02)02348-8 · Cited by 19

Lipid pickup and delivery

Riezman, H., & Gerrit van, M. E. E. R. (2004) · Nature Cell Biology · doi:10.1038/ncb0104-15 · Cited by 19

Fish environmental RNA sequencing sensitively captures accumulative stress responses through short-term aquarium sampling

Miyata, K., Inoue, Y., Yamane, M., & Honda, H. (2024) · The Science of The Total Environment · doi:10.1016/j.scitotenv.2024.178182 · Cited by 18

Analysis of ceramide metabolites in differentiating epidermal keratinocytes treated with calcium or vitamin C

Kim, J., Yun, H., & Cho, Y. (2011) · Nutrition Research and Practice · doi:10.4162/nrp.2011.5.5.396 · Cited by 17

Natural Products and Small Molecules Targeting Cellular Ceramide Metabolism to Enhance Apoptosis in Cancer Cells

Afrin, F., Mateen, S., Oman, J., Lai, J. C. K., Barrott, J. J., & Pashikanti, S. (2023) · Cancers · doi:10.3390/cancers15184645 · Cited by 15

Cell density-dependent reduction of dihydroceramide desaturase activity in neuroblastoma cells

Spassieva, S. D., Rahmaniyan, M., Bielawski, J., Clarke, C. J., Kraveka, J. M., & Obeid, L. M. (2012) · Journal of Lipid Research · doi:10.1194/jlr.m019075 · Cited by 17

Chemical and Apoptotic Properties of Hydroxy-Ceramides Containing Long-Chain Bases with Unusual Alkyl Chain Lengths

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Ezanno, H., Bloc’h, J. L., Beauchamp, E., Lagadic‐Gossmann, D., Legrand, P., & Rioux, V. (2011) · Lipids · doi:10.1007/s11745-011-3638-x · Cited by 15

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Dreesen, T. D., Adamson, A. W., Tekle, M., Tang, C., Cho, H. P., Clarke, S. D., & Gettys, T. W. (2006) · Prostaglandins Leukotrienes and Essential Fatty Acids · doi:10.1016/j.plefa.2006.05.001 · Cited by 13

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Wilding, M., Nachtschatt, M., Speight, R. E., & Scott, C. S. (2017) · Molecular Phylogenetics and Evolution · doi:10.1016/j.ympev.2017.07.012 · Cited by 12

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