Docosahexaenoic Acid Prevents Palmitate-Induced Activation of Proteolytic Systems in C2C12 Myotubes

Woodworth-Hobbs, Myra E.; Hudson, Matthew B.; Rahnert, Jill A.; Zheng, Bin; Franch, Harold A.; Price, S. Russ

doi:10.1016/j.jnutbio.2014.03.017

Cited by 71Muscle Physiology and DisordersMuscle metabolism and nutritionFatty Acid Research and Health

Docosahexaenoic Acid Prevents Palmitate-Induced Activation of Proteolytic Systems in C2C12 Myotubes

Open access

Woodworth-Hobbs, Myra E., Hudson, Matthew B., Rahnert, Jill A., Zheng, Bin, Franch, Harold A., Price, S. Russ·2014·The Journal of Nutritional Biochemistry

DOI 10.1016/j.jnutbio.2014.03.017PMC PMC4118671

Open this paper in CoChat — free account

Abstract

Saturated fatty acids like palmitate contribute to muscle atrophy in a number of conditions (e.g., type II diabetes) by altering insulin signaling. Akt is a key modulator of protein balance that inhibits the FoxO transcription factors (e.g., FoxO3) which selectively induce the expression of atrophy-inducing genes (atrogenes) in the ubiquitin-proteasome and autophagy-lysosome systems. Conversely, omega-3 polyunsaturated fatty acids have beneficial effects on insulin signaling and may preserve muscle mass. In an earlier report, the omega-3 fatty acid docosahexaenoic acid (DHA) protected myotubes from palmitate-induced atrophy; the mechanisms underlying the alterations in protein metabolism were not identified. This study investigated whether DHA prevents a palmitate-induced increase in proteolysis by restoring Akt/FoxO signaling. Palmitate increased the rate of protein degradation, while cotreatment with DHA prevented the response. Palmitate reduced the activation state of Akt and increased nuclear FoxO3 protein while decreasing its cytosolic level. Palmitate also increased the messenger RNAs (mRNAs) of two FoxO3 atrogene targets, the E3 ubiquitin ligase atrogin-1/MAFbx and the autophagy mediator Bnip3. DHA attenuated the effects of palmitate on Akt activation, FoxO3 localization and atrogene mRNAs. DHA, alone or in combination with palmitate and decreased the ratio of LC3B-II:LC3B-I protein as well as the rate of autophagosome formation, as indicated by reduced LC3B-II protein in the presence of 10 mmol/L methylamine, suggesting an independent effect of DHA on the macroautophagy pathway. These data indicate that palmitate induces myotube atrophy, at least in part, by activating multiple proteolytic systems and that DHA counters the catabolic effects of palmitate by restoring Akt/FoxO signaling.

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

Crossref · 10.1016/j.jnutbio.2014.03.017

Cites

42 of 42 references verified0 citation errors · 0 not checkable

Statistics

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?

DHA prevents muscle proteolytic induced by palmitate in C2C12 myotubes through reestablishment of Akt/FoxO signaling.
“Woodworth-Hobbs et al. found that docosahexaenoic acid prevents muscle proteolytic induced by palmitate in C2C12 myotubes through the reestablishment of the Akt/FoxO signaling pathway [73].”
From Nutraceuticals in the Prevention and Treatment of the Muscle Atrophy (2021) · cites this paper as [73]

Self-check

Percentages, sums and reported differences re-computed from the paper’s own numbers.

The self-check needs the paper’s full text.

Identification of ubiquitin ligases required for skeletal muscle atrophy.
Bodine, S. C., Latres, E., Baumhueter, S., Lai, V. K.-M., Nunez, L., Clarke, B. A., Poueymirou, W. T., Panaro, F. J., Na, E., Dharmarajan, K., et al. (2001) · Science · doi:10.1126/science.1065874 · Cited by 3,521 · see citing works
Foxo transcription factors induce the atrophy-related ubiquitin ligase atrogin-1 and cause skeletal muscle atrophy.
Sandri, M., Sandri, C., Gilbert, A., Skurk, C., Calabria, E., Picard, A., Walsh, K., Schiaffino, S., Lecker, S. H., & Goldberg, A. L. (2004) · Cell · doi:10.1016/s0092-8674(04)00400-3 · Cited by 3,012 · see citing works
The IGF-1/PI3K/Akt pathway prevents expression of muscle atrophy-induced ubiquitin ligases by inhibiting FOXO transcription factors.
Stitt, T. N., Drujan, D., Clarke, B. A., Panaro, F., Timofeyva, Y., Kline, W. O., Gonzalez, M., Yancopoulos, G. D., & Glass, D. J. (2004) · Molecular Cell · doi:10.1016/s1097-2765(04)00211-4 · Cited by 1,964 · see citing works
FoxO3 Controls Autophagy in Skeletal Muscle In Vivo
Mammucari, C., Milan, G., Romanello, V., Masiero, E., Rudolf, R., Del Piccolo, P., Burden, S. J., Di Lisi, R., Sandri, C., Zhao, J., et al. (2007) · Cell Metabolism · doi:10.1016/j.cmet.2007.11.001 · Cited by 1,953 · see citing works
Multiple types of skeletal muscle atrophy involve a common program of changes in gene expression
Lecker, S. H., Jagoe, R. T., Gilbert, A., Gomes, M., Baracos, V., Bailey, J., Price, S. R., Mitch, W. E., & Goldberg, A. L. (2004) · The FASEB Journal · doi:10.1096/fj.03-0610com · Cited by 1,539 · see citing works
Self-citation
IGF-I stimulates muscle growth by suppressing protein breakdown and expression of atrophy-related ubiquitin ligases, atrogin-1 and MuRF1
Sacheck, J. M., Ohtsuka, A., McLary, S. C., & Goldberg, A. L. (2004) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00073.2004 · Cited by 606 · see citing works
Overnight lowering of free fatty acids with Acipimox improves insulin resistance and glucose tolerance in obese diabetic and nondiabetic subjects.
Santomauro, A. T., Boden, G., Silva, M. E., Rocha, D. M., Santos, R. F., Ursich, M. J., Strassmann, P. G., & Wajchenberg, B. L. (1999) · Diabetes · doi:10.2337/diabetes.48.9.1836 · Cited by 431 · see citing works
Triacylglycerol accumulation in human obesity and type 2 diabetes is associated with increased rates of skeletal muscle fatty acid transport and increased sarcolemmal FAT/CD36
Bonen, A., Parolin, M. L., Steinberg, G. R., Calles‐Escandon, J., Tandon, N. N., Glatz, J. F. C., Luiken, J. J. F. P., Heigenhauser, G. J. F., & Dyck, D. J. (2004) · The FASEB Journal · doi:10.1096/fj.03-1065fje · Cited by 410 · see citing works
What do we really know about the ubiquitin-proteasome pathway in muscle atrophy?
Jagoe, R. T., & Goldberg, A. L. (2001) · Current Opinion in Clinical Nutrition and Metabolic Care · doi:10.1097/00075197-200105000-00003 · Cited by 399 · see citing works
(n-3) Fatty Acids and Cardiovascular Health: Are Effects of EPA and DHA Shared or Complementary?
Mozaffarian, D., & Wu, J. H. Y. (2012) · The Journal of Nutrition · doi:10.3945/jn.111.149633 · Cited by 368 · see citing works
Muscle wasting in insulinopenic rats results from activation of the ATP-dependent, ubiquitin-proteasome proteolytic pathway by a mechanism including gene transcription.
Price, S. R., Bailey, J. L., Wang, X., Jurkovitz, C. T., England, B. K., Ding, X., Phillips, L. S., & Mitch, W. E. (1996) · Journal of Clinical Investigation · doi:10.1172/jci118968 · Cited by 348 · see citing works
Self-citation
Regulation of Muscle Protein Degradation
Lee, S. W., Dai, G., Hu, Z., Wang, X., Du, J., & Mitch, W. E. (2004) · Journal of the American Society of Nephrology · doi:10.1097/01.asn.0000127211.86206.e1 · Cited by 323 · see citing works
Nutritional intervention with fish oil provides a benefit over standard of care for weight and skeletal muscle mass in patients with nonsmall cell lung cancer receiving chemotherapy
Murphy, R. A., Mourtzakis, M., Chu, Q. S.-C., Baracos, V. E., Reiman, T., & Mazurak, V. C. (2011) · Cancer · doi:10.1002/cncr.25709 · Cited by 286 · see citing works
Different effects of oleate vs. palmitate on mitochondrial function, apoptosis, and insulin signaling in L6 skeletal muscle cells: role of oxidative stress
Yuzefovych, L., Wilson, G., & Rachek, L. (2010) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00238.2010 · Cited by 280 · see citing works
Mechanical Ventilation–induced Diaphragm Disuse in Humans Triggers Autophagy
Hussain, S. N. A., Mofarrahi, M., Sigala, I., Kim, H. C., Vassilakopoulos, T., Maltais, F., Bellenis, I. P., Chaturvedi, R. K., Gottfried, S. B., Metrakos, P. P., et al. (2010) · American Journal of Respiratory and Critical Care Medicine · doi:10.1164/rccm.201002-0234oc · Cited by 264 · see citing works
Human Light Chain 3/MAP1LC3B Is Cleaved at Its Carboxyl-terminal Met121 to Expose Gly120 for Lipidation and Targeting to Autophagosomal Membranes
Tanida, I., Ueno, T., & Kominami, E. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m407016200 · Cited by 244 · see citing works
Chronic Kidney Disease Causes Defects in Signaling through the Insulin Receptor Substrate/Phosphatidylinositol 3-Kinase/Akt Pathway
Bailey, J. L., Zheng, B., Hu, Z., Price, S. R., & Mitch, W. E. (2006) · Journal of the American Society of Nephrology · doi:10.1681/asn.2004100842 · Cited by 238 · see citing works
Self-citation
Saturated fatty acid‐induced insulin resistance is associated with mitochondrial dysfunction in skeletal muscle cells
Hirabara, S. M., Curi, R., & Maechler, P. (2010) · Journal of Cellular Physiology · doi:10.1002/jcp.21936 · Cited by 215 · see citing works
n -3 Polyunsaturated fatty acids prevent the defect of insulin receptor signaling in muscle
Taouis, M., Dagou, C., Ster, C., Durand, G., Pinault, M., & Delarue, J. (2002) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00320.2001 · Cited by 181 · see citing works
Diet-induced obesity alters signalling pathways and induces atrophy and apoptosis in skeletal muscle in a prediabetic rat model: Diet-induced obesity and skeletal muscle
Sishi, B., Loos, B., Ellis, B., Smith, W., du Toit, E. F., & Engelbrecht, A.-M. (2011) · Experimental Physiology · doi:10.1113/expphysiol.2010.054189 · Cited by 162 · see citing works
Effect of supplementation with different doses of DHA on the levels of circulating DHA as non-esterified fatty acid in subjects of Asian Indian background.
Conquer, J. A., & Holub, B. J. (1998) · Journal of Lipid Research · doi:10.1016/s0022-2275(20)33890-6 · Cited by 153 · see citing works
FOXO3a mediates signaling crosstalk that coordinates ubiquitin and atrogin-1/MAFbx expression during glucocorticoid-induced skeletal muscle atrophy
Zheng, B., Ohkawa, S., Li, H., Roberts‐Wilson, T. K., & Price, S. R. (2010) · The FASEB Journal · doi:10.1096/fj.09-151480 · Cited by 145 · see citing works
Self-citation
The effect of eicosapentaenoic and docosahexaenoic acid on protein synthesis and breakdown in murine C2C12 myotubes
Kamolrat, T., & Gray, S. R. (2013) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2013.02.041 · Cited by 108 · see citing works
Evidence for Adipose-Muscle Cross Talk: Opposing Regulation of Muscle Proteolysis by Adiponectin and Fatty Acids
Zhou, Q., Du, J., Hu, Z., Walsh, K. X., & Wang, X. H. (2007) · Endocrinology · doi:10.1210/en.2007-0183 · Cited by 103 · see citing works
Resistance exercise and nutrition to counteract muscle wasting
Little, J. P., & Phillips, S. M. (2009) · Applied Physiology, Nutrition, and Metabolism · doi:10.1139/h09-093 · Cited by 100 · see citing works
Regulation of protein synthesis and degradation in L8 myotubes. Effects of serum, insulin and insulin-like growth factors
Gulve, E. A., & Dice, J. F. (1989) · Biochemical Journal · doi:10.1042/bj2600377 · Cited by 99 · see citing works
Molecular signaling pathways regulating muscle proteolysis during atrophy
Franch, H. A., & Price, S. R. (2005) · Current Opinion in Clinical Nutrition & Metabolic Care · doi:10.1097/01.mco.0000165005.01331.45 · Cited by 92 · see citing works
Self-citation
Dietary fish oil alleviates soleus atrophy during immobilization in association with Akt signaling to p70s6k and E3 ubiquitin ligases in rats
You, J.-S., Park, M.-N., Song, W., & Lee, Y.-S. (2010) · Applied Physiology Nutrition and Metabolism · doi:10.1139/h10-022 · Cited by 88 · see citing works
Acidosis impairs insulin receptor substrate-1-associated phosphoinositide 3-kinase signaling in muscle cells: consequences on proteolysis
Franch, H. A., Raissi, S., Wang, X., Zheng, B., Bailey, J. L., & Price, S. R. (2004) · American Journal of Physiology-Renal Physiology · doi:10.1152/ajprenal.00440.2003 · Cited by 80 · see citing works
Self-citation
Docosahexaenoic Acid Protects Muscle Cells from Palmitate-Induced Atrophy
Bryner, R. W., Woodworth‐Hobbs, M. E., Williamson, D. L., & Alway, S. E. (2012) · ISRN Obesity · doi:10.5402/2012/647348 · Cited by 66 · see citing works
Self-citation
Insulin-stimulated glucose uptake and pathways regulating energy metabolism in skeletal muscle cells: The effects of subcutaneous and visceral fat, and long-chain saturated, n-3 and n-6 polyunsaturated fatty acids
Lam, Y. Y., Hatzinikolas, G., Weir, J. M., Janovská, A., McAinch, A. J., Game, P. A., Meikle, P. J., & Wittert, G. (2011) · Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids · doi:10.1016/j.bbalip.2011.04.011 · Cited by 58 · see citing works
Targeting the Ubiquitin E3 Ligase MuRF1 to Inhibit Muscle Atrophy
Eddins, M. J., Marblestone, J. G., Kumar, S., Leach, C. A., Sterner, D. E., Mattern, M. R., & Nicholson, B. (2011) · Cell Biochemistry and Biophysics · doi:10.1007/s12013-011-9175-7 · Cited by 58 · see citing works
Muscular response and adaptation to diabetes mellitus
Sun, Z. (2008) · Frontiers in bioscience · doi:10.2741/3038 · Cited by 56 · see citing works
Treatment with Docosahexaenoic Acid, but Not Eicosapentaenoic Acid, Delays Ca2+-Induced Mitochondria Permeability Transition in Normal and Hypertrophied Myocardium
Khairallah, R. J., O’Shea, K. M., Brown, B. H., Khanna, N., Rosiers, C. D., & Stanley, W. C. (2010) · Journal of Pharmacology and Experimental Therapeutics · doi:10.1124/jpet.110.170605 · Cited by 56 · see citing works
Increased plasma n‐3 polyunsaturated fatty acid is associated with improved insulin sensitivity in type 2 diabetes in China
Huang, T., Wahlqvist, M. L., Xu, T., Xu, A., Zhang, A., & Li, D. (2009) · Molecular Nutrition & Food Research · doi:10.1002/mnfr.200900189 · Cited by 53 · see citing works
Pathophysiological Role of Autophagy: Lesson from Autophagy-Deficient Mouse Models
Ichimura, Y., & Komatsu, M. (2011) · EXPERIMENTAL ANIMALS · doi:10.1538/expanim.60.329 · Cited by 48 · see citing works
New findings of lysosomal proteolysis in skeletal muscle
Sandri, M. (2011) · Current Opinion in Clinical Nutrition & Metabolic Care · doi:10.1097/mco.0b013e3283457a75 · Cited by 46 · see citing works
Regulation of caspase-3 activity by insulin in skeletal muscle cells involves both PI3-kinase and MEK-1/2
Gao, Y., Ordas, R. J., Klein, J. D., & Price, S. R. (2008) · Journal of Applied Physiology · doi:10.1152/japplphysiol.90636.2008 · Cited by 44 · see citing works
Self-citation
Bax signaling regulates palmitate-mediated apoptosis in C2C12myotubes
Peterson, J. M., Wang, Y., Bryner, R. W., Williamson, D. L., & Alway, S. E. (2008) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00738.2007 · Cited by 41 · see citing works
A decreased<i>n</i>-6/<i>n</i>-3 ratio in the fat-1 mouse is associated with improved glucose tolerance
Smith, B. K., Holloway, G. P., Reza-Lopez, S., Jeram, S. M., Kang, J. X., & Ma, D. W. L. (2010) · Applied Physiology Nutrition and Metabolism · doi:10.1139/h10-066 · Cited by 35 · see citing works
Characterization of Intra-myocellular Lipids Using 2d Localized Correlated Spectroscopy and Abdominal Fat Using Mri in Type 2 Diabetes
Srikanthan, P., Singhal, A., Lee, C. C., Nagarajan, R., Wilson, N. E., Roberts, C. K., Hahn, T. J., & Thomas, M. A. (2012) · Magnetic Resonance Insights · doi:10.4137/mri.s10489 · Cited by 28 · see citing works
DHA reduces the atrophy-associated Fn14 protein in differentiated myotubes during coculture with macrophages
Finlin, B. S., Varma, V., Nolen, G. T., Dubé, J. J., Starnes, C. P., Rasouli, N., Kern, P. A., & Peterson, C. A. (2012) · The Journal of Nutritional Biochemistry · doi:10.1016/j.jnutbio.2011.04.013 · Cited by 10 · see citing works

Flagged first, then by citations

Sorted by citations

Lipid modulation of skeletal muscle mass and function
Lipina, C., & Hundal, H. S. (2017) · Journal of Cachexia, Sarcopenia and Muscle · doi:10.1002/jcsm.12144 · Cited by 247 · see citing works
Resveratrol prevents sarcopenic obesity by reversing mitochondrial dysfunction and oxidative stress via the PKA/LKB1/AMPK pathway
Huang, Y., Zhu, X., Chen, K., Lang, H., Zhang, Y., Hou, P., Ran, L., Zhou, M., Zheng, J., Yi, L., et al. (2019) · Aging · doi:10.18632/aging.101910 · Cited by 167 · see citing works
Potential Roles of n-3 PUFAs during Skeletal Muscle Growth and Regeneration
Tachtsis, B., Camera, D., & Lacham-Kaplan, O. (2018) · Nutrients · doi:10.3390/nu10030309 · Cited by 104 · see citing works
Nutraceuticals in the Prevention and Treatment of the Muscle Atrophy
Wang, Y., Liu, Q., Quan, H., Kang, S.-G., Huang, K., & Tong, T. (2021) · Nutrients · doi:10.3390/nu13061914 · Cited by 61 · see citing works
Short-Term High-Fat Feeding Does Not Alter Mitochondrial Lipid Respiratory Capacity but Triggers Mitophagy Response in Skeletal Muscle of Mice
Ehrlicher, S. E., Stierwalt, H. D., Newsom, S. A., & Robinson, M. M. (2021) · Frontiers in Endocrinology · doi:10.3389/fendo.2021.651211 · Cited by 25 · see citing works

A novel protein encoded by circKANSL1L regulates skeletal myogenesis via the Akt-FoxO3 signaling axis
Lin, Z., Xie, F., Xiao, H., Wang, J., Luo, J., Chen, T., Jiang, Q., Xi, Q., Zhang, Y., & Sun, J. (2023) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2023.128609 · Cited by 19 · see citing works
Fucoxanthin rescues dexamethasone induced C2C12 myotubes atrophy
Zhiyin, L., Jinliang, C., Qiunan, C., Yunfei, Y., & Xiao, Q. (2021) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2021.111590 · Cited by 46 · see citing works
Regulation of muscle atrophy-related genes by the opposing transcriptional activities of ZEB1/CtBP and FOXO3
Ninfali, C., Siles, L., Darling, D. S., & Postigo, A. A. (2018) · Nucleic Acids Research · doi:10.1093/nar/gky835 · Cited by 45 · see citing works
Foxo transcription factors induce the atrophy-related ubiquitin ligase atrogin-1 and cause skeletal muscle atrophy.
Sandri, M., Sandri, C., Gilbert, A., Skurk, C., Calabria, E., Picard, A., Walsh, K., Schiaffino, S., Lecker, S. H., & Goldberg, A. L. (2004) · Cell · doi:10.1016/s0092-8674(04)00400-3 · Cited by 3,012 · see citing works
Long Noncoding RNA lncMUMA Reverses Established Skeletal Muscle Atrophy following Mechanical Unloading
Zhang, Z., Li, J., Guan, D., Liang, C., Zhuo, Z., Liu, J., Lü, A., Zhang, G., & Zhang, B. (2018) · Molecular Therapy · doi:10.1016/j.ymthe.2018.09.014 · Cited by 62 · see citing works

Authors: Woodworth-Hobbs, M. E., Hudson, M. B., Rahnert, J. A., Zheng, B., Franch, H. A., & Price, S. R.
Affiliations: Emory University (US)
ORCID: Woodworth-Hobbs, Myra E.
Hudson, Matthew B.
Franch, Harold A.
Price, S. Russ
Venue: The Journal of Nutritional Biochemistry
Publisher: Elsevier BV
Published: 2014-08
Volume: 25
Issue: 8
Pages: 868-874
ISSN: 0955-2863 (ISSN-L)
DOI: 10.1016/j.jnutbio.2014.03.017
PMC: PMC4118671
OpenAlex: W2048654753
Cited by: 71
References: 42
Citations by year: 2026: 3 · 2025: 3 · 2024: 7 · 2023: 11 · 2022: 6 · 2021: 6 · 2020: 7 · 2019: 6 · 2018: 5 · 2017: 6 · 2016: 7 · 2015: 4
FWCI: 2.32
Type: journal article
Language: en
Open access: green
www.ncbi.nlm.nih.gov
Licence: www.elsevier.com/tdm/userlicense/1.0/ (tdm)
www.elsevier.com/legal/tdmrep-license (tdm)
Locations: The Journal of Nutritional Biochemistry (publishedVersion)
PubMed (publishedVersion)
PubMed Central (acceptedVersion)
Funders: U.S. Department of Veterans Affairs (I01‐BX001456)
National Institute of Diabetes and Digestive and Kidney Diseases (T32DK007734, R01DK095610, R01 DK-95610, T32DK007656)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Muscle Physiology and Disorders
Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Muscle metabolism and nutrition
Health Sciences › Nursing › Nutrition and Dietetics › Fatty Acid Research and Health
Keywords: docosahexaenoic acid, palmitate, muscle atrophy, myotubes, Akt signaling, FOXO3, atrogenes, atrogin-1/MAFbx, BNIP3, autophagy, ubiquitin-proteasome system, omega-3 fatty acids, saturated fatty acids, protein degradation, LC3B, insulin signaling
MeSH terms: Forkhead Box Protein O3, Animals, Autophagy, Cell Line, Docosahexaenoic Acids, Membrane Proteins, Microtubule-Associated Proteins, Muscle Proteins, Muscular Atrophy, Palmitates, Proteins, Signal Transduction, Muscle Fibers, Skeletal, Mitochondrial Proteins, SKP Cullin F-Box Protein Ligases, Proto-Oncogene Proteins c-akt, Mice, Forkhead Transcription Factors

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

Docosahexaenoic Acid Prevents Palmitate-Induced Activation of Proteolytic Systems in C2C12 Myotubes

Abstract

Integrity signals

Claims the paper makes

Claims other papers make about this one

Self-check

Cites

Cited by

Related

Record

About these checks