The DOI matches its Crossref record; 92 of the 92 references it cites were found in a registry or an index.
Ferulic Acid: A Hope for Alzheimer’s Disease Therapy from Plants
Open accessAbstract
Alzheimer’s disease (AD) is a neurodegenerative disorder characterized by the deposition of extracellular amyloid-beta peptide (Aβ) and intracellular neurofibrillar tangles, associated with loss of neurons in the brain and consequent learning and memory deficits. Aβ is the major component of the senile plaques and is believed to play a central role in the development and progress of AD both in oligomer and fibril forms. Inhibition of the formation of Aβ fibrils as well as the destabilization of preformed Aβ in the Central Nervous System (CNS) would be an attractive therapeutic target for the treatment of AD. Moreover, a large number of studies indicate that oxidative stress and mitochondrial dysfunction may play an important role in AD and their suppression or reduction via antioxidant use could be a promising preventive or therapeutic intervention for AD patients. Many antioxidant compounds have been demonstrated to protect the brain from Aβ neurotoxicity. Ferulic acid (FA) is an antioxidant naturally present in plant cell walls with anti-inflammatory activities and it is able to act as a free radical scavenger. Here we present the role of FA as inhibitor or disaggregating agent of amyloid structures as well as its effects on biological models.
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Citations
Cites
Global prevalence of dementia: a Delphi consensus study
Ferri, C. P., Prince, M., Brayne, C., Brodaty, H., Fratiglioni, L., Ganguli, M., Hall, K., Hasegawa, K., Hendrie, H., Huang, Y., et al. (2005) · The Lancet · doi:10.1016/s0140-6736(05)67889-0 · Cited by 5,332
Lignin Biosynthesis and Structure
Vanholme, R., Demedts, B., Morreel, K., Ralph, J., & Boerjan, W. (2010) · Plant Physiology · doi:10.1104/pp.110.155119 · Cited by 2,664
Mitogen-activated protein kinase pathways
Robinson, M. J., & Cobb, M. H. (1997) · Current Opinion in Cell Biology · doi:10.1016/s0955-0674(97)80061-0 · Cited by 2,474
Oxidative stress hypothesis in Alzheimer’s disease
Markesbery, W. R. (1997) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(96)00629-6 · Cited by 2,383
Yang, F., Lim, G. P., Begum, A. N., Ubeda, O. J., Simmons, M. R., Ambegaokar, S. S., Chen, P. P., Kayed, R., Glabe, C. G., Frautschy, S. A., et al. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m404751200 · Cited by 2,336
Mitogen-activated protein kinases in apoptosis regulation
Wada, T., & Penninger, J. M. (2004) · Oncogene · doi:10.1038/sj.onc.1207556 · Cited by 1,432 · cited 1×
“Apoptosis is controlled by different proteins of the kinase family, such as the mammalian mitogen–activated protein kinases (MAPKs) [89].”
BackgroundChlorogenic acids and other cinnamates - nature, occurrence and dietary burden
Clifford, M. N. (1999) · Journal of the Science of Food and Agriculture · doi:10.1002/(sici)1097-0010(19990301)79:3<362::aid-jsfa256>3.0.co;2-d · Cited by 1,335
Beta-amyloid neurotoxicity requires fibril formation and is inhibited by congo red.
Lorenzo, A., & Yankner, B. A. (1994) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.91.25.12243 · Cited by 1,324
A possible role for π‐stacking in the self‐assembly of amyloid fibrils
Gazit, E. (2002) · The FASEB Journal · doi:10.1096/fj.01-0442hyp · Cited by 1,133
Antioxidant potential of ferulic acid
Graf, E. (1992) · Free Radical Biology and Medicine · doi:10.1016/0891-5849(92)90184-i · Cited by 1,115
Ferulic Acid: Therapeutic Potential Through Its Antioxidant Property
Srinivasan, M., Sudheer, A. R., & Menon, V. P. (2007) · Journal of Clinical Biochemistry and Nutrition · doi:10.3164/jcbn.40.92 · Cited by 1,075
Porat, Y., Abramowitz, A., & Gazit, E. (2006) · Chemical Biology & Drug Design · doi:10.1111/j.1747-0285.2005.00318.x · Cited by 989
Potential applications of ferulic acid from natural sources
Kumar, N., & Pruthi, V. (2014) · Biotechnology Reports · doi:10.1016/j.btre.2014.09.002 · Cited by 962
Occurrence and content of hydroxycinnamic and hydroxybenzoic acid compounds in foods
Herrmann, K., & Nagel, C. W. (1989) · Critical Reviews in Food Science and Nutrition · doi:10.1080/10408398909527504 · Cited by 578
Ferulic acid: Pharmacological and toxicological aspects
Mancuso, C., & Santangelo, R. (2014) · Food and Chemical Toxicology · doi:10.1016/j.fct.2013.12.024 · Cited by 572
Akt Regulates Cell Survival and Apoptosis at a Postmitochondrial Level
Zhou, H., Li, X.-M., Meinkoth, J., & Pittman, R. N. (2000) · The Journal of Cell Biology · doi:10.1083/jcb.151.3.483 · Cited by 511
Kanski, J., Aksenova, M., Stoyanova, A., & Butterfield, D. A. (2002) · The Journal of Nutritional Biochemistry · doi:10.1016/s0955-2863(01)00215-7 · Cited by 502
Sosulski, F., Krygier, K., & Hogge, L. (1982) · Journal of Agricultural and Food Chemistry · doi:10.1021/jf00110a030 · Cited by 470
REVIEW: Curcumin and Alzheimer’s disease
Hamaguchi, T., Ono, K., & Yamada, M. (2010) · CNS Neuroscience & Therapeutics · doi:10.1111/j.1755-5949.2010.00147.x · Cited by 450
Hamaguchi, T., Ono, K., Murase, A., & Yamada, M. (2009) · The American Journal of Pathology · doi:10.2353/ajpath.2009.090417 · Cited by 398
Ferulic Acid Stabilizes a Solution of Vitamins C and E and Doubles its Photoprotection of Skin
Lin, F.-H., Lin, J.-Y., Gupta, R. D., Tournas, J. A., Burch, J. A., Angelica Selim, M., Monteiro-Riviere, N. A., Grichnik, J. M., Zielinski, J., & Pinnell, S. R. (2005) · Journal of Investigative Dermatology · doi:10.1111/j.0022-202x.2005.23768.x · Cited by 365
Protection against β‐amyloid peptide toxicity in vivo with long‐term administration of ferulic acid
Yan, J., Cho, J., Kim, H., Kim, K., Jung, J., Huh, S., Suh, H., Kim, Y., & Song, D. (2001) · British Journal of Pharmacology · doi:10.1038/sj.bjp.0704047 · Cited by 364
Oxidative stress in Alzheimer's disease
Chauhan, V., & Chauhan, A. (2006) · Pathophysiology · doi:10.1016/j.pathophys.2006.05.004 · Cited by 342
Pappolla, M. A., Chyan, Y., Omar, R. A., Hsiao, K., Perry, G. L., Smith, M. A., & Bozner, P. (1998) · Europe PMC (PubMed Central) · Cited by 328
Morris, A. M., Watzky, M. A., Agar, J. N., & Finke, R. G. (2008) · Biochemistry · doi:10.1021/bi701899y · Cited by 306
Review: Biocatalytic transformations of ferulic acid: An abundant aromatic natural product
Rosazza, J. P. N., Huang, Z., Dostal, L., Volm, T., & Rousseau, B. (1995) · Journal of Industrial Microbiology · doi:10.1007/bf01570016 · Cited by 301
Ferulic acid and its therapeutic potential as a hormetin for age-related diseases
Barone, E., Calabrese, V., & Mancuso, C. (2009) · Biogerontology · doi:10.1007/s10522-008-9160-8 · Cited by 296
Mancuso, C. (2007) · Frontiers in Bioscience · doi:10.2741/2130 · Cited by 294
A Three-Stage Kinetic Model of Amyloid Fibrillation
Lee, C.-C., Nayak, A., Sethuraman, A., Belfort, G., & McRae, G. J. (2007) · Biophysical Journal · doi:10.1529/biophysj.106.098608 · Cited by 278
Sultana, R., Ravagna, A., Mohmmad‐Abdul, H., Calabrese, V., & Butterfield, D. A. (2005) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2004.02899.x · Cited by 276
Jung, E. H., Ran Kim, S., Hwang, I. K., & Youl Ha, T. (2007) · Journal of Agricultural and Food Chemistry · doi:10.1021/jf0714463 · Cited by 264
Ono, K., Li, L., Takamura, Y., Yoshiike, Y., Zhu, L., Han, F., Mao, X., Ikeda, T., Takasaki, J.-I., Nishijo, H., et al. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.325456 · Cited by 251
Amyloid Fibrils of Mammalian Prion Protein Are Highly Toxic to Cultured Cells and Primary Neurons
Novitskaya, V., Bocharova, O. V., Bronstein, I., & Baskakov, I. V. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m511174200 · Cited by 247
ITAGAKI, S., KUROKAWA, T., NAKATA, C., SAITO, Y., OIKAWA, S., KOBAYASHI, M., HIRANO, T., & ISEKI, K. (2009) · Food Chemistry · doi:10.1016/j.foodchem.2008.09.073 · Cited by 219
Plants as natural antioxidants
Gupta, V., & Sharma, S. K. (2006) · Cited by 218
Cheng, C.-Y., Su, S.-Y., Tang, N.-Y., Ho, T.-Y., Chiang, S.-Y., & Hsieh, C.-L. (2008) · Brain Research · doi:10.1016/j.brainres.2008.02.090 · Cited by 217
Lempereur, I., Rouau, X., & Abecassis, J. (1997) · Journal of Cereal Science · doi:10.1006/jcrs.1996.0090 · Cited by 217
Zhao, Z., Egashira, Y., & Sanada, H. (2004) · The Journal of Nutrition · doi:10.1093/jn/134.11.3083 · Cited by 216
Fetoni, A. R., De Bartolo, P., Eramo, S. L. M., Rolesi, R., Paciello, F., Bergamini, C., Fato, R., Paludetti, G., Petrosini, L., & Troiani, D. (2013) · The Journal of Neuroscience · doi:10.1523/jneurosci.2282-12.2013 · Cited by 213
Gharibyan, A. L., Zamotin, V., Yanamandra, K., Moskaleva, O. S., Margulis, B. A., Kostanyan, I. A., & Morozova-Roche, L. A. (2007) · Journal of Molecular Biology · doi:10.1016/j.jmb.2006.10.101 · Cited by 206
Mannini, B., Mulvihill, E., Sgromo, C., Cascella, R., Khodarahmi, R., Ramazzotti, M., Dobson, C. M., Cecchi, C., & Chiti, F. (2014) · ACS Chemical Biology · doi:10.1021/cb500505m · Cited by 204
Mori, T., Koyama, N., Guillot-Sestier, M.-V., Tan, J., & Town, T. (2013) · PLoS ONE · doi:10.1371/journal.pone.0055774 · Cited by 189
Bound Ferulic Acid from Bran Is More Bioavailable than the Free Compound in Rat
Rondini, L., Peyrat-Maillard, M.-N., Marsset-Baglieri, A., Fromentin, G., Durand, P., Tomé, D., Prost, M., & Berset, C. (2004) · Journal of Agricultural and Food Chemistry · doi:10.1021/jf0348323 · Cited by 178
Ferulic acid destabilizes preformed β-amyloid fibrils in vitro
Ono, K., Hirohata, M., & Yamada, M. (2005) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2005.08.148 · Cited by 172
Picone, P., Bondì, M. L., Picone, P., Bondì, M. L., Montana, G., Bruno, A., Pitarresi, G. L., Giammona, G., & Carlo, M. D. (2009) · Free Radical Research · doi:10.1080/10715760903214454 · Cited by 156
Ferulic acid induces neural progenitor cell proliferation in vitro and in vivo
Yabe, T., Hirahara, H., Harada, N., Ito, N., Nagai, T., Sanagi, T., & Yamada, H. (2009) · Neuroscience · doi:10.1016/j.neuroscience.2009.10.023 · Cited by 150
Serafim, T. L., Carvalho, F. S., Marques, M. P. M., Calheiros, R., Silva, T., Garrido, J. M. P. J., Milhazes, N., Borges, F., Roleira, F. M. F., da Silva, E. J. T., et al. (2011) · Chemical Research in Toxicology · doi:10.1021/tx200126r · Cited by 149
Kern, S. M., Bennett, R. N., Needs, P. W., Mellon, F. A., Kroon, P. A., & García‐Conesa, M. (2003) · Journal of Agricultural and Food Chemistry · doi:10.1021/jf030470n · Cited by 147
Phenolic Acids Are Absorbed from the Rat Stomach with Different Absorption Rates
Konishi, Y., Zhao, Z., & Shimizu, M. (2006) · Journal of Agricultural and Food Chemistry · doi:10.1021/jf061554+ · Cited by 143
Ardiansyah, A., Ohsaki, Y., Shirakawa, H., Koseki, T., & Komai, M. (2008) · Journal of Agricultural and Food Chemistry · doi:10.1021/jf072896y · Cited by 133
Howlett, D. R., George, A. R., OWEN, D. E., Ward, R. V., & Markwell, R. E. (1999) · Biochemical Journal · doi:10.1042/bj3430419 · Cited by 133
Garrett, A. J. M. (1991) · Springer eBooks · doi:10.1007/978-94-011-3460-6_36 · Cited by 132
Zhao, Z., Egashira, Y., & Sanada, H. (2003) · Journal of Nutrition · doi:10.1093/jn/133.5.1355 · Cited by 132
Digestion and Absorption of Ferulic Acid Sugar Esters in Rat Gastrointestinal Tract
Zhao, Z., Egashira, Y., & Sanada, H. (2003) · Journal of Agricultural and Food Chemistry · doi:10.1021/jf034455u · Cited by 130
Wu, W., Lee, S. Y., Wu, X., Tyler, J. Y., Wang, H., Ouyang, Z., Park, K., Xu, X., & Cheng, J. (2013) · Biomaterials · doi:10.1016/j.biomaterials.2013.11.074 · Cited by 130
Toxic effects of amyloid fibrils on cell membranes: the importance of ganglioside GM1
Bucciantini, M., Nosi, D., Forzan, M., Russo, E., Calamai, M., Pieri, L., Formigli, L., Quercioli, F., Soria, S., Pavone, F. S., et al. (2011) · The FASEB Journal · doi:10.1096/fj.11-189381 · Cited by 126
Howlett, D. R., George, A. R., OWEN, D. E., Ward, R. V., & Markwell, R. E. (1999) · PubMed Central · Cited by 123
Assessing the role of aromatic residues in the amyloid aggregation of human muscle acylphosphatase
Bemporad, F., Taddei, N., Stefani, M., & Chiti, F. (2006) · Protein Science · doi:10.1110/ps.051915806 · Cited by 122
Trombino, S., Cassano, R., Ferrarelli, T., Barone, E., Picci, N., & Mancuso, C. (2013) · Colloids and Surfaces B Biointerfaces · doi:10.1016/j.colsurfb.2013.04.005 · Cited by 121
Carlo, M. D., Giacomazza, D., Picone, P., Nuzzo, D., & Biagio, P. L. S. (2012) · Free Radical Research · doi:10.3109/10715762.2012.714466 · Cited by 111
Self-citationAbsorption of ferulic acid from low-alcohol beer
Bourne, L., Paganga, G., Baxter, D., Hughes, P., & Rice-Evans, C. A. (2000) · Free Radical Research · doi:10.1080/10715760000300281 · Cited by 110
Yan, J.-J., Jung, J., Kim, T.-K., Hasan, M. A., Hong, C.-W., Nam, J., & Song, D. (2012) · Biological and Pharmaceutical Bulletin · doi:10.1248/bpb.b12-00798 · Cited by 107
Calabrese, V., Calafato, S., Puleo, E., Cornelius, C., Sapienza, M. A., Morganti, P., & Mancuso, C. (2008) · Clinics in Dermatology · doi:10.1016/j.clindermatol.2008.01.005 · Cited by 107
Amyloid Aggregation: Role of Biological Membranes and the Aggregate–Membrane System
Bucciantini, M., Rigacci, S., & Stefani, M. (2014) · The Journal of Physical Chemistry Letters · doi:10.1021/jz4024354 · Cited by 106
Endogenous pine wood nematicidal substances in pines, Pinus massoniana, P. strobus and P. palustris
Suga, T., Ohta, S., Munesada, K., Ide, N., Kurokawa, M., Shimizu, M., & Ohta, E. (1993) · Phytochemistry · doi:10.1016/0031-9422(93)85098-c · Cited by 105
Kim, H., Cho, J.-Y., Kim, D.-H., Yan, J.-J., Lee, H., Suh, H., & Song, D. (2004) · Biological and Pharmaceutical Bulletin · doi:10.1248/bpb.27.120 · Cited by 105
Picone, P., Carrotta, R., Montana, G., Nobile, M. R., Biagio, P. L. S., & Carlo, M. D. (2009) · Biophysical Journal · doi:10.1016/j.bpj.2008.11.056 · Cited by 97
Mediterranean diet and healthy ageing: a Sicilian perspective
Vasto, S., Buscemi, S., Barera, A., Di Carlo, M., Accardi, G., & Caruso, C. (2014) · Gerontology · doi:10.1159/000363060 · Cited by 94
Virgili, F., Pagana, G., Bourne, L., Rimbach, G. H., Natella, F., Rice-Evans, C. A., & Packer, L. (2000) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(00)00244-6 · Cited by 93
Amyloid binding ligands as Alzheimer’s disease therapies
Lee, V. M. ‐. (2002) · Neurobiology of Aging · doi:10.1016/s0197-4580(02)00121-5 · Cited by 80
Jin, Y. H., Yan, E., Fan, Y., Zong, Z., Zhi-min, Q. I., & Li, Z. (2005) · Acta Pharmacologica Sinica · doi:10.1111/j.1745-7254.2005.00158.x · Cited by 79
Cho, J., Kim, H., Kim, D., Yan, J.-J., Suh, H., & Song, D. (2005) · Progress in Neuro-Psychopharmacology and Biological Psychiatry · doi:10.1016/j.pnpbp.2005.04.022 · Cited by 75
Cheng, C.-Y., Su, S.-Y., Tang, N.-Y., Ho, T., Lo, W., & Hsieh, C. (2010) · Acta Pharmacologica Sinica · doi:10.1038/aps.2010.66 · Cited by 71
Natural Biomolecules and Protein Aggregation: Emerging Strategies against Amyloidogenesis
Sgarbossa, A. (2012) · International Journal of Molecular Sciences · doi:10.3390/ijms131217121 · Cited by 70
Self-citationBondì, M. L., Montana, G., Craparo, E. F., Picone, P., Capuano, G., Carlo, M. D., & Giammona, G. (2009) · Current Nanoscience · doi:10.2174/157341309787314656 · Cited by 70
Ferulic acid prevents the cerebral ischemic injury-induced decrease of Akt and Bad phosphorylation
Koh, P. (2011) · Neuroscience Letters · doi:10.1016/j.neulet.2011.12.012 · Cited by 67
Mediterranean Diet And Longevity: An Example Of Nutraceuticals?
Vasto, S., Barera, A., Rizzo, C., Carlo, M. D., Caruso, C., & Panotopoulos, G. (2013) · Current Vascular Pharmacology · doi:10.2174/1570161111666131219111818 · Cited by 62
Cui, L., Zhang, Y., Cao, H., Wang, Y., Teng, T., Ma, G., Li, Y., Li, K., & Zhang, Y. (2013) · Journal of Alzheimer s Disease · doi:10.3233/jad-130164 · Cited by 60
Pharmacologists and Alzheimer disease therapy: to boldly go where no scientist has gone before
Mancuso, C., Siciliano, R., Barone, E., Butterfield, D. A., & Preziosi, P. (2011) · Expert Opinion on Investigational Drugs · doi:10.1517/13543784.2011.601740 · Cited by 53
Effect of Phenolic Compounds Against Aβ Aggregation and Aβ-Induced Toxicity in Transgenic C. elegans
Jagota, S., & Rajadas, J. (2011) · Neurochemical Research · doi:10.1007/s11064-011-0580-5 · Cited by 52
Goldsbury, C. S., Whiteman, I. T., Jeong, E. V., & Lim, Y. (2008) · Aging Cell · doi:10.1111/j.1474-9726.2008.00423.x · Cited by 45
Ying, J. I. N., Fan, Y., Yan, E., Liu, Z., Zong, Z., & Zhi-min, Q. I. (2006) · Acta Pharmacologica Sinica · doi:10.1111/j.1745-7254.2006.00414.x · Cited by 40
β-Amyloid Amorphous Aggregates Induced by the Small Natural Molecule Ferulic Acid
Bramanti, E., Fulgentini, L., Bizzarri, R., Lenci, F., & Sgarbossa, A. (2013) · The Journal of Physical Chemistry B · doi:10.1021/jp4079986 · Cited by 40
Self-citationEffects of hypericin on the structure and aggregation properties of β-amyloid peptides
Bramanti, E., Lenci, F., & Sgarbossa, A. (2010) · European Biophysics Journal · doi:10.1007/s00249-010-0607-x · Cited by 34
Self-citationYang, C. Y., Tian, Y., Zhang, Z., Xu, F., & Chen, Y. (2006) · Journal of Pharmaceutical and Biomedical Analysis · doi:10.1016/j.jpba.2006.09.027 · Cited by 33
Szwajgier, D., & Jakubczyk, A. (2010) · Acta Scientiarum Polonorum Technologia Alimentaria · Cited by 27
Sgarbossa, A., Monti, S., Lenci, F., Bramanti, E., Bizzarri, R., & Barone, V. (2013) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2012.12.023 · Cited by 27
Self-citationChemical Constituents of Black Locust Bark and their Biocidal Activity
Putman, L. J., Laks, P. E., & Pruner, M. S. (1989) · Holzforschung · doi:10.1515/hfsg.1989.43.4.219 · Cited by 24
Nutritional antioxidants: A battle for better health
Rathore, G. S., Suthar, M., Pareek, A., & Gupta, R. (2011) · Journal of Natural Pharmaceuticals · doi:10.4103/2229-5119.78490 · Cited by 22
Mancuso, C. (2015) · Frontiers in Pharmacology · doi:10.3389/fphar.2015.00086 · Cited by 18
Nanostructures for Bypassing Blood Brain Barrier
Wang, J., Valmikinathan, C. M., & Yu, X. (2009) · Current Bioactive Compounds · doi:10.2174/157340709789054777 · Cited by 10
A MODERN REVIEW ON SOLID LIPID NANOPARTICLES AS NOVEL CONTROLLED DRUG DELIVERY SYSTEM
Reddy, A., Parthiban, S., Vikneswari, A., & Senthilkumar, G. P. (2014) · Cited by 10
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Berding, K., Vlckova, K., Marx, W., Schellekens, H., Stanton, C., Clarke, G., Jacka, F., Dinan, T. G., & Cryan, J. F. (2021) · Advances in Nutrition · doi:10.1093/advances/nmaa181 · Cited by 451
Review of Distribution, Extraction Methods, and Health Benefits of Bound Phenolics in Food Plants
Wang, Z., Li, S., Ge, S., & Lin, S. (2020) · Journal of Agricultural and Food Chemistry · doi:10.1021/acs.jafc.9b06574 · Cited by 269
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Anand, A., Patience, A. A., Sharma, N., & Khurana, N. (2017) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2017.09.043 · Cited by 174
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Pasinetti, G. M., Singh, R., Westfall, S., Herman, F., Faith, J., & Ho, L. (2018) · Journal of Alzheimer s Disease · doi:10.3233/jad-171151 · Cited by 112
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Metadata
- Authors
- Sgarbossa, A., Giacomazza, D., & Di Carlo, M.
- Venue
- Nutrients
- Publisher
- MDPI AG
- Published
- 2015-07-15
- Volume
- 7
- Issue
- 7
- Pages
- 5764-5782
- ISSN
- 2072-6643 (ISSN-L)
- OpenAlex
- W1570813833
- Cited by
- 282
- References
- 92
- FWCI
- 12.91
- Type
- journal article
- Language
- en
- Open access
- gold
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