Cited by 174Microtubule and mitosis dynamicsPlant Molecular Biology ResearchCancer-related Molecular Pathways

The DOI matches its Crossref record; 31 of the 31 references it cites were found in a registry or an index.

A soybean cDNA encoding a chromatin-binding peptide inhibits mitosis of mammalian cells.

Galvez, Alfredo F., de Lumen, Benito O.·1999·Nature Biotechnology

Open this paper in CoChat — free account

Abstract

A soybean cDNA encoding the small subunit peptide of a cotyledon-specific 2S albumin (Gm2S-1) is thought to play a role in arresting mitosis during the DNA endoreduplication and cell expansion phase of seed development. The peptide (termed lunasin) contains the cell adhesion motif Arg-Gly-Asp (RGD) followed by eight aspartic acid residues at its C-terminal end. A chimeric gene encoding the lunasin peptide tagged with green fluorescent protein (GFP) arrested cell division, caused abnormal spindle fiber elongation, chromosomal fragmentation, and cell lysis when transiently transfected into murine embryo fibroblast, murine hepatoma, and human breast cancer cells. Deletion of the polyaspartyl end abolished the antimitotic effect. Subcellular localization of lunasin and immunobinding assay using synthetic peptides revealed the preferential adherence of lunasin to chromatin. Immunofluorescence showed that kinetochore proteins were displaced from the centromere in lunasin-transfected cells. These observations suggest that lunasin binds to the chromatin, leading to disruption of kinetochore formation and inhibition of mitosis.

Integrity signals

Registry

Crossref · 10.1038/8676

Cites

31 of 31 references verified0 citation errors · 0 not checkable

Statistics

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

Claims the paper makes

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

Claims other papers make about this one

Each is checked against this paper’s own text: does it say what the citing paper says it does?

Crystal structure of the nucleosome core particle at 2.8 Å resolution
Luger, K., Mäder, A. W., Richmond, R. K., Sargent, D. F., & Richmond, T. J. (1997) · Nature · doi:10.1038/38444 · Cited by 9,466
Arg-Gly-Asp: A versatile cell recognition signal
Ruoslahti, E., & Pierschbacher, M. D. (1986) · Cell · doi:10.1016/0092-8674(86)90259-x · Cited by 1,397
Taxol: A Novel Investigational Antimicrotubule Agent
Rowinsky, E. K., Cazenave, L. A., & Donehower, R. C. (1990) · JNCI Journal of the National Cancer Institute · doi:10.1093/jnci/82.15.1247 · Cited by 1,090
Association of Spindle Assembly Checkpoint Component XMAD2 with Unattached Kinetochores
Chen, R.-H., Waters, J. C., Salmon, E. D., & Murray, A. W. (1996) · Science · doi:10.1126/science.274.5285.242 · Cited by 783
Histone H3 and H4 N-termini interact with SIR3 and SIR4 proteins: A molecular model for the formation of heterochromatin in yeast
Hecht, A., Laroche, T., Strahl-Bolsinger, S., Gasser, S. M., & Grunstein, M. (1995) · Cell · doi:10.1016/0092-8674(95)90512-x · Cited by 780
Plant Embryogenesis: Zygote to Seed
Goldberg, R. B., de Paiva, G., & Yadegari, R. (1994) · Science · doi:10.1126/science.266.5185.605 · Cited by 613
Identification of a Human Mitotic Checkpoint Gene: hsMAD2
Li, Y., & Benezra, R. (1996) · Science · doi:10.1126/science.274.5285.246 · Cited by 598
The Cell Nucleus
BUSCH, H. (1966) · Nature · doi:10.1038/2111347a0 · Cited by 515
Molecular cloning of cDNA for CENP-B, the major human centromere autoantigen
Earnshaw, W., Sullivan, K., Machlin, P., Cooke, C., Kaiser, D., Pollard, T., Rothfield, N., & Cleveland, D. (1987) · The Journal of cell biology · doi:10.1083/jcb.104.4.817 · Cited by 425
Eukaryotic DNA topoisomerases: two forms of type I DNA topoisomerases from HeLa cell nuclei.
Liu, L. F., & Miller, K. G. (1981) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.78.6.3487 · Cited by 346

Show all 31 references

Research works printed but not linked: 3

Wilson, L. & Jordan, M.A. in Microtubules (eds. Hyams, J. & Lloyd, C.) 59–84 (Wiley-Liss Inc., New York, 1994).
Rowinsky, E.K., Casenave, L.H. & Donehower, R.C. Taxol: a novel investigational antimicrotubule agent. J. Natl. Cancer Inst. 82, 1247– 1259 (1990). · DOI · Paper page
Maniatis, T., Fritsch, E.F. & Sambrook, J. in Molecular Cloning 368– 369 (Cold Spring Harbor Laboratory Press, Cold Spring Harbor, New York, 1982).

Nutritional and Health Benefits of Soy Proteins
Friedman, M., & Brandon, D. L. (2001) · Journal of Agricultural and Food Chemistry · doi:10.1021/jf0009246 · Cited by 916
How the sourdough may affect the functional features of leavened baked goods
Gobbetti, M., Rizzello, C. G., Di Cagno, R., & De Angelis, M. (2014) · Food Microbiology · doi:10.1016/j.fm.2013.04.012 · Cited by 397
A New Frontier in Soy Bioactive Peptides that May Prevent Age‐related Chronic Diseases
Wang, W., & De Mejia, E. G. (2005) · Comprehensive Reviews in Food Science and Food Safety · doi:10.1111/j.1541-4337.2005.tb00075.x · Cited by 393
Bioactive Molecules Released in Food by Lactic Acid Bacteria: Encrypted Peptides and Biogenic Amines
Pessione, E., & Cirrincione, S. (2016) · Frontiers in Microbiology · doi:10.3389/fmicb.2016.00876 · Cited by 333
Bioactive Peptides in Amaranth (Amaranthus hypochondriacus) Seed
Silva-Sánchez, C., de la Rosa, A. P. B., León-Galván, M. F., de Lumen, B. O., de León-Rodríguez, A., & de Mejía, E. G. (2008) · Journal of Agricultural and Food Chemistry · doi:10.1021/jf072911z · Cited by 278
Structural-features of food-derived bioactive peptides with anti-inflammatory activity: A brief review
Guha, S., & Majumder, K. (2018) · Journal of Food Biochemistry · doi:10.1111/jfbc.12531 · Cited by 245
Chemopreventive property of a soybean peptide (lunasin) that binds to deacetylated histones and inhibits acetylation.
Galvez, A. F., Chen, N., Macasieb, J., & de Lumen, B. O. (2001) · PubMed · Cited by 232
Self-citation
Bioactive peptides in cereals and legumes: agronomical, biochemical and clinical aspects.
Malaguti, M., Dinelli, G., Leoncini, E., Bregola, V., Bosi, S., Cicero, A., & Hrelia, S. (2014) · International Journal of Molecular Sciences · doi:10.3390/ijms151121120 · Cited by 180
The role of nutraceutical proteins and peptides in apoptosis, angiogenesis, and metastasis of cancer cells
de Mejía, E. G., & Día, V. P. (2010) · Cancer and Metastasis Reviews · doi:10.1007/s10555-010-9241-4 · Cited by 180
Bioactive Food Peptides in Health and Disease
Hernandez-Ledesma, B., & Hsieh, C. (2013) · InTech eBooks · doi:10.5772/3318 · Cited by 171
Lunasin, a novel seed peptide for cancer prevention
Hernández‐Ledesma, B., Hsieh, C. C., & de Lumen, B. O. (2008) · Peptides · doi:10.1016/j.peptides.2008.11.002 · Cited by 148
Lunasin: A Cancer-Preventive Soy Peptide
de Lumen, B. O. (2005) · Nutrition Reviews · doi:10.1111/j.1753-4887.2005.tb00106.x · Cited by 146
Complementary Roles in Cancer Prevention: Protease Inhibitor Makes the Cancer Preventive Peptide Lunasin Bioavailable
Hsieh, C., Hernández‐Ledesma, B., Jeong, H. J., Park, J. H., & de Lumen, B. O. (2010) · PLoS ONE · doi:10.1371/journal.pone.0008890 · Cited by 143
The cancer preventive peptide lunasin from wheat inhibits core histone acetylation
Jeong, H. J., Jeong, J. B., Kim, D. S., Park, J. H., Lee, J. B., Kweon, D., Chung, G. Y., Seo, E. W., & de Lumen, B. O. (2007) · Cancer Letters · doi:10.1016/j.canlet.2007.03.022 · Cited by 125
Antioxidant activity and protective effects of peptide lunasin against oxidative stress in intestinal Caco-2 cells
García‐Nebot, M. J., Recio, I., & Hernández‐Ledesma, B. (2013) · Food and Chemical Toxicology · doi:10.1016/j.fct.2013.12.021 · Cited by 119
Characterization of Lunasin Isolated from Soybean
Jeong, H. J., Park, J. H., Lam, Y. H., & de Lumen, B. O. (2003) · Journal of Agricultural and Food Chemistry · doi:10.1021/jf034460y · Cited by 117
Bioactive peptide with antioxidant and anticancer activities from black soybean [Glycine max (L.) Merr.] byproduct: isolation, identification and molecular docking study
Chen, Z., Li, W., Santhanam, R. K., Wang, C., Gao, X., Chen, Y., Wang, C., Xu, L., & Chen, H. (2018) · European Food Research and Technology · doi:10.1007/s00217-018-3190-5 · Cited by 115
“Potential Health Benefits of Lunasin: A Multifaceted Soy‐Derived Bioactive Peptide”
Lule, V. K., Garg, S., Pophaly, S. D., Hitesh, H., & Tomar, S. K. (2015) · Journal of Food Science · doi:10.1111/1750-3841.12786 · Cited by 111
Barley Lunasin Suppresses ras-Induced Colony Formation and Inhibits Core Histone Acetylation in Mammalian Cells
Jeong, H. J., Lam, Y. H., & de Lumen, B. O. (2002) · Journal of Agricultural and Food Chemistry · doi:10.1021/jf0256945 · Cited by 108
Lunasin Concentration in Different Soybean Genotypes, Commercial Soy Protein, and Isoflavone Products
de Mejía, E. G., Vásconez, M., de Lumen, B. O., & Nelson, R. L. (2004) · Journal of Agricultural and Food Chemistry · doi:10.1021/jf0496752 · Cited by 100
Lunasin induces apoptosis and modifies the expression of genes associated with extracellular matrix and cell adhesion in human metastatic colon cancer cells
Día, V. P., & de Mejía, E. G. (2011) · Molecular Nutrition & Food Research · doi:10.1002/mnfr.201000419 · Cited by 100
Lunasin™ Suppresses E1A-Mediated Transformation of Mammalian Cells but Does Not Inhibit Growth of Immortalized and Established Cancer Cell Lines
Lam, Y. H., Galvez, A. F., & de Lumen, B. O. (2003) · Nutrition and Cancer · doi:10.1207/s15327914nc4701_11 · Cited by 99
Self-citation
Synthesis of the Cancer Preventive Peptide Lunasin by Lactic Acid Bacteria During Sourdough Fermentation
Rizzello, C. G., Nionelli, L., Coda, R., & Gobbetti, M. (2011) · Nutrition and Cancer · doi:10.1080/01635581.2012.630159 · Cited by 90
Soybean bioactive peptides: A new horizon in preventing chronic diseases
DEMEJIA, E., & Delumen, B. O. (2006) · Sexuality, reproduction & menopause · doi:10.1016/j.sram.2006.08.012 · Cited by 86
Self-citation
Inhibition of Core Histone Acetylation by the Cancer Preventive Peptide Lunasin
Jeong, H. J., Jeong, J. B., Kim, D. S., & de Lumen, B. O. (2007) · Journal of Agricultural and Food Chemistry · doi:10.1021/jf062405u · Cited by 86
Lunasin suppresses the migration and invasion of breast cancer cells by inhibiting matrix metalloproteinase-2/-9 via the FAK/Akt/ERK and NF-κB signaling pathways
Jiang, Q., Pan, Y., Cheng, Y., Li, H., Liu, D., & Li, H. (2016) · Oncology Reports · doi:10.3892/or.2016.4798 · Cited by 82
Anticancer peptides mechanisms, simple and complex
Norouzi, P., Mirmohammadi, M., & Tehrani, M. H. H. (2022) · Chemico-Biological Interactions · doi:10.1016/j.cbi.2022.110194 · Cited by 81
Chemopreventive role of food-derived proteins and peptides: A review
Hernández‐Ledesma, B., & Hsieh, C. (2015) · Critical Reviews in Food Science and Nutrition · doi:10.1080/10408398.2015.1057632 · Cited by 78
Soy bioactive peptides and the gut microbiota modulation
Ashaolu, T. J. (2020) · Applied Microbiology and Biotechnology · doi:10.1007/s00253-020-10799-2 · Cited by 78
Amaranth lunasin-like peptide internalizes into the cell nucleus and inhibits chemical carcinogen-induced transformation of NIH-3T3 cells
Cervantes, E. M., Jeong, H. J., León‐Galván, M. F., Barrera-Pacheco, A., León‐Rodríguez, A. D., de Mejía, E. G., de Lumen, B. O., & de la Rosa, A. P. B. (2010) · Peptides · doi:10.1016/j.peptides.2010.06.014 · Cited by 77
Lunasin, a novel seed peptide, sensitizes human breast cancer MDA-MB-231 cells to aspirin-arrested cell cycle and induced apoptosis
Hsieh, C., Hernández‐Ledesma, B., & de Lumen, B. O. (2010) · Chemico-Biological Interactions · doi:10.1016/j.cbi.2010.04.027 · Cited by 71
Antioxidants in Potatoes: A Functional View on One of the Major Food Crops Worldwide
Hellmann, H. A., Goyer, A., & Navarre, D. A. (2021) · Molecules · doi:10.3390/molecules26092446 · Cited by 71
Lunasin, with an arginine–glycine–aspartic acid motif, causes apoptosis to L1210 leukemia cells by activation of caspase‐3
de Mejía, E. G., Wang, W., & Día, V. P. (2009) · Molecular Nutrition & Food Research · doi:10.1002/mnfr.200900073 · Cited by 70
Scalable Purification and Characterization of the Anticancer Lunasin Peptide from Soybean
Seber, L. E., Barnett, B. W., McConnell, E. J., Hume, S. D., Cai, J., Boles, K., & Davis, K. (2012) · PLoS ONE · doi:10.1371/journal.pone.0035409 · Cited by 69
Bioactive Proteins and Peptides from Soybeans
Agyei, D. (2015) · Recent Patents on Food Nutrition & Agriculture · doi:10.2174/2212798407666150629134141 · Cited by 67
Relationship between lunasin's sequence and its inhibitory activity of histones H3 and H4 acetylation
Hernández‐Ledesma, B., Hsieh, C., & de Lumen, B. O. (2011) · Molecular Nutrition & Food Research · doi:10.1002/mnfr.201000632 · Cited by 66
The soybean peptide lunasin promotes apoptosis of mammary epithelial cells via induction of tumor suppressor PTEN: similarities and distinct actions from soy isoflavone genistein
Pabona, J. M. P., Dave, B., Su, Y., Montales, M. T. E., de Lumen, B. O., de Mejía, E. G., Rahal, O. M., & Simmen, R. C. M. (2012) · Genes & Nutrition · doi:10.1007/s12263-012-0307-5 · Cited by 65
In Vitro Digestibility of the Cancer-Preventive Soy Peptides Lunasin and BBI
Park, J. H., Jeong, H. J., & de Lumen, B. O. (2007) · Journal of Agricultural and Food Chemistry · doi:10.1021/jf072107c · Cited by 63
Health Applications of Soy Protein Hydrolysates
Ashaolu, T. J. (2020) · International Journal of Peptide Research and Therapeutics · doi:10.1007/s10989-020-10018-6 · Cited by 62
Unravelling the molecular mechanisms associated with the role of food-derived bioactive peptides in promoting cardiovascular health
Martínez-Sánchez, S. M., Gabaldón, J. A., & Montoro‐García, S. (2019) · Journal of Functional Foods · doi:10.1016/j.jff.2019.103645 · Cited by 60
Updating the research on the chemopreventive and therapeutic role of the peptide lunasin
Hsieh, C., Martínez‐Villaluenga, C., de Lumen, B. O., & Hernández‐Ledesma, B. (2017) · Journal of the Science of Food and Agriculture · doi:10.1002/jsfa.8719 · Cited by 57
A soy protein Lunasin can ameliorate amyloid-beta 42 mediated neurodegeneration in Drosophila eye
Sarkar, A., Gogia, N., Glenn, N. W., Singh, A. P., Jones, G. E., Powers, N., Srivastava, A., Singh, A., & Singh, A. (2018) · Scientific Reports · doi:10.1038/s41598-018-31787-7 · Cited by 53
Soypeptide lunasin in cytokine immunotherapy for lymphoma
Chang, H., Lewis, D., Tung, C.-Y., Han, L., Henriquez, S. M. P., Voiles, L., Lupov, I. P., Pelloso, D., Sinn, A. L., Pollok, K. E., et al. (2013) · Cancer Immunology Immunotherapy · doi:10.1007/s00262-013-1513-8 · Cited by 53
Lunasin: A promising polypeptide for the prevention and treatment of cancer
Wan, X., Liu, H., Sun, Y., Zhang, J., Chen, X., & Chen, N. (2017) · Oncology Letters · doi:10.3892/ol.2017.6017 · Cited by 52
Legumes as Functional Food for Cardiovascular Disease
Angeles, J. G. C., Villanueva, J. C., Uy, L. Y., Mercado, S. M. Q., Tsuchiya, M. C., Lado, J. P., Angelia, M. R. N., Bercansil, M. C. M. L., Estacio, M. A. C., & Torio, M. A. O. (2021) · Applied Sciences · doi:10.3390/app11125475 · Cited by 51
Dynamics of Keratinocytes in Vivo using 2H2O Labeling: A Sensitive Marker of Epidermal Proliferation State
Hsieh, E. A., Chai, C. M., Lumen, B. O. D., Neese, R. A., & Hellerstein, M. K. (2004) · Journal of Investigative Dermatology · doi:10.1111/j.0022-202x.2004.23303.x · Cited by 52
The Potential Allergenicity of Two 2S Albumins from Soybean (Glycine max): A Protein Microarray Approach
Lin, J., Shewry, P. R., Archer, D. B., Beyer, K., Niggemann, B., Haas, H., Wilson, P. B., & Alcocer, M. J. C. (2006) · International Archives of Allergy and Immunology · doi:10.1159/000094535 · Cited by 50
Lunasin is a novel therapeutic agent for targeting melanoma cancer stem cells
Shidal, C., Al-Rayyan, N., Yaddanapudi, K., & Davis, K. (2016) · Oncotarget · doi:10.18632/oncotarget.11554 · Cited by 48
Lunasin attenuates obesity-related inflammation in RAW264.7 cells and 3T3-L1 adipocytes by inhibiting inflammatory cytokine production
Hsieh, C., Chou, M.-J., & Wang, C.-H. (2017) · PLoS ONE · doi:10.1371/journal.pone.0171969 · Cited by 42
Lunasin as a Promising Plant-Derived Peptide for Cancer Therapy
de Souza, S. M. A., Hernández‐Ledesma, B., & de Souza, T. L. F. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23179548 · Cited by 42
Recombinant production of the therapeutic peptide lunasin
Kyle, S., James, K., & McPherson, M. J. (2012) · Microbial Cell Factories · doi:10.1186/1475-2859-11-28 · Cited by 40
Amaranthus Cruentus Taxonomy, Botanical Description, and Review of its Seed Chemical Composition
Wołosik, K., & Markowska, A. (2019) · Natural Product Communications · doi:10.1177/1934578x19844141 · Cited by 40
Lunasin Attenuates Obesity-Associated Metastasis of 4T1 Breast Cancer Cell through Anti-Inflammatory Property
Hsieh, C., Wang, C.-H., & Huang, Y. (2016) · International Journal of Molecular Sciences · doi:10.3390/ijms17122109 · Cited by 38
High-Yield, In Vitro Protein Expression Using a Continuous-Exchange, Coupled Transcription/Translation System
Martin, G. A., Kawaguchi, R., Lam, Y. H., DeGiovanni, A., Fukushima, M., & Mutter, W. (2001) · BioTechniques · doi:10.2144/01314pf01 · Cited by 37
The expression and processing of two recombinant 2S albumins from soybean (Glycine max) in the yeast Pichia pastoris
Lin, J., Fido, R., Shewry, P. R., Archer, D. B., & Alcocer, M. J. C. (2003) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2003.12.001 · Cited by 36
Lunasin Inhibits Cell Proliferation via Apoptosis and Reduces the Production of Proinflammatory Cytokines in Cultured Rheumatoid Arthritis Synovial Fibroblasts
Jia, S., Zhang, S., Yuan, H., & Chen, N. (2015) · BioMed Research International · doi:10.1155/2015/346839 · Cited by 35
Recombinant expression of bioactive peptide lunasin in Escherichia coli
Liu, C., & Pan, T. (2010) · Applied Microbiology and Biotechnology · doi:10.1007/s00253-010-2754-5 · Cited by 35
Cell proliferation inhibitory and apoptosis-inducing properties of anacardic acid and lunasin in human breast cancer MDA-MB-231 cells
Hsieh, C., Hernández‐Ledesma, B., & de Lumen, B. O. (2010) · Food Chemistry · doi:10.1016/j.foodchem.2010.09.051 · Cited by 34
An updated review of functional properties, debittering methods, and applications of soybean functional peptides
Hu, X., Zhang, Q., Zhang, Q., Ding, J., Liu, Y., & Qin, W. (2022) · Critical Reviews in Food Science and Nutrition · doi:10.1080/10408398.2022.2062587 · Cited by 33
Lunasin Alleviates Allergic Airway Inflammation while Increases Antigen-Specific Tregs
Yang, X., Zhu, J., Tung, C.-Y., Gardiner, G. J., Wang, Q., Chang, H., & Zhou, B. (2015) · PLoS ONE · doi:10.1371/journal.pone.0115330 · Cited by 32
Differential Expression of Thrombospondin (THBS1) in Tumorigenic and Nontumorigenic Prostate Epithelial Cells in Response to a Chromatin-Binding Soy Peptide
Galvez, A. F., Huang, L., Magbanua, M. J., Dawson, K., & Rodriguez, R. L. (2011) · Nutrition and Cancer · doi:10.1080/01635581.2011.539312 · Cited by 32
Self-citation
Chemical biology of Histone acetyltransferase natural compounds modulators
Piaz, F. D., Vassallo, A., Cuesta‐Rubio, O., Castellano, S., Sbardella, G., & Tommasi, N. D. (2010) · Molecular Diversity · doi:10.1007/s11030-010-9299-5 · Cited by 32
Analysis of Lunasin in Commercial and Pilot Plant Produced Soybean Products and an Improved Method of Lunasin Purification
Cavazos, A., Morales, E., Día, V. P., & de Mejía, E. G. (2012) · Journal of Food Science · doi:10.1111/j.1750-3841.2012.02676.x · Cited by 31
Kunitz trypsin inhibitor in addition to Bowman-Birk inhibitor influence stability of lunasin against pepsin-pancreatin hydrolysis
Price, S. J., Pangloli, P., Krishnan, H. B., & Día, V. P. (2016) · Food Research International · doi:10.1016/j.foodres.2016.10.051 · Cited by 29
Seed peptide lunasin ameliorates obesity-induced inflammation and regulates immune responses in C57BL/6J mice fed high-fat diet
Hsieh, C., Wang, Y.-F., Lin, P.-Y., Peng, S., & Chou, M.-J. (2020) · Food and Chemical Toxicology · doi:10.1016/j.fct.2020.111908 · Cited by 28
Lunasin–Aspirin Combination Against NIH/3T3 Cells Transformation Induced by Chemical Carcinogens
Hsieh, C., Hernández‐Ledesma, B., & de Lumen, B. O. (2011) · Plant Foods for Human Nutrition · doi:10.1007/s11130-011-0229-1 · Cited by 28
Commercial processed soy-based food product contains glycated and glycoxidated lunasin proteoforms
Serra, A., Gallart‐Palau, X., See-Toh, R. S.-E., Hemu, X., Tam, J. P., & Sze, S. K. (2016) · Scientific Reports · doi:10.1038/srep26106 · Cited by 28
Health Implications of Bioactive Peptides: A Review
Nourmohammadi, E., & Mahoonak, A. S. (2018) · International Journal for Vitamin and Nutrition Research · doi:10.1024/0300-9831/a000418 · Cited by 28
Lunasin in wheat: A chemical and molecular study on its presence or absence
Dinelli, G., Bregola, V., Bosi, S., Fiori, J., Gotti, R., Simonetti, E., Trozzi, C., Leoncini, E., Prata, C., Massaccesi, L., et al. (2013) · Food Chemistry · doi:10.1016/j.foodchem.2013.11.119 · Cited by 27
Development of the plant-derived peptide lunasin as an anticancer agent
Vuyyuri, S. B., Shidal, C., & Davis, K. (2018) · Current Opinion in Pharmacology · doi:10.1016/j.coph.2018.04.006 · Cited by 27
Lunasin: A Novel Cancer Preventive Seed Peptide
Hernández‐Ledesma, B., & de Lumen, B. O. (2008) · Perspectives in Medicinal Chemistry · doi:10.4137/pmc.s372 · Cited by 27
Activation of dendritic cell function by soypeptide lunasin as a novel vaccine adjuvant
Tung, C.-Y., Lewis, D. E., Han, L., Jaja, M., Yao, S., Li, F., Robertson, M. J., Zhou, B., Sun, J., & Chang, H. (2014) · Vaccine · doi:10.1016/j.vaccine.2014.07.103 · Cited by 26
Soybeans as a Powerhouse of Nutrients and Phytochemicals
Liu, K. (2004) · AOCS Publishing eBooks · doi:10.1201/9781439822203.ch1 · Cited by 23
Bioactive Peptides from Legumes and Their Bioavailability
Indrati, R. (2021) · IntechOpen eBooks · doi:10.5772/intechopen.99979 · Cited by 23
Lunasin in cereal seeds: What is the origin?
Mitchell, R. A. C., Lovegrove, A., & Shewry, P. R. (2013) · Journal of Cereal Science · doi:10.1016/j.jcs.2013.01.013 · Cited by 22
Biologically active components of soybeans and soy protein products: A review
Barać, M., Stanojević, S. P., & Pešić, M. B. (2005) · Acta periodica technologica · doi:10.2298/apt0536155b · Cited by 22
Antioxidant Properties of Protein-Rich Plant Foods in Gastrointestinal Digestion—Peanuts as Our Antioxidant Friend or Foe in Allergies
Prodić, I., Ristivojević, M. K., & Smiljanić, K. (2023) · Antioxidants · doi:10.3390/antiox12040886 · Cited by 21
Beneficial Effects of Bioactive Peptides Derived from Soybean on Human Health and Their Production by Genetic Engineering
Feng, C., & Ming, T. (2011) · InTech eBooks · doi:10.5772/18678 · Cited by 21
Immunological Investigation for the Presence of Lunasin, a Chemopreventive Soybean Peptide, in the Seeds of Diverse Plants
Alaswad, A. A., & Krishnan, H. B. (2016) · Journal of Agricultural and Food Chemistry · doi:10.1021/acs.jafc.6b00445 · Cited by 21
Structural property of soybean lunasin and development of a method to quantify lunasin in plasma using an optimized immunoassay protocol
Día, V. P., Frankland‐Searby, S., del Hierro, F. L., Garcia, G., & de Mejía, E. G. (2012) · Food Chemistry · doi:10.1016/j.foodchem.2012.09.101 · Cited by 20
Overexpression of Soybean-Derived Lunasin in Wheat and Assessment of Its Anti-Proliferative Activity in Colorectal Cancer HT-29 Cells
Fan, X. M., Qin, P., Hao, Y., Guo, H., Blecker, C. S., Everaert, N., & Ren, G. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21249594 · Cited by 20
Lunasin abrogates the expression of matrix metalloproteinases and reduction of type II collagen
Dai, W., Liang, Z., Liu, H., Zhao, G., & Ju, C. (2019) · Artificial Cells Nanomedicine and Biotechnology · doi:10.1080/21691401.2019.1623227 · Cited by 19
Lunasin and Its Epigenetic Impact in Cancer Chemoprevention
Kaufman‐Szymczyk, A., Kaczmarek, W., Fabianowska‐Majewska, K., & Lubecka, K. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24119187 · Cited by 18
Immunomodulatory effects of seed peptide lunasin in RAW264.7 macrophages in obese microenvironments
Huang, P., & Hsieh, C. (2023) · Journal of Functional Foods · doi:10.1016/j.jff.2023.105719 · Cited by 18
Lunasin and Bowman-Birk Protease Inhibitor Concentrations of Protein Extracts from Enzyme-Assisted Aqueous Extraction of Soybeans
de Moura, J. M. L. N., Hernández‐Ledesma, B., de Almeida, N. M., Hsieh, C., de Lumen, B. O., & Johnson, L. A. (2011) · Journal of Agricultural and Food Chemistry · doi:10.1021/jf200183m · Cited by 17
Lunasin is a redox sensitive intrinsically disordered peptide with two transiently populated α-helical regions
Aleksis, R., Jaudzems, K., Muceniece, R., & Liepinsh, E. (2016) · Peptides · doi:10.1016/j.peptides.2016.09.006 · Cited by 17
Peptide nutraceuticals
Girija, A. R. (2017) · Elsevier eBooks · doi:10.1016/b978-0-08-100736-5.00006-5 · Cited by 17
Bioactivity Profiling of Peptides From Food Proteins
Agyei, D., Pan, S., Acquah, C., & Danquah, M. K. (2017) · Elsevier eBooks · doi:10.1016/b978-0-12-811412-4.00003-5 · Cited by 16
An effective and simple procedure to isolate abundant quantities of biologically active chemopreventive Lunasin Protease Inhibitor Concentrate (LPIC) from soybean
Krishnan, H. B., & Wang, T. T. Y. (2015) · Food Chemistry · doi:10.1016/j.foodchem.2015.01.006 · Cited by 16
Understanding Lunasin’s biology and potential as a cancer therapeutic by utilizing Drosophila genetics
Jones, G. E., & Srivastava, A. K. (2014) · Experimental Biology and Medicine · doi:10.1177/1535370214522180 · Cited by 15
Lunasin abrogates monocytes to endothelial cells
Zhu, Y., Li, H., & Wang, X. (2017) · Molecular Immunology · doi:10.1016/j.molimm.2017.09.004 · Cited by 15
Potential of Lunasin Orally-Administered in Comparison to Intraperitoneal Injection to Inhibit Colon Cancer Metastasis in Vivo
Día, V. P., & de Mejía, E. G. (2013) · Journal of Cancer Therapy · doi:10.4236/jct.2013.46a2005 · Cited by 15
Lunasin peptide promotes lysosome-mitochondrial mediated apoptosis and mitotic termination in MDA-MB-231 cells
Hao, Y., Guo, H., Hong, Y., Fan, X. M., Su, Y., Yang, X., & Ren, G. (2022) · Food Science and Human Wellness · doi:10.1016/j.fshw.2022.06.018 · Cited by 14
The Effect of Soybean Lunasin on Cardiometabolic Risk Factors: A Randomized Clinical Trial
Tabrizi, S. H., Haddad, E. H., Rajaram, S., Oda, K., Kaur, A., & Sabaté, J. (2019) · Journal of Dietary Supplements · doi:10.1080/19390211.2019.1577937 · Cited by 14
Aureobasidium pullulans produced β-glucan is effective to enhance Kurosengoku soybean extract induced Thrombospondin-1 expression
Muramatsu, D., Okabe, M., Takaoka, A., Kida, H., & Iwai, A. (2017) · Scientific Reports · doi:10.1038/s41598-017-03053-9 · Cited by 14
Up to 92 % increase of cancer-preventing lunasin in organic spring barley
Legzdiņa, L., Nakurte, I., Kirhnere, I., Namniece, J., Krigere, L., Saleniece, K., Beinaroviča, I., & Muceniece, R. (2014) · Agronomy for Sustainable Development · doi:10.1007/s13593-013-0203-4 · Cited by 13
Physicochemical and structural properties of lunasin revealed by spectroscopic, chromatographic and molecular dynamics approaches
de Souza, S. M. A., Fernandes, T. V. A., Kalume, D. E., Lima, L. M. T. R., Pascutti, P. G., & de Souza, T. L. F. (2020) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2020.140440 · Cited by 12
1997-2012: Fifteen Years of Research on Peptide Lunasin
Hernández‐Ledesma, B., de Lumen, B. O., & Hsieh, C. (2013) · InTech eBooks · doi:10.5772/52368 · Cited by 12
Reduced mammary tumor progression in a transgenic mouse model fed an isoflavone‐poor soy protein concentrate
Chiesa, G., Rigamonti, E., Lovati, M. R., Disconzi, E., Soldati, S., Sacco, M. G., Catò, E. M., Patton, V., Scanziani, E., Vezzoni, P., et al. (2008) · Molecular Nutrition & Food Research · doi:10.1002/mnfr.200700296 · Cited by 12
LEGUMES | Dietary Importance
Lam, Y. H., & Lumen, B. O. D. (2003) · Elsevier eBooks · doi:10.1016/b0-12-227055-x/00694-5 · Cited by 11

Authors: Galvez, A. F., & de Lumen, B. O.
Affiliations: University of California, Berkeley (US)
Venue: Nature Biotechnology
Publisher: Springer Science and Business Media LLC
Published: 1999-05
Volume: 17
Issue: 5
Pages: 495-500
ISSN: 0733-222X (ISSN-L)
1087-0156
1546-1696
DOI: 10.1038/8676
OpenAlex: W1572828491
Cited by: 174
References: 31
Citations by year: 2026: 4 · 2025: 7 · 2024: 6 · 2023: 5 · 2022: 8 · 2021: 7 · 2020: 9 · 2019: 8 · 2018: 7 · 2017: 11 · 2016: 9 · 2015: 8 · 2014: 8 · 2013: 14 · 2012: 6
FWCI: 0.82
Type: journal article
Language: en
Open access: closed
Licence: www.springer.com/tdm (tdm)
Locations: Nature Biotechnology (publishedVersion)
PubMed (publishedVersion)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Microtubule and mitosis dynamics
Life Sciences › Agricultural and Biological Sciences › Plant Science › Plant Molecular Biology Research
Health Sciences › Medicine › Oncology › Cancer-related Molecular Pathways
Keywords: lunasin, 2S albumin, soybean, mitosis inhibition, antimitotic activity, centromere, chromosomal fragmentation, seed development
MeSH terms: Animals, Cell Division, Cell Line, Chromatin, Flow Cytometry, Humans, Mitosis, Peptides, Plant Proteins, Glycine max, Transfection, DNA, Complementary, Kinetochores, Fluorescent Antibody Technique, Indirect, Soybean Proteins, Mice, DNA Fragmentation

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

Data sources

Bibliographic data: Semantic Scholar, OpenAlex, Crossref.

Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.

A soybean cDNA encoding a chromatin-binding peptide inhibits mitosis of mammalian cells.

Abstract

Overview

Integrity signals

Verification

Claims the paper makes

Claims other papers make about this one

Citations

Cites

Cited by

Related

Metadata

Record

About these checks

Data sources