The DOI matches its Crossref record; 23 of the 23 references it cites were found in a registry or an index.
Ginkgolic Acid Inhibits Protein SUMOylation by Blocking Formation of the E1-SUMO Intermediate
Open accessAbstract
Protein modification by small ubiquitin-related modifier proteins (SUMOs) controls diverse cellular functions. Dysregulation of SUMOylation or deSUMOylation processes has been implicated in the development of cancer and neurodegenerative diseases. However, no small-molecule inhibiting protein SUMOylation has been reported so far. Here, we report inhibition of SUMOylation by ginkgolic acid and its analog, anacardic acid. Ginkgolic acid and anacardic acid inhibit protein SUMOylation both in vitro and in vivo without affecting in vivo ubiquitination. Binding assays with a fluorescently labeled probe showed that ginkgolic acid directly binds E1 and inhibits the formation of the E1-SUMO intermediate. These studies will provide not only a useful tool for investigating the roles of SUMO conjugations in a variety of pathways in cells, but also a basis for the development of drugs targeted against diseases involving aberrant SUMOylation.
Overview
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
Cites
Statistics
Verification
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?
In the citing paper
“Furthermore, the use of anacardic acid, an inhibitor of protein SUMOylation, 16 abrogated pksC E. coliinduced senescence (unpublished data).”
From The bacterial genotoxin colibactin promotes colon tumor growth by modifying the tumor microenvironment (2014) · cites this paper as [16]
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
Mechanisms Underlying Ubiquitination
Pickart, C. M. (2001) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.70.1.503 · Cited by 3,184
Johnson, E. S. (2004) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.73.011303.074118 · Cited by 1,711
Lysine Acetylation: Codified Crosstalk with Other Posttranslational Modifications
Yang, X.-J., & Seto, E. (2008) · Molecular Cell · doi:10.1016/j.molcel.2008.07.002 · Cited by 1,006
SUMO‐1 modification activates the transcriptional response of p53
Rodríguez, M. S., Desterro, J. M. P., Laı́n, S., Midgley, C., Lane, D. P., & Hay, R. T. (1999) · The EMBO Journal · doi:10.1093/emboj/18.22.6455 · Cited by 639
p300/CBP‐mediated p53 acetylation is commonly induced by p53‐activating agents and inhibited by MDM2
Ito, A., Lai, C.-H., Zhao, X., Saito, S., Hamilton, M. H., Appella, E., & Yao, T. (2001) · The EMBO Journal · doi:10.1093/emboj/20.6.1331 · Cited by 597
Self-citationSmall Molecule Modulators of Histone Acetyltransferase p300
Balasubramanyam, K., Swaminathan, V., Ranganathan, A., & Kundu, T. K. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m301580200 · Cited by 518
Activation of p53 by conjugation to the ubiquitin‐like protein SUMO‐1
Gostissa, M., Hengstermann, A., Fogal, V., Sandy, P., Schwarz, S. E., Scheffner, M., & Sal, G. D. (1999) · The EMBO Journal · doi:10.1093/emboj/18.22.6462 · Cited by 512
Inhibitors of Ubiquitin-Activating Enzyme (E1), a New Class of Potential Cancer Therapeutics
Yang, Y., Kitagaki, J., Dai, R., Tsai, Y. C., Lorick, K. L., Ludwig, R. L., Pierre, S. A., Jensen, J. P., Davydov, I. V., Oberoi, P., et al. (2007) · Cancer Research · doi:10.1158/0008-5472.can-07-0568 · Cited by 442
Regulation of SUMOylation by Reversible Oxidation of SUMO Conjugating Enzymes
Bossis, G., & Melchior, F. (2006) · Molecular Cell · doi:10.1016/j.molcel.2005.12.019 · Cited by 406
The emerging field of dynamic lysine methylation of non-histone proteins
Huang, J. L., & Berger, S. L. (2008) · Current Opinion in Genetics & Development · doi:10.1016/j.gde.2008.01.012 · Cited by 296
Sung, B., Pandey, M. K., Ahn, K. S., Yi, T., Chaturvedi, M. M., Liu, M., & Aggarwal, B. B. (2008) · Blood · doi:10.1182/blood-2007-10-117994 · Cited by 265
SUMO on the road to neurodegeneration
Dorval, V., & Fraser, P. E. (2007) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2007.03.017 · Cited by 188
Mabb, A. M., & Miyamoto, S. (2007) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-007-7005-2 · Cited by 101
Ginkgolic acids induce neuronal death and activate protein phosphatase type-2C
Ahlemeyer, B., Selke, D., Schaper, C., Klumpp, S., & Krieglstein, J. (2001) · European Journal of Pharmacology · doi:10.1016/s0014-2999(01)01237-7 · Cited by 101
Tsukamoto, S., Hirota, H., Imachi, M., Fujimuro, M., Onuki, H., Ohta, T., & Yokosawa, H. (2004) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2004.10.012 · Cited by 101
Panepophenanthrin, from a Mushroom Strain, a Novel Inhibitor of the Ubiquitin-Activating Enzyme
Sekizawa, R., Ikeno, S., Nakamura, H., NAGANAWA, H., Matsui, S., IINUMA, H., & TAKEUCHI, T. (2002) · Journal of Natural Products · doi:10.1021/np020098q · Cited by 97
Inhibition of lipoxygenase and prostaglandin endoperoxide synthase by anacardic acids
Grazzini, R., Hesk, D., Heininger, E. E., Hildenbrandt, G. R., Reddy, C. C., Cox-Foster, D., Medford, J. I., Craig, R., & Mumma, R. O. (1991) · Biochemical and Biophysical Research Communications · doi:10.1016/s0006-291x(05)80252-9 · Cited by 72
In situ SUMOylation analysis reveals a modulatory role of RanBP2 in the nuclear rim and PML bodies
Saitoh, N., Uchimura, Y., Tachibana, T., Sugahara, S., Saitoh, H., & Nakao, M. (2006) · Experimental Cell Research · doi:10.1016/j.yexcr.2006.01.013 · Cited by 66
Self-citationUchimura, Y., Nakao, M., & Saitoh, H. (2004) · FEBS Letters · doi:10.1016/s0014-5793(04)00321-7 · Cited by 59
Self-citationSUMO in Cancer - Wrestlers Wanted
Alarcon-Vargas, D., & Ronai, Z. A. (2002) · Cancer Biology & Therapy · doi:10.4161/cbt.74 · Cited by 55
Cytotoxic activity of Ozoroa insignis from Zimbabwe
Rea, A. I. (2003) · Fitoterapia · doi:10.1016/j.fitote.2003.08.007 · Cited by 52
Kishore, A. H., Vedamurthy, B. M., Mantelingu, K., Agrawal, S., Reddy, B. A., Roy, S., Rangappa, K. S., & Kundu, T. K. (2008) · Journal of Medicinal Chemistry · doi:10.1021/jm700954w · Cited by 48
Rouleau, N., Wang, J., Karras, L., Andrews, E., Bielefeld-Sévigny, M., & Chen, Y. (2007) · Analytical Biochemistry · doi:10.1016/j.ab.2007.11.024 · Cited by 14
Flagged first, then by citations
Cited by
Sorted by citations
Sumoylated hnRNPA2B1 controls the sorting of miRNAs into exosomes through binding to specific motifs
Villarroya-Beltri, C., Gutiérrez-Vázquez, C., Sánchez-Cabo, F., Pérez-Hernández, D., Vázquez, J., Martin-Cofreces, N., Martinez-Herrera, D. J., Pascual-Montano, A., Mittelbrunn, M., & Sánchez-Madrid, F. (2013) · Nature Communications · doi:10.1038/ncomms3980 · Cited by 1,971
The SUMO pathway: emerging mechanisms that shape specificity, conjugation and recognition
Gareau, J. R., & Lima, C. D. (2010) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3011 · Cited by 1,145
Bertrand, S., Bohni, N., Schnée, S., Schumpp, O., Gindro, K., & Wolfender, J. (2014) · Biotechnology Advances · doi:10.1016/j.biotechadv.2014.03.001 · Cited by 514
SUMO and the robustness of cancer
Seeler, J.-S., & Dejean, A. (2017) · Nature reviews. Cancer · doi:10.1038/nrc.2016.143 · Cited by 443
Signalling mechanisms and cellular functions of SUMO
Vertegaal, A. C. O. (2022) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-022-00500-y · Cited by 394
Metadata
- Authors
- Fukuda, I., Ito, A., Hirai, G., Nishimura, S., Kawasaki, H., Saitoh, H., Kimura, K.-I., Sodeoka, M., & Yoshida, M.
- Affiliations
- RIKEN Advanced Science Institute (JP)
- Japan Science and Technology Agency (JP)
- RIKEN (JP)
- Tokyo Denki University (JP)
- Institute of Molecular Embryology and Genetics, Kumamoto University (JP)
- Iwate University (JP)
- Corresponding author
- Ito, Akihiro
- ORCID
- Venue
- Chemistry & Biology
- Publisher
- Elsevier BV
- Published
- 2009-02
- Volume
- 16
- Issue
- 2
- Pages
- 133-140
- ISSN
- 1074-5521 (ISSN-L)
- OpenAlex
- W1978693761
- Cited by
- 355
- References
- 23
- Citations by year
- 2026: 14 · 2025: 23 · 2024: 25 · 2023: 23 · 2022: 21 · 2021: 27 · 2020: 28 · 2019: 27 · 2018: 31 · 2017: 30 · 2016: 23 · 2015: 20 · 2014: 31 · 2013: 9 · 2012: 6
- FWCI
- 3.08
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Chemistry & Biology (publishedVersion)
- PubMed (publishedVersion)
- Institutional Repositories DataBase (IRDB) (submittedVersion)
- Sakura: Saitama United Cyber Repository of Academic Resources (Saitama University) (submittedVersion)
- Funders
- Core Research for Evolutional Science and Technology
- Advanced Science Institute
- Japan Science and Technology Corporation
- Ministry of Education, Culture, Sports, Science and Technology
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ubiquitin and proteasome pathways
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Degradation and Inhibitors
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Cancer-related gene regulation
- Keywords
- ginkgolic acid, anacardic acid, protein sumoylation, SUMOylation inhibition, small molecule inhibitors, SUMO conjugation, ubiquitination, drug development
- MeSH terms
- Plant Extracts, Protein Binding, Salicylates, Structure-Activity Relationship, Plant Leaves, Ginkgo biloba, Small Ubiquitin-Related Modifier Proteins, Anacardic Acids, Small Molecule Libraries, Ubiquitination
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
