The DOI matches its Crossref record; 3 of the 3 references it cites were found in a registry or an index.
Proteasome Activation by Small Molecules
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?
The cited source says what the claim attributes to it.
In the citing paper
“Using a proteasome activity binding probe (Berkers et al., 2007, Leestemaker et al., 2017), we found that CE reduction through either statins or efavirenz increased total cellular proteasome activity in both APPdp and NDC neurons (Figures 5F–5I).”
From Cholesterol Metabolism Is a Druggable Axis that Independently Regulates Tau and Amyloid-β in iPSC-Derived Alzheimer’s Disease Neurons (2019) · cites this paper as Leestemaker et al., 2017
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
Phthalimide conjugation as a strategy for in vivo target protein degradation
Winter, G. E., Buckley, D. L., Paulk, J., Roberts, J. M., Souza, A., Dhe-Paganon, S., & Bradner, J. E. (2015) · Science · doi:10.1126/science.aab1433 · Cited by 1,760
The roles of intracellular protein-degradation pathways in neurodegeneration
Rubinsztein, D. C. (2006) · Nature · doi:10.1038/nature05291 · Cited by 1,625
Regulation of the proteasome by neuronal activity and calcium/calmodulin-dependent protein kinase II
Djakovic, S. N., Schwarz, L. A., Barylko, B., DeMartino, G. N., & Patrick, G. N. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.021956 · Cited by 236 · cited 4×
“…through direct phosphorylation of the 19S RP, including ASK1 (Um et al., 2010), p38 MAPK (Lee et al., 2010b), the calcium/calmodulin-dependent protein kinase II (CaMKII) (Djakovic et al., 2009), PKA (Asai et al., 2009; Lokireddy et al., 2015; Zhang et al., 2007), and DYRK2 (Guo et al., 2015).”
BackgroundInfluential
Research works printed but not linked: 50
- Abelin, 2016, Reduced-representation phosphosignatures measured by quantitative targeted MS capture cellular states and enable large-scale comparison of drug-induced phenotypes, Mol. Cell Proteomics, 15, 1622, 10.1074/mcp.M116.058354 · DOI
- Al-Ramahi, 2006, CHIP protects from the neurotoxicity of expanded and wild-type ataxin-1 and promotes their ubiquitination and degradation, J. Biol. Chem., 281, 26714, 10.1074/jbc.M601603200 · DOI
- Anderson, 2007, Pyrrolopyridine inhibitors of mitogen-activated protein kinase-activated protein kinase 2 (MK-2), J. Med. Chem., 50, 2647, 10.1021/jm0611004 · DOI
- Asai, 2009, PKA rapidly enhances proteasome assembly and activity in in vivo canine hearts, J. Mol. Cell Cardiol., 46, 452, 10.1016/j.yjmcc.2008.11.001 · DOI
- Atzori, 2001, Activation of the JNK/p38 pathway occurs in diseases characterized by tau protein pathology and is related to tau phosphorylation but not to apoptosis, J. Neuropathol. Exp. Neurol., 60, 1190, 10.1093/jnen/60.12.1190 · DOI
- Avitzour, 2007, Intrinsically active variants of all human p38 isoforms, FEBS J., 274, 963, 10.1111/j.1742-4658.2007.05644.x · DOI
- Bendotti, 2004, Activated p38MAPK is a novel component of the intracellular inclusions found in human amyotrophic lateral sclerosis and mutant SOD1 transgenic mice, J. Neuropathol. Exp. Neurol., 63, 113, 10.1093/jnen/63.2.113 · DOI
- Benjamini, 1995, Controlling the false discovery rate: a practical and powerful approach to multiple testing, J. R. Stat. Soc. Ser. B (Methodological), 57, 289, 10.1111/j.2517-6161.1995.tb02031.x · DOI · Paper page
- Berkers, 2005, Activity probe for in vivo profiling of the specificity of proteasome inhibitor bortezomib, Nat. Methods, 2, 357, 10.1038/nmeth759 · DOI
- Berkers, 2007, Profiling proteasome activity in tissue with fluorescent probes, Mol. Pharm., 4, 739, 10.1021/mp0700256 · DOI · Paper page
- Borst, 2013, Skepinone-L, a novel potent and highly selective inhibitor of p38 MAP kinase, effectively impairs platelet activation and thrombus formation, Cell Physiol. Biochem., 31, 914, 10.1159/000350110 · DOI
- Dahlmann, 2000, Different proteasome subtypes in a single tissue exhibit different enzymatic properties, J. Mol. Biol., 303, 643, 10.1006/jmbi.2000.4185 · DOI
- Dantuma, 2014, The ubiquitin-proteasome system in neurodegenerative diseases: precipitating factor, yet part of the solution, Front. Mol. Neurosci., 7, 70, 10.3389/fnmol.2014.00070 · DOI
- Dantuma, 2000, Short-lived green fluorescent proteins for quantifying ubiquitin/proteasome-dependent proteolysis in living cells, Nat. Biotechnol., 18, 538, 10.1038/75406 · DOI · Paper page
- de Jong, 2012, Fluorescence-based proteasome activity profiling, Methods Mol. Biol., 803, 183, 10.1007/978-1-61779-364-6_13 · DOI
- de Wit, 2009, Matrix-dependent local retention of secretory vesicle cargo in cortical neurons, J. Neurosci., 29, 23, 10.1523/JNEUROSCI.3931-08.2009 · DOI
- Ebrahimi-Fakhari, 2011, Distinct roles in vivo for the ubiquitin-proteasome system and the autophagy-lysosomal pathway in the degradation of α-synuclein, J. Neurosci., 31, 14508, 10.1523/JNEUROSCI.1560-11.2011 · DOI
- Glickman, 2002, The ubiquitin-proteasome proteolytic pathway: destruction for the sake of construction, Physiol. Rev., 82, 373, 10.1152/physrev.00027.2001 · DOI
- Guo, 2015, Site-specific proteasome phosphorylation controls cell proliferation and tumorigenesis, Nat. Cell Biol., 18, 202, 10.1038/ncb3289 · DOI · Paper page
- Heubner, 2011, The prognostic impact of circulating proteasome concentrations in patients with epithelial ovarian cancer, Gynecol. Oncol., 120, 233, 10.1016/j.ygyno.2010.10.014 · DOI
- Hideshima, 2001, The proteasome inhibitor PS-341 inhibits growth, induces apoptosis, and overcomes drug resistance in human multiple myeloma cells, Cancer Res., 61, 3071
- Kim, 2010, Pathological roles of MAPK signaling pathways in human diseases, Biochim. Biophys. Acta, 1802, 396, 10.1016/j.bbadis.2009.12.009 · DOI · Paper page
- Kniepert, 2014, The unique functions of tissue-specific proteasomes, Trends Biochem. Sci., 39, 17, 10.1016/j.tibs.2013.10.004 · DOI
- Koeberle, 2012, Skepinone-L is a selective p38 mitogen-activated protein kinase inhibitor, Nat. Chem. Biol., 8, 141, 10.1038/nchembio.761 · DOI
- Köhler, 2001, The axial channel of the proteasome core particle is gated by the Rpt2 ATPase and controls both substrate entry and product release, Mol. Cell, 7, 1143, 10.1016/S1097-2765(01)00274-X · DOI
- Kristiansen, 2007, Disease-associated prion protein oligomers inhibit the 26S proteasome, Mol. Cell, 26, 175, 10.1016/j.molcel.2007.04.001 · DOI
- Lee, 2009, The role of ubiquitin linkages on alpha-synuclein induced-toxicity in a Drosophila model of Parkinson's disease, J. Neurochem., 110, 208, 10.1111/j.1471-4159.2009.06124.x · DOI
- Lee, 2010, Enhancement of proteasome activity by a small-molecule inhibitor of USP14, Nature, 467, 179, 10.1038/nature09299 · DOI · Paper page
- Lee, 2010, Osmotic stress inhibits proteasome by p38 MAPK-dependent phosphorylation, J. Biol. Chem., 285, 41280, 10.1074/jbc.M110.182188 · DOI
- Li, 2004, Stabilization of alpha-synuclein protein with aging and familial Parkinson's disease-linked A53T mutation, J. Neurosci., 24, 7400, 10.1523/JNEUROSCI.1370-04.2004 · DOI
- Li, 2009, Variably modulated gating of the 26S proteasome by ATP and polyubiquitin, Biochem. J., 421, 397, 10.1042/BJ20090528 · DOI
- Lin, 2013, Regulation of feedback between protein kinase A and the proteasome system worsens Huntington's disease, Mol. Cell Biol., 33, 1073, 10.1128/MCB.01434-12 · DOI · Paper page
- Liu, 2014, Sulforaphane enhances proteasomal and autophagic activities in mice and is a potential therapeutic reagent for Huntington's disease, J. Neurochem., 129, 539, 10.1111/jnc.12647 · DOI
- Lokireddy, 2015, cAMP-induced phosphorylation of 26S proteasomes on Rpn6/PSMD11 enhances their activity and the degradation of misfolded proteins, Proc. Natl. Acad. Sci. USA, 112, E7176, 10.1073/pnas.1522332112 · DOI · Paper page
- Myeku, 2016, Tau-driven 26S proteasome impairment and cognitive dysfunction can be prevented early in disease by activating cAMP-PKA signaling, Nat. Med., 22, 46, 10.1038/nm.4011 · DOI · Paper page
- Outeiro, 2008, Formation of toxic oligomeric alpha-synuclein species in living cells, PLoS One, 3, e1867, 10.1371/journal.pone.0001867 · DOI
- Pelletier, 2010, Quantifying cross-tissue diversity in proteasome complexes by mass spectrometry, Mol. Biosyst., 6, 1450, 10.1039/c004989a · DOI
- Perrotton, 2007, (R)- and (S)-verapamil differentially modulate the multidrug-resistant protein MRP1, J. Biol. Chem., 282, 31542, 10.1074/jbc.M703964200 · DOI
- Peth, 2009, Ubiquitinated proteins activate the proteasome by binding to Usp14/Ubp6, which causes 20S gate opening, Mol. Cell, 36, 794, 10.1016/j.molcel.2009.11.015 · DOI
- Ross, 2000, Systematic variation in gene expression patterns in human cancer cell lines, Nat. Genet., 24, 227, 10.1038/73432 · DOI · Paper page
- Sakamoto, 2001, Protacs: chimeric molecules that target proteins to the Skp1-Cullin-F box complex for ubiquitination and degradation, Proc. Natl. Acad. Sci. USA, 98, 8554, 10.1073/pnas.141230798 · DOI · Paper page
- Snyder, 2003, Aggregated and monomeric alpha-synuclein bind to the S6' proteasomal protein and inhibit proteasomal function, J. Biol. Chem., 278, 11753, 10.1074/jbc.M208641200 · DOI
- Tortarolo, 2003, Persistent activation of p38 mitogen-activated protein kinase in a mouse model of familial amyotrophic lateral sclerosis correlates with disease progression, Mol. Cell Neurosci., 23, 180, 10.1016/S1044-7431(03)00022-8 · DOI
- Tsai, 2003, Parkin facilitates the elimination of expanded polyglutamine proteins and leads to preservation of proteasome function, J. Biol. Chem., 278, 22044, 10.1074/jbc.M212235200 · DOI
- Tyanova, 2016, The Perseus computational platform for comprehensive analysis of (prote)omics data, Nat. Methods, 13, 731, 10.1038/nmeth.3901 · DOI · Paper page
- Um, 2010, ASK1 negatively regulates the 26 S proteasome, J. Biol. Chem., 285, 36434, 10.1074/jbc.M110.133777 · DOI
- Wang, 2007, Mass spectrometric characterization of the affinity-purified human 26S proteasome complex, Biochemistry, 46, 3553, 10.1021/bi061994u · DOI · Paper page
- Zhang, 2007, Proteasome function is regulated by cyclic AMP-dependent protein kinase through phosphorylation of Rpt6, J. Biol. Chem., 282, 22460, 10.1074/jbc.M702439200 · DOI
- Zhou, 2013, Robust phosphoproteome enrichment using monodisperse microsphere-based immobilized titanium (IV) ion affinity chromatography, Nat. Protoc., 8, 461, 10.1038/nprot.2013.010 · DOI
- Zhu, 2000, Activation of p38 kinase links tau phosphorylation, oxidative stress, and cell cycle-related events in Alzheimer disease, J. Neuropathol. Exp. Neurol., 59, 880, 10.1093/jnen/59.10.880 · DOI · Paper page
Cited by
Sorted by citations
Kinase inhibitors: the road ahead
Ferguson, F. M., & Gray, N. S. (2018) · Nature Reviews Drug Discovery · doi:10.1038/nrd.2018.21 · Cited by 1,009
van der Kant, R., Langness, V. F., Herrera, C. M., Williams, D. A., Fong, L. K., Leestemaker, Y., Steenvoorden, E., Rynearson, K. D., Brouwers, J. F., Helms, J. B., et al. (2019) · Cell Stem Cell · doi:10.1016/j.stem.2018.12.013 · Cited by 350
Self-citationDegradation of proteins by PROTACs and other strategies
Wang, Y., Jiang, X., Feng, F., Liu, W., & Sun, H. (2020) · Acta Pharmaceutica Sinica B · doi:10.1016/j.apsb.2019.08.001 · Cited by 335
Targeting aging mechanisms: pharmacological perspectives
Moskalev, A., Guvatova, Z., Lopes, I. D. A., Beckett, C. W., Kennedy, B. K., De Magalhaes, J. P., & Makarov, A. A. (2022) · Trends in Endocrinology & Metabolism · doi:10.1016/j.tem.2022.01.007 · Cited by 164
The Proteasome in Modern Drug Discovery: Second Life of a Highly Valuable Drug Target
Cromm, P. M., & Crews, C. M. (2017) · ACS Central Science · doi:10.1021/acscentsci.7b00252 · Cited by 136
Salemi, M., Mogavero, M. P., Lanza, G., Mongioì, L. M., Calogero, A. E., & Ferri, R. (2022) · Cells · doi:10.3390/cells11121930 · Cited by 39
Unifying Catalysis Framework to Dissect Proteasomal Degradation Paradigms
Rodriguez-Rivera, F. P., & Levi, S. M. (2021) · ACS Central Science · doi:10.1021/acscentsci.1c00389 · Cited by 30
Cuinat, S., Bézieau, S., Deb, W., Mercier, S., Vignard, V., Isidor, B., Küry, S., & Ebstein, F. (2024) · Genes & Diseases · doi:10.1016/j.gendis.2023.101130 · Cited by 10
Metadata
- Authors
- Leestemaker, Y., de Jong, A., Witting, K. F., Penning, R., Schuurman, K., Rodenko, B., Zaal, E. A., van de Kooij, B., Laufer, S., Heck, A. J. R., Borst, J., Scheper, W., Berkers, C. R., & Ovaa, H.
- Venue
- Cell Chemical Biology
- Publisher
- Elsevier BV
- Published
- 2017-06
- Volume
- 24
- Issue
- 6
- Pages
- 725-736.e7
- ISSN
- 2451-9456
- Cited by
- 144
- References
- 3
- Language
- en
- Licence
- Funders
- Netherlands Organisation for Scientific Research (724.013.002, 722.013.009, 184.032.201)
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