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The DOI matches its Crossref record; 5 of the 5 references it cites were found in a registry or an index.

Direct cellular delivery of human proteasomes to delay tau aggregation

Han, Dong Hoon, Na, Hee-Kyung, Choi, Won Hoon, Lee, Jung Hoon, Kim, Yun Kyung, Won, Cheolhee, Lee, Seung-Han, Kim, Kwang Pyo, Kuret, Jeff, Min, Dal-Hee, Lee, Min Jae·2014·Nature Communications
DOI 10.1038/ncomms6633
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Research works printed but not linked: 26

  1. Finley, D. Recognition and processing of ubiquitin-protein conjugates by the proteasome. Annu. Rev. Biochem. 78, 477–513 (2009). · DOI · Paper page
  2. Tai, H. C. & Schuman, E. M. Ubiquitin, the proteasome and protein degradation in neuronal function and dysfunction. Nat. Rev. Neurosci. 9, 826–838 (2008). · DOI · Paper page
  3. Finley, D., Ciechanover, A. & Varshavsky, A. Ubiquitin as a central cellular regulator. Cell 116, S29–S32 (2004). · DOI
  4. Glickman, M. H. & Ciechanover, A. The ubiquitin-proteasome proteolytic pathway: destruction for the sake of construction. Physiol. Rev. 82, 373–428 (2002). · DOI
  5. Ravid, T. & Hochstrasser, M. Diversity of degradation signals in the ubiquitin-proteasome system. Nat. Rev. Mol. Cell Biol. 9, 679–690 (2008). · DOI
  6. Lee, M. J., Lee, J. H. & Rubinsztein, D. C. Tau degradation: the ubiquitin-proteasome system versus the autophagy-lysosome system. Prog. Neurobiol. 105, 49–59 (2013). · DOI · Paper page
  7. Lee, B. H. et al. Enhancement of proteasome activity by a small-molecule inhibitor of Usp14. Nature 467, 179–184 (2010). · DOI · Paper page
  8. Kruegel, U. et al. Elevated proteasome capacity extends replicative lifespan in Saccharomyces cerevisiae. PLoS Genet. 7, e1002253 (2011). · DOI · Paper page
  9. Na, H. K. et al. Efficient functional delivery of siRNA using mesoporous silica nanoparticles with ultralarge pores. Small 8, 1752–1761 (2012). · DOI
  10. Kim, M. H. et al. Facile synthesis of monodispersed mesoporous silica nanoparticles with ultralarge pores and their application in gene delivery. ACS Nano 5, 3568–3576 (2011). · DOI
  11. Guerrero, C., Tagwerker, C., Kaiser, P. & Huang, L. An integrated mass spectrometry-based proteomic approach: quantitative analysis of tandem affinity-purified in vivo cross-linked protein complexes (QTAX) to decipher the 26S proteasome-interacting network. Mol. Cell. Proteomics 5, 366–378 (2006). · DOI
  12. Lee, M. J., Lee, B. H., Hanna, J., King, R. W. & Finley, D. Trimming of ubiquitin chains by proteasome-associated deubiquitinating enzymes. Mol. Cell. Proteomics. 10, R110.003871 (2011). · DOI
  13. Saeki, Y., Isono, E. & Toh, E. A. Preparation of ubiquitinated substrates by the PY motif-insertion method for monitoring 26S proteasome activity. Methods Enzymol. 399, 215–227 (2005). · DOI
  14. Kwak, M. K., Wakabayashi, N., Greenlaw, J. L., Yamamoto, M. & Kensler, T. W. Antioxidants enhance mammalian proteasome expression through the Keap1-Nrf2 signaling pathway. Mol. Cell Biol. 23, 8786–8794 (2003). · DOI
  15. Rejman, J., Oberle, V., Zuhorn, I. S. & Hoekstra, D. Size-dependent internalization of particles via the pathways of clathrin- and caveolae-mediated endocytosis. Biochem. J. 377, 159–169 (2004). · DOI
  16. Bandyopadhyay, B., Li, G., Yin, H. & Kuret, J. Tau aggregation and toxicity in a cell culture model of tauopathy. J. Biol. Chem. 282, 16454–16464 (2007). · DOI
  17. Bhutani, N., Venkatraman, P. & Goldberg, A. L. Puromycin-sensitive aminopeptidase is the major peptidase responsible for digesting polyglutamine sequences released by proteasomes during protein degradation. EMBO J. 26, 1385–1396 (2007). · DOI
  18. Tak, H. et al. Bimolecular fluorescence complementation; lighting-up tau-tau interaction in living cells. PLoS ONE 8, e81682 (2013). · DOI
  19. Re, F., Gregori, M. & Masserini, M. Nanotechnology for neurodegenerative disorders. Maturitas 73, 45–51 (2012). · DOI
  20. Balch, W. E., Morimoto, R. I., Dillin, A. & Kelly, J. W. Adapting proteostasis for disease intervention. Science 319, 916–919 (2008). · DOI · Paper page
  21. Stefani, M. & Dobson, C. M. Protein aggregation and aggregate toxicity: new insights into protein folding, misfolding diseases and biological evolution. J. Mol. Med. 81, 678–699 (2003). · DOI
  22. Pang, S. C. et al. Photoswitchable fluorescent diarylethene in a turn-on mode for live cell imaging. Chem. Commun. 48, 3745–3747 (2012). · DOI
  23. Elsasser, S., Schmidt, M. & Finley, D. Characterization of the proteasome using native gel electrophoresis. Methods Enzymol. 398, 353–363 (2005). · DOI
  24. Zhang, X. et al. The proteasome: a target of oxidative damage in cultured human retina pigment epithelial cells. Invest. Ophthalmol. Vis. Sci. 49, 3622–3630 (2008). · DOI
  25. Bence, N. F., Bennett, E. J. & Kopito, R. R. Application and analysis of the GFPu family of ubiquitin-proteasome system reporters. Methods Enzymol. 399, 481–490 (2005). · DOI
  26. Hoyt, M. A., Zhang, M. & Coffino, P. Probing the ubiquitin/proteasome system with ornithine decarboxylase, a ubiquitin-independent substrate. Methods Enzymol. 398, 399–413 (2005). · DOI

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Metadata

Authors
Han, D. H., Na, H.-K., Choi, W. H., Lee, J. H., Kim, Y. K., Won, C., Lee, S.-H., Kim, K. P., Kuret, J., Min, D.-H., & Lee, M. J.
Venue
Nature Communications
Publisher
Springer Science and Business Media LLC
Published
2014-12-05
Volume
5
Issue
1
ISSN
2041-1723
DOI
10.1038/ncomms6633
Cited by
88
References
5
Language
en
Licence

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CoChat. (2026). Citation check: Direct cellular delivery of human proteasomes to delay tau aggregation. https://app.cochat.ai/papers/10.1038/ncomms6633
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Han, D. H., Na, H.-K., Choi, W. H., Lee, J. H., Kim, Y. K., Won, C., Lee, S.-H., Kim, K. P., Kuret, J., Min, D.-H., & Lee, M. J. (2014). Direct cellular delivery of human proteasomes to delay tau aggregation. Nature Communications. https://doi.org/10.1038/ncomms6633