DOI: 10.1038/ncomms4396. Quantitative live-cell imaging reveals spatio-temporal dynamics and cytoplasmic assembly of the 26S proteasome

Quantitative live-cell imaging reveals spatio-temporal dynamics and cytoplasmic assembly of the 26S proteasome

10.1038/ncomms4396

Crossref journal-article

Springer Science and Business Media LLC

Nature Communications (297)

Bibliography

Pack, C.-G., Yukii, H., Toh-e, A., Kudo, T., Tsuchiya, H., Kaiho, A., Sakata, E., Murata, S., Yokosawa, H., Sako, Y., Baumeister, W., Tanaka, K., & Saeki, Y. (2014). Quantitative live-cell imaging reveals spatio-temporal dynamics and cytoplasmic assembly of the 26S proteasome. Nature Communications, 5(1).

Authors 13

Chan-Gi Pack (first)
Haruka Yukii (additional)
Akio Toh-e (additional)
Tai Kudo (additional)
Hikaru Tsuchiya (additional)
Ai Kaiho (additional)
Eri Sakata (additional)
Shigeo Murata (additional)
Hideyoshi Yokosawa (additional)
Yasushi Sako (additional)
Wolfgang Baumeister (additional)
Keiji Tanaka (additional)
Yasushi Saeki (additional)

References 58 Referenced 116

Baumeister, W., Walz, J., Zuhl, F. & Seemuller, E. The proteasome: paradigm of a self-compartmentalizing protease. Cell 92, 367–380 (1998). (10.1016/S0092-8674(00)80929-0) / Cell by W Baumeister (1998)
Glickman, M. H. & Ciechanover, A. The ubiquitin-proteasome proteolytic pathway: destruction for the sake of construction. Physiol. Rev. 82, 373–428 (2002). (10.1152/physrev.00027.2001) / Physiol. Rev. by MH Glickman (2002)
Finley, D. Recognition and processing of ubiquitin-protein conjugates by the proteasome. Annu. Rev. Biochem. 78, 477–513 (2009). (10.1146/annurev.biochem.78.081507.101607) / Annu. Rev. Biochem. by D Finley (2009)
Schwartz, A. L. & Ciechanover, A. Targeting proteins for destruction by the ubiquitin system: implications for human pathobiology. Annu. Rev. Pharmacol. Toxicol. 49, 73–96 (2009). (10.1146/annurev.pharmtox.051208.165340) / Annu. Rev. Pharmacol. Toxicol. by AL Schwartz (2009)
Lander, G. C. et al. Complete subunit architecture of the proteasome regulatory particle. Nature 482, 186–191 (2012). (10.1038/nature10774) / Nature by GC Lander (2012)
Lasker, K. et al. Molecular architecture of the 26S proteasome holocomplex determined by an integrative approach. Proc. Natl Acad. Sci. USA 109, 1380–1387 (2012). (10.1073/pnas.1120559109) / Proc. Natl Acad. Sci. USA by K Lasker (2012)
Sakata, E. et al. Localization of the proteasomal ubiquitin receptors Rpn10 and Rpn13 by electron cryomicroscopy. Proc. Natl Acad. Sci. USA 109, 1479–1484 (2012). (10.1073/pnas.1119394109) / Proc. Natl Acad. Sci. USA by E Sakata (2012)
da Fonseca, P. C., He, J. & Morris, E. P. Molecular model of the human 26S proteasome. Mol. Cell 46, 54–66 (2012). (10.1016/j.molcel.2012.03.026) / Mol. Cell by PC da Fonseca (2012)
Saeki, Y. & Tanaka, K. Assembly and function of the proteasome. Methods Mol. Biol. 832, 315–337 (2012). (10.1007/978-1-61779-474-2_22) / Methods Mol. Biol. by Y Saeki (2012)
Murata, S., Yashiroda, H. & Tanaka, K. Molecular mechanisms of proteasome assembly. Nat. Rev. Mol. Cell Biol. 10, 104–115 (2009). (10.1038/nrm2630) / Nat. Rev. Mol. Cell Biol. by S Murata (2009)
Tomko, R. J. Jr & Hochstrasser, M. Order of the proteasomal ATPases and eukaryotic proteasome assembly. Cell Biochem. Biophys. 60, 13–20 (2011). (10.1007/s12013-011-9178-4) / Cell Biochem. Biophys. by RJ Tomko Jr (2011)
Bedford, L., Paine, S., Sheppard, P. W., Mayer, R. J. & Roelofs, J. Assembly, structure, and function of the 26S proteasome. Trends Cell. Biol. 20, 391–401 (2010). (10.1016/j.tcb.2010.03.007) / Trends Cell. Biol. by L Bedford (2010)
Nederlof, P. M., Wang, H. R. & Baumeister, W. Nuclear localization signals of human and Thermoplasma proteasomal alpha subunits are functional in vitro. Proc. Natl Acad. Sci. USA 92, 12060–12064 (1995). (10.1073/pnas.92.26.12060) / Proc. Natl Acad. Sci. USA by PM Nederlof (1995)
Enenkel, C., Lehmann, A. & Kloetzel, P. M. Subcellular distribution of proteasomes implicates a major location of protein degradation in the nuclear envelope-ER network in yeast. EMBO J. 17, 6144–6154 (1998). (10.1093/emboj/17.21.6144) / EMBO J. by C Enenkel (1998)
Wilkinson, C. R. et al. Localization of the 26S proteasome during mitosis and meiosis in fission yeast. EMBO J. 17, 6465–6476 (1998). (10.1093/emboj/17.22.6465) / EMBO J. by CR Wilkinson (1998)
Amsterdam, A., Pitzer, F. & Baumeister, W. Changes in intracellular localization of proteasomes in immortalized ovarian granulosa cells during mitosis associated with a role in cell cycle control. Proc. Natl Acad. Sci. USA 90, 99–103 (1993). (10.1073/pnas.90.1.99) / Proc. Natl Acad. Sci. USA by A Amsterdam (1993)
Tsuchiya, H., Arai, N., Tanaka, K. & Saeki, Y. Cytoplasmic proteasomes are not indispensable for cell growth in Saccharomyces cerevisiae. Biochem. Biophys. Res. Commun. 436, 372–376 (2013). (10.1016/j.bbrc.2013.05.105) / Biochem. Biophys. Res. Commun. by H Tsuchiya (2013)
Wang, H. R., Kania, M., Baumeister, W. & Nederlof, P. M. Import of human and Thermoplasma 20S proteasomes into nuclei of HeLa cells requires functional NLS sequences. Eur. J. Cell Biol. 73, 105–113 (1997). / Eur. J. Cell Biol. by HR Wang (1997)
Wendler, P., Lehmann, A., Janek, K., Baumgart, S. & Enenkel, C. The bipartite nuclear localization sequence of Rpn2 is required for nuclear import of proteasomal base complexes via karyopherin alphabeta and proteasome functions. J. Biol. Chem. 279, 37751–37762 (2004). (10.1074/jbc.M403551200) / J. Biol. Chem. by P Wendler (2004)
Lehmann, A., Janek, K., Braun, B., Kloetzel, P. M. & Enenkel, C. 20S proteasomes are imported as precursor complexes into the nucleus of yeast. J. Mol. Biol. 317, 401–413 (2002). (10.1006/jmbi.2002.5443) / J. Mol. Biol. by A Lehmann (2002)
Isono, E. et al. The assembly pathway of the 19S regulatory particle of the yeast 26S proteasome. Mol. Biol. Cell 18, 569–580 (2007). (10.1091/mbc.e06-07-0635) / Mol. Biol. Cell by E Isono (2007)
Chen, L. et al. Sts1 plays a key role in targeting proteasomes to the nucleus. J. Biol. Chem. 286, 3104–3118 (2011). (10.1074/jbc.M110.135863) / J. Biol. Chem. by L Chen (2011)
Savulescu, A. F. et al. Nuclear import of an intact preassembled proteasome particle. Mol. Biol. Cell 22, 880–891 (2011). (10.1091/mbc.e10-07-0595) / Mol. Biol. Cell by AF Savulescu (2011)
Reits, E. A., Benham, A. M., Plougastel, B., Neefjes, J. & Trowsdale, J. Dynamics of proteasome distribution in living cells. EMBO J. 16, 6087–6094 (1997). (10.1093/emboj/16.20.6087) / EMBO J. by EA Reits (1997)
Pante, N. & Kann, M. Nuclear pore complex is able to transport macromolecules with diameters of about 39 nm. Mol. Biol. Cell 13, 425–434 (2002). (10.1091/mbc.01-06-0308) / Mol. Biol. Cell by N Pante (2002)
Hoelz, A., Debler, E. W. & Blobel, G. The structure of the nuclear pore complex. Annu. Rev. Biochem. 80, 613–643 (2011). (10.1146/annurev-biochem-060109-151030) / Annu. Rev. Biochem. by A Hoelz (2011)
Slaughter, B. D. & Li, R. Toward quantitative "in vivo biochemistry" with fluorescence fluctuation spectroscopy. Mol. Biol. Cell 21, 4306–4311 (2010). (10.1091/mbc.e10-05-0451) / Mol. Biol. Cell by BD Slaughter (2010)
Sako, Y. et al. Live cell single-molecule detection in systems biology. Wiley Interdiscip. Rev. Syst. Biol. Med. 4, 183–192 (2012). (10.1002/wsbm.161) / Wiley Interdiscip. Rev. Syst. Biol. Med. by Y Sako (2012)
Petrasek, Z., Ries, J. & Schwille, P. Scanning FCS for the characterization of protein dynamics in live cells. Methods Enzymol. 472, 317–343 (2010). (10.1016/S0076-6879(10)72005-X) / Methods Enzymol. by Z Petrasek (2010)
Slaughter, B. D., Schwartz, J. W. & Li, R. Mapping dynamic protein interactions in MAP kinase signaling using live-cell fluorescence fluctuation spectroscopy and imaging. Proc. Natl Acad. Sci. USA 104, 20320–20325 (2007). (10.1073/pnas.0710336105) / Proc. Natl Acad. Sci. USA by BD Slaughter (2007)
Pack, C., Saito, K., Tamura, M. & Kinjo, M. Microenvironment and effect of energy depletion in the nucleus analyzed by mobility of multiple oligomeric EGFPs. Biophys. J. 91, 3921–3936 (2006). (10.1529/biophysj.105.079467) / Biophys. J. by C Pack (2006)
Wendler, P. et al. Atypical AAA+ subunit packing creates an expanded cavity for disaggregation by the protein-remodeling factor Hsp104. Cell 131, 1366–1377 (2007). (10.1016/j.cell.2007.10.047) / Cell by P Wendler (2007)
Verschoor, A., Warner, J. R., Srivastava, S., Grassucci, R. A. & Frank, J. Three-dimensional structure of the yeast ribosome. Nucleic Acids Res. 26, 655–661 (1998). (10.1093/nar/26.2.655) / Nucleic Acids Res. by A Verschoor (1998)
Laporte, D., Salin, B., Daignan-Fornier, B. & Sagot, I. Reversible cytoplasmic localization of the proteasome in quiescent yeast cells. J. Cell Biol. 181, 737–745 (2008). (10.1083/jcb.200711154) / J. Cell Biol. by D Laporte (2008)
Haarer, B., Aggeli, D., Viggiano, S., Burke, D. J. & Amberg, D. C. Novel interactions between actin and the proteasome revealed by complex haploinsufficiency. PLoS Genet. 7, e1002288 (2011). (10.1371/journal.pgen.1002288) / PLoS Genet. by B Haarer (2011)
Geng, F., Wenzel, S. & Tansey, W. P. Ubiquitin and proteasomes in transcription. Annu. Rev. Biochem. 81, 177–201 (2012). (10.1146/annurev-biochem-052110-120012) / Annu. Rev. Biochem. by F Geng (2012)
Roelofs, J. et al. Chaperone-mediated pathway of proteasome regulatory particle assembly. Nature 459, 861–865 (2009). (10.1038/nature08063) / Nature by J Roelofs (2009)
Funakoshi, M., Tomko, R. J. Jr, Kobayashi, H. & Hochstrasser, M. Multiple assembly chaperones govern biogenesis of the proteasome regulatory particle base. Cell 137, 887–899 (2009). (10.1016/j.cell.2009.04.061) / Cell by M Funakoshi (2009)
Park, S. et al. Hexameric assembly of the proteasomal ATPases is templated through their C termini. Nature 459, 866–870 (2009). (10.1038/nature08065) / Nature by S Park (2009)
Saeki, Y., Toh-e, A., Kudo, T., Kawamura, H. & Tanaka, K. Multiple proteasome-interacting proteins assist the assembly of the yeast 19S regulatory particle. Cell 137, 900–913 (2009). (10.1016/j.cell.2009.05.005) / Cell by Y Saeki (2009)
Mannhaupt, G., Schnall, R., Karpov, V., Vetter, I. & Feldmann, H. Rpn4p acts as a transcription factor by binding to PACE, a nonamer box found upstream of 26S proteasomal and other genes in yeast. FEBS Lett. 450, 27–34 (1999). (10.1016/S0014-5793(99)00467-6) / FEBS Lett. by G Mannhaupt (1999)
Wang, X., Yen, J., Kaiser, P. & Huang, L. Regulation of the 26S proteasome complex during oxidative stress. Sci. Signal. 3, ra88 (2010). / Sci. Signal. by X Wang (2010)
Gonzalez, F., Delahodde, A., Kodadek, T. & Johnston, S. A. Recruitment of a 19S proteasome subcomplex to an activated promoter. Science 296, 548–550 (2002). (10.1126/science.1069490) / Science by F Gonzalez (2002)
Lassot, I. et al. The proteasome regulates HIV-1 transcription by both proteolytic and nonproteolytic mechanisms. Mol. Cell 25, 369–383 (2007). (10.1016/j.molcel.2006.12.020) / Mol. Cell by I Lassot (2007)
Nakamura, M. et al. Spt6 levels are modulated by PAAF1 and proteasome to regulate the HIV-1 LTR. Retrovirology 9, 13 (2012). (10.1186/1742-4690-9-13) / Retrovirology by M Nakamura (2012)
Geng, F. & Tansey, W. P. Similar temporal and spatial recruitment of native 19 and 20S proteasome subunits to transcriptionally active chromatin. Proc. Natl Acad. Sci. USA 109, 6060–6065 (2012). (10.1073/pnas.1200854109) / Proc. Natl Acad. Sci. USA by F Geng (2012)
Mullard, A. Next-generation proteasome blockers promise safer cancer therapy. Nat. Med. 18, 7 (2012). (10.1038/nm0112-7a) / Nat. Med. by A Mullard (2012)
Sherman, F. Getting started with yeast. Methods Enzymol. 194, 3–21 (1991). (10.1016/0076-6879(91)94004-V) / Methods Enzymol. by F Sherman (1991)
Fukunaga, K., Kudo, T., Toh-e, A., Tanaka, K. & Saeki, Y. Dissection of the assembly pathway of the proteasome lid in Saccharomyces cerevisiae. Biochem. Biophys. Res. Commun. 396, 1048–1053 (2010). (10.1016/j.bbrc.2010.05.061) / Biochem. Biophys. Res. Commun. by K Fukunaga (2010)
Fox, T. D. et al. Analysis and manipulation of yeast mitochondrial genes. Methods Enzymol. 194, 149–165 (1991). (10.1016/0076-6879(91)94013-3) / Methods Enzymol. by TD Fox (1991)
Kawai-Noma, S. et al. Dynamics of yeast prion aggregates in single living cells. Genes Cells 11, 1085–1096 (2006). (10.1111/j.1365-2443.2006.01004.x) / Genes Cells by S Kawai-Noma (2006)
Park, H., Pack, C., Kinjo, M. & Kaang, B. K. In vivo quantitative analysis of PKA subunit interaction and cAMP level by dual color fluorescence cross correlation spectroscopy. Mol. Cells 26, 87–92 (2008). (10.1016/S1016-8478(23)13968-9) / Mol. Cells by H Park (2008)
Noda, Y. et al. Reciprocal interaction with G-actin and tropomyosin is essential for aquaporin-2 trafficking. J. Cell Biol. 182, 587–601 (2008). (10.1083/jcb.200709177) / J. Cell Biol. by Y Noda (2008)
Haupts, U., Maiti, S., Schwille, P. & Webb, W. W. Dynamics of fluorescence fluctuations in green fluorescent protein observed by fluorescence correlation spectroscopy. Proc. Natl Acad. Sci. USA 95, 13573–13578 (1998). (10.1073/pnas.95.23.13573) / Proc. Natl Acad. Sci. USA by U Haupts (1998)
Pack, C. G. et al. Analysis of interaction between chaperonin GroEL and its substrate using fluorescence correlation spectroscopy. Cytometry 36, 247–253 (1999). (10.1002/(SICI)1097-0320(19990701)36:3<247::AID-CYTO15>3.0.CO;2-#) / Cytometry by CG Pack (1999)
Kawai-Noma, S. et al. In vivo evidence for the fibrillar structures of Sup35 prions in yeast cells. J. Cell Biol. 190, 223–231 (2010). (10.1083/jcb.201002149) / J. Cell Biol. by S Kawai-Noma (2010)
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). (10.1016/S0076-6879(05)99014-9) / Methods Enzymol. by Y Saeki (2005)
Scheres, S. H., Nunez-Ramirez, R., Sorzano, C. O., Carazo, J. M. & Marabini, R. Image processing for electron microscopy single-particle analysis using XMIPP. Nat. Protoc. 3, 977–990 (2008). (10.1038/nprot.2008.62) / Nat. Protoc. by SH Scheres (2008)

Dates

Type	When
Created	11 years, 5 months ago (March 6, 2014, 6:35 a.m.)
Deposited	1 year, 2 months ago (May 24, 2024, 4:58 p.m.)
Indexed	2 weeks, 3 days ago (Aug. 6, 2025, 9:46 a.m.)
Issued	11 years, 5 months ago (March 6, 2014)
Published	11 years, 5 months ago (March 6, 2014)
Published Online	11 years, 5 months ago (March 6, 2014)

Funders 0

None

BibTeX

@article{Pack_2014, title={Quantitative live-cell imaging reveals spatio-temporal dynamics and cytoplasmic assembly of the 26S proteasome}, volume={5}, ISSN={2041-1723}, url={http://dx.doi.org/10.1038/ncomms4396}, DOI={10.1038/ncomms4396}, number={1}, journal={Nature Communications}, publisher={Springer Science and Business Media LLC}, author={Pack, Chan-Gi and Yukii, Haruka and Toh-e, Akio and Kudo, Tai and Tsuchiya, Hikaru and Kaiho, Ai and Sakata, Eri and Murata, Shigeo and Yokosawa, Hideyoshi and Sako, Yasushi and Baumeister, Wolfgang and Tanaka, Keiji and Saeki, Yasushi}, year={2014}, month=mar }

JSON

{
  "indexed": {
    "date-parts": [
      [
        2025,
        8,
        6
      ]
    ],
    "date-time": "2025-08-06T13:46:29Z",
    "timestamp": 1754487989045
  },
  "reference-count": 58,
  "publisher": "Springer Science and Business Media LLC",
  "issue": "1",
  "license": [
    {
      "start": {
        "date-parts": [
          [
            2014,
            3,
            6
          ]
        ],
        "date-time": "2014-03-06T00:00:00Z",
        "timestamp": 1394064000000
      },
      "content-version": "tdm",
      "delay-in-days": 0,
      "URL": "https://www.springernature.com/gp/researchers/text-and-data-mining"
    },
    {
      "start": {
        "date-parts": [
          [
            2014,
            3,
            6
          ]
        ],
        "date-time": "2014-03-06T00:00:00Z",
        "timestamp": 1394064000000
      },
      "content-version": "vor",
      "delay-in-days": 0,
      "URL": "https://www.springernature.com/gp/researchers/text-and-data-mining"
    }
  ],
  "content-domain": {
    "domain": [
      "link.springer.com"
    ],
    "crossmark-restriction": false
  },
  "DOI": "10.1038/ncomms4396",
  "type": "journal-article",
  "created": {
    "date-parts": [
      [
        2014,
        3,
        6
      ]
    ],
    "date-time": "2014-03-06T11:35:45Z",
    "timestamp": 1394105745000
  },
  "update-policy": "http://dx.doi.org/10.1007/springer_crossmark_policy",
  "source": "Crossref",
  "is-referenced-by-count": 116,
  "title": "Quantitative live-cell imaging reveals spatio-temporal dynamics and cytoplasmic assembly of the 26S proteasome",
  "prefix": "10.1038",
  "volume": "5",
  "author": [
    {
      "given": "Chan-Gi",
      "family": "Pack",
      "sequence": "first",
      "affiliation": []
    },
    {
      "given": "Haruka",
      "family": "Yukii",
      "sequence": "additional",
      "affiliation": []
    },
    {
      "given": "Akio",
      "family": "Toh-e",
      "sequence": "additional",
      "affiliation": []
    },
    {
      "given": "Tai",
      "family": "Kudo",
      "sequence": "additional",
      "affiliation": []
    },
    {
      "given": "Hikaru",
      "family": "Tsuchiya",
      "sequence": "additional",
      "affiliation": []
    },
    {
      "given": "Ai",
      "family": "Kaiho",
      "sequence": "additional",
      "affiliation": []
    },
    {
      "given": "Eri",
      "family": "Sakata",
      "sequence": "additional",
      "affiliation": []
    },
    {
      "given": "Shigeo",
      "family": "Murata",
      "sequence": "additional",
      "affiliation": []
    },
    {
      "given": "Hideyoshi",
      "family": "Yokosawa",
      "sequence": "additional",
      "affiliation": []
    },
    {
      "given": "Yasushi",
      "family": "Sako",
      "sequence": "additional",
      "affiliation": []
    },
    {
      "given": "Wolfgang",
      "family": "Baumeister",
      "sequence": "additional",
      "affiliation": []
    },
    {
      "given": "Keiji",
      "family": "Tanaka",
      "sequence": "additional",
      "affiliation": []
    },
    {
      "given": "Yasushi",
      "family": "Saeki",
      "sequence": "additional",
      "affiliation": []
    }
  ],
  "member": "297",
  "published-online": {
    "date-parts": [
      [
        2014,
        3,
        6
      ]
    ]
  },
  "reference": [
    {
      "key": "BFncomms4396_CR1",
      "doi-asserted-by": "publisher",
      "first-page": "367",
      "DOI": "10.1016/S0092-8674(00)80929-0",
      "volume": "92",
      "author": "W Baumeister",
      "year": "1998",
      "unstructured": "Baumeister, W., Walz, J., Zuhl, F. & Seemuller, E. The proteasome: paradigm of a self-compartmentalizing protease. Cell 92, 367\u2013380 (1998).",
      "journal-title": "Cell"
    },
    {
      "key": "BFncomms4396_CR2",
      "doi-asserted-by": "publisher",
      "first-page": "373",
      "DOI": "10.1152/physrev.00027.2001",
      "volume": "82",
      "author": "MH Glickman",
      "year": "2002",
      "unstructured": "Glickman, M. H. & Ciechanover, A. The ubiquitin-proteasome proteolytic pathway: destruction for the sake of construction. Physiol. Rev. 82, 373\u2013428 (2002).",
      "journal-title": "Physiol. Rev."
    },
    {
      "key": "BFncomms4396_CR3",
      "doi-asserted-by": "publisher",
      "first-page": "477",
      "DOI": "10.1146/annurev.biochem.78.081507.101607",
      "volume": "78",
      "author": "D Finley",
      "year": "2009",
      "unstructured": "Finley, D. Recognition and processing of ubiquitin-protein conjugates by the proteasome. Annu. Rev. Biochem. 78, 477\u2013513 (2009).",
      "journal-title": "Annu. Rev. Biochem."
    },
    {
      "key": "BFncomms4396_CR4",
      "doi-asserted-by": "publisher",
      "first-page": "73",
      "DOI": "10.1146/annurev.pharmtox.051208.165340",
      "volume": "49",
      "author": "AL Schwartz",
      "year": "2009",
      "unstructured": "Schwartz, A. L. & Ciechanover, A. Targeting proteins for destruction by the ubiquitin system: implications for human pathobiology. Annu. Rev. Pharmacol. Toxicol. 49, 73\u201396 (2009).",
      "journal-title": "Annu. Rev. Pharmacol. Toxicol."
    },
    {
      "key": "BFncomms4396_CR5",
      "doi-asserted-by": "publisher",
      "first-page": "186",
      "DOI": "10.1038/nature10774",
      "volume": "482",
      "author": "GC Lander",
      "year": "2012",
      "unstructured": "Lander, G. C. et al. Complete subunit architecture of the proteasome regulatory particle. Nature 482, 186\u2013191 (2012).",
      "journal-title": "Nature"
    },
    {
      "key": "BFncomms4396_CR6",
      "doi-asserted-by": "publisher",
      "first-page": "1380",
      "DOI": "10.1073/pnas.1120559109",
      "volume": "109",
      "author": "K Lasker",
      "year": "2012",
      "unstructured": "Lasker, K. et al. Molecular architecture of the 26S proteasome holocomplex determined by an integrative approach. Proc. Natl Acad. Sci. USA 109, 1380\u20131387 (2012).",
      "journal-title": "Proc. Natl Acad. Sci. USA"
    },
    {
      "key": "BFncomms4396_CR7",
      "doi-asserted-by": "publisher",
      "first-page": "1479",
      "DOI": "10.1073/pnas.1119394109",
      "volume": "109",
      "author": "E Sakata",
      "year": "2012",
      "unstructured": "Sakata, E. et al. Localization of the proteasomal ubiquitin receptors Rpn10 and Rpn13 by electron cryomicroscopy. Proc. Natl Acad. Sci. USA 109, 1479\u20131484 (2012).",
      "journal-title": "Proc. Natl Acad. Sci. USA"
    },
    {
      "key": "BFncomms4396_CR8",
      "doi-asserted-by": "publisher",
      "first-page": "54",
      "DOI": "10.1016/j.molcel.2012.03.026",
      "volume": "46",
      "author": "PC da Fonseca",
      "year": "2012",
      "unstructured": "da Fonseca, P. C., He, J. & Morris, E. P. Molecular model of the human 26S proteasome. Mol. Cell 46, 54\u201366 (2012).",
      "journal-title": "Mol. Cell"
    },
    {
      "key": "BFncomms4396_CR9",
      "doi-asserted-by": "publisher",
      "first-page": "315",
      "DOI": "10.1007/978-1-61779-474-2_22",
      "volume": "832",
      "author": "Y Saeki",
      "year": "2012",
      "unstructured": "Saeki, Y. & Tanaka, K. Assembly and function of the proteasome. Methods Mol. Biol. 832, 315\u2013337 (2012).",
      "journal-title": "Methods Mol. Biol."
    },
    {
      "key": "BFncomms4396_CR10",
      "doi-asserted-by": "publisher",
      "first-page": "104",
      "DOI": "10.1038/nrm2630",
      "volume": "10",
      "author": "S Murata",
      "year": "2009",
      "unstructured": "Murata, S., Yashiroda, H. & Tanaka, K. Molecular mechanisms of proteasome assembly. Nat. Rev. Mol. Cell Biol. 10, 104\u2013115 (2009).",
      "journal-title": "Nat. Rev. Mol. Cell Biol."
    },
    {
      "key": "BFncomms4396_CR11",
      "doi-asserted-by": "publisher",
      "first-page": "13",
      "DOI": "10.1007/s12013-011-9178-4",
      "volume": "60",
      "author": "RJ Tomko Jr",
      "year": "2011",
      "unstructured": "Tomko, R. J. Jr & Hochstrasser, M. Order of the proteasomal ATPases and eukaryotic proteasome assembly. Cell Biochem. Biophys. 60, 13\u201320 (2011).",
      "journal-title": "Cell Biochem. Biophys."
    },
    {
      "key": "BFncomms4396_CR12",
      "doi-asserted-by": "publisher",
      "first-page": "391",
      "DOI": "10.1016/j.tcb.2010.03.007",
      "volume": "20",
      "author": "L Bedford",
      "year": "2010",
      "unstructured": "Bedford, L., Paine, S., Sheppard, P. W., Mayer, R. J. & Roelofs, J. Assembly, structure, and function of the 26S proteasome. Trends Cell. Biol. 20, 391\u2013401 (2010).",
      "journal-title": "Trends Cell. Biol."
    },
    {
      "key": "BFncomms4396_CR13",
      "doi-asserted-by": "publisher",
      "first-page": "12060",
      "DOI": "10.1073/pnas.92.26.12060",
      "volume": "92",
      "author": "PM Nederlof",
      "year": "1995",
      "unstructured": "Nederlof, P. M., Wang, H. R. & Baumeister, W. Nuclear localization signals of human and Thermoplasma proteasomal alpha subunits are functional in vitro. Proc. Natl Acad. Sci. USA 92, 12060\u201312064 (1995).",
      "journal-title": "Proc. Natl Acad. Sci. USA"
    },
    {
      "key": "BFncomms4396_CR14",
      "doi-asserted-by": "publisher",
      "first-page": "6144",
      "DOI": "10.1093/emboj/17.21.6144",
      "volume": "17",
      "author": "C Enenkel",
      "year": "1998",
      "unstructured": "Enenkel, C., Lehmann, A. & Kloetzel, P. M. Subcellular distribution of proteasomes implicates a major location of protein degradation in the nuclear envelope-ER network in yeast. EMBO J. 17, 6144\u20136154 (1998).",
      "journal-title": "EMBO J."
    },
    {
      "key": "BFncomms4396_CR15",
      "doi-asserted-by": "publisher",
      "first-page": "6465",
      "DOI": "10.1093/emboj/17.22.6465",
      "volume": "17",
      "author": "CR Wilkinson",
      "year": "1998",
      "unstructured": "Wilkinson, C. R. et al. Localization of the 26S proteasome during mitosis and meiosis in fission yeast. EMBO J. 17, 6465\u20136476 (1998).",
      "journal-title": "EMBO J."
    },
    {
      "key": "BFncomms4396_CR16",
      "doi-asserted-by": "publisher",
      "first-page": "99",
      "DOI": "10.1073/pnas.90.1.99",
      "volume": "90",
      "author": "A Amsterdam",
      "year": "1993",
      "unstructured": "Amsterdam, A., Pitzer, F. & Baumeister, W. Changes in intracellular localization of proteasomes in immortalized ovarian granulosa cells during mitosis associated with a role in cell cycle control. Proc. Natl Acad. Sci. USA 90, 99\u2013103 (1993).",
      "journal-title": "Proc. Natl Acad. Sci. USA"
    },
    {
      "key": "BFncomms4396_CR17",
      "doi-asserted-by": "publisher",
      "first-page": "372",
      "DOI": "10.1016/j.bbrc.2013.05.105",
      "volume": "436",
      "author": "H Tsuchiya",
      "year": "2013",
      "unstructured": "Tsuchiya, H., Arai, N., Tanaka, K. & Saeki, Y. Cytoplasmic proteasomes are not indispensable for cell growth in Saccharomyces cerevisiae. Biochem. Biophys. Res. Commun. 436, 372\u2013376 (2013).",
      "journal-title": "Biochem. Biophys. Res. Commun."
    },
    {
      "key": "BFncomms4396_CR18",
      "first-page": "105",
      "volume": "73",
      "author": "HR Wang",
      "year": "1997",
      "unstructured": "Wang, H. R., Kania, M., Baumeister, W. & Nederlof, P. M. Import of human and Thermoplasma 20S proteasomes into nuclei of HeLa cells requires functional NLS sequences. Eur. J. Cell Biol. 73, 105\u2013113 (1997).",
      "journal-title": "Eur. J. Cell Biol."
    },
    {
      "key": "BFncomms4396_CR19",
      "doi-asserted-by": "publisher",
      "first-page": "37751",
      "DOI": "10.1074/jbc.M403551200",
      "volume": "279",
      "author": "P Wendler",
      "year": "2004",
      "unstructured": "Wendler, P., Lehmann, A., Janek, K., Baumgart, S. & Enenkel, C. The bipartite nuclear localization sequence of Rpn2 is required for nuclear import of proteasomal base complexes via karyopherin alphabeta and proteasome functions. J. Biol. Chem. 279, 37751\u201337762 (2004).",
      "journal-title": "J. Biol. Chem."
    },
    {
      "key": "BFncomms4396_CR20",
      "doi-asserted-by": "publisher",
      "first-page": "401",
      "DOI": "10.1006/jmbi.2002.5443",
      "volume": "317",
      "author": "A Lehmann",
      "year": "2002",
      "unstructured": "Lehmann, A., Janek, K., Braun, B., Kloetzel, P. M. & Enenkel, C. 20S proteasomes are imported as precursor complexes into the nucleus of yeast. J. Mol. Biol. 317, 401\u2013413 (2002).",
      "journal-title": "J. Mol. Biol."
    },
    {
      "key": "BFncomms4396_CR21",
      "doi-asserted-by": "publisher",
      "first-page": "569",
      "DOI": "10.1091/mbc.e06-07-0635",
      "volume": "18",
      "author": "E Isono",
      "year": "2007",
      "unstructured": "Isono, E. et al. The assembly pathway of the 19S regulatory particle of the yeast 26S proteasome. Mol. Biol. Cell 18, 569\u2013580 (2007).",
      "journal-title": "Mol. Biol. Cell"
    },
    {
      "key": "BFncomms4396_CR22",
      "doi-asserted-by": "publisher",
      "first-page": "3104",
      "DOI": "10.1074/jbc.M110.135863",
      "volume": "286",
      "author": "L Chen",
      "year": "2011",
      "unstructured": "Chen, L. et al. Sts1 plays a key role in targeting proteasomes to the nucleus. J. Biol. Chem. 286, 3104\u20133118 (2011).",
      "journal-title": "J. Biol. Chem."
    },
    {
      "key": "BFncomms4396_CR23",
      "doi-asserted-by": "publisher",
      "first-page": "880",
      "DOI": "10.1091/mbc.e10-07-0595",
      "volume": "22",
      "author": "AF Savulescu",
      "year": "2011",
      "unstructured": "Savulescu, A. F. et al. Nuclear import of an intact preassembled proteasome particle. Mol. Biol. Cell 22, 880\u2013891 (2011).",
      "journal-title": "Mol. Biol. Cell"
    },
    {
      "key": "BFncomms4396_CR24",
      "doi-asserted-by": "publisher",
      "first-page": "6087",
      "DOI": "10.1093/emboj/16.20.6087",
      "volume": "16",
      "author": "EA Reits",
      "year": "1997",
      "unstructured": "Reits, E. A., Benham, A. M., Plougastel, B., Neefjes, J. & Trowsdale, J. Dynamics of proteasome distribution in living cells. EMBO J. 16, 6087\u20136094 (1997).",
      "journal-title": "EMBO J."
    },
    {
      "key": "BFncomms4396_CR25",
      "doi-asserted-by": "publisher",
      "first-page": "425",
      "DOI": "10.1091/mbc.01-06-0308",
      "volume": "13",
      "author": "N Pante",
      "year": "2002",
      "unstructured": "Pante, N. & Kann, M. Nuclear pore complex is able to transport macromolecules with diameters of about 39\u2009nm. Mol. Biol. Cell 13, 425\u2013434 (2002).",
      "journal-title": "Mol. Biol. Cell"
    },
    {
      "key": "BFncomms4396_CR26",
      "doi-asserted-by": "publisher",
      "first-page": "613",
      "DOI": "10.1146/annurev-biochem-060109-151030",
      "volume": "80",
      "author": "A Hoelz",
      "year": "2011",
      "unstructured": "Hoelz, A., Debler, E. W. & Blobel, G. The structure of the nuclear pore complex. Annu. Rev. Biochem. 80, 613\u2013643 (2011).",
      "journal-title": "Annu. Rev. Biochem."
    },
    {
      "key": "BFncomms4396_CR27",
      "doi-asserted-by": "publisher",
      "first-page": "4306",
      "DOI": "10.1091/mbc.e10-05-0451",
      "volume": "21",
      "author": "BD Slaughter",
      "year": "2010",
      "unstructured": "Slaughter, B. D. & Li, R. Toward quantitative \"in vivo biochemistry\" with fluorescence fluctuation spectroscopy. Mol. Biol. Cell 21, 4306\u20134311 (2010).",
      "journal-title": "Mol. Biol. Cell"
    },
    {
      "key": "BFncomms4396_CR28",
      "doi-asserted-by": "publisher",
      "first-page": "183",
      "DOI": "10.1002/wsbm.161",
      "volume": "4",
      "author": "Y Sako",
      "year": "2012",
      "unstructured": "Sako, Y. et al. Live cell single-molecule detection in systems biology. Wiley Interdiscip. Rev. Syst. Biol. Med. 4, 183\u2013192 (2012).",
      "journal-title": "Wiley Interdiscip. Rev. Syst. Biol. Med."
    },
    {
      "key": "BFncomms4396_CR29",
      "doi-asserted-by": "publisher",
      "first-page": "317",
      "DOI": "10.1016/S0076-6879(10)72005-X",
      "volume": "472",
      "author": "Z Petrasek",
      "year": "2010",
      "unstructured": "Petrasek, Z., Ries, J. & Schwille, P. Scanning FCS for the characterization of protein dynamics in live cells. Methods Enzymol. 472, 317\u2013343 (2010).",
      "journal-title": "Methods Enzymol."
    },
    {
      "key": "BFncomms4396_CR30",
      "doi-asserted-by": "publisher",
      "first-page": "20320",
      "DOI": "10.1073/pnas.0710336105",
      "volume": "104",
      "author": "BD Slaughter",
      "year": "2007",
      "unstructured": "Slaughter, B. D., Schwartz, J. W. & Li, R. Mapping dynamic protein interactions in MAP kinase signaling using live-cell fluorescence fluctuation spectroscopy and imaging. Proc. Natl Acad. Sci. USA 104, 20320\u201320325 (2007).",
      "journal-title": "Proc. Natl Acad. Sci. USA"
    },
    {
      "key": "BFncomms4396_CR31",
      "doi-asserted-by": "publisher",
      "first-page": "3921",
      "DOI": "10.1529/biophysj.105.079467",
      "volume": "91",
      "author": "C Pack",
      "year": "2006",
      "unstructured": "Pack, C., Saito, K., Tamura, M. & Kinjo, M. Microenvironment and effect of energy depletion in the nucleus analyzed by mobility of multiple oligomeric EGFPs. Biophys. J. 91, 3921\u20133936 (2006).",
      "journal-title": "Biophys. J."
    },
    {
      "key": "BFncomms4396_CR32",
      "doi-asserted-by": "publisher",
      "first-page": "1366",
      "DOI": "10.1016/j.cell.2007.10.047",
      "volume": "131",
      "author": "P Wendler",
      "year": "2007",
      "unstructured": "Wendler, P. et al. Atypical AAA+ subunit packing creates an expanded cavity for disaggregation by the protein-remodeling factor Hsp104. Cell 131, 1366\u20131377 (2007).",
      "journal-title": "Cell"
    },
    {
      "key": "BFncomms4396_CR33",
      "doi-asserted-by": "publisher",
      "first-page": "655",
      "DOI": "10.1093/nar/26.2.655",
      "volume": "26",
      "author": "A Verschoor",
      "year": "1998",
      "unstructured": "Verschoor, A., Warner, J. R., Srivastava, S., Grassucci, R. A. & Frank, J. Three-dimensional structure of the yeast ribosome. Nucleic Acids Res. 26, 655\u2013661 (1998).",
      "journal-title": "Nucleic Acids Res."
    },
    {
      "key": "BFncomms4396_CR34",
      "doi-asserted-by": "publisher",
      "first-page": "737",
      "DOI": "10.1083/jcb.200711154",
      "volume": "181",
      "author": "D Laporte",
      "year": "2008",
      "unstructured": "Laporte, D., Salin, B., Daignan-Fornier, B. & Sagot, I. Reversible cytoplasmic localization of the proteasome in quiescent yeast cells. J. Cell Biol. 181, 737\u2013745 (2008).",
      "journal-title": "J. Cell Biol."
    },
    {
      "key": "BFncomms4396_CR35",
      "doi-asserted-by": "publisher",
      "first-page": "e1002288",
      "DOI": "10.1371/journal.pgen.1002288",
      "volume": "7",
      "author": "B Haarer",
      "year": "2011",
      "unstructured": "Haarer, B., Aggeli, D., Viggiano, S., Burke, D. J. & Amberg, D. C. Novel interactions between actin and the proteasome revealed by complex haploinsufficiency. PLoS Genet. 7, e1002288 (2011).",
      "journal-title": "PLoS Genet."
    },
    {
      "key": "BFncomms4396_CR36",
      "doi-asserted-by": "publisher",
      "first-page": "177",
      "DOI": "10.1146/annurev-biochem-052110-120012",
      "volume": "81",
      "author": "F Geng",
      "year": "2012",
      "unstructured": "Geng, F., Wenzel, S. & Tansey, W. P. Ubiquitin and proteasomes in transcription. Annu. Rev. Biochem. 81, 177\u2013201 (2012).",
      "journal-title": "Annu. Rev. Biochem."
    },
    {
      "key": "BFncomms4396_CR37",
      "doi-asserted-by": "publisher",
      "first-page": "861",
      "DOI": "10.1038/nature08063",
      "volume": "459",
      "author": "J Roelofs",
      "year": "2009",
      "unstructured": "Roelofs, J. et al. Chaperone-mediated pathway of proteasome regulatory particle assembly. Nature 459, 861\u2013865 (2009).",
      "journal-title": "Nature"
    },
    {
      "key": "BFncomms4396_CR38",
      "doi-asserted-by": "publisher",
      "first-page": "887",
      "DOI": "10.1016/j.cell.2009.04.061",
      "volume": "137",
      "author": "M Funakoshi",
      "year": "2009",
      "unstructured": "Funakoshi, M., Tomko, R. J. Jr, Kobayashi, H. & Hochstrasser, M. Multiple assembly chaperones govern biogenesis of the proteasome regulatory particle base. Cell 137, 887\u2013899 (2009).",
      "journal-title": "Cell"
    },
    {
      "key": "BFncomms4396_CR39",
      "doi-asserted-by": "publisher",
      "first-page": "866",
      "DOI": "10.1038/nature08065",
      "volume": "459",
      "author": "S Park",
      "year": "2009",
      "unstructured": "Park, S. et al. Hexameric assembly of the proteasomal ATPases is templated through their C termini. Nature 459, 866\u2013870 (2009).",
      "journal-title": "Nature"
    },
    {
      "key": "BFncomms4396_CR40",
      "doi-asserted-by": "publisher",
      "first-page": "900",
      "DOI": "10.1016/j.cell.2009.05.005",
      "volume": "137",
      "author": "Y Saeki",
      "year": "2009",
      "unstructured": "Saeki, Y., Toh-e, A., Kudo, T., Kawamura, H. & Tanaka, K. Multiple proteasome-interacting proteins assist the assembly of the yeast 19S regulatory particle. Cell 137, 900\u2013913 (2009).",
      "journal-title": "Cell"
    },
    {
      "key": "BFncomms4396_CR41",
      "doi-asserted-by": "publisher",
      "first-page": "27",
      "DOI": "10.1016/S0014-5793(99)00467-6",
      "volume": "450",
      "author": "G Mannhaupt",
      "year": "1999",
      "unstructured": "Mannhaupt, G., Schnall, R., Karpov, V., Vetter, I. & Feldmann, H. Rpn4p acts as a transcription factor by binding to PACE, a nonamer box found upstream of 26S proteasomal and other genes in yeast. FEBS Lett. 450, 27\u201334 (1999).",
      "journal-title": "FEBS Lett."
    },
    {
      "key": "BFncomms4396_CR42",
      "first-page": "ra88",
      "volume": "3",
      "author": "X Wang",
      "year": "2010",
      "unstructured": "Wang, X., Yen, J., Kaiser, P. & Huang, L. Regulation of the 26S proteasome complex during oxidative stress. Sci. Signal. 3, ra88 (2010).",
      "journal-title": "Sci. Signal."
    },
    {
      "key": "BFncomms4396_CR43",
      "doi-asserted-by": "publisher",
      "first-page": "548",
      "DOI": "10.1126/science.1069490",
      "volume": "296",
      "author": "F Gonzalez",
      "year": "2002",
      "unstructured": "Gonzalez, F., Delahodde, A., Kodadek, T. & Johnston, S. A. Recruitment of a 19S proteasome subcomplex to an activated promoter. Science 296, 548\u2013550 (2002).",
      "journal-title": "Science"
    },
    {
      "key": "BFncomms4396_CR44",
      "doi-asserted-by": "publisher",
      "first-page": "369",
      "DOI": "10.1016/j.molcel.2006.12.020",
      "volume": "25",
      "author": "I Lassot",
      "year": "2007",
      "unstructured": "Lassot, I. et al. The proteasome regulates HIV-1 transcription by both proteolytic and nonproteolytic mechanisms. Mol. Cell 25, 369\u2013383 (2007).",
      "journal-title": "Mol. Cell"
    },
    {
      "key": "BFncomms4396_CR45",
      "doi-asserted-by": "publisher",
      "first-page": "13",
      "DOI": "10.1186/1742-4690-9-13",
      "volume": "9",
      "author": "M Nakamura",
      "year": "2012",
      "unstructured": "Nakamura, M. et al. Spt6 levels are modulated by PAAF1 and proteasome to regulate the HIV-1 LTR. Retrovirology 9, 13 (2012).",
      "journal-title": "Retrovirology"
    },
    {
      "key": "BFncomms4396_CR46",
      "doi-asserted-by": "publisher",
      "first-page": "6060",
      "DOI": "10.1073/pnas.1200854109",
      "volume": "109",
      "author": "F Geng",
      "year": "2012",
      "unstructured": "Geng, F. & Tansey, W. P. Similar temporal and spatial recruitment of native 19 and 20S proteasome subunits to transcriptionally active chromatin. Proc. Natl Acad. Sci. USA 109, 6060\u20136065 (2012).",
      "journal-title": "Proc. Natl Acad. Sci. USA"
    },
    {
      "key": "BFncomms4396_CR47",
      "doi-asserted-by": "publisher",
      "first-page": "7",
      "DOI": "10.1038/nm0112-7a",
      "volume": "18",
      "author": "A Mullard",
      "year": "2012",
      "unstructured": "Mullard, A. Next-generation proteasome blockers promise safer cancer therapy. Nat. Med. 18, 7 (2012).",
      "journal-title": "Nat. Med."
    },
    {
      "key": "BFncomms4396_CR48",
      "doi-asserted-by": "publisher",
      "first-page": "3",
      "DOI": "10.1016/0076-6879(91)94004-V",
      "volume": "194",
      "author": "F Sherman",
      "year": "1991",
      "unstructured": "Sherman, F. Getting started with yeast. Methods Enzymol. 194, 3\u201321 (1991).",
      "journal-title": "Methods Enzymol."
    },
    {
      "key": "BFncomms4396_CR49",
      "doi-asserted-by": "publisher",
      "first-page": "1048",
      "DOI": "10.1016/j.bbrc.2010.05.061",
      "volume": "396",
      "author": "K Fukunaga",
      "year": "2010",
      "unstructured": "Fukunaga, K., Kudo, T., Toh-e, A., Tanaka, K. & Saeki, Y. Dissection of the assembly pathway of the proteasome lid in Saccharomyces cerevisiae. Biochem. Biophys. Res. Commun. 396, 1048\u20131053 (2010).",
      "journal-title": "Biochem. Biophys. Res. Commun."
    },
    {
      "key": "BFncomms4396_CR50",
      "doi-asserted-by": "publisher",
      "first-page": "149",
      "DOI": "10.1016/0076-6879(91)94013-3",
      "volume": "194",
      "author": "TD Fox",
      "year": "1991",
      "unstructured": "Fox, T. D. et al. Analysis and manipulation of yeast mitochondrial genes. Methods Enzymol. 194, 149\u2013165 (1991).",
      "journal-title": "Methods Enzymol."
    },
    {
      "key": "BFncomms4396_CR51",
      "doi-asserted-by": "publisher",
      "first-page": "1085",
      "DOI": "10.1111/j.1365-2443.2006.01004.x",
      "volume": "11",
      "author": "S Kawai-Noma",
      "year": "2006",
      "unstructured": "Kawai-Noma, S. et al. Dynamics of yeast prion aggregates in single living cells. Genes Cells 11, 1085\u20131096 (2006).",
      "journal-title": "Genes Cells"
    },
    {
      "key": "BFncomms4396_CR52",
      "doi-asserted-by": "crossref",
      "first-page": "87",
      "DOI": "10.1016/S1016-8478(23)13968-9",
      "volume": "26",
      "author": "H Park",
      "year": "2008",
      "unstructured": "Park, H., Pack, C., Kinjo, M. & Kaang, B. K. In vivo quantitative analysis of PKA subunit interaction and cAMP level by dual color fluorescence cross correlation spectroscopy. Mol. Cells 26, 87\u201392 (2008).",
      "journal-title": "Mol. Cells"
    },
    {
      "key": "BFncomms4396_CR53",
      "doi-asserted-by": "publisher",
      "first-page": "587",
      "DOI": "10.1083/jcb.200709177",
      "volume": "182",
      "author": "Y Noda",
      "year": "2008",
      "unstructured": "Noda, Y. et al. Reciprocal interaction with G-actin and tropomyosin is essential for aquaporin-2 trafficking. J. Cell Biol. 182, 587\u2013601 (2008).",
      "journal-title": "J. Cell Biol."
    },
    {
      "key": "BFncomms4396_CR54",
      "doi-asserted-by": "publisher",
      "first-page": "13573",
      "DOI": "10.1073/pnas.95.23.13573",
      "volume": "95",
      "author": "U Haupts",
      "year": "1998",
      "unstructured": "Haupts, U., Maiti, S., Schwille, P. & Webb, W. W. Dynamics of fluorescence fluctuations in green fluorescent protein observed by fluorescence correlation spectroscopy. Proc. Natl Acad. Sci. USA 95, 13573\u201313578 (1998).",
      "journal-title": "Proc. Natl Acad. Sci. USA"
    },
    {
      "key": "BFncomms4396_CR55",
      "doi-asserted-by": "publisher",
      "first-page": "247",
      "DOI": "10.1002/(SICI)1097-0320(19990701)36:3<247::AID-CYTO15>3.0.CO;2-#",
      "volume": "36",
      "author": "CG Pack",
      "year": "1999",
      "unstructured": "Pack, C. G. et al. Analysis of interaction between chaperonin GroEL and its substrate using fluorescence correlation spectroscopy. Cytometry 36, 247\u2013253 (1999).",
      "journal-title": "Cytometry"
    },
    {
      "key": "BFncomms4396_CR56",
      "doi-asserted-by": "publisher",
      "first-page": "223",
      "DOI": "10.1083/jcb.201002149",
      "volume": "190",
      "author": "S Kawai-Noma",
      "year": "2010",
      "unstructured": "Kawai-Noma, S. et al. In vivo evidence for the fibrillar structures of Sup35 prions in yeast cells. J. Cell Biol. 190, 223\u2013231 (2010).",
      "journal-title": "J. Cell Biol."
    },
    {
      "key": "BFncomms4396_CR57",
      "doi-asserted-by": "publisher",
      "first-page": "215",
      "DOI": "10.1016/S0076-6879(05)99014-9",
      "volume": "399",
      "author": "Y Saeki",
      "year": "2005",
      "unstructured": "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\u2013227 (2005).",
      "journal-title": "Methods Enzymol."
    },
    {
      "key": "BFncomms4396_CR58",
      "doi-asserted-by": "publisher",
      "first-page": "977",
      "DOI": "10.1038/nprot.2008.62",
      "volume": "3",
      "author": "SH Scheres",
      "year": "2008",
      "unstructured": "Scheres, S. H., Nunez-Ramirez, R., Sorzano, C. O., Carazo, J. M. & Marabini, R. Image processing for electron microscopy single-particle analysis using XMIPP. Nat. Protoc. 3, 977\u2013990 (2008).",
      "journal-title": "Nat. Protoc."
    }
  ],
  "container-title": "Nature Communications",
  "original-title": [],
  "language": "en",
  "link": [
    {
      "URL": "https://www.nature.com/articles/ncomms4396.pdf",
      "content-type": "application/pdf",
      "content-version": "vor",
      "intended-application": "text-mining"
    },
    {
      "URL": "https://www.nature.com/articles/ncomms4396",
      "content-type": "text/html",
      "content-version": "vor",
      "intended-application": "text-mining"
    },
    {
      "URL": "https://www.nature.com/articles/ncomms4396.pdf",
      "content-type": "application/pdf",
      "content-version": "vor",
      "intended-application": "similarity-checking"
    }
  ],
  "deposited": {
    "date-parts": [
      [
        2024,
        5,
        24
      ]
    ],
    "date-time": "2024-05-24T20:58:49Z",
    "timestamp": 1716584329000
  },
  "score": 1,
  "resource": {
    "primary": {
      "URL": "https://www.nature.com/articles/ncomms4396"
    }
  },
  "subtitle": [],
  "short-title": [],
  "issued": {
    "date-parts": [
      [
        2014,
        3,
        6
      ]
    ]
  },
  "references-count": 58,
  "journal-issue": {
    "issue": "1",
    "published-online": {
      "date-parts": [
        [
          2014,
          5,
          20
        ]
      ]
    }
  },
  "alternative-id": [
    "BFncomms4396"
  ],
  "URL": "http://dx.doi.org/10.1038/ncomms4396",
  "relation": {},
  "ISSN": [
    "2041-1723"
  ],
  "subject": [],
  "container-title-short": "Nat Commun",
  "published": {
    "date-parts": [
      [
        2014,
        3,
        6
      ]
    ]
  },
  "assertion": [
    {
      "value": "26 December 2013",
      "order": 1,
      "name": "received",
      "label": "Received",
      "group": {
        "name": "ArticleHistory",
        "label": "Article History"
      }
    },
    {
      "value": "6 February 2014",
      "order": 2,
      "name": "accepted",
      "label": "Accepted",
      "group": {
        "name": "ArticleHistory",
        "label": "Article History"
      }
    },
    {
      "value": "6 March 2014",
      "order": 3,
      "name": "first_online",
      "label": "First Online",
      "group": {
        "name": "ArticleHistory",
        "label": "Article History"
      }
    },
    {
      "value": "The authors declare no competing financial interests.",
      "order": 1,
      "name": "Ethics",
      "group": {
        "name": "EthicsHeading",
        "label": "Competing interests"
      }
    }
  ],
  "article-number": "3396"
}