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Volumn 351, Issue 6275, 2016, Pages

Rpn1 provides adjacent receptor sites for substrate binding and deubiquitination by the proteasome

Author keywords

[No Author keywords available]

Indexed keywords

DEUBIQUITINASE; LYSINE; PROTEASOME; PROTEIN; RAD23 PROTEIN; RPN1 PROTEIN; UBIQUITIN; UBP6 PROTEIN; UNCLASSIFIED DRUG; DNA BINDING PROTEIN; PROTEINASE; RAD23 PROTEIN, S CEREVISIAE; RPN1 PROTEIN, S CEREVISIAE; SACCHAROMYCES CEREVISIAE PROTEIN; UBP6 PROTEIN, S CEREVISIAE;

EID: 84959019581     PISSN: 00368075     EISSN: 10959203     Source Type: Journal    
DOI: 10.1126/science.aad9421     Document Type: Article
Times cited : (223)

References (49)
  • 1
    • 84909949812 scopus 로고    scopus 로고
    • Meta-analysis of Ubiquilin1 gene polymorphism and Alzheimer's disease risk
    • pmid: 25387430
    • T. Zhang, Y. Jia, Meta-analysis of Ubiquilin1 gene polymorphism and Alzheimer's disease risk. Med. Sci. Monit. 20, 2250-2255 (2014). doi: 10.12659/MSM.891030; pmid: 25387430
    • (2014) Med. Sci. Monit. , vol.20 , pp. 2250-2255
    • Zhang, T.1    Jia, Y.2
  • 2
    • 80052580969 scopus 로고    scopus 로고
    • Mutations in UBQLN2 cause dominant X-linked juvenile and adult-onset ALS and ALS/dementia
    • pmid: 21857683
    • H.-X. Deng et al., Mutations in UBQLN2 cause dominant X-linked juvenile and adult-onset ALS and ALS/dementia. Nature 477, 211-215 (2011). doi: 10.1038/nature10353; pmid: 21857683
    • (2011) Nature , vol.477 , pp. 211-215
    • Deng, H.-X.1
  • 3
    • 0028235965 scopus 로고
    • A 26 S protease subunit that binds ubiquitin conjugates
    • pmid: 8125911
    • Q. Deveraux, V. Ustrell, C. Pickart, M. Rechsteiner, A 26 S protease subunit that binds ubiquitin conjugates. J. Biol. Chem. 269, 7059-7061 (1994). pmid: 8125911
    • (1994) J. Biol. Chem. , vol.269 , pp. 7059-7061
    • Deveraux, Q.1    Ustrell, V.2    Pickart, C.3    Rechsteiner, M.4
  • 4
    • 0029806477 scopus 로고    scopus 로고
    • The multiubiquitin-chain-binding protein Mcb1 is a component of the 26S proteasome in Saccharomyces cerevisiae and plays a nonessential, substrate-specific role in protein turnover
    • pmid: 8887631
    • S. Van Nocker et al., The multiubiquitin-chain-binding protein Mcb1 is a component of the 26S proteasome in Saccharomyces cerevisiae and plays a nonessential, substrate-specific role in protein turnover. Mol. Cell. Biol. 16, 6020-6028 (1996). doi: 10.1128/MCB.16.11.6020; pmid: 8887631
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 6020-6028
    • Van Nocker, S.1
  • 5
    • 0031890210 scopus 로고    scopus 로고
    • Multiubiquitin chain binding and protein degradation are mediated by distinct domains within the 26 S proteasome subunit Mcb1
    • pmid: 9442033
    • H. Fu et al., Multiubiquitin chain binding and protein degradation are mediated by distinct domains within the 26 S proteasome subunit Mcb1. J. Biol. Chem. 273, 1970-1981 (1998). doi: 10.1074/jbc.273.4.1970; pmid: 9442033
    • (1998) J. Biol. Chem. , vol.273 , pp. 1970-1981
    • Fu, H.1
  • 6
    • 44349116590 scopus 로고    scopus 로고
    • Proteasome subunit Rpn13 is a novel ubiquitin receptor
    • pmid: 18497817
    • K. Husnjak et al., Proteasome subunit Rpn13 is a novel ubiquitin receptor. Nature 453, 481-488 (2008). doi: 10.1038/nature06926; pmid: 18497817
    • (2008) Nature , vol.453 , pp. 481-488
    • Husnjak, K.1
  • 7
    • 44349094727 scopus 로고    scopus 로고
    • Ubiquitin docking at the proteasome through a novel pleckstrin-homology domain interaction
    • pmid: 18497827
    • P. Schreiner et al., Ubiquitin docking at the proteasome through a novel pleckstrin-homology domain interaction. Nature 453, 548-552 (2008). doi: 10.1038/nature06924; pmid: 18497827
    • (2008) Nature , vol.453 , pp. 548-552
    • Schreiner, P.1
  • 8
    • 3042677641 scopus 로고    scopus 로고
    • Rad23 and Rpn10 serve as alternative ubiquitin receptors for the proteasome
    • pmid: 15117949
    • S. Elsasser, D. Chandler-Militello, B. Müller, J. Hanna, D. Finley, Rad23 and Rpn10 serve as alternative ubiquitin receptors for the proteasome. J. Biol. Chem. 279, 26817-26822 (2004). doi: 10.1074/jbc.M404020200; pmid: 15117949
    • (2004) J. Biol. Chem. , vol.279 , pp. 26817-26822
    • Elsasser, S.1    Chandler-Militello, D.2    Müller, B.3    Hanna, J.4    Finley, D.5
  • 9
    • 3142566639 scopus 로고    scopus 로고
    • Multiubiquitin chain receptors define a layer of substrate selectivity in the ubiquitin-proteasome system
    • pmid: 15242647
    • R. Verma, R. Oania, J. Graumann, R. J. Deshaies, Multiubiquitin chain receptors define a layer of substrate selectivity in the ubiquitin-proteasome system. Cell 118, 99-110 (2004). doi: 10.1016/j.cell.2004.06.014; pmid: 15242647
    • (2004) Cell , vol.118 , pp. 99-110
    • Verma, R.1    Oania, R.2    Graumann, J.3    Deshaies, R.J.4
  • 10
    • 0037154160 scopus 로고    scopus 로고
    • Budding yeast Dsk2p is a polyubiquitin-binding protein that can interact with the proteasome
    • pmid: 11805328
    • M. Funakoshi, T. Sasaki, T. Nishimoto, H. Kobayashi, Budding yeast Dsk2p is a polyubiquitin-binding protein that can interact with the proteasome. Proc. Natl. Acad. Sci. U.S.A. 99, 745-750 (2002). doi: 10.1073/pnas.012585199; pmid: 11805328
    • (2002) Proc. Natl. Acad. Sci. U.S.A. , vol.99 , pp. 745-750
    • Funakoshi, M.1    Sasaki, T.2    Nishimoto, T.3    Kobayashi, H.4
  • 11
    • 20444417275 scopus 로고    scopus 로고
    • The DNA damage-inducible UbL-UbA protein Ddi1 participates in Mec1-mediated degradation of Ho endonuclease
    • pmid: 15964793
    • L. Kaplun et al., The DNA damage-inducible UbL-UbA protein Ddi1 participates in Mec1-mediated degradation of Ho endonuclease. Mol. Cell. Biol. 25, 5355-5362 (2005). doi: 10.1128/MCB.25.13.5355-5362.2005; pmid: 15964793
    • (2005) Mol. Cell. Biol. , vol.25 , pp. 5355-5362
    • Kaplun, L.1
  • 12
    • 84864003919 scopus 로고    scopus 로고
    • Transfer of Ho endonuclease and Ufo1 to the proteasome by the UbL-UbA shuttle protein, Ddi1, analysed by complex formation in vitro
    • pmid: 22815701
    • O. Voloshin, A. Bakhrat, S. Herrmann, D. Raveh, Transfer of Ho endonuclease and Ufo1 to the proteasome by the UbL-UbA shuttle protein, Ddi1, analysed by complex formation in vitro. PLOS ONE 7, e39210 (2012). doi: 10.1371/journal. pone.0039210; pmid: 22815701
    • (2012) PLOS ONE , vol.7 , pp. e39210
    • Voloshin, O.1    Bakhrat, A.2    Herrmann, S.3    Raveh, D.4
  • 13
    • 11844263929 scopus 로고    scopus 로고
    • A series of ubiquitin binding factors connects CDC48/p97 to substrate multiubiquitylation and proteasomal targeting
    • pmid: 15652483
    • H. Richly et al., A series of ubiquitin binding factors connects CDC48/p97 to substrate multiubiquitylation and proteasomal targeting. Cell 120, 73-84 (2005). doi: 10.1016/j.cell.2004.11.013; pmid: 15652483
    • (2005) Cell , vol.120 , pp. 73-84
    • Richly, H.1
  • 14
    • 84922539969 scopus 로고    scopus 로고
    • Dss1 is a 26S proteasome ubiquitin receptor
    • pmid: 25306921
    • K. Paraskevopoulos et al., Dss1 is a 26S proteasome ubiquitin receptor. Mol. Cell 56, 453-461 (2014). doi: 10.1016/j.molcel.2014.09.008; pmid: 25306921
    • (2014) Mol. Cell , vol.56 , pp. 453-461
    • Paraskevopoulos, K.1
  • 15
    • 28844484999 scopus 로고    scopus 로고
    • Preparation of ubiquitinated substrates by the PY motif-insertion method for monitoring 26S proteasome activity
    • pmid: 16338358
    • Y. Saeki, E. Isono, A. Toh-E, Preparation of ubiquitinated substrates by the PY motif-insertion method for monitoring 26S proteasome activity. Methods Enzymol. 399, 215-227 (2005). doi: 10.1016/S0076-6879(05)99014-9; pmid: 16338358
    • (2005) Methods Enzymol. , vol.399 , pp. 215-227
    • Saeki, Y.1    Isono, E.2    Toh-E, A.3
  • 16
    • 0036713383 scopus 로고    scopus 로고
    • Proteasome subunit Rpn1 binds ubiquitin-like protein domains
    • pmid: 12198498
    • S. Elsasser et al., Proteasome subunit Rpn1 binds ubiquitin-like protein domains. Nat. Cell Biol. 4, 725-730 (2002). doi: 10.1038/ncb845; pmid: 12198498
    • (2002) Nat. Cell Biol. , vol.4 , pp. 725-730
    • Elsasser, S.1
  • 17
    • 79957637389 scopus 로고    scopus 로고
    • Identification of a functional docking site in the Rpn1 LRR domain for the UBA-UBL domain protein Ddi1
    • pmid: 21627799
    • T. A. Gomez, N. Kolawa, M. Gee, M. J. Sweredoski, R. J. Deshaies, Identification of a functional docking site in the Rpn1 LRR domain for the UBA-UBL domain protein Ddi1. BMC Biol. 9, 33 (2011). doi: 10.1186/1741-7007-9-33; pmid: 21627799
    • (2011) BMC Biol. , vol.9 , pp. 33
    • Gomez, T.A.1    Kolawa, N.2    Gee, M.3    Sweredoski, M.J.4    Deshaies, R.J.5
  • 18
    • 84860376787 scopus 로고    scopus 로고
    • Rpn1 and Rpn2 coordinate ubiquitin processing factors at proteasome
    • pmid: 22318722
    • R. Rosenzweig, V. Bronner, D. Zhang, D. Fushman, M. H. Glickman, Rpn1 and Rpn2 coordinate ubiquitin processing factors at proteasome. J. Biol. Chem. 287, 14659-14671 (2012). doi: 10.1074/jbc.M111.316323; pmid: 22318722
    • (2012) J. Biol. Chem. , vol.287 , pp. 14659-14671
    • Rosenzweig, R.1    Bronner, V.2    Zhang, D.3    Fushman, D.4    Glickman, M.H.5
  • 19
    • 84857935771 scopus 로고    scopus 로고
    • The structure of the 26S proteasome subunit Rpn2 reveals its PC repeat domain as a closed toroid of two concentric a-helical rings
    • pmid: 22405010
    • J. He et al., The structure of the 26S proteasome subunit Rpn2 reveals its PC repeat domain as a closed toroid of two concentric a-helical rings. Structure 20, 513-521 (2012). doi: 10.1016/j.str.2011.12.015; pmid: 22405010
    • (2012) Structure , vol.20 , pp. 513-521
    • He, J.1
  • 20
    • 0037147328 scopus 로고    scopus 로고
    • What curves alpha-solenoids? Evidence for an alpha-helical toroid structure of Rpn1 and Rpn2 proteins of the 26 S proteasome
    • pmid: 12270919
    • A. V. Kajava, What curves alpha-solenoids? Evidence for an alpha-helical toroid structure of Rpn1 and Rpn2 proteins of the 26 S proteasome. J. Biol. Chem. 277, 49791-49798 (2002). doi: 10.1074/jbc.M204982200; pmid: 12270919
    • (2002) J. Biol. Chem. , vol.277 , pp. 49791-49798
    • Kajava, A.V.1
  • 21
    • 17144417404 scopus 로고    scopus 로고
    • Structure of S5a bound to monoubiquitin provides a model for polyubiquitin recognition
    • pmid: 15826667
    • Q. Wang, P. Young, K. J. Walters, Structure of S5a bound to monoubiquitin provides a model for polyubiquitin recognition. J. Mol. Biol. 348, 727-739 (2005). doi: 10.1016/j.jmb.2005.03.007; pmid: 15826667
    • (2005) J. Mol. Biol. , vol.348 , pp. 727-739
    • Wang, Q.1    Young, P.2    Walters, K.J.3
  • 22
    • 84863281982 scopus 로고    scopus 로고
    • Identifying and studying ubiquitin receptors by NMR
    • pmid: 22350893
    • X. Chen, K. J. Walters, Identifying and studying ubiquitin receptors by NMR. Methods Mol. Biol. 832, 279-303 (2012). doi: 10.1007/978-1-61779-474-2-20; pmid: 22350893
    • (2012) Methods Mol. Biol. , vol.832 , pp. 279-303
    • Chen, X.1    Walters, K.J.2
  • 23
    • 77954757965 scopus 로고    scopus 로고
    • Multitasking with ubiquitin through multivalent interactions
    • pmid: 20181483
    • F. Liu, K. J. Walters, Multitasking with ubiquitin through multivalent interactions. Trends Biochem. Sci. 35, 352-360 (2010). pmid: 20181483
    • (2010) Trends Biochem. Sci. , vol.35 , pp. 352-360
    • Liu, F.1    Walters, K.J.2
  • 24
    • 72149114101 scopus 로고    scopus 로고
    • Together Rpn10 and Dsk2 can serve as a polyubiquitin chain-length sensor
    • pmid: 20064467
    • D. Zhang et al., Together, Rpn10 and Dsk2 can serve as a polyubiquitin chain-length sensor. Mol. Cell 36, 1018-1033 (2009). pmid: 20064467
    • (2009) Mol. Cell , vol.36 , pp. 1018-1033
    • Zhang, D.1
  • 25
    • 33745742269 scopus 로고    scopus 로고
    • Quantitative analysis of in vitro ubiquitinated cyclin B1 reveals complex chain topology
    • pmid: 16799550
    • D. S. Kirkpatrick et al., Quantitative analysis of in vitro ubiquitinated cyclin B1 reveals complex chain topology. Nat. Cell Biol. 8, 700-710 (2006). doi: 10.1038/ncb1436; pmid: 16799550
    • (2006) Nat. Cell Biol. , vol.8 , pp. 700-710
    • Kirkpatrick, D.S.1
  • 26
    • 33749049581 scopus 로고    scopus 로고
    • Deubiquitinating enzyme Ubp6 functions noncatalytically to delay proteasomal degradation
    • pmid: 17018280
    • J. Hanna et al., Deubiquitinating enzyme Ubp6 functions noncatalytically to delay proteasomal degradation. Cell 127, 99-111 (2006). doi: 10.1016/j.cell.2006.07.038; pmid: 17018280
    • (2006) Cell , vol.127 , pp. 99-111
    • Hanna, J.1
  • 27
    • 84862776836 scopus 로고    scopus 로고
    • APC/C-mediated multiple monoubiquitylation provides an alternative degradation signal for cyclin B1
    • pmid: 22286100
    • N. V. Dimova et al., APC/C-mediated multiple monoubiquitylation provides an alternative degradation signal for cyclin B1. Nat. Cell Biol. 14, 168-176 (2012). doi: 10.1038/ncb2425; pmid: 22286100
    • (2012) Nat. Cell Biol. , vol.14 , pp. 168-176
    • Dimova, N.V.1
  • 28
    • 0032879814 scopus 로고    scopus 로고
    • Pleiotropic defects caused by loss of the proteasome-interacting factors Rad23 and Rpn10 of Saccharomyces cerevisiae
    • pmid: 10471701
    • D. Lambertson, L. Chen, K. Madura, Pleiotropic defects caused by loss of the proteasome-interacting factors Rad23 and Rpn10 of Saccharomyces cerevisiae. Genetics 153, 69-79 (1999). pmid: 10471701
    • (1999) Genetics , vol.153 , pp. 69-79
    • Lambertson, D.1    Chen, L.2    Madura, K.3
  • 29
    • 55049090325 scopus 로고    scopus 로고
    • Extraproteasomal Rpn10 restricts access of the polyubiquitin-binding protein Dsk2 to proteasome
    • pmid: 18995839
    • Y. Matiuhin et al., Extraproteasomal Rpn10 restricts access of the polyubiquitin-binding protein Dsk2 to proteasome. Mol. Cell 32, 415-425 (2008). doi: 10.1016/j.molcel.2008.10.011; pmid: 18995839
    • (2008) Mol. Cell , vol.32 , pp. 415-425
    • Matiuhin, Y.1
  • 30
    • 0142215475 scopus 로고    scopus 로고
    • Global analysis of protein expression in yeast
    • pmid: 14562106
    • S. Ghaemmaghami et al., Global analysis of protein expression in yeast. Nature 425, 737-741 (2003). doi: 10.1038/nature02046; pmid: 14562106
    • (2003) Nature , vol.425 , pp. 737-741
    • Ghaemmaghami, S.1
  • 31
    • 0035876040 scopus 로고    scopus 로고
    • The 19S complex of the proteasome regulates nucleotide excision repair in yeast
    • pmid: 11410533
    • T. G. Gillette et al., The 19S complex of the proteasome regulates nucleotide excision repair in yeast. Genes Dev. 15, 1528-1539 (2001). doi: 10.1101/gad.869601; pmid: 11410533
    • (2001) Genes Dev. , vol.15 , pp. 1528-1539
    • Gillette, T.G.1
  • 32
    • 68349135106 scopus 로고    scopus 로고
    • Structure of the S5a:K48-linked diubiquitin complex and its interactions with Rpn13
    • pmid: 19683493
    • N. Zhang et al., Structure of the S5a:K48-linked diubiquitin complex and its interactions with Rpn13. Mol. Cell 35, 280-290 (2009). doi: 10.1016/j.molcel.2009.06.010; pmid: 19683493
    • (2009) Mol. Cell , vol.35 , pp. 280-290
    • Zhang, N.1
  • 33
    • 84952639230 scopus 로고    scopus 로고
    • Gates, channels, and switches: Elements of the proteasome machine
    • pmid: 26643069
    • D. Finley, X. Chen, K. J. Walters, Gates, channels, and switches: Elements of the proteasome machine. Trends Biochem. Sci. 41, 77-93 (2016). doi: 10.1016/j.tibs.2015.10.009; pmid: 26643069
    • (2016) Trends Biochem. Sci. , vol.41 , pp. 77-93
    • Finley, D.1    Chen, X.2    Walters, K.J.3
  • 34
    • 0036753063 scopus 로고    scopus 로고
    • Multiple associated proteins regulate proteasome structure and function
    • pmid: 12408819
    • D. S. Leggett et al., Multiple associated proteins regulate proteasome structure and function. Mol. Cell 10, 495-507 (2002). doi: 10.1016/S1097-2765(02)00638-X; pmid: 12408819
    • (2002) Mol. Cell , vol.10 , pp. 495-507
    • Leggett, D.S.1
  • 35
    • 84937111175 scopus 로고    scopus 로고
    • Structural characterization of the interaction of Ubp6 with the 26S proteasome
    • pmid: 26130806
    • A. Aufderheide et al., Structural characterization of the interaction of Ubp6 with the 26S proteasome. Proc. Natl. Acad. Sci. U.S.A. 112, 8626-8631 (2015). doi: 10.1073/pnas.1510449112; pmid: 26130806
    • (2015) Proc. Natl. Acad. Sci. U.S.A. , vol.112 , pp. 8626-8631
    • Aufderheide, A.1
  • 36
    • 84940984237 scopus 로고    scopus 로고
    • Ubp6 deubiquitinase controls conformational dynamics and substrate degradation of the 26S proteasome
    • pmid: 26301997
    • C. Bashore et al., Ubp6 deubiquitinase controls conformational dynamics and substrate degradation of the 26S proteasome. Nat. Struct. Mol. Biol. 22, 712-719 (2015). doi: 10.1038/nsmb.3075; pmid: 26301997
    • (2015) Nat. Struct. Mol. Biol. , vol.22 , pp. 712-719
    • Bashore, C.1
  • 37
    • 79951887389 scopus 로고    scopus 로고
    • Hydrogen exchange mass spectrometry for studying protein structure and dynamics
    • pmid: 21173980
    • L. Konermann, J. Pan, Y.-H. Liu, Hydrogen exchange mass spectrometry for studying protein structure and dynamics. Chem. Soc. Rev. 40, 1224-1234 (2011). doi: 10.1039/C0CS00113A; pmid: 21173980
    • (2011) Chem. Soc. Rev. , vol.40 , pp. 1224-1234
    • Konermann, L.1    Pan, J.2    Liu, Y.-H.3
  • 38
    • 84858277365 scopus 로고    scopus 로고
    • Probing protein interactions with hydrogen/deuterium exchange and mass spectrometry-A review
    • pmid: 22405295
    • A. J. Percy, M. Rey, K. M. Burns, D. C. Schriemer, Probing protein interactions with hydrogen/deuterium exchange and mass spectrometry-a review. Anal. Chim. Acta 721, 7-21 (2012). doi: 10.1016/j.aca.2012.01.037; pmid: 22405295
    • (2012) Anal. Chim. Acta , vol.721 , pp. 7-21
    • Percy, A.J.1    Rey, M.2    Burns, K.M.3    Schriemer, D.C.4
  • 39
    • 33644761306 scopus 로고    scopus 로고
    • Hydrogen exchange mass spectrometry for the analysis of protein dynamics
    • pmid: 16208684
    • T. E. Wales, J. R. Engen, Hydrogen exchange mass spectrometry for the analysis of protein dynamics. Mass Spectrom. Rev. 25, 158-170 (2006). doi: 10.1002/mas.20064; pmid: 16208684
    • (2006) Mass Spectrom. Rev. , vol.25 , pp. 158-170
    • Wales, T.E.1    Engen, J.R.2
  • 40
    • 84862520497 scopus 로고    scopus 로고
    • Protein hydrogen exchange: Testing current models
    • pmid: 22544567
    • J. J. Skinner, W. K. Lim, S. Bédard, B. E. Black, S. W. Englander, Protein hydrogen exchange: Testing current models. Protein Sci. 21, 987-995 (2012). doi: 10.1002/pro.2082; pmid: 22544567
    • (2012) Protein Sci. , vol.21 , pp. 987-995
    • Skinner, J.J.1    Lim, W.K.2    Bédard, S.3    Black, B.E.4    Englander, S.W.5
  • 41
    • 49549086897 scopus 로고    scopus 로고
    • Protein structure and dynamics studied by mass spectrometry: H/D exchange, hydroxyl radical labeling, and related approaches
    • pmid: 18523973
    • L. Konermann, X. Tong, Y. Pan, Protein structure and dynamics studied by mass spectrometry: H/D exchange, hydroxyl radical labeling, and related approaches. J. Mass Spectrom. 43, 1021-1036 (2008). doi: 10.1002/jms.1435; pmid: 18523973
    • (2008) J. Mass Spectrom. , vol.43 , pp. 1021-1036
    • Konermann, L.1    Tong, X.2    Pan, Y.3
  • 42
    • 33749326831 scopus 로고    scopus 로고
    • Identification and characterization of EX1 kinetics in H/D exchange mass spectrometry by peak width analysis
    • pmid: 16875839
    • D. D. Weis, T. E. Wales, J. R. Engen, M. Hotchko, L. F. Ten Eyck, Identification and characterization of EX1 kinetics in H/D exchange mass spectrometry by peak width analysis. J. Am. Soc. Mass Spectrom. 17, 1498-1509 (2006). doi: 10.1016/j.jasms.2006.05.014; pmid: 16875839
    • (2006) J. Am. Soc. Mass Spectrom. , vol.17 , pp. 1498-1509
    • Weis, D.D.1    Wales, T.E.2    Engen, J.R.3    Hotchko, M.4    Ten Eyck, L.F.5
  • 43
    • 13244258262 scopus 로고    scopus 로고
    • Mapping protein energy landscapes with amide hydrogen exchange and mass spectrometry: I. A generalized model for a two-state protein and comparison with experiment
    • pmid: 15659380
    • H. Xiao et al., Mapping protein energy landscapes with amide hydrogen exchange and mass spectrometry: I. A generalized model for a two-state protein and comparison with experiment. Protein Sci. 14, 543-557 (2005). doi: 10.1110/ps.041001705; pmid: 15659380
    • (2005) Protein Sci. , vol.14 , pp. 543-557
    • Xiao, H.1
  • 44
    • 33645073892 scopus 로고    scopus 로고
    • Partial unfolding of diverse SH3 domains on a wide timescale
    • pmid: 16487539
    • T. E. Wales, J. R. Engen, Partial unfolding of diverse SH3 domains on a wide timescale. J. Mol. Biol. 357, 1592-1604 (2006). doi: 10.1016/j.jmb.2006.01.075; pmid: 16487539
    • (2006) J. Mol. Biol. , vol.357 , pp. 1592-1604
    • Wales, T.E.1    Engen, J.R.2
  • 45
    • 84927535922 scopus 로고    scopus 로고
    • Substrate degradation by the proteasome: A single-molecule kinetic analysis
    • pmid: 25859050
    • Y. Lu, B. H. Lee, R. W. King, D. Finley, M. W. Kirschner, Substrate degradation by the proteasome: A single-molecule kinetic analysis. Science 348, 1250834 (2015). doi: 10.1126/science.1250834; pmid: 25859050
    • (2015) Science , vol.348 , pp. 1250834
    • Lu, Y.1    Lee, B.H.2    King, R.W.3    Finley, D.4    Kirschner, M.W.5
  • 46
    • 4344559454 scopus 로고    scopus 로고
    • An unstructured initiation site is required for efficient proteasome-mediated degradation
    • pmid: 15311270
    • S. Prakash, L. Tian, K. S. Ratliff, R. E. Lehotzky, A. Matouschek, An unstructured initiation site is required for efficient proteasome-mediated degradation. Nat. Struct. Mol. Biol. 11, 830-837 (2004). doi: 10.1038/nsmb814; pmid: 15311270
    • (2004) Nat. Struct. Mol. Biol. , vol.11 , pp. 830-837
    • Prakash, S.1    Tian, L.2    Ratliff, K.S.3    Lehotzky, R.E.4    Matouschek, A.5
  • 47
    • 84898807479 scopus 로고    scopus 로고
    • Deep classification of a large cryo-EM dataset defines the conformational landscape of the 26S proteasome
    • pmid: 24706844
    • P. Unverdorben et al., Deep classification of a large cryo-EM dataset defines the conformational landscape of the 26S proteasome. Proc. Natl. Acad. Sci. U.S.A. 111, 5544-5549 (2014). doi: 10.1073/pnas.1403409111; pmid: 24706844
    • (2014) Proc. Natl. Acad. Sci. U.S.A. , vol.111 , pp. 5544-5549
    • Unverdorben, P.1
  • 48
    • 45849131354 scopus 로고    scopus 로고
    • Recognition dynamics up to microseconds revealed from an RDC-derived ubiquitin ensemble in solution
    • pmid: 18556554
    • O. F. Lange et al., Recognition dynamics up to microseconds revealed from an RDC-derived ubiquitin ensemble in solution. Science 320, 1471-1475 (2008). doi: 10.1126/science.1157092; pmid: 18556554
    • (2008) Science , vol.320 , pp. 1471-1475
    • Lange, O.F.1
  • 49
    • 84955171039 scopus 로고    scopus 로고
    • Mycobacterium tuberculosis copperregulated protein SocB is an intrinsically disordered protein that folds upon interaction with a synthetic phospholipid bilayer
    • Pmid: 26650755
    • U. Nowicka et al., Mycobacterium tuberculosis copperregulated protein SocB is an intrinsically disordered protein that folds upon interaction with a synthetic phospholipid bilayer. Proteins 84, 193-200 (2016). doi: 10.1002/prot.24970; pmid: 26650755
    • (2016) Proteins , vol.84 , pp. 193-200
    • Nowicka, U.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.