메뉴 건너뛰기




Volumn 110, Issue 28, 2013, Pages 11379-11384

Conformational dynamics control ubiquitin-deubiquitinase interactions and influence in vivo signaling

Author keywords

Computational design; Phage display; Protein dynamics; Protein Protein interactions; Ubiquitin signaling

Indexed keywords

DEUBIQUITINASE; ISOPROTEIN; PROTEASOME; UBIQUITIN; UNCLASSIFIED DRUG; USP14 DEUBIQUITINASE;

EID: 84879923631     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1302407110     Document Type: Article
Times cited : (43)

References (35)
  • 1
    • 70350150000 scopus 로고    scopus 로고
    • The emerging complexity of protein ubiquitination
    • Komander D (2009) The emerging complexity of protein ubiquitination. Biochem Soc Trans 37(Pt 5):937-953.
    • (2009) Biochem Soc Trans , vol.37 , Issue.PART 5 , pp. 937-953
    • Komander, D.1
  • 2
    • 82455179484 scopus 로고    scopus 로고
    • Systematic and quantitative assessment of the ubiquitin-modified proteome
    • Kim W, et al. (2011) Systematic and quantitative assessment of the ubiquitin-modified proteome. Mol Cell 44(2):325-340.
    • (2011) Mol Cell , vol.44 , Issue.2 , pp. 325-340
    • Kim, W.1
  • 3
    • 9644272423 scopus 로고    scopus 로고
    • The ubiquitin system: Pathogenesis of human diseases and drug targeting
    • DOI 10.1016/j.bbamcr.2004.09.018, PII S0167488904002344, The Ubiquitin-Proteasome System
    • Ciechanover A, Schwartz AL (2004) The ubiquitin system: Pathogenesis of human diseases and drug targeting. Biochim Biophys Acta 1695(1-3):3-17. (Pubitemid 39574964)
    • (2004) Biochimica et Biophysica Acta - Molecular Cell Research , vol.1695 , Issue.1-3 , pp. 3-17
    • Ciechanover, A.1    Schwartz, A.L.2
  • 4
    • 78049315806 scopus 로고    scopus 로고
    • Ubiquitin becomes ubiquitous in cancer: Emerging roles of ubiquitin ligases and deubiquitinases in tumorigenesis and as therapeutic targets
    • Shi D, Grossman SR (2010) Ubiquitin becomes ubiquitous in cancer: Emerging roles of ubiquitin ligases and deubiquitinases in tumorigenesis and as therapeutic targets. Cancer Biol Ther 10(8):737-747.
    • (2010) Cancer Biol Ther , vol.10 , Issue.8 , pp. 737-747
    • Shi, D.1    Grossman, S.R.2
  • 5
    • 68049084674 scopus 로고    scopus 로고
    • Breaking the chains: Structure and function of the deubiquitinases
    • Komander D, Clague MJ, Urbé S (2009) Breaking the chains: Structure and function of the deubiquitinases. Nat Rev Mol Cell Biol 10(8):550-563.
    • (2009) Nat Rev Mol Cell Biol , vol.10 , Issue.8 , pp. 550-563
    • Komander, D.1    Clague, M.J.2    Urbé, S.3
  • 6
    • 79251473377 scopus 로고    scopus 로고
    • Will the ubiquitin system furnish as many drug targets as protein kinases?
    • Cohen P, Tcherpakov M (2010) Will the ubiquitin system furnish as many drug targets as protein kinases? Cell 143(5):686-693.
    • (2010) Cell , vol.143 , Issue.5 , pp. 686-693
    • Cohen, P.1    Tcherpakov, M.2
  • 7
    • 77956527159 scopus 로고    scopus 로고
    • Enhancement of proteasome activity by a small-molecule inhibitor of USP14
    • Lee B-H, et al. (2010) Enhancement of proteasome activity by a small-molecule inhibitor of USP14. Nature 467(7312):179-184.
    • (2010) Nature , vol.467 , Issue.7312 , pp. 179-184
    • Lee, B.-H.1
  • 8
    • 84856085129 scopus 로고    scopus 로고
    • Inhibition of proteasome deubiquitinating activity as a new cancer therapy
    • D' Arcy P, et al. (2011) Inhibition of proteasome deubiquitinating activity as a new cancer therapy. Nat Med 17(12):1636-1640.
    • (2011) Nat Med , vol.17 , Issue.12 , pp. 1636-1640
    • D'Arcy, P.1
  • 9
    • 34547093612 scopus 로고    scopus 로고
    • Active-site directed probes to report enzymatic action in the ubiquitin proteasome system
    • Ovaa H (2007) Active-site directed probes to report enzymatic action in the ubiquitin proteasome system. Nat Rev Cancer 7(8):613-620.
    • (2007) Nat Rev Cancer , vol.7 , Issue.8 , pp. 613-620
    • Ovaa, H.1
  • 10
    • 33845438397 scopus 로고    scopus 로고
    • Substrate recognition and catalysis by UCH-L1
    • DOI 10.1021/bi061406c
    • Luchansky SJ, Lansbury PT, Jr., Stein RL (2006) Substrate recognition and catalysis by UCH-L1. Biochemistry 45(49):14717-14725. (Pubitemid 44906987)
    • (2006) Biochemistry , vol.45 , Issue.49 , pp. 14717-14725
    • Luchansky, S.J.1    Lansbury Jr., P.T.2    Stein, R.L.3
  • 13
    • 73349117207 scopus 로고    scopus 로고
    • Conformational selection and induced fit mechanism underlie specificity in noncovalent interactions with ubiquitin
    • Wlodarski T, Zagrovic B (2009) Conformational selection and induced fit mechanism underlie specificity in noncovalent interactions with ubiquitin. Proc Natl Acad Sci USA 106(46):19346-19351.
    • (2009) Proc Natl Acad Sci USA , vol.106 , Issue.46 , pp. 19346-19351
    • Wlodarski, T.1    Zagrovic, B.2
  • 14
    • 79955562619 scopus 로고    scopus 로고
    • In silico elucidation of the recognition dynamics of ubiquitin
    • Long D, Brüschweiler R (2011) In silico elucidation of the recognition dynamics of ubiquitin. PLOS Comput Biol 7(4):e1002035.
    • (2011) PLOS Comput Biol , vol.7 , Issue.4
    • Long, D.1    Brüschweiler, R.2
  • 15
    • 84868090870 scopus 로고    scopus 로고
    • Ubiquitin dynamics in complexes reveal molecular recognition mechanisms beyond induced fit and conformational selection
    • Peters JH, de Groot BL (2012) Ubiquitin dynamics in complexes reveal molecular recognition mechanisms beyond induced fit and conformational selection. PLOS Comput Biol 8(10):e1002704.
    • (2012) PLOS Comput Biol , vol.8 , Issue.10
    • Peters, J.H.1    De Groot, B.L.2
  • 17
    • 77955578700 scopus 로고    scopus 로고
    • Ubiquitin - Molecular mechanisms for recognition of different structures
    • Perica T, Chothia C (2010) Ubiquitin - molecular mechanisms for recognition of different structures. Curr Opin Struct Biol 20(3):367-376.
    • (2010) Curr Opin Struct Biol , vol.20 , Issue.3 , pp. 367-376
    • Perica, T.1    Chothia, C.2
  • 18
    • 84865781586 scopus 로고    scopus 로고
    • Structure of a RING E3 ligase and ubiquitin-loaded E2 primed for catalysis
    • Plechanovová A, Jaffray EG, Tatham MH, Naismith JH, Hay RT (2012) Structure of a RING E3 ligase and ubiquitin-loaded E2 primed for catalysis. Nature 489(7414):115-120.
    • (2012) Nature , vol.489 , Issue.7414 , pp. 115-120
    • Plechanovová, A.1    Jaffray, E.G.2    Tatham, M.H.3    Naismith, J.H.4    Hay, R.T.5
  • 20
    • 79959615159 scopus 로고    scopus 로고
    • RosettaScripts: A scripting language interface to the Rosetta macromolecular modeling suite
    • Fleishman SJ, et al. (2011) RosettaScripts: A scripting language interface to the Rosetta macromolecular modeling suite. PLoS ONE 6(6):e20161.
    • (2011) PLoS ONE , vol.6 , Issue.6
    • Fleishman, S.J.1
  • 21
    • 0037217406 scopus 로고    scopus 로고
    • Automated design of specificity in molecular recognition
    • DOI 10.1038/nsb877
    • Havranek JJ, Harbury PB (2003) Automated design of specificity in molecular recognition. Nat Struct Biol 10(1):45-52. (Pubitemid 36034176)
    • (2003) Nature Structural Biology , vol.10 , Issue.1 , pp. 45-52
    • Havranek, J.J.1    Harbury, P.B.2
  • 22
    • 84871298878 scopus 로고    scopus 로고
    • Conformational stabilization of ubiquitin yields potent and selective inhibitors of USP7
    • Zhang Y, et al. (2013) Conformational stabilization of ubiquitin yields potent and selective inhibitors of USP7. Nat Chem Biol 9(1):51-58 http://www.nature.com/doifinder/10.1038/nchembio.1134.
    • (2013) Nat Chem Biol , vol.9 , Issue.1 , pp. 51-58
    • Zhang, Y.1
  • 23
    • 0037470496 scopus 로고    scopus 로고
    • Antibody multispecificity mediated by conformational diversity
    • DOI 10.1126/science.1079731
    • James LC, Roversi P, Tawfik DS (2003) Antibody multispecificity mediated by conformational diversity. Science 299(5611):1362-1367. (Pubitemid 36254643)
    • (2003) Science , vol.299 , Issue.5611 , pp. 1362-1367
    • James, L.C.1    Roversi, P.2    Tawfik, D.S.3
  • 25
    • 69549120472 scopus 로고    scopus 로고
    • Conformational selection or induced fit: A flux description of reaction mechanism
    • Hammes GG, Chang Y-C, Oas TG (2009) Conformational selection or induced fit: A flux description of reaction mechanism. Proc Natl Acad Sci USA 106(33):13737-13741.
    • (2009) Proc Natl Acad Sci USA , vol.106 , Issue.33 , pp. 13737-13741
    • Hammes, G.G.1    Chang, Y.-C.2    Oas, T.G.3
  • 26
    • 80052401629 scopus 로고    scopus 로고
    • Solution structure of a minor and transiently formed state of a T4 lysozyme mutant
    • Bouvignies G, et al. (2011) Solution structure of a minor and transiently formed state of a T4 lysozyme mutant. Nature 477(7362):111-114.
    • (2011) Nature , vol.477 , Issue.7362 , pp. 111-114
    • Bouvignies, G.1
  • 28
    • 0034919305 scopus 로고    scopus 로고
    • Nuclear magnetic resonance methods for quantifying microsecond-to- millisecond motions in biological macromolecules
    • DOI 10.1016/S0076-6879(01)39315-1
    • Palmer AG, 3rd, Kroenke CD, Loria JP (2001) Nuclear magnetic resonance methods for quantifying microsecond-to-millisecond motions in biological macromolecules. Methods Enzymol 339:204-238. (Pubitemid 32666562)
    • (2001) Methods in Enzymology , vol.339 , pp. 204-238
    • Palmer III, A.G.1    Kroenke, C.D.2    Loria, J.P.3
  • 29
    • 70450184385 scopus 로고    scopus 로고
    • Selective characterization of microsecond motions in proteins by NMR relaxation
    • Hansen DF, Feng H, Zhou Z, Bai Y, Kay LE (2009) Selective characterization of microsecond motions in proteins by NMR relaxation. J Am Chem Soc 131(44):16257-16265.
    • (2009) J Am Chem Soc , vol.131 , Issue.44 , pp. 16257-16265
    • Hansen, D.F.1    Feng, H.2    Zhou, Z.3    Bai, Y.4    Kay, L.E.5
  • 30
    • 14144250990 scopus 로고    scopus 로고
    • 1rho relaxation experiments
    • DOI 10.1110/ps.041139505
    • Massi F, Grey MJ, Palmer AG, 3rd (2005) Microsecond timescale backbone conformational dynamics in ubiquitin studied with NMR R1rho relaxation experiments. Protein Sci 14(3):735-742. (Pubitemid 40283912)
    • (2005) Protein Science , vol.14 , Issue.3 , pp. 735-742
    • Massi, F.1    Grey, M.J.2    Palmer III, A.G.3
  • 31
    • 81755177781 scopus 로고    scopus 로고
    • Kinetics of conformational sampling in ubiquitin
    • Ban D, et al. (2011) Kinetics of conformational sampling in ubiquitin. Angew Chem Int Ed Engl 50(48):11437-11440.
    • (2011) Angew Chem Int Ed Engl , vol.50 , Issue.48 , pp. 11437-11440
    • Ban, D.1
  • 32
    • 0344629427 scopus 로고    scopus 로고
    • Ubiquitin depletion as a key mediator of toxicity by translational inhibitors
    • Hanna J, Leggett DS, Finley D (2003) Ubiquitin depletion as a key mediator of toxicity by translational inhibitors. Mol Cell Biol 23(24):9251- 9261.
    • (2003) Mol Cell Biol , vol.23 , Issue.24 , pp. 9251-9261
    • Hanna, J.1    Leggett, D.S.2    Finley, D.3
  • 33
    • 61449172037 scopus 로고    scopus 로고
    • Systematic and integrative analysis of large gene lists using DAVID bioinformatics resources
    • Huang W, Sherman BT, Lempicki RA (2009) Systematic and integrative analysis of large gene lists using DAVID bioinformatics resources. Nat Protoc 4(1):44-57.
    • (2009) Nat Protoc , vol.4 , Issue.1 , pp. 44-57
    • Huang, W.1    Sherman, B.T.2    Lempicki, R.A.3
  • 34
    • 71449103005 scopus 로고    scopus 로고
    • Hidden alternative structures of proline isomerase essential for catalysis
    • Fraser JS, et al. (2009) Hidden alternative structures of proline isomerase essential for catalysis. Nature 462(7273):669-673.
    • (2009) Nature , vol.462 , Issue.7273 , pp. 669-673
    • Fraser, J.S.1
  • 35
    • 84862776988 scopus 로고    scopus 로고
    • Exploiting a natural conformational switch to engineer an interleukin-2 'superkine'
    • Levin AM, et al. (2012) Exploiting a natural conformational switch to engineer an interleukin-2 'superkine' Nature 484(7395):529-533.
    • (2012) Nature , vol.484 , Issue.7395 , pp. 529-533
    • Levin, A.M.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.