메뉴 건너뛰기




Volumn 589, Issue 19, 2015, Pages 2552-2560

Structural disorder and its role in proteasomal degradation

Author keywords

26S proteasome; Disordered protein segment; Low complexity region; Protein degradation; Proteostasis; Structural variability

Indexed keywords

ADENOSINE TRIPHOSPHATASE; CELL PROTEIN; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; INTRINSICALLY DISORDERED PROTEIN; OLIGOSACCHARIDE; PROTEASOME; PROTEASOME INTERACTING PROTEIN; RPN PROTEIN; RPT PROTEIN; UBIQUITIN; UBP6 PROTEIN; UNCLASSIFIED DRUG; ATP DEPENDENT 26S PROTEASE; PROTEIN;

EID: 84942292342     PISSN: 00145793     EISSN: 18733468     Source Type: Journal    
DOI: 10.1016/j.febslet.2015.07.034     Document Type: Review
Times cited : (24)

References (110)
  • 1
    • 0034296394 scopus 로고    scopus 로고
    • Basic medical research award. The ubiquitin system
    • A. Hershko, A. Ciechanover, and A. Varshavsky Basic medical research award. The ubiquitin system Nat. Med. 6 2000 1073 1081
    • (2000) Nat. Med. , vol.6 , pp. 1073-1081
    • Hershko, A.1    Ciechanover, A.2    Varshavsky, A.3
  • 2
    • 33747589184 scopus 로고    scopus 로고
    • The anaphase promoting complex/cyclosome: A machine designed to destroy
    • J.M. Peters The anaphase promoting complex/cyclosome: A machine designed to destroy Nat. Rev. Mol. Cell Biol. 7 2006 644 656
    • (2006) Nat. Rev. Mol. Cell Biol. , vol.7 , pp. 644-656
    • Peters, J.M.1
  • 3
    • 78649357985 scopus 로고    scopus 로고
    • Protein quality control in the cytosol and the endoplasmic reticulum: Brothers in arms
    • A. Buchberger, B. Bukau, and T. Sommer Protein quality control in the cytosol and the endoplasmic reticulum: brothers in arms Mol. Cell 40 2010 238 252
    • (2010) Mol. Cell , vol.40 , pp. 238-252
    • Buchberger, A.1    Bukau, B.2    Sommer, T.3
  • 4
    • 0026068805 scopus 로고
    • Naming a targeting signal
    • A. Varshavsky Naming a targeting signal Cell 64 1991 13 15
    • (1991) Cell , vol.64 , pp. 13-15
    • Varshavsky, A.1
  • 5
    • 11244351579 scopus 로고    scopus 로고
    • Function and regulation of cullin-RING ubiquitin ligases
    • M.D. Petroski, and R.J. Deshaies Function and regulation of cullin-RING ubiquitin ligases Nat. Rev. Mol. Cell Biol. 6 2005 9 20
    • (2005) Nat. Rev. Mol. Cell Biol. , vol.6 , pp. 9-20
    • Petroski, M.D.1    Deshaies, R.J.2
  • 6
    • 79955982521 scopus 로고    scopus 로고
    • Structure, function and mechanism of the anaphase promoting complex (APC/C)
    • D. Barford Structure, function and mechanism of the anaphase promoting complex (APC/C) Q. Rev. Biophys. 44 2011 153 190
    • (2011) Q. Rev. Biophys. , vol.44 , pp. 153-190
    • Barford, D.1
  • 7
    • 0342265782 scopus 로고
    • A soluble ATP-dependent proteolytic system responsible for the degradation of abnormal proteins in reticulocytes
    • J.D. Etlinger, and A.L. Goldberg A soluble ATP-dependent proteolytic system responsible for the degradation of abnormal proteins in reticulocytes Proc. Natl. Acad. Sci. USA 74 1977 54 58
    • (1977) Proc. Natl. Acad. Sci. USA , vol.74 , pp. 54-58
    • Etlinger, J.D.1    Goldberg, A.L.2
  • 9
    • 79951850741 scopus 로고    scopus 로고
    • Defining the geometry of the two-component proteasome degron
    • T. Inobe, S. Fishbain, S. Prakash, and A. Matouschek Defining the geometry of the two-component proteasome degron Nat. Chem. Biol. 7 2011 161 167
    • (2011) Nat. Chem. Biol. , vol.7 , pp. 161-167
    • Inobe, T.1    Fishbain, S.2    Prakash, S.3    Matouschek, A.4
  • 10
    • 0028951190 scopus 로고
    • Methotrexate inhibits proteolysis of dihydrofolate reductase by the N-end rule pathway
    • J.A. Johnston, E.S. Johnson, P.R. Waller, and A. Varshavsky Methotrexate inhibits proteolysis of dihydrofolate reductase by the N-end rule pathway J. Biol. Chem. 270 1995 8172 8178
    • (1995) J. Biol. Chem. , vol.270 , pp. 8172-8178
    • Johnston, J.A.1    Johnson, E.S.2    Waller, P.R.3    Varshavsky, A.4
  • 11
    • 84889025427 scopus 로고    scopus 로고
    • Slippery substrates impair ATP-dependent protease function by slowing unfolding
    • D.A. Kraut Slippery substrates impair ATP-dependent protease function by slowing unfolding J. Biol. Chem. 288 2013 34729 34735
    • (2013) J. Biol. Chem. , vol.288 , pp. 34729-34735
    • Kraut, D.A.1
  • 12
    • 0031904016 scopus 로고    scopus 로고
    • A minimal glycine-alanine repeat prevents the interaction of ubiquitinated I kappaB alpha with the proteasome: A new mechanism for selective inhibition of proteolysis
    • A. Sharipo, M. Imreh, A. Leonchiks, S. Imreh, and M.G. Masucci A minimal glycine-alanine repeat prevents the interaction of ubiquitinated I kappaB alpha with the proteasome: A new mechanism for selective inhibition of proteolysis Nat. Med. 4 1998 939 944
    • (1998) Nat. Med. , vol.4 , pp. 939-944
    • Sharipo, A.1    Imreh, M.2    Leonchiks, A.3    Imreh, S.4    Masucci, M.G.5
  • 13
    • 84883472009 scopus 로고    scopus 로고
    • Unveiling the long-held secrets of the 26S proteasome
    • F. Förster, P. Unverdorben, P. Sledz, and W. Baumeister Unveiling the long-held secrets of the 26S proteasome Structure 21 2013 1551 1562
    • (2013) Structure , vol.21 , pp. 1551-1562
    • Förster, F.1    Unverdorben, P.2    Sledz, P.3    Baumeister, W.4
  • 15
    • 0029042511 scopus 로고
    • Crystal structure of the 20S proteasome from the archaeon T. Acidophilum at 3.4 A resolution
    • J. Lowe, D. Stock, B. Jap, P. Zwickl, W. Baumeister, and R. Huber Crystal structure of the 20S proteasome from the archaeon T. acidophilum at 3.4 A resolution Science 268 1995 533 539
    • (1995) Science , vol.268 , pp. 533-539
    • Lowe, J.1    Stock, D.2    Jap, B.3    Zwickl, P.4    Baumeister, W.5    Huber, R.6
  • 16
    • 0024972956 scopus 로고
    • The multicatalytic proteinase (prosome) is ubiquitous from eukaryotes to archaebacteria
    • B. Dahlmann, F. Kopp, L. Kuehn, B. Niedel, G. Pfeifer, R. Hegerl, and W. Baumeister The multicatalytic proteinase (prosome) is ubiquitous from eukaryotes to archaebacteria FEBS Lett. 251 1989 125 131
    • (1989) FEBS Lett. , vol.251 , pp. 125-131
    • Dahlmann, B.1    Kopp, F.2    Kuehn, L.3    Niedel, B.4    Pfeifer, G.5    Hegerl, R.6    Baumeister, W.7
  • 17
    • 77649243592 scopus 로고    scopus 로고
    • Structure of a Blm10 complex reveals common mechanisms for proteasome binding and gate opening
    • K. Sadre-Bazzaz, F.G. Whitby, H. Robinson, T. Formosa, and C.P. Hill Structure of a Blm10 complex reveals common mechanisms for proteasome binding and gate opening Mol. Cell 37 2010 728 735
    • (2010) Mol. Cell , vol.37 , pp. 728-735
    • Sadre-Bazzaz, K.1    Whitby, F.G.2    Robinson, H.3    Formosa, T.4    Hill, C.P.5
  • 20
    • 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
    • S. van Nocker, S. Sadis, D.M. Rubin, M. Glickman, H. Fu, O. Coux, I. Wefes, D. Finley, and R.D. Vierstra 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 1996 6020 6028
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 6020-6028
    • Van Nocker, S.1    Sadis, S.2    Rubin, D.M.3    Glickman, M.4    Fu, H.5    Coux, O.6    Wefes, I.7    Finley, D.8    Vierstra, R.D.9
  • 24
    • 0037179694 scopus 로고    scopus 로고
    • A cryptic protease couples deubiquitination and degradation by the proteasome
    • T. Yao, and R.E. Cohen A cryptic protease couples deubiquitination and degradation by the proteasome Nature 419 2002 403 407
    • (2002) Nature , vol.419 , pp. 403-407
    • Yao, T.1    Cohen, R.E.2
  • 25
    • 84885094614 scopus 로고    scopus 로고
    • The ATP costs and time required to degrade ubiquitinated proteins by the 26 s proteasome
    • A. Peth, J.A. Nathan, and A.L. Goldberg The ATP costs and time required to degrade ubiquitinated proteins by the 26 s proteasome J. Biol. Chem. 288 2013 29215 29222
    • (2013) J. Biol. Chem. , vol.288 , pp. 29215-29222
    • Peth, A.1    Nathan, J.A.2    Goldberg, A.L.3
  • 28
    • 79959389010 scopus 로고    scopus 로고
    • AAA+ proteases: ATP-fueled machines of protein destruction
    • R.T. Sauer, and T.A. Baker AAA+ proteases: ATP-fueled machines of protein destruction Annu. Rev. Biochem. 80 2011 587 612
    • (2011) Annu. Rev. Biochem. , vol.80 , pp. 587-612
    • Sauer, R.T.1    Baker, T.A.2
  • 33
    • 84880157841 scopus 로고    scopus 로고
    • Conformational switching of the 26S proteasome enables substrate degradation
    • M.E. Matyskiela, G.C. Lander, and A. Martin Conformational switching of the 26S proteasome enables substrate degradation Nat. Struct. Mol. Biol. 20 2013 781 788
    • (2013) Nat. Struct. Mol. Biol. , vol.20 , pp. 781-788
    • Matyskiela, M.E.1    Lander, G.C.2    Martin, A.3
  • 34
    • 84876909425 scopus 로고    scopus 로고
    • Structure of the 26S proteasome with ATP-gammaS bound provides insights into the mechanism of nucleotide-dependent substrate translocation
    • P. Sledz, P. Unverdorben, F. Beck, G. Pfeifer, A. Schweitzer, F. Förster, and W. Baumeister Structure of the 26S proteasome with ATP-gammaS bound provides insights into the mechanism of nucleotide-dependent substrate translocation Proc. Natl. Acad. Sci. USA 110 2013 7264 7269
    • (2013) Proc. Natl. Acad. Sci. USA , vol.110 , pp. 7264-7269
    • Sledz, P.1    Unverdorben, P.2    Beck, F.3    Pfeifer, G.4    Schweitzer, A.5    Förster, F.6    Baumeister, W.7
  • 35
    • 50149086108 scopus 로고    scopus 로고
    • Diversity of degradation signals in the ubiquitin-proteasome system
    • T. Ravid, and M. Hochstrasser Diversity of degradation signals in the ubiquitin-proteasome system Nat. Rev. Mol. Cell Biol. 9 2008 679 690
    • (2008) Nat. Rev. Mol. Cell Biol. , vol.9 , pp. 679-690
    • Ravid, T.1    Hochstrasser, M.2
  • 36
    • 34249695447 scopus 로고    scopus 로고
    • Local structural disorder imparts plasticity on linear motifs
    • M. Fuxreiter, P. Tompa, and I. Simon Local structural disorder imparts plasticity on linear motifs Bioinformatics 23 2007 950 956
    • (2007) Bioinformatics , vol.23 , pp. 950-956
    • Fuxreiter, M.1    Tompa, P.2    Simon, I.3
  • 38
    • 84885588582 scopus 로고    scopus 로고
    • Ubiquitination site preferences in anaphase promoting complex/cyclosome (APC/C) substrates
    • M. Min, U. Mayor, and C. Lindon Ubiquitination site preferences in anaphase promoting complex/cyclosome (APC/C) substrates Open Biol. 3 2013 130097
    • (2013) Open Biol. , vol.3 , pp. 130097
    • Min, M.1    Mayor, U.2    Lindon, C.3
  • 39
    • 84927555890 scopus 로고    scopus 로고
    • Specificity of the anaphase-promoting complex: A single-molecule study
    • Y. Lu, W. Wang, and M.W. Kirschner Specificity of the anaphase-promoting complex: A single-molecule study Science 348 2015 1248737
    • (2015) Science , vol.348 , pp. 1248737
    • Lu, Y.1    Wang, W.2    Kirschner, M.W.3
  • 40
    • 0141838136 scopus 로고    scopus 로고
    • Mathematical modeling suggests cooperative interactions between a disordered polyvalent ligand and a single receptor site
    • P. Klein, T. Pawson, and M. Tyers Mathematical modeling suggests cooperative interactions between a disordered polyvalent ligand and a single receptor site Curr. Biol. 13 2003 1669 1678
    • (2003) Curr. Biol. , vol.13 , pp. 1669-1678
    • Klein, P.1    Pawson, T.2    Tyers, M.3
  • 41
    • 35648993510 scopus 로고    scopus 로고
    • To be, or not to be - molecular chaperones in protein degradation
    • V. Arndt, C. Rogon, and J. Hohfeld To be, or not to be - molecular chaperones in protein degradation Cell. Mol. Life Sci. 64 2007 2525 2541
    • (2007) Cell. Mol. Life Sci. , vol.64 , pp. 2525-2541
    • Arndt, V.1    Rogon, C.2    Hohfeld, J.3
  • 42
    • 64749087257 scopus 로고    scopus 로고
    • Misfolded membrane proteins are specifically recognized by the transmembrane domain of the Hrd1p ubiquitin ligase
    • B.K. Sato, D. Schulz, P.H. Do, and R.Y. Hampton Misfolded membrane proteins are specifically recognized by the transmembrane domain of the Hrd1p ubiquitin ligase Mol. Cell 34 2009 212 222
    • (2009) Mol. Cell , vol.34 , pp. 212-222
    • Sato, B.K.1    Schulz, D.2    Do, P.H.3    Hampton, R.Y.4
  • 43
    • 0027980321 scopus 로고
    • The ubiquitin-proteasome pathway is required for processing the NF-kappa B1 precursor protein and the activation of NF-kappa B
    • V.J. Palombella, O.J. Rando, A.L. Goldberg, and T. Maniatis The ubiquitin-proteasome pathway is required for processing the NF-kappa B1 precursor protein and the activation of NF-kappa B Cell 78 1994 773 785
    • (1994) Cell , vol.78 , pp. 773-785
    • Palombella, V.J.1    Rando, O.J.2    Goldberg, A.L.3    Maniatis, T.4
  • 44
    • 0036091848 scopus 로고    scopus 로고
    • Taking a bite: Proteasomal protein processing
    • M. Rape, and S. Jentsch Taking a bite: proteasomal protein processing Nat. Cell Biol. 4 2002 E113 E116
    • (2002) Nat. Cell Biol. , vol.4 , pp. E113-E116
    • Rape, M.1    Jentsch, S.2
  • 45
    • 33746786326 scopus 로고    scopus 로고
    • Proteasome-mediated protein processing by bidirectional degradation initiated from an internal site
    • W. Piwko, and S. Jentsch Proteasome-mediated protein processing by bidirectional degradation initiated from an internal site Nat. Struct. Mol. Biol. 13 2006 691 697
    • (2006) Nat. Struct. Mol. Biol. , vol.13 , pp. 691-697
    • Piwko, W.1    Jentsch, S.2
  • 46
    • 4344559454 scopus 로고    scopus 로고
    • An unstructured initiation site is required for efficient proteasome-mediated degradation
    • S. Prakash, L. Tian, K.S. Ratliff, R.E. Lehotzky, and A. Matouschek An unstructured initiation site is required for efficient proteasome-mediated degradation Nat. Struct. Mol. Biol. 11 2004 830 837
    • (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
    • 57749102552 scopus 로고    scopus 로고
    • Substrate selection by the proteasome during degradation of protein complexes
    • S. Prakash, T. Inobe, A.J. Hatch, and A. Matouschek Substrate selection by the proteasome during degradation of protein complexes Nat. Chem. Biol. 5 2009 29 36
    • (2009) Nat. Chem. Biol. , vol.5 , pp. 29-36
    • Prakash, S.1    Inobe, T.2    Hatch, A.J.3    Matouschek, A.4
  • 52
    • 0029814693 scopus 로고    scopus 로고
    • Cdc48p interacts with Ufd3p, a WD repeat protein required for ubiquitin-mediated proteolysis in Saccharomyces cerevisiae
    • M. Ghislain, R.J. Dohmen, F. Levy, and A. Varshavsky Cdc48p interacts with Ufd3p, a WD repeat protein required for ubiquitin-mediated proteolysis in Saccharomyces cerevisiae EMBO J. 15 1996 4884 4899
    • (1996) EMBO J. , vol.15 , pp. 4884-4899
    • Ghislain, M.1    Dohmen, R.J.2    Levy, F.3    Varshavsky, A.4
  • 53
    • 23144449583 scopus 로고    scopus 로고
    • Delivery of ubiquitinated substrates to protein-unfolding machines
    • S. Elsasser, and D. Finley Delivery of ubiquitinated substrates to protein-unfolding machines Nat. Cell Biol. 7 2005 742 749
    • (2005) Nat. Cell Biol. , vol.7 , pp. 742-749
    • Elsasser, S.1    Finley, D.2
  • 56
    • 33846216003 scopus 로고    scopus 로고
    • Proteasome substrate degradation requires association plus extended peptide
    • J. Takeuchi, H. Chen, and P. Coffino Proteasome substrate degradation requires association plus extended peptide EMBO J. 26 2007 123 131
    • (2007) EMBO J. , vol.26 , pp. 123-131
    • Takeuchi, J.1    Chen, H.2    Coffino, P.3
  • 58
    • 0033543648 scopus 로고    scopus 로고
    • An archaebacterial ATPase, homologous to ATPases in the eukaryotic 26 S proteasome, activates protein breakdown by 20 S proteasomes
    • P. Zwickl, D. Ng, K.M. Woo, H.P. Klenk, and A.L. Goldberg An archaebacterial ATPase, homologous to ATPases in the eukaryotic 26 S proteasome, activates protein breakdown by 20 S proteasomes J. Biol. Chem. 274 1999 26008 26014
    • (1999) J. Biol. Chem. , vol.274 , pp. 26008-26014
    • Zwickl, P.1    Ng, D.2    Woo, K.M.3    Klenk, H.P.4    Goldberg, A.L.5
  • 64
    • 34548274872 scopus 로고    scopus 로고
    • Docking of the proteasomal ATPases' carboxyl termini in the 20S proteasome's alpha ring opens the gate for substrate entry
    • D.M. Smith, S.C. Chang, S. Park, D. Finley, Y. Cheng, and A.L. Goldberg Docking of the proteasomal ATPases' carboxyl termini in the 20S proteasome's alpha ring opens the gate for substrate entry Mol. Cell 27 2007 731 744
    • (2007) Mol. Cell , vol.27 , pp. 731-744
    • Smith, D.M.1    Chang, S.C.2    Park, S.3    Finley, D.4    Cheng, Y.5    Goldberg, A.L.6
  • 65
    • 42949096020 scopus 로고    scopus 로고
    • Mechanism of gate opening in the 20S proteasome by the proteasomal ATPases
    • J. Rabl, D.M. Smith, Y. Yu, S.C. Chang, A.L. Goldberg, and Y. Cheng Mechanism of gate opening in the 20S proteasome by the proteasomal ATPases Mol. Cell 30 2008 360 368
    • (2008) Mol. Cell , vol.30 , pp. 360-368
    • Rabl, J.1    Smith, D.M.2    Yu, Y.3    Chang, S.C.4    Goldberg, A.L.5    Cheng, Y.6
  • 68
  • 69
    • 79957637389 scopus 로고    scopus 로고
    • Identification of a functional docking site in the Rpn1 LRR domain for the UBA-UBL domain protein Ddi1
    • T.A. Gomez, N. Kolawa, M. Gee, M.J. Sweredoski, and R.J. Deshaies Identification of a functional docking site in the Rpn1 LRR domain for the UBA-UBL domain protein Ddi1 BMC Biol. 9 2011 33
    • (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
  • 70
    • 0036382885 scopus 로고    scopus 로고
    • Identification of ubiquitin-like protein-binding subunits of the 26S proteasome
    • Y. Saeki, T. Sone, A. Toh-e, and H. Yokosawa Identification of ubiquitin-like protein-binding subunits of the 26S proteasome Biochem. Biophys. Res. Commun. 296 2002 813 819
    • (2002) Biochem. Biophys. Res. Commun. , vol.296 , pp. 813-819
    • Saeki, Y.1    Sone, T.2    Toh-E, A.3    Yokosawa, H.4
  • 72
    • 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 alpha-helical rings
    • J. He, K. Kulkarni, P.C. da Fonseca, D. Krutauz, M.H. Glickman, D. Barford, and E.P. Morris The structure of the 26S proteasome subunit Rpn2 reveals its PC repeat domain as a closed toroid of two concentric alpha-helical rings Structure 20 2012 513 521
    • (2012) Structure , vol.20 , pp. 513-521
    • He, J.1    Kulkarni, K.2    Da Fonseca, P.C.3    Krutauz, D.4    Glickman, M.H.5    Barford, D.6    Morris, E.P.7
  • 76
    • 84895868714 scopus 로고    scopus 로고
    • Structure of the Rpn11-Rpn8 dimer reveals mechanisms of substrate deubiquitination during proteasomal degradation
    • E.J. Worden, C. Padovani, and A. Martin Structure of the Rpn11-Rpn8 dimer reveals mechanisms of substrate deubiquitination during proteasomal degradation Nat. Struct. Mol. Biol. 2014
    • (2014) Nat. Struct. Mol. Biol.
    • Worden, E.J.1    Padovani, C.2    Martin, A.3
  • 77
    • 84883488318 scopus 로고    scopus 로고
    • Formation of an intricate helical bundle dictates the assembly of the 26S proteasome lid
    • E. Estrin, J.R. Lopez-Blanco, P. Chacon, and A. Martin Formation of an intricate helical bundle dictates the assembly of the 26S proteasome lid Structure 21 2013 1624 1635
    • (2013) Structure , vol.21 , pp. 1624-1635
    • Estrin, E.1    Lopez-Blanco, J.R.2    Chacon, P.3    Martin, A.4
  • 80
    • 84857995395 scopus 로고    scopus 로고
    • Structural basis for the assembly and nucleic acid binding of the TREX-2 transcription-export complex
    • A.M. Ellisdon, L. Dimitrova, E. Hurt, and M. Stewart Structural basis for the assembly and nucleic acid binding of the TREX-2 transcription-export complex Nat. Struct. Mol. Biol. 19 2012 328 336
    • (2012) Nat. Struct. Mol. Biol. , vol.19 , pp. 328-336
    • Ellisdon, A.M.1    Dimitrova, L.2    Hurt, E.3    Stewart, M.4
  • 81
    • 17144417404 scopus 로고    scopus 로고
    • Structure of S5a bound to monoubiquitin provides a model for polyubiquitin recognition
    • Q. Wang, P. Young, and K.J. Walters Structure of S5a bound to monoubiquitin provides a model for polyubiquitin recognition J. Mol. Biol. 348 2005 727 739
    • (2005) J. Mol. Biol. , vol.348 , pp. 727-739
    • Wang, Q.1    Young, P.2    Walters, K.J.3
  • 82
    • 65649115267 scopus 로고    scopus 로고
    • Recognition and processing of ubiquitin-protein conjugates by the proteasome
    • D. Finley Recognition and processing of ubiquitin-protein conjugates by the proteasome Annu. Rev. Biochem. 78 2009 477 513
    • (2009) Annu. Rev. Biochem. , vol.78 , pp. 477-513
    • Finley, D.1
  • 83
    • 84867176120 scopus 로고    scopus 로고
    • The ubiquitin-proteasome system of Saccharomyces cerevisiae
    • D. Finley, H.D. Ulrich, T. Sommer, and P. Kaiser The ubiquitin-proteasome system of Saccharomyces cerevisiae Genetics 192 2012 319 360
    • (2012) Genetics , vol.192 , pp. 319-360
    • Finley, D.1    Ulrich, H.D.2    Sommer, T.3    Kaiser, P.4
  • 84
    • 26844433577 scopus 로고    scopus 로고
    • Proteasome-associated proteins: Regulation of a proteolytic machine
    • M. Schmidt, J. Hanna, S. Elsasser, and D. Finley Proteasome-associated proteins: regulation of a proteolytic machine Biol. Chem. 386 2005 725 737
    • (2005) Biol. Chem. , vol.386 , pp. 725-737
    • Schmidt, M.1    Hanna, J.2    Elsasser, S.3    Finley, D.4
  • 85
    • 84896032345 scopus 로고    scopus 로고
    • Paradigms of protein degradation by the proteasome
    • T. Inobe, and A. Matouschek Paradigms of protein degradation by the proteasome Curr. Opin. Struct. Biol. 24C 2014 156 164
    • (2014) Curr. Opin. Struct. Biol. , vol.24 C , pp. 156-164
    • Inobe, T.1    Matouschek, A.2
  • 86
    • 3142566639 scopus 로고    scopus 로고
    • Multiubiquitin chain receptors define a layer of substrate selectivity in the ubiquitin-proteasome system
    • R. Verma, R. Oania, J. Graumann, and R.J. Deshaies Multiubiquitin chain receptors define a layer of substrate selectivity in the ubiquitin-proteasome system Cell 118 2004 99 110
    • (2004) Cell , vol.118 , pp. 99-110
    • Verma, R.1    Oania, R.2    Graumann, J.3    Deshaies, R.J.4
  • 87
    • 68049084674 scopus 로고    scopus 로고
    • Breaking the chains: Structure and function of the deubiquitinases
    • D. Komander, M.J. Clague, and S. Urbe Breaking the chains: structure and function of the deubiquitinases Nat. Rev. Mol. Cell Biol. 10 2009 550 563
    • (2009) Nat. Rev. Mol. Cell Biol. , vol.10 , pp. 550-563
    • Komander, D.1    Clague, M.J.2    Urbe, S.3
  • 88
    • 79955470830 scopus 로고    scopus 로고
    • Trimming of ubiquitin chains by proteasome-associated deubiquitinating enzymes
    • M.J. Lee, B.H. Lee, J. Hanna, R.W. King, and D. Finley Trimming of ubiquitin chains by proteasome-associated deubiquitinating enzymes Mol. Cell. Proteomics 10 R110 2011 003871
    • (2011) Mol. Cell. Proteomics , vol.10 , Issue.R110 , pp. 003871
    • Lee, M.J.1    Lee, B.H.2    Hanna, J.3    King, R.W.4    Finley, D.5
  • 90
    • 0242300114 scopus 로고    scopus 로고
    • DNA-repair protein hHR23a alters its protein structure upon binding proteasomal subunit S5a
    • K.J. Walters, P.J. Lech, A.M. Goh, Q. Wang, and P.M. Howley DNA-repair protein hHR23a alters its protein structure upon binding proteasomal subunit S5a Proc. Natl. Acad. Sci. USA 100 2003 12694 12699
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 12694-12699
    • Walters, K.J.1    Lech, P.J.2    Goh, A.M.3    Wang, Q.4    Howley, P.M.5
  • 93
    • 75149172775 scopus 로고    scopus 로고
    • Cross-species divergence of the major recognition pathways of ubiquitylated substrates for ubiquitin/26S proteasome-mediated proteolysis
    • A.S. Fatimababy, Y.L. Lin, R. Usharani, R. Radjacommare, H.T. Wang, H.L. Tsai, Y. Lee, and H. Fu Cross-species divergence of the major recognition pathways of ubiquitylated substrates for ubiquitin/26S proteasome-mediated proteolysis FEBS J. 277 2010 796 816
    • (2010) FEBS J. , vol.277 , pp. 796-816
    • Fatimababy, A.S.1    Lin, Y.L.2    Usharani, R.3    Radjacommare, R.4    Wang, H.T.5    Tsai, H.L.6    Lee, Y.7    Fu, H.8
  • 94
    • 84865149961 scopus 로고    scopus 로고
    • A common ancestry for BAP1 and Uch37 regulators
    • L. Sanchez-Pulido, L. Kong, and C.P. Ponting A common ancestry for BAP1 and Uch37 regulators Bioinformatics 28 2012 1953 1956
    • (2012) Bioinformatics , vol.28 , pp. 1953-1956
    • Sanchez-Pulido, L.1    Kong, L.2    Ponting, C.P.3
  • 95
    • 33749348820 scopus 로고    scopus 로고
    • A novel proteasome interacting protein recruits the deubiquitinating enzyme UCH37 to 26S proteasomes
    • J. Hamazaki, S. Iemura, T. Natsume, H. Yashiroda, K. Tanaka, and S. Murata A novel proteasome interacting protein recruits the deubiquitinating enzyme UCH37 to 26S proteasomes EMBO J. 25 2006 4524 4536
    • (2006) EMBO J. , vol.25 , pp. 4524-4536
    • Hamazaki, J.1    Iemura, S.2    Natsume, T.3    Yashiroda, H.4    Tanaka, K.5    Murata, S.6
  • 96
    • 33845713194 scopus 로고    scopus 로고
    • HRpn13/ADRM1/GP110 is a novel proteasome subunit that binds the deubiquitinating enzyme, UCH37
    • X.B. Qiu, S.Y. Ouyang, C.J. Li, S. Miao, L. Wang, and A.L. Goldberg HRpn13/ADRM1/GP110 is a novel proteasome subunit that binds the deubiquitinating enzyme, UCH37 EMBO J. 25 2006 5742 5753
    • (2006) EMBO J. , vol.25 , pp. 5742-5753
    • Qiu, X.B.1    Ouyang, S.Y.2    Li, C.J.3    Miao, S.4    Wang, L.5    Goldberg, A.L.6
  • 100
    • 84923894408 scopus 로고    scopus 로고
    • Mechanism of UCH-L5 activation and inhibition by DEUBAD domains in RPN13 and INO80G
    • D.D. Sahtoe, W.J. van Dijk, F. El Oualid, R. Ekkebus, H. Ovaa, and T.K. Sixma Mechanism of UCH-L5 activation and inhibition by DEUBAD domains in RPN13 and INO80G Mol. Cell 57 2015 887 900
    • (2015) Mol. Cell , vol.57 , pp. 887-900
    • Sahtoe, D.D.1    Van Dijk, W.J.2    El Oualid, F.3    Ekkebus, R.4    Ovaa, H.5    Sixma, T.K.6
  • 101
    • 84867582157 scopus 로고    scopus 로고
    • C-terminal UBA domains protect ubiquitin receptors by preventing initiation of protein degradation
    • C. Heinen, K. Acs, D. Hoogstraten, and N.P. Dantuma C-terminal UBA domains protect ubiquitin receptors by preventing initiation of protein degradation Nat. Commun. 2 2011 191
    • (2011) Nat. Commun. , vol.2 , pp. 191
    • Heinen, C.1    Acs, K.2    Hoogstraten, D.3    Dantuma, N.P.4
  • 102
    • 78649289427 scopus 로고    scopus 로고
    • ATP-dependent steps in the binding of ubiquitin conjugates to the 26S proteasome that commit to degradation
    • A. Peth, T. Uchiki, and A.L. Goldberg ATP-dependent steps in the binding of ubiquitin conjugates to the 26S proteasome that commit to degradation Mol. Cell 40 2010 671 681
    • (2010) Mol. Cell , vol.40 , pp. 671-681
    • Peth, A.1    Uchiki, T.2    Goldberg, A.L.3
  • 103
    • 78549254832 scopus 로고    scopus 로고
    • Binding-induced folding of prokaryotic ubiquitin-like protein on the mycobacterium proteasomal ATPase targets substrates for degradation
    • T. Wang, K.H. Darwin, and H. Li Binding-induced folding of prokaryotic ubiquitin-like protein on the mycobacterium proteasomal ATPase targets substrates for degradation Nat. Struct. Mol. Biol. 17 2010 1352 1357
    • (2010) Nat. Struct. Mol. Biol. , vol.17 , pp. 1352-1357
    • Wang, T.1    Darwin, K.H.2    Li, H.3
  • 104
    • 77951972141 scopus 로고    scopus 로고
    • Structure of proteasome ubiquitin receptor hRpn13 and its activation by the scaffolding protein hRpn2
    • X. Chen, B.H. Lee, D. Finley, and K.J. Walters Structure of proteasome ubiquitin receptor hRpn13 and its activation by the scaffolding protein hRpn2 Mol. Cell 38 2010 404 415
    • (2010) Mol. Cell , vol.38 , pp. 404-415
    • Chen, X.1    Lee, B.H.2    Finley, D.3    Walters, K.J.4
  • 105
    • 24044538903 scopus 로고    scopus 로고
    • IUPred: Web server for the prediction of intrinsically unstructured regions of proteins based on estimated energy content
    • Z. Dosztanyi, V. Csizmok, P. Tompa, and I. Simon IUPred: web server for the prediction of intrinsically unstructured regions of proteins based on estimated energy content Bioinformatics 21 2005 3433 3434
    • (2005) Bioinformatics , vol.21 , pp. 3433-3434
    • Dosztanyi, Z.1    Csizmok, V.2    Tompa, P.3    Simon, I.4
  • 106
    • 14844342815 scopus 로고    scopus 로고
    • The pairwise energy content estimated from amino acid composition discriminates between folded and intrinsically unstructured proteins
    • Z. Dosztanyi, V. Csizmok, P. Tompa, and I. Simon The pairwise energy content estimated from amino acid composition discriminates between folded and intrinsically unstructured proteins J. Mol. Biol. 347 2005 827 839
    • (2005) J. Mol. Biol. , vol.347 , pp. 827-839
    • Dosztanyi, Z.1    Csizmok, V.2    Tompa, P.3    Simon, I.4
  • 107
    • 84855184716 scopus 로고    scopus 로고
    • SPINE-D: Accurate prediction of short and long disordered regions by a single neural-network based method
    • T. Zhang, E. Faraggi, B. Xue, A.K. Dunker, V.N. Uversky, and Y. Zhou SPINE-D: Accurate prediction of short and long disordered regions by a single neural-network based method J. Biomol. Struct. Dyn. 29 2012 799 813
    • (2012) J. Biomol. Struct. Dyn. , vol.29 , pp. 799-813
    • Zhang, T.1    Faraggi, E.2    Xue, B.3    Dunker, A.K.4    Uversky, V.N.5    Zhou, Y.6
  • 108
    • 0032568655 scopus 로고    scopus 로고
    • SMART, a simple modular architecture research tool: Identification of signaling domains
    • J. Schultz, F. Milpetz, P. Bork, and C.P. Ponting SMART, a simple modular architecture research tool: identification of signaling domains Proc. Natl. Acad. Sci. USA 95 1998 5857 5864
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 5857-5864
    • Schultz, J.1    Milpetz, F.2    Bork, P.3    Ponting, C.P.4
  • 110
    • 80855133523 scopus 로고    scopus 로고
    • Identifying conformational states of macromolecules by eigen-analysis of resampled cryo-EM images
    • P.A. Penczek, M. Kimmel, and C.M. Spahn Identifying conformational states of macromolecules by eigen-analysis of resampled cryo-EM images Structure 19 2011 1582 1590
    • (2011) Structure , vol.19 , pp. 1582-1590
    • Penczek, P.A.1    Kimmel, M.2    Spahn, C.M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.