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Volumn 6, Issue 10, 2011, Pages 1087-1095

Proteasomal degradation from internal sites favors partial proteolysis via remote domain stabilization

Author keywords

[No Author keywords available]

Indexed keywords

DIHYDROFOLATE REDUCTASE; METHIONINE; POLYPEPTIDE; PROTEASOME; SULFUR 35; UBIQUITIN;

EID: 80055022365     PISSN: 15548929     EISSN: 15548937     Source Type: Journal    
DOI: 10.1021/cb2002285     Document Type: Article
Times cited : (26)

References (61)
  • 1
    • 65649115267 scopus 로고    scopus 로고
    • Recognition and processing of ubiquitin-protein conjugates by the proteasome
    • Finley, D. (2009) Recognition and processing of ubiquitin-protein conjugates by the proteasome Annu. Rev. Biochem. 78, 477-513
    • (2009) Annu. Rev. Biochem. , vol.78 , pp. 477-513
    • Finley, D.1
  • 2
    • 0032867676 scopus 로고    scopus 로고
    • The 26S proteasome: A molecular machine designed for controlled proteolysis
    • DOI 10.1146/annurev.biochem.68.1.1015
    • Voges, D., Zwickl, P., and Baumeister, W. (1999) The 26S proteasome: a molecular machine designed for controlled proteolysis Annu. Rev. Biochem. 68, 1015-1068 (Pubitemid 29449214)
    • (1999) Annual Review of Biochemistry , vol.68 , pp. 1015-1068
    • Voges, D.1    Zwickl, P.2    Baumeister, W.3
  • 3
    • 21144447324 scopus 로고    scopus 로고
    • Molecular machines for protein degradation
    • DOI 10.1002/cbic.200400313
    • Groll, M., Bochtler, M., Brandstetter, H., Clausen, T., and Huber, R. (2005) Molecular machines for protein degradation ChemBioChem 6, 222-256 (Pubitemid 40879733)
    • (2005) ChemBioChem , vol.6 , Issue.2 , pp. 222-256
    • Groll, M.1    Bochtler, M.2    Brandstetter, H.3    Clausen, T.4    Huber, R.5
  • 4
    • 39149135202 scopus 로고    scopus 로고
    • Protein targeting to ATP-dependent proteases
    • Inobe, T. and Matouschek, A. (2008) Protein targeting to ATP-dependent proteases Curr. Opin. Struct. Biol. 18, 43-51
    • (2008) Curr. Opin. Struct. Biol. , vol.18 , pp. 43-51
    • Inobe, T.1    Matouschek, A.2
  • 7
    • 79951850741 scopus 로고    scopus 로고
    • Defining the geometry of the two-component proteasome degron
    • Inobe, T., Fishbain, S., Prakash, S., and Matouschek, A. (2011) Defining the geometry of the two-component proteasome degron Nat. Chem. Biol. 7, 161-167
    • (2011) Nat. Chem. Biol. , vol.7 , pp. 161-167
    • Inobe, T.1    Fishbain, S.2    Prakash, S.3    Matouschek, A.4
  • 8
    • 55549088522 scopus 로고    scopus 로고
    • Pore loops of the AAA+ ClpX machine grip substrates to drive translocation and unfolding
    • Martin, A., Baker, T. A., and Sauer, R. T. (2008) Pore loops of the AAA+ ClpX machine grip substrates to drive translocation and unfolding Nat. Struct. Mol. Biol. 15, 1147-1151
    • (2008) Nat. Struct. Mol. Biol. , vol.15 , pp. 1147-1151
    • Martin, A.1    Baker, T.A.2    Sauer, R.T.3
  • 9
    • 0035266072 scopus 로고    scopus 로고
    • ATP-dependent proteases degrade their substrates by processively unraveling them from the degradation signal
    • DOI 10.1016/S1097-2765(01)00209-X
    • Lee, C., Schwartz, M. P., Prakash, S., Iwakura, M., and Matouschek, A. (2001) ATP-dependent proteases degrade their substrates by processively unraveling them from the degradation signal Mol. Cell 7, 627-637 (Pubitemid 32706354)
    • (2001) Molecular Cell , vol.7 , Issue.3 , pp. 627-637
    • Lee, C.1    Schwartz, M.P.2    Prakash, S.3    Iwakura, M.4    Matouschek, A.5
  • 10
    • 0037449572 scopus 로고    scopus 로고
    • Endoproteolytic activity of the proteasome
    • DOI 10.1126/science.1079293
    • Liu, C.-W., Corboy, M. J., DeMartino, G. N., and Thomas, P. J. (2003) Endoproteolytic activity of the proteasome Science 299, 408-411 (Pubitemid 36120047)
    • (2003) Science , vol.299 , Issue.5605 , pp. 408-411
    • Liu, C.-W.1    Corboy, M.J.2    DeMartino, G.N.3    Thomas, P.J.4
  • 11
    • 33746786326 scopus 로고    scopus 로고
    • Proteasome-mediated protein processing by bidirectional degradation initiated from an internal site
    • DOI 10.1038/nsmb1122, PII NSMB1122
    • Piwko, W. and Jentsch, S. (2006) Proteasome-mediated protein processing by bidirectional degradation initiated from an internal site Nat. Struct. Mol. Biol. 13, 691-697 (Pubitemid 44175161)
    • (2006) Nature Structural and Molecular Biology , vol.13 , Issue.8 , pp. 691-697
    • Piwko, W.1    Jentsch, S.2
  • 12
    • 57749102552 scopus 로고    scopus 로고
    • Substrate selection by the proteasome during degradation of protein complexes
    • Prakash, S., Inobe, T., Hatch, A., and Matouschek, A. (2009) Substrate selection by the proteasome during degradation of protein complexes Nat. Chem. Biol. 5, 29-36
    • (2009) Nat. Chem. Biol. , vol.5 , pp. 29-36
    • Prakash, S.1    Inobe, T.2    Hatch, A.3    Matouschek, A.4
  • 13
    • 77951199144 scopus 로고    scopus 로고
    • Degradation of some polyubiquitinated proteins requires an intrinsic proteasomal binding element in the substrates
    • Zhao, M., Zhang, N.-Y., Zurawel, A., Hansen, K. C., and Liu, C.-W. (2010) Degradation of some polyubiquitinated proteins requires an intrinsic proteasomal binding element in the substrates J. Biol. Chem. 285, 4771-4780
    • (2010) J. Biol. Chem. , vol.285 , pp. 4771-4780
    • Zhao, M.1    Zhang, N.-Y.2    Zurawel, A.3    Hansen, K.C.4    Liu, C.-W.5
  • 14
    • 84867582157 scopus 로고    scopus 로고
    • C-terminal UBA domains protect ubiquitin receptors by preventing initiation of protein degradation
    • Heinen, C., Acs, K., Hoogstraten, D., and Dantuma, N. P. (2011) C-terminal UBA domains protect ubiquitin receptors by preventing initiation of protein degradation Nat. Commun. 2, 191
    • (2011) Nat. Commun. , vol.2 , pp. 191
    • Heinen, C.1    Acs, K.2    Hoogstraten, D.3    Dantuma, N.P.4
  • 15
    • 84878270699 scopus 로고    scopus 로고
    • Rad23 escapes degradation because it lacks a proteasome initiation region
    • Fishbain, S., Prakash, S., Herrig, A., Elsasser, S., and Matouschek, A. (2011) Rad23 escapes degradation because it lacks a proteasome initiation region Nat. Commun. 2, 192
    • (2011) Nat. Commun. , vol.2 , pp. 192
    • Fishbain, S.1    Prakash, S.2    Herrig, A.3    Elsasser, S.4    Matouschek, A.5
  • 16
    • 0037144567 scopus 로고    scopus 로고
    • Concurrent translocation of multiple polypeptide chains through the proteasomal degradation channel
    • Lee, C., Prakash, S., and Matouschek, A. (2002) Concurrent translocation of multiple polypeptide chains through the proteasomal degradation channel J. Biol. Chem. 277, 34760-34765
    • (2002) J. Biol. Chem. , vol.277 , pp. 34760-34765
    • Lee, C.1    Prakash, S.2    Matouschek, A.3
  • 18
    • 0027980321 scopus 로고
    • The ubiquitin-proteasome pathway is required for processing the NF-κB1 precursor protein and the activation of NF-κB
    • DOI 10.1016/S0092-8674(94)90482-0
    • Palombella, V. J., Rando, O. J., Goldberg, A. L., and Maniatis, T. (1994) The ubiquitin-proteasome pathway is required for processing the NF-kappa B1 precursor protein and the activation of NF-kappa B Cell 78, 773-785 (Pubitemid 24294453)
    • (1994) Cell , vol.78 , Issue.5 , pp. 773-785
    • Palombella, V.J.1    Rando, O.J.2    Goldberg, A.L.3    Maniatis, T.4
  • 19
    • 0029924035 scopus 로고    scopus 로고
    • A glycine-rich region in NF-κB p105 functions as a processing signal for the generation of the p50 subunit
    • Lin, L. and Ghosh, S. (1996) A glycine-rich region in NF-kappaB p105 functions as a processing signal for the generation of the p50 subunit Mol. Cell. Biol. 16, 2248-2254 (Pubitemid 26123745)
    • (1996) Molecular and Cellular Biology , vol.16 , Issue.5 , pp. 2248-2254
    • Lin, L.1    Ghosh, S.2
  • 20
    • 28544434064 scopus 로고    scopus 로고
    • A conserved processing mechanism regulates the activity of transcription factors Cubitus interruptus and NF-κB
    • DOI 10.1038/nsmb1018
    • Tian, L., Holmgren, R. A., and Matouschek, A. (2005) A conserved processing mechanism regulates the activity of transcription factors Cubitus interruptus and NF-kappaB Nat. Struct. Mol. Biol. 12, 1045-1053 (Pubitemid 41746774)
    • (2005) Nature Structural and Molecular Biology , vol.12 , Issue.12 , pp. 1045-1053
    • Tian, L.1    Holmgren, R.A.2    Matouschek, A.3
  • 21
    • 0031587830 scopus 로고    scopus 로고
    • Proteolysis that is inhibited by hedgehog targets cubitus interruptus protein to the nucleus and converts it to a repressor
    • Aza-Blanc, P., Ramírez-Weber, F. A., Laget, M. P., Schwartz, C., and Kornberg, T. B. (1997) Proteolysis that is inhibited by hedgehog targets Cubitus interruptus protein to the nucleus and converts it to a repressor Cell 89, 1043-1053 (Pubitemid 127678738)
    • (1997) Cell , vol.89 , Issue.7 , pp. 1043-1053
    • Aza-Blanc, P.1    Ramirez- Weber, F.-A.2    Laget, M.-P.3    Schwartz, C.4    Kornberg, T.B.5
  • 22
    • 0036091848 scopus 로고    scopus 로고
    • Taking a bite: Proteasomal protein processing
    • Rape, M. and Jentsch, S. (2002) Taking a bite: proteasomal protein processing Nat. Cell Biol. 4, E113-116
    • (2002) Nat. Cell Biol. , vol.4 , pp. 113-116
    • Rape, M.1    Jentsch, S.2
  • 23
    • 0034268493 scopus 로고    scopus 로고
    • Activation of a membrane-bound transcription factor by regulated ubiquitin/proteasome-dependent processing
    • Hoppe, T., Matuschewski, K., Rape, M., Schlenker, S., Ulrich, H. D., and Jentsch, S. (2000) Activation of a membrane-bound transcription factor by regulated ubiquitin/proteasome-dependent processing Cell 102, 577-586
    • (2000) Cell , vol.102 , pp. 577-586
    • Hoppe, T.1    Matuschewski, K.2    Rape, M.3    Schlenker, S.4    Ulrich, H.D.5    Jentsch, S.6
  • 24
    • 0034681266 scopus 로고    scopus 로고
    • Hedgehog-regulated processing of Gli3 produces an anterior/posterior repressor gradient in the developing vertebrate limb
    • Wang, B., Fallon, J. F., and Beachy, P. A. (2000) Hedgehog-regulated processing of Gli3 produces an anterior/posterior repressor gradient in the developing vertebrate limb Cell 100, 423-434
    • (2000) Cell , vol.100 , pp. 423-434
    • Wang, B.1    Fallon, J.F.2    Beachy, P.A.3
  • 25
    • 33646270662 scopus 로고    scopus 로고
    • Sonic hedgehog signaling regulates Gli2 transcriptional activity by suppressing its processing and degradation
    • Pan, Y., Bai, C. B., Joyner, A. L., and Wang, B. (2006) Sonic hedgehog signaling regulates Gli2 transcriptional activity by suppressing its processing and degradation Mol. Cell. Biol. 26, 3365-3377
    • (2006) Mol. Cell. Biol. , vol.26 , pp. 3365-3377
    • Pan, Y.1    Bai, C.B.2    Joyner, A.L.3    Wang, B.4
  • 26
    • 0032954038 scopus 로고    scopus 로고
    • Structural motifs involved in ubiquitin-mediated processing of the NF- κB precursor p105: Roles of the Glycine-rich region and a downstream ubiquitination domain
    • Orian, A., Schwartz, A. L., Israël, A., Whiteside, S., Kahana, C., and Ciechanover, A. (1999) Structural motifs involved in ubiquitin-mediated processing of the NF-kappaB precursor p105: roles of the glycine-rich region and a downstream ubiquitination domain Mol. Cell. Biol. 19, 3664-3673 (Pubitemid 29193826)
    • (1999) Molecular and Cellular Biology , vol.19 , Issue.5 , pp. 3664-3673
    • Orian, A.1    Schwartz, A.L.2    Israel, A.3    Whiteside, S.4    Kahana, C.5    Ciechanover, A.6
  • 28
    • 33751208606 scopus 로고    scopus 로고
    • Regulation of Hh/Gli signaling by dual ubiquitin pathways
    • Jiang, J. (2006) Regulation of Hh/Gli signaling by dual ubiquitin pathways Cell Cycle 5, 2457-2463 (Pubitemid 44785822)
    • (2006) Cell Cycle , vol.5 , Issue.21 , pp. 2457-2463
    • Jiang, J.1
  • 29
    • 75849129292 scopus 로고    scopus 로고
    • Multiple Ser/Thr-rich degrons mediate the degradation of Ci/Gli by the Cul3-HIB/SPOP E3 ubiquitin ligase
    • Zhang, Q., Shi, Q., Chen, Y., Yue, T., Li, S., Wang, B., and Jiang, J. (2009) Multiple Ser/Thr-rich degrons mediate the degradation of Ci/Gli by the Cul3-HIB/SPOP E3 ubiquitin ligase Proc. Natl. Acad. Sci. U.S.A. 106, 21191-21196
    • (2009) Proc. Natl. Acad. Sci. U.S.A. , vol.106 , pp. 21191-21196
    • Zhang, Q.1    Shi, Q.2    Chen, Y.3    Yue, T.4    Li, S.5    Wang, B.6    Jiang, J.7
  • 30
    • 33646893705 scopus 로고    scopus 로고
    • A Hedgehog-Induced BTB Protein Modulates Hedgehog Signaling by Degrading Ci/Gli Transcription Factor
    • DOI 10.1016/j.devcel.2006.05.004, PII S1534580706002127
    • Zhang, Q., Zhang, L., Wang, B., Ou, C.-Y., Chien, C.-T., and Jiang, J. (2006) A hedgehog-induced BTB protein modulates hedgehog signaling by degrading Ci/Gli transcription factor Dev. Cell. 10, 719-729 (Pubitemid 43779117)
    • (2006) Developmental Cell , vol.10 , Issue.6 , pp. 719-729
    • Zhang, Q.1    Zhang, L.2    Wang, B.3    Ou, C.-Y.4    Chien, C.-T.5    Jiang, J.6
  • 31
    • 33646875414 scopus 로고    scopus 로고
    • Roadkill attenuates Hedgehog responses through degradation of Cubitus interruptus
    • DOI 10.1242/dev.02370
    • Kent, D., Bush, E. W., and Hooper, J. E. (2006) Roadkill attenuates Hedgehog responses through degradation of Cubitus interruptus Development 133, 2001-2010 (Pubitemid 43881265)
    • (2006) Development , vol.133 , Issue.10 , pp. 2001-2010
    • Kent, D.1    Bush, E.W.2    Hooper, J.E.3
  • 32
    • 0032510057 scopus 로고    scopus 로고
    • Rad23 links DNA repair to the ubiquitin/proteasome pathway
    • DOI 10.1038/35661
    • Schauber, C., Chen, L., Tongaonkar, P., Vega, I., Lambertson, D., Potts, W., and Madura, K. (1998) Rad23 links DNA repair to the ubiquitin/proteasome pathway Nature 391, 715-718 (Pubitemid 28113221)
    • (1998) Nature , vol.391 , Issue.6668 , pp. 715-718
    • Schauber, C.1    Chen, L.2    Tongaonkar, P.3    Vega, I.4    Lambertson, D.5    Potts, W.6    Madura, K.7
  • 34
    • 0027385015 scopus 로고
    • The refolding of cis- and trans-peptidylprolyl isomers of barstar
    • DOI 10.1021/bi00092a032
    • Schreiber, G. and Fersht, A. R. (1993) The refolding of cis- and trans-peptidylprolyl isomers of barstar Biochemistry 32, 11195-11203 (Pubitemid 23332028)
    • (1993) Biochemistry , vol.32 , Issue.41 , pp. 11195-11203
    • Schreiber, G.1    Fersht, A.R.2
  • 35
    • 0026553768 scopus 로고
    • The folding of an enzyme. II. Substructure of barnase and the contribution of different interactions to protein stability
    • Serrano, L., Kellis, J. T., Cann, P., Matouschek, A., and Fersht, A. R. (1992) The folding of an enzyme. II. Substructure of barnase and the contribution of different interactions to protein stability J. Mol. Biol. 224, 783-804
    • (1992) J. Mol. Biol. , vol.224 , pp. 783-804
    • Serrano, L.1    Kellis, J.T.2    Cann, P.3    Matouschek, A.4    Fersht, A.R.5
  • 36
    • 0028834886 scopus 로고
    • The folding and stability of titin immunoglobulin-like modules, with implications for the mechanism of elasticity
    • Politou, A. S., Thomas, D. J., and Pastore, A. (1995) The folding and stability of titin immunoglobulin-like modules, with implications for the mechanism of elasticity Biophys. J. 69, 2601-2610
    • (1995) Biophys. J. , vol.69 , pp. 2601-2610
    • Politou, A.S.1    Thomas, D.J.2    Pastore, A.3
  • 37
    • 0028951190 scopus 로고
    • Methotrexate inhibits proteolysis of dihydrofolate reductase by the N-end rule pathway
    • Johnston, J. A., Johnson, E. S., Waller, P. R., and Varshavsky, A. (1995) Methotrexate inhibits proteolysis of dihydrofolate reductase by the N-end rule pathway J. Biol. Chem. 270, 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
  • 39
    • 64849084080 scopus 로고    scopus 로고
    • Isolation of mammalian 26S proteasomes and p97/VCP complexes using the ubiquitin-like domain from HHR23B reveals novel proteasome-associated proteins
    • Besche, H., Haas, W., Gygi, S., and Goldberg, A. (2009) Isolation of mammalian 26S proteasomes and p97/VCP complexes using the ubiquitin-like domain from HHR23B reveals novel proteasome-associated proteins Biochemistry 48, 2538-2549
    • (2009) Biochemistry , vol.48 , pp. 2538-2549
    • Besche, H.1    Haas, W.2    Gygi, S.3    Goldberg, A.4
  • 40
    • 0034283010 scopus 로고    scopus 로고
    • Cotranslational dimerization of the Rel homology domain of NF-kappaB1 generates p50-p105 heterodimers and is required for effective p50 production
    • Lin, L., DeMartino, G. N., and Greene, W. C. (2000) Cotranslational dimerization of the Rel homology domain of NF-kappaB1 generates p50-p105 heterodimers and is required for effective p50 production EMBO J. 19, 4712-4722
    • (2000) EMBO J. , vol.19 , pp. 4712-4722
    • Lin, L.1    Demartino, G.N.2    Greene, W.C.3
  • 41
    • 0346156074 scopus 로고    scopus 로고
    • Conditional Protein Alleles Using Knockin Mice and a Chemical Inducer of Dimerization
    • DOI 10.1016/S1097-2765(03)00491-X
    • Stankunas, K., Bayle, J. H., Gestwicki, J. E., Lin, Y.-M., Wandless, T. J., and Crabtree, G. R. (2003) Conditional protein alleles using knockin mice and a chemical inducer of dimerization Mol. Cell 12, 1615-1624 (Pubitemid 38037028)
    • (2003) Molecular Cell , vol.12 , Issue.6 , pp. 1615-1624
    • Stankunas, K.1    Bayle, J.H.2    Gestwicki, J.E.3    Lin, Y.-M.4    Wandless, T.J.5    Crabtree, G.R.6
  • 42
    • 79953888421 scopus 로고    scopus 로고
    • Single-molecule protein unfolding and translocation by an ATP-fueled proteolytic machine
    • Aubin-Tam, M.-E., Olivares, A. O., Sauer, R. T., Baker, T. A., and Lang, M. J. (2011) Single-molecule protein unfolding and translocation by an ATP-fueled proteolytic machine Cell 145, 257-267
    • (2011) Cell , vol.145 , pp. 257-267
    • Aubin-Tam, M.-E.1    Olivares, A.O.2    Sauer, R.T.3    Baker, T.A.4    Lang, M.J.5
  • 44
    • 21244480104 scopus 로고    scopus 로고
    • Loops in the central channel of ClpA chaperone mediate protein binding, unfolding, and translocation
    • DOI 10.1016/j.cell.2005.04.012, PII S0092867405003922
    • Hinnerwisch, J., Fenton, W. A., Furtak, K. J., Farr, G. W., and Horwich, A. L. (2005) Loops in the central channel of ClpA chaperone mediate protein binding, unfolding, and translocation Cell 121, 1029-1041 (Pubitemid 40894633)
    • (2005) Cell , vol.121 , Issue.7 , pp. 1029-1041
    • Hinnerwisch, J.1    Fenton, W.A.2    Furtak, K.J.3    Farr, G.W.4    Horwich, A.L.5
  • 46
    • 79952816898 scopus 로고    scopus 로고
    • Structure and mechanism of the hexameric MecA-ClpC molecular machine
    • Wang, F., Mei, Z., Qi, Y., Yan, C., Hu, Q., Wang, J., and Shi, Y. (2011) Structure and mechanism of the hexameric MecA-ClpC molecular machine Nature 471, 331-335
    • (2011) Nature , vol.471 , pp. 331-335
    • Wang, F.1    Mei, Z.2    Qi, Y.3    Yan, C.4    Hu, Q.5    Wang, J.6    Shi, Y.7
  • 47
    • 13444306170 scopus 로고    scopus 로고
    • Partitioning between unfolding and release of native domains during ClpXP degradation determines substrate selectivity and partial processing
    • DOI 10.1073/pnas.0409634102
    • Kenniston, J. A., Baker, T. A., and Sauer, R. T. (2005) Partitioning between unfolding and release of native domains during ClpXP degradation determines substrate selectivity and partial processing Proc. Natl. Acad. Sci. U.S.A. 102, 1390-1395 (Pubitemid 40209180)
    • (2005) Proceedings of the National Academy of Sciences of the United States of America , vol.102 , Issue.5 , pp. 1390-1395
    • Kenniston, J.A.1    Baker, T.A.2    Sauer, R.T.3
  • 49
    • 0023993152 scopus 로고
    • Latent membrane perturbation activity of a mitochondrial precursor protein is exposed by unfolding
    • Endo, T. and Schatz, G. (1988) Latent membrane perturbation activity of a mitochondrial precursor protein is exposed by unfolding EMBO J. 7, 1153-1158
    • (1988) EMBO J. , vol.7 , pp. 1153-1158
    • Endo, T.1    Schatz, G.2
  • 50
    • 0033923044 scopus 로고    scopus 로고
    • Systematic circular permutation of an entire protein reveals essential folding elements
    • DOI 10.1038/76811
    • Iwakura, M., Nakamura, T., Yamane, C., and Maki, K. (2000) Systematic circular permutation of an entire protein reveals essential folding elements Nat. Struct. Biol. 7, 580-585 (Pubitemid 30445916)
    • (2000) Nature Structural Biology , vol.7 , Issue.7 , pp. 580-585
    • Iwakura, M.1    Nakamura, T.2    Yamane, C.3    Maki, K.4
  • 51
    • 0035807936 scopus 로고    scopus 로고
    • Studies of the ankyrin repeats of the Drosophila melanogaster Notch receptor. 2. Solution stability and cooperativity of unfolding
    • DOI 10.1021/bi011436+
    • Zweifel, M. E. and Barrick, D. (2001) Studies of the ankyrin repeats of the Drosophila melanogaster Notch receptor. 2. Solution stability and cooperativity of unfolding Biochemistry 40, 14357-14367 (Pubitemid 33111717)
    • (2001) Biochemistry , vol.40 , Issue.48 , pp. 14357-14367
    • Zweifel, M.E.1    Barrick, D.2
  • 52
    • 38049063892 scopus 로고    scopus 로고
    • Folding and unfolding mechanism of highly stable full-consensus ankyrin repeat proteins
    • Wetzel, S. K., Settanni, G., Kenig, M., Binz, H. K., and Plückthun, A. (2008) Folding and unfolding mechanism of highly stable full-consensus ankyrin repeat proteins J. Mol. Biol. 376, 241-257
    • (2008) J. Mol. Biol. , vol.376 , pp. 241-257
    • Wetzel, S.K.1    Settanni, G.2    Kenig, M.3    Binz, H.K.4    Plückthun, A.5
  • 55
    • 75749101797 scopus 로고    scopus 로고
    • The ubiquitin ligase Hul5 promotes proteasomal processivity
    • Aviram, S. and Kornitzer, D. (2010) The ubiquitin ligase Hul5 promotes proteasomal processivity Mol. Cell. Biol. 30, 985-994
    • (2010) Mol. Cell. Biol. , vol.30 , pp. 985-994
    • Aviram, S.1    Kornitzer, D.2
  • 56
    • 0037095730 scopus 로고    scopus 로고
    • DNAWorks: An automated method for designing oligonucleotides for PCR-based gene synthesis
    • Hoover, D. M. and Lubkowski, J. (2002) DNAWorks: an automated method for designing oligonucleotides for PCR-based gene synthesis Nucleic Acids Res. 30, e43
    • (2002) Nucleic Acids Res. , vol.30 , pp. 43
    • Hoover, D.M.1    Lubkowski, J.2
  • 57
    • 34250802058 scopus 로고    scopus 로고
    • Rational design, structural and thermodynamic characterization of a hyperstable variant of the villin headpiece helical subdomain
    • DOI 10.1021/bi6026314
    • Bi, Y., Cho, J.-H., Kim, E.-Y., Shan, B., Schindelin, H., and Raleigh, D. P. (2007) Rational design, structural and thermodynamic characterization of a hyperstable variant of the villin headpiece helical subdomain Biochemistry 46, 7497-7505 (Pubitemid 46986376)
    • (2007) Biochemistry , vol.46 , Issue.25 , pp. 7497-7505
    • Bi, Y.1    Cho, J.-H.2    Kim, E.-Y.3    Shan, B.4    Schindelin, H.5    Raleigh, D.P.6
  • 58
    • 28844484999 scopus 로고    scopus 로고
    • Preparation of ubiquitinated substrates by the PY motif-insertion method for monitoring 26S proteasome activity
    • DOI 10.1016/S0076-6879(05)99014-9, PII S0076687905990149, 14, Ubiquitin and Protein Degradation, Part B
    • Saeki, Y., Isono, E., and Toh-E, A. (2005) Preparation of ubiquitinated substrates by the PY motif-insertion method for monitoring 26S proteasome activity Methods Enzymol. 399, 215-227 (Pubitemid 41772731)
    • (2005) Methods in Enzymology , vol.399 , pp. 215-227
    • Saeki, Y.1    Isono, E.2    Toh-E, A.3
  • 60
    • 78651225388 scopus 로고    scopus 로고
    • Global analysis of lysine ubiquitination by ubiquitin remnant immunoaffinity profiling
    • Xu, G., Paige, J. S., and Jaffrey, S. R. (2010) Global analysis of lysine ubiquitination by ubiquitin remnant immunoaffinity profiling Nat. Biotechnol. 28, 868-873
    • (2010) Nat. Biotechnol. , vol.28 , pp. 868-873
    • Xu, G.1    Paige, J.S.2    Jaffrey, S.R.3
  • 61
    • 1542358787 scopus 로고    scopus 로고
    • Prediction and Functional Analysis of Native Disorder in Proteins from the Three Kingdoms of Life
    • DOI 10.1016/j.jmb.2004.02.002, PII S0022283604001482
    • Ward, J. J., Sodhi, J. S., McGuffin, L. J., Buxton, B. F., and Jones, D. T. (2004) Prediction and functional analysis of native disorder in proteins from the three kingdoms of life J. Mol. Biol. 337, 635-645 (Pubitemid 38326883)
    • (2004) Journal of Molecular Biology , vol.337 , Issue.3 , pp. 635-645
    • Ward, J.J.1    Sodhi, J.S.2    McGuffin, L.J.3    Buxton, B.F.4    Jones, D.T.5


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