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Volumn 13, Issue 1, 2003, Pages 98-109

Protein unfolding - An important process in vivo?

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATE; CARRIER PROTEIN; POLYPEPTIDE; PROTEIN; PROTEINASE;

EID: 0037308999     PISSN: 0959440X     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0959-440X(03)00010-1     Document Type: Review
Times cited : (138)

References (112)
  • 2
    • 0032188847 scopus 로고    scopus 로고
    • Tom40 forms the hydrophilic channel of the mitochondrial import pore for preproteins
    • Hill K., Model K., Ryan M.T., Dietmeier K., Martin F., Wagner R., Pfanner N. Tom40 forms the hydrophilic channel of the mitochondrial import pore for preproteins. Nature. 395:1998;516-521.
    • (1998) Nature , vol.395 , pp. 516-521
    • Hill, K.1    Model, K.2    Ryan, M.T.3    Dietmeier, K.4    Martin, F.5    Wagner, R.6    Pfanner, N.7
  • 3
    • 0033539505 scopus 로고    scopus 로고
    • The dimensions of the protein import channels in the outer and inner mitochondrial membranes
    • Schwartz M.P., Matouschek A. The dimensions of the protein import channels in the outer and inner mitochondrial membranes. Proc. Natl. Acad. Sci. USA. 96:1999;13086-13090.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 13086-13090
    • Schwartz, M.P.1    Matouschek, A.2
  • 4
    • 0033617338 scopus 로고    scopus 로고
    • The structure of precursor proteins during import into mitochondria
    • Schwartz M.P., Huang S., Matouschek A. The structure of precursor proteins during import into mitochondria. J. Biol. Chem. 274:1999;12759-12764.
    • (1999) J. Biol. Chem. , vol.274 , pp. 12759-12764
    • Schwartz, M.P.1    Huang, S.2    Matouschek, A.3
  • 6
    • 0022515029 scopus 로고
    • Binding of a specific ligand inhibits import of a purified precursor protein into mitochondria
    • Eilers M., Schatz G. Binding of a specific ligand inhibits import of a purified precursor protein into mitochondria. Nature. 322:1986;228-232.
    • (1986) Nature , vol.322 , pp. 228-232
    • Eilers, M.1    Schatz, G.2
  • 7
    • 0024202929 scopus 로고
    • A chimeric mitochondrial precursor protein with internal disulfide bridges blocks import of authentic precursors into mitochondria and allows quantitation of import sites
    • Vestweber D., Schatz G. A chimeric mitochondrial precursor protein with internal disulfide bridges blocks import of authentic precursors into mitochondria and allows quantitation of import sites. J. Cell Biol. 107:1988;2037-2043.
    • (1988) J. Cell Biol. , vol.107 , pp. 2037-2043
    • Vestweber, D.1    Schatz, G.2
  • 8
    • 0030969942 scopus 로고    scopus 로고
    • Protein import into mitochondria
    • Neupert W. Protein import into mitochondria. Annu. Rev. Biochem. 66:1997;863-917.
    • (1997) Annu. Rev. Biochem. , vol.66 , pp. 863-917
    • Neupert, W.1
  • 9
    • 0035344460 scopus 로고    scopus 로고
    • Versatility of the mitochondrial protein import machinery
    • Pfanner N., Geissler A. Versatility of the mitochondrial protein import machinery. Nat. Rev. Mol. Cell Biol. 2:2001;1-11.
    • (2001) Nat. Rev. Mol. Cell Biol. , vol.2 , pp. 1-11
    • Pfanner, N.1    Geissler, A.2
  • 10
    • 0028289504 scopus 로고
    • Protein import into mitochondria: The requirement for external ATP is precursor-specific whereas intramitochondrial ATP is universally needed for translocation into the matrix
    • Wachter C., Schatz G., Glick B.S. Protein import into mitochondria: the requirement for external ATP is precursor-specific whereas intramitochondrial ATP is universally needed for translocation into the matrix. Mol. Biol. Cell. 5:1994;465-474.
    • (1994) Mol. Biol. Cell , vol.5 , pp. 465-474
    • Wachter, C.1    Schatz, G.2    Glick, B.S.3
  • 11
    • 0030021114 scopus 로고    scopus 로고
    • Cytoplasmic chaperones in precursor targeting to mitochondria: The role of MSF and hsp70
    • Mihara K., Omura T. Cytoplasmic chaperones in precursor targeting to mitochondria: the role of MSF and hsp70. Trends Cell Biol. 6:1996;104-108.
    • (1996) Trends Cell Biol. , vol.6 , pp. 104-108
    • Mihara, K.1    Omura, T.2
  • 12
    • 0023882692 scopus 로고
    • Modulation of folding pathways of exported proteins by the leader sequence
    • Park S., Liu G., Topping T.B., Cover W.H., Randall L.L. Modulation of folding pathways of exported proteins by the leader sequence. Science. 239:1988;1033-1035.
    • (1988) Science , vol.239 , pp. 1033-1035
    • Park, S.1    Liu, G.2    Topping, T.B.3    Cover, W.H.4    Randall, L.L.5
  • 13
    • 0034328890 scopus 로고    scopus 로고
    • Protein unfolding by mitochondria. The Hsp70 import motor
    • Matouschek A., Pfanner N., Voos W. Protein unfolding by mitochondria. The Hsp70 import motor. EMBO Rep. 1:2000;404-410.
    • (2000) EMBO Rep. , vol.1 , pp. 404-410
    • Matouschek, A.1    Pfanner, N.2    Voos, W.3
  • 15
  • 16
    • 0030844281 scopus 로고    scopus 로고
    • Recombination of protein domains facilitated by co-translational folding in eukaryotes
    • Netzer W., Hartl F. Recombination of protein domains facilitated by co-translational folding in eukaryotes. Nature. 388:1997;343-349.
    • (1997) Nature , vol.388 , pp. 343-349
    • Netzer, W.1    Hartl, F.2
  • 17
    • 0032549815 scopus 로고    scopus 로고
    • Cotranslational biogenesis of NF-κB p50 by the 26S proteasome
    • Lin L., DeMartino G.N., Greene W.C. Cotranslational biogenesis of NF-κB p50 by the 26S proteasome. Cell. 92:1998;819-828.
    • (1998) Cell , vol.92 , pp. 819-828
    • Lin, L.1    DeMartino, G.N.2    Greene, W.C.3
  • 19
    • 0023993152 scopus 로고
    • Latent membrane perturbation activity of a mitochondrial precursor protein is exposed by unfolding
    • Endo T., Schatz G. Latent membrane perturbation activity of a mitochondrial precursor protein is exposed by unfolding. EMBO J. 7:1988;1153-1158.
    • (1988) EMBO J. , vol.7 , pp. 1153-1158
    • Endo, T.1    Schatz, G.2
  • 20
    • 0027442670 scopus 로고
    • Structural features which control folding of homologous proteins in cell-free translation systems. The effect of a mitochondrial-targeting presequence on aspartate aminotransferase
    • Mattingly J.R. Jr., Iriarte A., Martinez-Carrion M. Structural features which control folding of homologous proteins in cell-free translation systems. The effect of a mitochondrial-targeting presequence on aspartate aminotransferase. J. Biol. Chem. 268:1993;26320-26327.
    • (1993) J. Biol. Chem. , vol.268 , pp. 26320-26327
    • Mattingly J.R., Jr.1    Iriarte, A.2    Martinez-Carrion, M.3
  • 21
    • 0035282966 scopus 로고    scopus 로고
    • The mitochondrial Hsp70-dependent import system actively unfolds preproteins and shortens the lag phase of translocation
    • Lim J.H., Martin F., Guiard B., Pfanner N., Voos W. The mitochondrial Hsp70-dependent import system actively unfolds preproteins and shortens the lag phase of translocation. EMBO J. 20:2001;941-950.
    • (2001) EMBO J. , vol.20 , pp. 941-950
    • Lim, J.H.1    Martin, F.2    Guiard, B.3    Pfanner, N.4    Voos, W.5
  • 22
    • 0030781431 scopus 로고    scopus 로고
    • Active unfolding of precursor proteins during mitochondrial protein import
    • Matouschek A., Azem A., Ratliff K., Glick B.S., Schmid K., Schatz G. Active unfolding of precursor proteins during mitochondrial protein import. EMBO J. 16:1997;6727-6736.
    • (1997) EMBO J. , vol.16 , pp. 6727-6736
    • Matouschek, A.1    Azem, A.2    Ratliff, K.3    Glick, B.S.4    Schmid, K.5    Schatz, G.6
  • 23
    • 0024358426 scopus 로고
    • Mapping the transition state and pathway of protein folding by protein engineering
    • Matouschek A., Kellis J.T. Jr., Serrano L., Fersht A.R. Mapping the transition state and pathway of protein folding by protein engineering. Nature. 340:1989;122-126.
    • (1989) Nature , vol.340 , pp. 122-126
    • Matouschek, A.1    Kellis J.T., Jr.2    Serrano, L.3    Fersht, A.R.4
  • 24
    • 0034700142 scopus 로고    scopus 로고
    • Effect of the protein import machinery at the mitochondrial surface on precursor stability
    • Huang S., Murphy S., Matouschek A. Effect of the protein import machinery at the mitochondrial surface on precursor stability. Proc. Natl. Acad. Sci. USA. 97:2000;12991-12996.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 12991-12996
    • Huang, S.1    Murphy, S.2    Matouschek, A.3
  • 25
    • 0032502788 scopus 로고    scopus 로고
    • Cis and trans sites of the TOM complex of mitochondria in unfolding and initial translocation of preproteins
    • Rapaport D., Mayer A., Neupert W., Lill R. cis and trans sites of the TOM complex of mitochondria in unfolding and initial translocation of preproteins. J. Biol. Chem. 273:1998;8806-8813.
    • (1998) J. Biol. Chem. , vol.273 , pp. 8806-8813
    • Rapaport, D.1    Mayer, A.2    Neupert, W.3    Lill, R.4
  • 26
    • 0028117097 scopus 로고
    • The role of hsp70 in conferring unidirectionality on protein translocation into mitochondria
    • Ungermann C., Neupert W., Cyr D.M. The role of hsp70 in conferring unidirectionality on protein translocation into mitochondria. Science. 266:1994;1250-1253.
    • (1994) Science , vol.266 , pp. 1250-1253
    • Ungermann, C.1    Neupert, W.2    Cyr, D.M.3
  • 27
    • 0036221085 scopus 로고    scopus 로고
    • Protein unfolding by the mitochondrial membrane potential
    • This study showed that mitochondria can induce the unfolding of a precursor protein at the mitochondrial surface; the electrical potential across the inner membrane acts directly on the charged amino acids in the targeting sequence. The paper suggests that most proteins will be unfolded by the electrical potential rather than by mtHsp70. The debate about the mechanism of mitochondrial unfolding was focused on the mechanism of action of Hsp70.
    • Huang S., Ratliff K.S., Matouschek A. Protein unfolding by the mitochondrial membrane potential. Nat. Struct. Biol. 9:2002;301-307 This study showed that mitochondria can induce the unfolding of a precursor protein at the mitochondrial surface; the electrical potential across the inner membrane acts directly on the charged amino acids in the targeting sequence. The paper suggests that most proteins will be unfolded by the electrical potential rather than by mtHsp70. The debate about the mechanism of mitochondrial unfolding was focused on the mechanism of action of Hsp70.
    • (2002) Nat. Struct. Biol. , vol.9 , pp. 301-307
    • Huang, S.1    Ratliff, K.S.2    Matouschek, A.3
  • 28
    • 0025953614 scopus 로고
    • Role of an energized inner membrane in mitochondrial protein import. Δψdrives the movement of presequences
    • Martin J., Mahlke K., Pfanner N. Role of an energized inner membrane in mitochondrial protein import. Δψdrives the movement of presequences. J. Biol. Chem. 266:1991;18051-18057.
    • (1991) J. Biol. Chem. , vol.266 , pp. 18051-18057
    • Martin, J.1    Mahlke, K.2    Pfanner, N.3
  • 29
    • 0029670827 scopus 로고    scopus 로고
    • The Δψ and Hsp70/MIM44-dependent reaction cycle driving early steps of protein import into mitochondria
    • Ungermann C., Guiard B., Neupert W., Cyr D.M. The Δψ and Hsp70/MIM44-dependent reaction cycle driving early steps of protein import into mitochondria. EMBO J. 15:1996;735-744.
    • (1996) EMBO J. , vol.15 , pp. 735-744
    • Ungermann, C.1    Guiard, B.2    Neupert, W.3    Cyr, D.M.4
  • 30
    • 0030272378 scopus 로고    scopus 로고
    • Role of Tim23 as voltage sensor and presequence receptor in protein import into mitochondria
    • Bauer M.F., Sirrenberg C., Neupert W., Brunner M. Role of Tim23 as voltage sensor and presequence receptor in protein import into mitochondria. Cell. 87:1996;33-41.
    • (1996) Cell , vol.87 , pp. 33-41
    • Bauer, M.F.1    Sirrenberg, C.2    Neupert, W.3    Brunner, M.4
  • 31
    • 0025039149 scopus 로고
    • Requirement for hsp70 in the mitochondrial matrix for translocation and folding of precursor proteins
    • Kang P.-L., Ostermann J., Shilling J., Neupert W., Craig E.A., Pfanner N. Requirement for hsp70 in the mitochondrial matrix for translocation and folding of precursor proteins. Nature. 348:1990;137-143.
    • (1990) Nature , vol.348 , pp. 137-143
    • Kang, P.-L.1    Ostermann, J.2    Shilling, J.3    Neupert, W.4    Craig, E.A.5    Pfanner, N.6
  • 32
    • 0026070260 scopus 로고
    • Sequential action of mitochondrial chaperones in protein import into the matrix
    • Manning-Krieg U., Scherer P.E., Schatz G. Sequential action of mitochondrial chaperones in protein import into the matrix. EMBO J. 10:1991;3273-3280.
    • (1991) EMBO J. , vol.10 , pp. 3273-3280
    • Manning-Krieg, U.1    Scherer, P.E.2    Schatz, G.3
  • 33
    • 0027490849 scopus 로고
    • A dual role for mitochondrial heat shock protein 70 in membrane translocation of preproteins
    • Gambill B.D., Voos W., Kang P.J., Miao B., Langer T., Craig E.A., Pfanner N. A dual role for mitochondrial heat shock protein 70 in membrane translocation of preproteins. J. Cell Biol. 123:1993;109-117.
    • (1993) J. Cell Biol. , vol.123 , pp. 109-117
    • Gambill, B.D.1    Voos, W.2    Kang, P.J.3    Miao, B.4    Langer, T.5    Craig, E.A.6    Pfanner, N.7
  • 34
    • 0029934520 scopus 로고    scopus 로고
    • Differential requirement for the mitochondrial Hsp70-Tim44 complex in unfolding and translocation of preproteins
    • Voos W., von Ahsen O., Muller H., Guiard B., Rassow J., Pfanner N. Differential requirement for the mitochondrial Hsp70-Tim44 complex in unfolding and translocation of preproteins. EMBO J. 15:1996;2668-2677.
    • (1996) EMBO J. , vol.15 , pp. 2668-2677
    • Voos, W.1    Von Ahsen, O.2    Muller, H.3    Guiard, B.4    Rassow, J.5    Pfanner, N.6
  • 35
    • 0033612301 scopus 로고    scopus 로고
    • The protein import motor of mitochondria: Unfolding and trapping of preproteins are distinct and separable functions of matrix Hsp70
    • Voisine C., Craig E.A., Zufall N., von Ahsen O., Pfanner N., Voos W. The protein import motor of mitochondria: unfolding and trapping of preproteins are distinct and separable functions of matrix Hsp70. Cell. 97:1999;565-574.
    • (1999) Cell , vol.97 , pp. 565-574
    • Voisine, C.1    Craig, E.A.2    Zufall, N.3    Von Ahsen, O.4    Pfanner, N.5    Voos, W.6
  • 36
    • 0031918163 scopus 로고    scopus 로고
    • Strong precursor-pore interactions constrain models for mitochondrial protein import
    • Chauwin J.F., Oster G., Glick B.S. Strong precursor-pore interactions constrain models for mitochondrial protein import. Biophys. J. 74:1998;1732-1743.
    • (1998) Biophys. J. , vol.74 , pp. 1732-1743
    • Chauwin, J.F.1    Oster, G.2    Glick, B.S.3
  • 37
    • 0024454311 scopus 로고
    • Translocation arrest by reversible folding of a precursor protein imported into mitochondria. A means to quantitate translocation contact sites
    • Rassow J., Guiard B., Wienhues U., Herzog V., Hartl F.U., Neupert W. Translocation arrest by reversible folding of a precursor protein imported into mitochondria. A means to quantitate translocation contact sites. J. Cell Biol. 109:1989;1421-1428.
    • (1989) J. Cell Biol. , vol.109 , pp. 1421-1428
    • Rassow, J.1    Guiard, B.2    Wienhues, U.3    Herzog, V.4    Hartl, F.U.5    Neupert, W.6
  • 39
    • 0027332553 scopus 로고
    • 2 to the mitochondrial intermembrane space: The tightly folded heme-binding domain makes import dependent upon matrix ATP
    • 2 to the mitochondrial intermembrane space: the tightly folded heme-binding domain makes import dependent upon matrix ATP. Protein Sci. 2:1993;1901-1917.
    • (1993) Protein Sci. , vol.2 , pp. 1901-1917
    • Glick, B.S.1    Wachter, C.2    Reid, G.A.3    Schatz, G.4
  • 40
    • 0027362778 scopus 로고
    • Presequence and mature part of preproteins strongly influence the dependence of mitochondrial protein import on heat shock protein 70 in the matrix
    • Voos W., Gambill B.D., Guiard B., Pfanner N., Craig E.A. Presequence and mature part of preproteins strongly influence the dependence of mitochondrial protein import on heat shock protein 70 in the matrix. J. Cell Biol. 123:1993;119-126.
    • (1993) J. Cell Biol. , vol.123 , pp. 119-126
    • Voos, W.1    Gambill, B.D.2    Guiard, B.3    Pfanner, N.4    Craig, E.A.5
  • 41
    • 0035266072 scopus 로고    scopus 로고
    • ATP-dependent proteases degrade their substrates by processively unraveling them from the degradation signal
    • This paper showed that several ATP-dependent proteases can unfold their substrates by changing the substrates' unfolding pathways. It suggested that the mechanisms of unfolding by mitochondria and proteases are very similar. The study found that some protein folds are more difficult to unravel by the proteases than others and demonstrated that these differences in resistance to unfolding could explain the mechanism by which the proteasome activates a transcription factor by partial degradation.
    • Lee C., Schwartz M.P., Prakash S., Iwakura M., Matouschek A. ATP-dependent proteases degrade their substrates by processively unraveling them from the degradation signal. Mol. Cell. 7:2001;627-637 This paper showed that several ATP-dependent proteases can unfold their substrates by changing the substrates' unfolding pathways. It suggested that the mechanisms of unfolding by mitochondria and proteases are very similar. The study found that some protein folds are more difficult to unravel by the proteases than others and demonstrated that these differences in resistance to unfolding could explain the mechanism by which the proteasome activates a transcription factor by partial degradation.
    • (2001) Mol. Cell , vol.7 , pp. 627-637
    • Lee, C.1    Schwartz, M.P.2    Prakash, S.3    Iwakura, M.4    Matouschek, A.5
  • 42
    • 0021767867 scopus 로고
    • The amino-terminal region of an imported mitochondrial precursor polypeptide can direct cytoplasmic dihydrofolate reductase into the mitochondrial matrix
    • Hurt E.C., Pesold-Hurt B., Schatz G. The amino-terminal region of an imported mitochondrial precursor polypeptide can direct cytoplasmic dihydrofolate reductase into the mitochondrial matrix. EMBO J. 3:1984;3149-3156.
    • (1984) EMBO J. , vol.3 , pp. 3149-3156
    • Hurt, E.C.1    Pesold-Hurt, B.2    Schatz, G.3
  • 43
    • 0022065342 scopus 로고
    • A leader peptide is sufficient to direct mitochondrial import of a chimeric protein
    • Horwich A.L., Kalousek F., Mellman I., Rosenberg L.E. A leader peptide is sufficient to direct mitochondrial import of a chimeric protein. EMBO J. 4:1985;1129-1135.
    • (1985) EMBO J. , vol.4 , pp. 1129-1135
    • Horwich, A.L.1    Kalousek, F.2    Mellman, I.3    Rosenberg, L.E.4
  • 44
    • 0024317055 scopus 로고
    • The mitochondrial targeting function of randomly generated peptide sequences correlates with predicted helical amphiphilicity
    • Lemire B.D., Fankhauser C., Baker A., Schatz G. The mitochondrial targeting function of randomly generated peptide sequences correlates with predicted helical amphiphilicity. J. Biol. Chem. 264:1989;20206-20215.
    • (1989) J. Biol. Chem. , vol.264 , pp. 20206-20215
    • Lemire, B.D.1    Fankhauser, C.2    Baker, A.3    Schatz, G.4
  • 45
    • 0023054140 scopus 로고
    • Targeting efficiency of a mitochondrial pre-sequence is dependent on the passenger protein
    • Van Steeg H., Oudshoorn P., Van Hell B., Polman J.E., Grivell L.A. Targeting efficiency of a mitochondrial pre-sequence is dependent on the passenger protein. EMBO J. 5:1986;3643-3650.
    • (1986) EMBO J. , vol.5 , pp. 3643-3650
    • Van Steeg, H.1    Oudshoorn, P.2    Van Hell, B.3    Polman, J.E.4    Grivell, L.A.5
  • 46
    • 0024317248 scopus 로고
    • Tight folding of a passenger protein can interfere with the targeting function of a mitochondrial presequence
    • Verner K., Lemire B.D. Tight folding of a passenger protein can interfere with the targeting function of a mitochondrial presequence. EMBO J. 8:1989;1491-1495.
    • (1989) EMBO J. , vol.8 , pp. 1491-1495
    • Verner, K.1    Lemire, B.D.2
  • 47
    • 0023987428 scopus 로고
    • Point mutations destabilizing a precursor protein enhance its post-translational import into mitochondria
    • Vestweber D., Schatz G. Point mutations destabilizing a precursor protein enhance its post-translational import into mitochondria. EMBO J. 7:1988;1147-1151.
    • (1988) EMBO J. , vol.7 , pp. 1147-1151
    • Vestweber, D.1    Schatz, G.2
  • 48
    • 0023989329 scopus 로고
    • Unfolding and refolding of a purified precursor protein during import into isolated mitochondria
    • Eilers M., Hwang S., Schatz G. Unfolding and refolding of a purified precursor protein during import into isolated mitochondria. EMBO J. 7:1988;1139-1145.
    • (1988) EMBO J. , vol.7 , pp. 1139-1145
    • Eilers, M.1    Hwang, S.2    Schatz, G.3
  • 49
    • 0030918441 scopus 로고    scopus 로고
    • A folded protein can be transported across the chloroplast envelope and thylakoid membranes
    • Clark S.A., Theg S.M. A folded protein can be transported across the chloroplast envelope and thylakoid membranes. Mol. Biol. Cell. 8:1997;923-934.
    • (1997) Mol. Biol. Cell , vol.8 , pp. 923-934
    • Clark, S.A.1    Theg, S.M.2
  • 50
    • 0027674916 scopus 로고
    • A strong protein unfolding activity is associated with the binding of precursor chloroplast proteins to chloroplast envelopes
    • Guera A., America T., van Waas M., Weisbeek P.J. A strong protein unfolding activity is associated with the binding of precursor chloroplast proteins to chloroplast envelopes. Plant Mol. Biol. 23:1993;309-324.
    • (1993) Plant Mol. Biol. , vol.23 , pp. 309-324
    • Guera, A.1    America, T.2    Van Waas, M.3    Weisbeek, P.J.4
  • 52
    • 0028907432 scopus 로고
    • Enzymatic product formation impairs both the chloroplast receptor-binding function as well as translocation competence of the NADPH: Protochlorophyllide oxidoreductase, a nuclear-encoded plastid precursor protein
    • Reinbothe S., Reinbothe C., Runge S., Apel K. Enzymatic product formation impairs both the chloroplast receptor-binding function as well as translocation competence of the NADPH: protochlorophyllide oxidoreductase, a nuclear-encoded plastid precursor protein. J. Cell Biol. 129:1995;299-308.
    • (1995) J. Cell Biol. , vol.129 , pp. 299-308
    • Reinbothe, S.1    Reinbothe, C.2    Runge, S.3    Apel, K.4
  • 53
    • 0028595688 scopus 로고
    • Identification of chloroplast envelope proteins in close physical proximity to a partially translocated chimeric precursor protein
    • Wu C., Seibert F.S., Ko K. Identification of chloroplast envelope proteins in close physical proximity to a partially translocated chimeric precursor protein. J. Biol. Chem. 269:1994;32264-32271.
    • (1994) J. Biol. Chem. , vol.269 , pp. 32264-32271
    • Wu, C.1    Seibert, F.S.2    Ko, K.3
  • 54
    • 0027469030 scopus 로고
    • Identification of intermediates in the pathway of protein import into chloroplasts and their localization to envelope contact sites
    • Schnell D.J., Blobel G. Identification of intermediates in the pathway of protein import into chloroplasts and their localization to envelope contact sites. J. Cell Biol. 120:1993;103-115.
    • (1993) J. Cell Biol. , vol.120 , pp. 103-115
    • Schnell, D.J.1    Blobel, G.2
  • 55
    • 0028017537 scopus 로고
    • Chloroplast protein import. Chloroplast envelopes and thylakoids have different abilities to unfold proteins
    • Endo T., Kawakami M., Goto A., America T., Weisbeek P., Nakai M. Chloroplast protein import. Chloroplast envelopes and thylakoids have different abilities to unfold proteins. Eur. J. Biochem. 225:1994;403-409.
    • (1994) Eur. J. Biochem. , vol.225 , pp. 403-409
    • Endo, T.1    Kawakami, M.2    Goto, A.3    America, T.4    Weisbeek, P.5    Nakai, M.6
  • 56
    • 0030595327 scopus 로고    scopus 로고
    • Signal sequences: The same yet different
    • Zheng N., Gierasch L.M. Signal sequences: the same yet different. Cell. 86:1996;849-852.
    • (1996) Cell , vol.86 , pp. 849-852
    • Zheng, N.1    Gierasch, L.M.2
  • 57
    • 0030611388 scopus 로고    scopus 로고
    • The aqueous pore through the translocon has a diameter of 40-60 Å during cotranslational protein translocation at the ER membrane
    • Hamman B.D., Chen J.C., Johnson E.E., Johnson A.E. The aqueous pore through the translocon has a diameter of 40-60 Å during cotranslational protein translocation at the ER membrane. Cell. 89:1997;535-544.
    • (1997) Cell , vol.89 , pp. 535-544
    • Hamman, B.D.1    Chen, J.C.2    Johnson, E.E.3    Johnson, A.E.4
  • 58
  • 60
    • 2042451849 scopus 로고
    • Import of honeybee prepromelittin into the endoplasmic reticulum: Energy requirements for membrane insertion
    • Muller G., Zimmermann R. Import of honeybee prepromelittin into the endoplasmic reticulum: energy requirements for membrane insertion. EMBO J. 7:1988;639-648.
    • (1988) EMBO J. , vol.7 , pp. 639-648
    • Muller, G.1    Zimmermann, R.2
  • 61
    • 0029979607 scopus 로고    scopus 로고
    • Common principles of protein translocation across membranes
    • Schatz G., Dobberstein B. Common principles of protein translocation across membranes. Science. 271:1996;1519-1526.
    • (1996) Science , vol.271 , pp. 1519-1526
    • Schatz, G.1    Dobberstein, B.2
  • 62
    • 0033520987 scopus 로고    scopus 로고
    • Posttranslational quality control: Folding, refolding, and degrading proteins
    • Wickner S., Maurizi M.R., Gottesman S. Posttranslational quality control: folding, refolding, and degrading proteins. Science. 286:1999;1888-1893.
    • (1999) Science , vol.286 , pp. 1888-1893
    • Wickner, S.1    Maurizi, M.R.2    Gottesman, S.3
  • 63
    • 0032867676 scopus 로고    scopus 로고
    • The 26S proteasome: A molecular machine designed for controlled proteolysis
    • Voges D., Zwickl P., Baumeister W. The 26S proteasome: a molecular machine designed for controlled proteolysis. Annu. Rev. Biochem. 68:1999;1015-1068.
    • (1999) Annu. Rev. Biochem. , vol.68 , pp. 1015-1068
    • Voges, D.1    Zwickl, P.2    Baumeister, W.3
  • 64
    • 0032535483 scopus 로고    scopus 로고
    • The ubiquitin-proteasome pathway: On protein death and cell life
    • Ciechanover A. The ubiquitin-proteasome pathway: on protein death and cell life. EMBO J. 17:1998;7151-7160.
    • (1998) EMBO J. , vol.17 , pp. 7151-7160
    • Ciechanover, A.1
  • 65
    • 0033766480 scopus 로고    scopus 로고
    • A gated channel into the proteasome core particle
    • This paper describes how the channel through which substrate proteins access the active sites of proteolysis of the proteasome is gated by the N termini of α subunits physically blocking the entrance to the channel.
    • Groll M., Bajorek M., Kohler A., Moroder L., Rubin D.M., Huber R., Glickman M.H., Finley D. A gated channel into the proteasome core particle. Nat. Struct. Biol. 7:2000;1062-1067 This paper describes how the channel through which substrate proteins access the active sites of proteolysis of the proteasome is gated by the N termini of α subunits physically blocking the entrance to the channel.
    • (2000) Nat. Struct. Biol. , vol.7 , pp. 1062-1067
    • Groll, M.1    Bajorek, M.2    Kohler, A.3    Moroder, L.4    Rubin, D.M.5    Huber, R.6    Glickman, M.H.7    Finley, D.8
  • 66
    • 0034597824 scopus 로고    scopus 로고
    • Structural basis for the activation of 20S proteasomes by 11S regulators
    • This paper shows the structure of the opened substrate channel in the proteasome particle activated by 11S caps.
    • Whitby F.G., Masters E.I., Kramer L., Knowlton J.R., Yao Y., Wang C.C., Hill C.P. Structural basis for the activation of 20S proteasomes by 11S regulators. Nature. 408:2000;115-120 This paper shows the structure of the opened substrate channel in the proteasome particle activated by 11S caps.
    • (2000) Nature , vol.408 , pp. 115-120
    • Whitby, F.G.1    Masters, E.I.2    Kramer, L.3    Knowlton, J.R.4    Yao, Y.5    Wang, C.C.6    Hill, C.P.7
  • 67
    • 0032488846 scopus 로고    scopus 로고
    • The proteasome: Paradigm of a self-compartmentalizing protease
    • Baumeister W., Walz J., Zühl F., Seemüller E. The proteasome: paradigm of a self-compartmentalizing protease. Cell. 92:1998;367-380.
    • (1998) Cell , vol.92 , pp. 367-380
    • Baumeister, W.1    Walz, J.2    Zühl, F.3    Seemüller, E.4
  • 68
    • 0028951190 scopus 로고
    • Methotrexate inhibits proteolysis of dihydrofolate reductase by the N-end rule pathway
    • Johnston J.A., Johnson E.S., Waller P.R.H., Varshavsky A. 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.H.3    Varshavsky, A.4
  • 70
    • 0030726159 scopus 로고    scopus 로고
    • Protein translocation channels in the proteasome and other proteases
    • Larsen C.N., Finley D. Protein translocation channels in the proteasome and other proteases. Cell. 91:1997;431-434.
    • (1997) Cell , vol.91 , pp. 431-434
    • Larsen, C.N.1    Finley, D.2
  • 71
    • 0033517351 scopus 로고    scopus 로고
    • Global unfolding of a substrate protein by the Hsp100 chaperone ClpA
    • Weber-Ban E.U., Reid B.G., Miranker A.D., Horwich A.L. Global unfolding of a substrate protein by the Hsp100 chaperone ClpA. Nature. 401:1999;90-93.
    • (1999) Nature , vol.401 , pp. 90-93
    • Weber-Ban, E.U.1    Reid, B.G.2    Miranker, A.D.3    Horwich, A.L.4
  • 77
    • 0035694696 scopus 로고    scopus 로고
    • Proteins are unfolded on the surface of the ATPase ring before transport into the proteasome
    • •] also develop the finding that substrate proteins translocate from a site of unfolding at the caps near the end of the cylindrical protease particle towards the central proteolytic sites during degradation.
    • •] also develop the finding that substrate proteins translocate from a site of unfolding at the caps near the end of the cylindrical protease particle towards the central proteolytic sites during degradation.
    • (2001) Mol. Cell , vol.8 , pp. 1339-1349
    • Navon, A.1    Goldberg, A.L.2
  • 78
    • 0035957317 scopus 로고    scopus 로고
    • ClpA mediates directional translocation of the substrate proteins into the ClpP protease
    • This paper elegantly demonstrates the sequential degradation by ClpAP of a substrate protein from its C-terminal protease-targeting sequence to its N terminus. The authors come to this conclusion from fluorescence energy transfer experiments in which fluorescent labels are introduced at different ends of the substrate and in the protease.
    • Reid B.G., Fenton W.A., Horwich A.L., Weber-Ban E.U. ClpA mediates directional translocation of the substrate proteins into the ClpP protease. Proc. Natl. Acad. Sci. USA. 98:2001;3768-3772 This paper elegantly demonstrates the sequential degradation by ClpAP of a substrate protein from its C-terminal protease-targeting sequence to its N terminus. The authors come to this conclusion from fluorescence energy transfer experiments in which fluorescent labels are introduced at different ends of the substrate and in the protease.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 3768-3772
    • Reid, B.G.1    Fenton, W.A.2    Horwich, A.L.3    Weber-Ban, E.U.4
  • 79
    • 0034845197 scopus 로고    scopus 로고
    • Selective degradation of ubiquitinated Sic1 by purified 26S proteasome yields active S phase cyclin-Cdk
    • This important paper demonstrates that the proteasome can degrade specifically one component of a protein complex. The paper is also an experimental tour de force and describes the reconstitution from purified components of the ubiquitination machinery and proteasomal degradation machinery in vitro.
    • Verma R., McDonald H., Yates J.R. III, Deshaies R.J. Selective degradation of ubiquitinated Sic1 by purified 26S proteasome yields active S phase cyclin-Cdk. Mol. Cell. 8:2001;439-448 This important paper demonstrates that the proteasome can degrade specifically one component of a protein complex. The paper is also an experimental tour de force and describes the reconstitution from purified components of the ubiquitination machinery and proteasomal degradation machinery in vitro.
    • (2001) Mol. Cell , vol.8 , pp. 439-448
    • Verma, R.1    McDonald, H.2    Yates J.R. III3    Deshaies, R.J.4
  • 80
    • 0035139109 scopus 로고    scopus 로고
    • Cellular defenses against unfolded proteins: A cell biologist thinks about neurodegenerative diseases
    • Sherman M.Y., Goldberg A.L. Cellular defenses against unfolded proteins: a cell biologist thinks about neurodegenerative diseases. Neuron. 29:2001;15-32.
    • (2001) Neuron. , vol.29 , pp. 15-32
    • Sherman, M.Y.1    Goldberg, A.L.2
  • 82
    • 0030801746 scopus 로고    scopus 로고
    • The structure of amyloid fibrils by electron microscopy and X-ray diffraction
    • Sunde M., Blake C. The structure of amyloid fibrils by electron microscopy and X-ray diffraction. Adv. Protein Chem. 50:1997;123-159.
    • (1997) Adv. Protein Chem. , vol.50 , pp. 123-159
    • Sunde, M.1    Blake, C.2
  • 84
    • 0042847751 scopus 로고    scopus 로고
    • Cryo-electron microscopy structure of an SH3 amyloid fibril and model of the molecular packing
    • Jimenez J.L., Guijarro J.I., Orlova E., Zurdo J., Dobson C.M., Sunde M., Saibil H.R. Cryo-electron microscopy structure of an SH3 amyloid fibril and model of the molecular packing. EMBO J. 18:1999;815-821.
    • (1999) EMBO J. , vol.18 , pp. 815-821
    • Jimenez, J.L.1    Guijarro, J.I.2    Orlova, E.3    Zurdo, J.4    Dobson, C.M.5    Sunde, M.6    Saibil, H.R.7
  • 85
    • 0035826234 scopus 로고    scopus 로고
    • Amyloid fibrils from muscle myoglobin
    • Fandrich M., Fletcher M.A., Dobson C.M. Amyloid fibrils from muscle myoglobin. Nature. 410:2001;165-166.
    • (2001) Nature , vol.410 , pp. 165-166
    • Fandrich, M.1    Fletcher, M.A.2    Dobson, C.M.3
  • 86
    • 0028283985 scopus 로고
    • Glutamine repeats as polar zippers: Their possible role in inherited neurodegenerative diseases
    • Perutz M.F., Johnson T., Suzuki M., Finch J.T. Glutamine repeats as polar zippers: their possible role in inherited neurodegenerative diseases. Proc. Natl. Acad. Sci. USA. 91:1994;5355-5358.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 5355-5358
    • Perutz, M.F.1    Johnson, T.2    Suzuki, M.3    Finch, J.T.4
  • 87
    • 0034283837 scopus 로고    scopus 로고
    • The Rel/NF-κB family: Friend and foe
    • Perkins N.D. The Rel/NF-κB family: friend and foe. Trends Biochem. Sci. 25:2000;434-440.
    • (2000) Trends Biochem. Sci. , vol.25 , pp. 434-440
    • Perkins, N.D.1
  • 88
    • 0032576777 scopus 로고    scopus 로고
    • Regulation of the Hedgehog and Wingless signalling pathways by the F-box/WD40-repeat protein Slimb
    • Jiang J., Struhl G. Regulation of the Hedgehog and Wingless signalling pathways by the F-box/WD40-repeat protein Slimb. Nature. 391:1998;493-496.
    • (1998) Nature , vol.391 , pp. 493-496
    • Jiang, J.1    Struhl, G.2
  • 89
    • 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., Jentsch S. Activation of a membrane-bound transcription factor by regulated ubiquitin/proteasome-dependent processing. Cell. 102:2000;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
  • 90
    • 0036091848 scopus 로고    scopus 로고
    • Taking a bite: Proteasomal protein processing
    • An interesting review that describes different mechanisms that could lead to partial degradation of a substrate molecule.
    • Rape M., Jentsch S. Taking a bite: proteasomal protein processing. Nat. Cell Biol. 4:2002;E113-E116 An interesting review that describes different mechanisms that could lead to partial degradation of a substrate molecule.
    • (2002) Nat. Cell Biol. , vol.4
    • Rape, M.1    Jentsch, S.2
  • 93
    • 0031006659 scopus 로고    scopus 로고
    • Elasticity and unfolding of single molecules of the giant muscle protein titin
    • Tskhovrebova L., Trinick J., Sleep J.A., Simmons R.M. Elasticity and unfolding of single molecules of the giant muscle protein titin. Nature. 387:1997;308-312.
    • (1997) Nature , vol.387 , pp. 308-312
    • Tskhovrebova, L.1    Trinick, J.2    Sleep, J.A.3    Simmons, R.M.4
  • 94
    • 0031011695 scopus 로고    scopus 로고
    • Reversible unfolding of individual titin immunoglobulin domains by AFM
    • Rief M., Gautel M., Oesterhelt F., Fernandez J.M., Gaub H.E. Reversible unfolding of individual titin immunoglobulin domains by AFM. Science. 276:1997;1109-1112.
    • (1997) Science , vol.276 , pp. 1109-1112
    • Rief, M.1    Gautel, M.2    Oesterhelt, F.3    Fernandez, J.M.4    Gaub, H.E.5
  • 95
    • 0031002460 scopus 로고    scopus 로고
    • Folding-unfolding transitions in single titin molecules characterized with laser tweezers
    • Kellermayer M.S.Z., Smith S.B., Granzier H.L., Bustamante C. Folding-unfolding transitions in single titin molecules characterized with laser tweezers. Science. 276:1997;1112-1116.
    • (1997) Science , vol.276 , pp. 1112-1116
    • Kellermayer, M.S.Z.1    Smith, S.B.2    Granzier, H.L.3    Bustamante, C.4
  • 98
    • 0035115798 scopus 로고    scopus 로고
    • Unfolding of titin domains explains the viscoelastic behavior of skeletal myofibrils
    • Minajeva A., Kulke M., Fernandez J.M., Linke W.A. Unfolding of titin domains explains the viscoelastic behavior of skeletal myofibrils. Biophys. J. 80:2001;1442-1451.
    • (2001) Biophys. J. , vol.80 , pp. 1442-1451
    • Minajeva, A.1    Kulke, M.2    Fernandez, J.M.3    Linke, W.A.4
  • 99
    • 0033582763 scopus 로고    scopus 로고
    • Single molecule force spectroscopy of spectrin repeats: Low unfolding forces in helix bundles
    • Rief M., Pascual J., Saraste M., Gaub H.E. Single molecule force spectroscopy of spectrin repeats: low unfolding forces in helix bundles. J. Mol. Biol. 286:1999;553-561.
    • (1999) J. Mol. Biol. , vol.286 , pp. 553-561
    • Rief, M.1    Pascual, J.2    Saraste, M.3    Gaub, H.E.4
  • 100
    • 0034804341 scopus 로고    scopus 로고
    • Can non-mechanical proteins withstand force? Stretching barnase by atomic force microscopy and molecular dynamics simulation
    • Best R.B., Li B., Steward A., Daggett V., Clarke J. Can non-mechanical proteins withstand force? Stretching barnase by atomic force microscopy and molecular dynamics simulation. Biophys. J. 81:2001;2344-2356.
    • (2001) Biophys. J. , vol.81 , pp. 2344-2356
    • Best, R.B.1    Li, B.2    Steward, A.3    Daggett, V.4    Clarke, J.5
  • 102
    • 0032516205 scopus 로고    scopus 로고
    • The molecular elasticity of the extracellular matrix protein tenascin
    • Oberhauser A.F., Marszalek P.E., Erickson H.P., Fernandez J.M. The molecular elasticity of the extracellular matrix protein tenascin. Nature. 393:1998;181-185.
    • (1998) Nature , vol.393 , pp. 181-185
    • Oberhauser, A.F.1    Marszalek, P.E.2    Erickson, H.P.3    Fernandez, J.M.4
  • 103
    • 0033593272 scopus 로고    scopus 로고
    • Exploring the folding funnel of a polypeptide chain by biophysical studies on protein fragments
    • Neira J.L., Fersht A.R. Exploring the folding funnel of a polypeptide chain by biophysical studies on protein fragments. J. Mol. Biol. 285:1999;1309-1333.
    • (1999) J. Mol. Biol. , vol.285 , pp. 1309-1333
    • Neira, J.L.1    Fersht, A.R.2
  • 104
    • 0037099608 scopus 로고    scopus 로고
    • The protein import motor of mitochondria: A targeted molecular ratchet driving unfolding and translocation
    • Okamoto K., Brinker A., Paschen S.A., Moarefi I., Hayer-Hartl M., Neupert W., Brunner M. The protein import motor of mitochondria: a targeted molecular ratchet driving unfolding and translocation. EMBO J. 21:2002;3659-3671.
    • (2002) EMBO J. , vol.21 , pp. 3659-3671
    • Okamoto, K.1    Brinker, A.2    Paschen, S.A.3    Moarefi, I.4    Hayer-Hartl, M.5    Neupert, W.6    Brunner, M.7
  • 106
    • 0034624753 scopus 로고    scopus 로고
    • Autoinhibition and activation mechanisms of the Wiskott-Aldrich syndrome protein
    • This paper describes the conformational changes in WASP during its activation and shows that the changes are so extensive that they represent the unfolding of an entire domain. The study is part of a series of papers that describes the mechanism by which small G proteins regulate the formation of actin fibers.
    • Kim A.S., Kakalis L.T., Abdul-Manan N., Liu G.A., Rosen M.K. Autoinhibition and activation mechanisms of the Wiskott-Aldrich syndrome protein. Nature. 404:2000;151-158 This paper describes the conformational changes in WASP during its activation and shows that the changes are so extensive that they represent the unfolding of an entire domain. The study is part of a series of papers that describes the mechanism by which small G proteins regulate the formation of actin fibers.
    • (2000) Nature , vol.404 , pp. 151-158
    • Kim, A.S.1    Kakalis, L.T.2    Abdul-Manan, N.3    Liu, G.A.4    Rosen, M.K.5
  • 108
    • 0029042511 scopus 로고
    • Crystal structure of the 20S proteasome from the archaeon T. acidophilum at 3.4 Å resolution
    • Lowe J., Stock D., Jap B., Zwickl P., Baumeister W., Huber R. Crystal structure of the 20S proteasome from the archaeon T. acidophilum at 3.4 Å 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
  • 111
    • 0029126356 scopus 로고
    • Homology in structural organization between E. coli ClpAP protease and the eukaryotic 26 S proteasome
    • Kessel M., Maurizi M.R., Kim B., Kocsis E., Trus B.L., Singh S.K., Steven A.C. Homology in structural organization between E. coli ClpAP protease and the eukaryotic 26 S proteasome. J. Mol. Biol. 250:1995;587-594.
    • (1995) J. Mol. Biol. , vol.250 , pp. 587-594
    • Kessel, M.1    Maurizi, M.R.2    Kim, B.3    Kocsis, E.4    Trus, B.L.5    Singh, S.K.6    Steven, A.C.7
  • 112
    • 0030691115 scopus 로고    scopus 로고
    • The structure of ClpP at 2.3 Å resolution suggests a model for ATP-dependent proteolysis
    • Wang J., Hartling J.A., Flanagan J.M. The structure of ClpP at 2.3 Å resolution suggests a model for ATP-dependent proteolysis. Cell. 91:1997;447-456.
    • (1997) Cell , vol.91 , pp. 447-456
    • Wang, J.1    Hartling, J.A.2    Flanagan, J.M.3


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