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Volumn 273, Issue 3, 1997, Pages 752-762

Catalysis of protein folding by Parvulin

Author keywords

Autocatalytic folding; Folding enzyme; Parvulin; Prolyl isomerase; Protein folding

Indexed keywords

CYCLOPHILIN; ISOMERASE; PARVULIN; PROLINE; RIBONUCLEASE T1; TETRAPEPTIDE; UNCLASSIFIED DRUG;

EID: 0031592949     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1997.1301     Document Type: Article
Times cited : (50)

References (60)
  • 1
    • 0016711868 scopus 로고
    • Consideration of the possibility that the slow step in protein denaturation reactions is due tocistrans
    • Brandts J. F., Halvorson H. R., Brennan M. Consideration of the possibility that the slow step in protein denaturation reactions is due tocistrans. Biochemistry. 14:1975;4953-4963.
    • (1975) Biochemistry , vol.14 , pp. 4953-4963
    • Brandts, J.F.1    Halvorson, H.R.2    Brennan, M.3
  • 2
    • 0028789790 scopus 로고
    • Trigger factor, one of theEscherichia coli
    • Callebaut I., Mornon J. P. Trigger factor, one of theEscherichia coli. FEBS Letters. 374:1995;211-215.
    • (1995) FEBS Letters , vol.374 , pp. 211-215
    • Callebaut, I.1    Mornon, J.P.2
  • 4
    • 0023218558 scopus 로고
    • Proline isomerism in staphylococcal nuclease characterized by NMR and site directed mutagenesis
    • Evans P. A., Dobson C. M., Kautz R. A., Hatfull G., Fox R. O. Proline isomerism in staphylococcal nuclease characterized by NMR and site directed mutagenesis. Nature. 329:1987;266-268.
    • (1987) Nature , vol.329 , pp. 266-268
    • Evans, P.A.1    Dobson, C.M.2    Kautz, R.A.3    Hatfull, G.4    Fox, R.O.5
  • 5
    • 0028050923 scopus 로고
    • Peptidyl-prolylcistrans
    • Fischer G. Peptidyl-prolylcistrans. Agnew. Chem. Int. Ed. 33:1994;1415-1436.
    • (1994) Agnew. Chem. Int. Ed. , vol.33 , pp. 1415-1436
    • Fischer, G.1
  • 6
    • 0021668676 scopus 로고
    • Nachweis einer enzymkatalyse für diecistrans
    • Fischer G., Bang H., Mech C. Nachweis einer enzymkatalyse für diecistrans. Biomed. Biochim. Acta. 43:1984;1101-1111.
    • (1984) Biomed. Biochim. Acta , vol.43 , pp. 1101-1111
    • Fischer, G.1    Bang, H.2    Mech, C.3
  • 7
    • 0027940713 scopus 로고
    • Specific incorporation of cyclophilin A into HIV-1 virions
    • Franke E. K., Yuan H. E. H., Luban J. Specific incorporation of cyclophilin A into HIV-1 virions. Nature. 372:1994;359-362.
    • (1994) Nature , vol.372 , pp. 359-362
    • Franke, E.K.1    Yuan, H.E.H.2    Luban, J.3
  • 10
    • 0024448151 scopus 로고
    • Calculation of protein extinction coefficients from amino acid sequence data
    • Gill S. C., von Hippel P. H. Calculation of protein extinction coefficients from amino acid sequence data. Anal. Biochem. 182:1989;319-326.
    • (1989) Anal. Biochem. , vol.182 , pp. 319-326
    • Gill, S.C.1    Von Hippel, P.H.2
  • 11
  • 12
    • 0029069724 scopus 로고
    • PTF1 encodes an essential protein inSaccharomyces cerevisiae
    • Hani J., Stumpf G., Domdey H. PTF1 encodes an essential protein inSaccharomyces cerevisiae. FEBS Letters. 365:1995;198-202.
    • (1995) FEBS Letters , vol.365 , pp. 198-202
    • Hani, J.1    Stumpf, G.2    Domdey, H.3
  • 13
    • 11944257991 scopus 로고
    • Mechanistic studies of enzymic and nonenzymic prolylcistrans
    • Harrison R. K., Stein R. L. Mechanistic studies of enzymic and nonenzymic prolylcistrans. J. Am. Chem. Soc. 114:1992;3464-3471.
    • (1992) J. Am. Chem. Soc. , vol.114 , pp. 3464-3471
    • Harrison, R.K.1    Stein, R.L.2
  • 17
    • 0020024242 scopus 로고
    • Specific intermediates in the folding reactions of small proteins and the mechanism of protein folding
    • Kim P. S., Baldwin R. L. Specific intermediates in the folding reactions of small proteins and the mechanism of protein folding. Annu. Rev. Biochem. 51:1982;459-489.
    • (1982) Annu. Rev. Biochem. , vol.51 , pp. 459-489
    • Kim, P.S.1    Baldwin, R.L.2
  • 18
    • 0025345415 scopus 로고
    • Intermediates in the folding reactions of small proteins
    • Kim P. S., Baldwin R. L. Intermediates in the folding reactions of small proteins. Annu. Rev. Biochem. 59:1990;631-660.
    • (1990) Annu. Rev. Biochem. , vol.59 , pp. 631-660
    • Kim, P.S.1    Baldwin, R.L.2
  • 20
    • 0027222723 scopus 로고
    • The PrsA lipoprotein is essential for protein secretion inBacillus subtilis
    • Kontinen V. P., Sarvas M. The PrsA lipoprotein is essential for protein secretion inBacillus subtilis. Mol. Microbiol. 8:1993;727-737.
    • (1993) Mol. Microbiol. , vol.8 , pp. 727-737
    • Kontinen, V.P.1    Sarvas, M.2
  • 21
    • 0025287813 scopus 로고
    • The rate and structural consequences of prolinecistranscis
    • Kördel J., Forsen S., Drakenberg T., Chazin W. J. The rate and structural consequences of prolinecistranscis. Biochemistry. 29:1990;4400-4409.
    • (1990) Biochemistry , vol.29 , pp. 4400-4409
    • Kördel, J.1    Forsen, S.2    Drakenberg, T.3    Chazin, W.J.4
  • 22
    • 0023236959 scopus 로고
    • Catalysis of protein folding by prolyl isomerase
    • Lang K., Schmid F. X., Fischer G. Catalysis of protein folding by prolyl isomerase. Nature. 329:1987;268-270.
    • (1987) Nature , vol.329 , pp. 268-270
    • Lang, K.1    Schmid, F.X.2    Fischer, G.3
  • 23
    • 0029918686 scopus 로고    scopus 로고
    • SurA assists the folding ofEscherichia coli
    • Lazar S. W., Kolter R. SurA assists the folding ofEscherichia coli. J. Bacteriol. 178:1996;1770-1773.
    • (1996) J. Bacteriol. , vol.178 , pp. 1770-1773
    • Lazar, S.W.1    Kolter, R.2
  • 24
    • 0024285157 scopus 로고
    • Catalysis of proline isomerization during protein folding reactions
    • Lin L.-N., Hasumi H., Brandts J. F. Catalysis of proline isomerization during protein folding reactions. Biochim. Biophys. Acta. 956:1988;256-266.
    • (1988) Biochim. Biophys. Acta , vol.956 , pp. 256-266
    • Lin, L.-N.1    Hasumi, H.2    Brandts, J.F.3
  • 25
    • 0029916122 scopus 로고    scopus 로고
    • A human peptidyl-prolyl isomerase essential for regulation of mitosis
    • Lu K. P., Hanes S. D., Hunter T. A human peptidyl-prolyl isomerase essential for regulation of mitosis. Nature. 380:1996;544-547.
    • (1996) Nature , vol.380 , pp. 544-547
    • Lu, K.P.1    Hanes, S.D.2    Hunter, T.3
  • 26
    • 0025890946 scopus 로고
    • Influence of proline residues on protein conformation
    • Macarthur M. W., Thornton J. M. Influence of proline residues on protein conformation. J. Mol. Biol. 218:1991;397-412.
    • (1991) J. Mol. Biol. , vol.218 , pp. 397-412
    • Macarthur, M.W.1    Thornton, J.M.2
  • 28
    • 0029868655 scopus 로고    scopus 로고
    • Kinetic analysis of the unfolding and refolding of ribonuclease T1 by a stopped-flow double-mixing technique
    • Mayr L. M., Odefey C., Schutkowski M., Schmid F. X. Kinetic analysis of the unfolding and refolding of ribonuclease T1 by a stopped-flow double-mixing technique. Biochemistry. 35:1996;5550-5561.
    • (1996) Biochemistry , vol.35 , pp. 5550-5561
    • Mayr, L.M.1    Odefey, C.2    Schutkowski, M.3    Schmid, F.X.4
  • 29
    • 0031081341 scopus 로고    scopus 로고
    • Protein misfolding in the cell envelope ofEscherichia coli
    • Missiakas D., Raina S. Protein misfolding in the cell envelope ofEscherichia coli. Trends Biochem. Sci. 22:1997;59-63.
    • (1997) Trends Biochem. Sci. , vol.22 , pp. 59-63
    • Missiakas, D.1    Raina, S.2
  • 30
    • 0029765609 scopus 로고    scopus 로고
    • New components of protein folding in extracytoplasmic compartments ofEscherichia coli
    • Missiakas D., Betton J. M., Raina S. New components of protein folding in extracytoplasmic compartments ofEscherichia coli. Mol. Microbiol. 21:1996;871-884.
    • (1996) Mol. Microbiol. , vol.21 , pp. 871-884
    • Missiakas, D.1    Betton, J.M.2    Raina, S.3
  • 31
    • 0028606121 scopus 로고
    • Folding mechanism of ribonuclease T1 in the absence of the disulfide bonds
    • Mücke M., Schmid F. X. Folding mechanism of ribonuclease T1 in the absence of the disulfide bonds. Biochemistry. 33:1994;14608-14619.
    • (1994) Biochemistry , vol.33 , pp. 14608-14619
    • Mücke, M.1    Schmid, F.X.2
  • 32
    • 0000566719 scopus 로고
    • Limited proteolysis, domains, and the evolution of protein structure
    • Neurath H. Limited proteolysis, domains, and the evolution of protein structure. Chem. Script. sect. B. 27:1986a;221-229.
    • (1986) Chem. Script. Sect. B , vol.27 , pp. 221-229
    • Neurath, H.1
  • 33
    • 0022484841 scopus 로고
    • The versatility of proteolytic enzymes
    • Neurath H. The versatility of proteolytic enzymes. J. Cell. Biochem. 32:1986b;35-49.
    • (1986) J. Cell. Biochem. , vol.32 , pp. 35-49
    • Neurath, H.1
  • 34
    • 0026505603 scopus 로고
    • The plasmid-encoded lactococcal envelope-associated proteinase is encoded by a chromosomal gene inLactococcus lactis
    • Nissen Meyer J., Lillehaug D., Nes I. F. The plasmid-encoded lactococcal envelope-associated proteinase is encoded by a chromosomal gene inLactococcus lactis. Appl. Environ. Microbiol. 58:1992;750-753.
    • (1992) Appl. Environ. Microbiol. , vol.58 , pp. 750-753
    • Nissen Meyer, J.1    Lillehaug, D.2    Nes, I.F.3
  • 35
    • 0022555885 scopus 로고
    • Determination and analysis of urea and guanidine hydrochloride denaturation curves
    • Pace C. N. Determination and analysis of urea and guanidine hydrochloride denaturation curves. Methods Enzymol. 131:1986;266-280.
    • (1986) Methods Enzymol. , vol.131 , pp. 266-280
    • Pace, C.N.1
  • 38
    • 0008233581 scopus 로고    scopus 로고
    • Structural and functional analysis of the mitotic rotamase Pin1 suggests substrate recognition is phosphorylation dependent
    • Ranganathan R., Lu K. P., Hunter T., Noel J. P. Structural and functional analysis of the mitotic rotamase Pin1 suggests substrate recognition is phosphorylation dependent. Cell. 89:1997;875-886.
    • (1997) Cell , vol.89 , pp. 875-886
    • Ranganathan, R.1    Lu, K.P.2    Hunter, T.3    Noel, J.P.4
  • 39
    • 0028948314 scopus 로고
    • Cyclophilin 20 is involved in mitochondrial protein folding in cooperation with molecular chaperones Hsp70 and Hsp60
    • Rassow J., Mohrs K., Koidl S., Barthelmess I. B., Pfanner N., Tropschug M. Cyclophilin 20 is involved in mitochondrial protein folding in cooperation with molecular chaperones Hsp70 and Hsp60. Mol. Cell. Biol. 15:1995;2654-2662.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 2654-2662
    • Rassow, J.1    Mohrs, K.2    Koidl, S.3    Barthelmess, I.B.4    Pfanner, N.5    Tropschug, M.6
  • 40
    • 0030476750 scopus 로고    scopus 로고
    • SurA, a periplasmic protein with peptidyl-prolyl isomerase activity, participates in the assembly of outer membrane porins
    • Rouviere P. E., Gross C. A. SurA, a periplasmic protein with peptidyl-prolyl isomerase activity, participates in the assembly of outer membrane porins. Genes Dev. 10:1996;3170-3182.
    • (1996) Genes Dev. , vol.10 , pp. 3170-3182
    • Rouviere, P.E.1    Gross, C.A.2
  • 41
    • 0023697408 scopus 로고
    • Unfolding free energy changes determined by the linear extrapolation method. 1. Unfolding of phenylmethanesulfonyl α-chymotrypsin using different denaturants
    • Santoro M. M., Bolen D. W. Unfolding free energy changes determined by the linear extrapolation method. 1. Unfolding of phenylmethanesulfonyl α-chymotrypsin using different denaturants. Biochemistry. 27:1988;8063-8068.
    • (1988) Biochemistry , vol.27 , pp. 8063-8068
    • Santoro, M.M.1    Bolen, D.W.2
  • 43
    • 0022555898 scopus 로고
    • Fast-folding and slow-folding forms of unfolded proteins
    • Schmid F. X. Fast-folding and slow-folding forms of unfolded proteins. Methods Enzymol. 131:1986;71-82.
    • (1986) Methods Enzymol. , vol.131 , pp. 71-82
    • Schmid, F.X.1
  • 44
    • 0027256737 scopus 로고
    • Prolyl isomerase: Enzymatic catalysis of slow protein-folding reactions
    • Schmid F. X. Prolyl isomerase: enzymatic catalysis of slow protein-folding reactions. Annu. Rev. Biophys. Biomol. Struct. 22:1993;123-143.
    • (1993) Annu. Rev. Biophys. Biomol. Struct. , vol.22 , pp. 123-143
    • Schmid, F.X.1
  • 45
    • 0018143763 scopus 로고
    • Acid catalysis of the formation of the slow-folding species of RNase A: Evidence that the reaction is proline isomerization
    • Schmid F. X., Baldwin R. L. Acid catalysis of the formation of the slow-folding species of RNase A: evidence that the reaction is proline isomerization. Proc. Natl Acad. Sci. USA. 75:1978;4764-4768.
    • (1978) Proc. Natl Acad. Sci. USA , vol.75 , pp. 4764-4768
    • Schmid, F.X.1    Baldwin, R.L.2
  • 48
    • 0031029046 scopus 로고    scopus 로고
    • Cooperation of enzymatic and chaperone functions of trigger factor in the catalysis of protein folding
    • Scholz C., Stoller G., Zarnt T., Fischer G., Schmid F. X. Cooperation of enzymatic and chaperone functions of trigger factor in the catalysis of protein folding. EMBO J. 16:1997;54-58.
    • (1997) EMBO J. , vol.16 , pp. 54-58
    • Scholz, C.1    Stoller, G.2    Zarnt, T.3    Fischer, G.4    Schmid, F.X.5
  • 50
    • 0026030568 scopus 로고
    • Chemistry and biology of the immunophilins and their immunosuppresive ligands
    • Schreiber S. L. Chemistry and biology of the immunophilins and their immunosuppresive ligands. Science. 251:1991;283-287.
    • (1991) Science , vol.251 , pp. 283-287
    • Schreiber, S.L.1
  • 51
    • 0027817195 scopus 로고
    • Mechanism of enzymatic and nonenzymatic prolylcistrans
    • Stein R. L. Mechanism of enzymatic and nonenzymatic prolylcistrans. Advan. Protein Chem. 44:1993;1-24.
    • (1993) Advan. Protein Chem. , vol.44 , pp. 1-24
    • Stein, R.L.1
  • 52
    • 0025299887 scopus 로고
    • Occurrence and role of cis peptide bonds in protein structures
    • Stewart D. E., Sarkar A., Wampler J. E. Occurrence and role of cis peptide bonds in protein structures. J. Mol. Biol. 214:1990;253-260.
    • (1990) J. Mol. Biol. , vol.214 , pp. 253-260
    • Stewart, D.E.1    Sarkar, A.2    Wampler, J.E.3
  • 54
  • 60
    • 0031568329 scopus 로고    scopus 로고
    • Cyclophilin A complexed with a fragment of HIV-1 gag protein: Insights into HIV-1 infectious activity
    • Zhao Y. D., Chen Y. Q., Schutkowski M., Fischer G., Ke H. M. Cyclophilin A complexed with a fragment of HIV-1 gag protein: insights into HIV-1 infectious activity. Structure. 5:1997;139-146.
    • (1997) Structure , vol.5 , pp. 139-146
    • Zhao, Y.D.1    Chen, Y.Q.2    Schutkowski, M.3    Fischer, G.4    Ke, H.M.5


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