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Volumn 405, Issue 3, 2011, Pages 804-818

Recognition of mitochondrial targeting sequences by the import receptors Tom20 and Tom22

Author keywords

mitochondria; presequence; protein import; TOM complex

Indexed keywords

CARRIER PROTEINS AND BINDING PROTEINS; TRANSLOCASE OF OUTER MITOCHONDRIAL MEMBRANE 20; TRANSLOCASE OF OUTER MITOCHONDRIAL MEMBRANE 22; UNCLASSIFIED DRUG;

EID: 78650907489     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2010.11.017     Document Type: Article
Times cited : (42)

References (57)
  • 1
    • 33746575844 scopus 로고    scopus 로고
    • Evolution of the molecular machines for protein import into mitochondria
    • DOI 10.1126/science.1127895
    • Dolezal P., Likic V., Tachezy J., and Lithgow T. Evolution of the molecular machines for protein import into mitochondria Science 313 2006 314 318 (Pubitemid 44480948)
    • (2006) Science , vol.313 , Issue.5785 , pp. 314-318
    • Dolezal, P.1    Likic, V.2    Tachezy, J.3    Lithgow, T.4
  • 2
    • 0033525788 scopus 로고    scopus 로고
    • Mitochondrial evolution
    • Gray M.W., Burger G., and Lang B.F. Mitochondrial evolution Science 283 1999 1476 1481
    • (1999) Science , vol.283 , pp. 1476-1481
    • Gray, M.W.1    Burger, G.2    Lang, B.F.3
  • 4
    • 34249873947 scopus 로고    scopus 로고
    • Translocation of proteins into mitochondria
    • Neupert W., and Herrmann J.M. Translocation of proteins into mitochondria Annu. Rev. Biochem. 76 2007 723 749
    • (2007) Annu. Rev. Biochem. , vol.76 , pp. 723-749
    • Neupert, W.1    Herrmann, J.M.2
  • 5
    • 0034598904 scopus 로고    scopus 로고
    • Structural basis of presequence recognition by the mitochondrial protein import receptor Tom20
    • Abe Y., Shodai T., Muto T., Mihara K., Torii H., and Nishikawa S. Structural basis of presequence recognition by the mitochondrial protein import receptor Tom20 Cell 100 2000 551 560
    • (2000) Cell , vol.100 , pp. 551-560
    • Abe, Y.1    Shodai, T.2    Muto, T.3    Mihara, K.4    Torii, H.5    Nishikawa, S.6
  • 6
    • 0024542834 scopus 로고
    • Domain structure of mitochondrial and chloroplast targeting peptides
    • von Heijne G., Steppuhn J., and Herrmann R.G. Domain structure of mitochondrial and chloroplast targeting peptides Eur. J. Biochem. 180 1989 535 545
    • (1989) Eur. J. Biochem. , vol.180 , pp. 535-545
    • Von Heijne, G.1    Steppuhn, J.2    Herrmann, R.G.3
  • 8
    • 0037009087 scopus 로고    scopus 로고
    • Functions of outer membrane receptors in mitochondrial protein import
    • Endo T., and Kohda D. Functions of outer membrane receptors in mitochondrial protein import Biochim. Biophys. Acta Mol. Cell Res. 1592 2002 3 14
    • (2002) Biochim. Biophys. Acta Mol. Cell Res. , vol.1592 , pp. 3-14
    • Endo, T.1    Kohda, D.2
  • 9
    • 0032188847 scopus 로고    scopus 로고
    • Tom40 forms the hydrophilic channel of the mitochondrial import pore for preproteins [see comment]
    • Hill K., Model K., Ryan M.T., Dietmeier K., Martin F., Wagner R., and Pfanner N. Tom40 forms the hydrophilic channel of the mitochondrial import pore for preproteins [see comment] 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
  • 10
    • 0025606107 scopus 로고
    • Identification of a mitochondrial receptor complex required for recognition and membrane insertion of precursor proteins
    • Kiebler M., Pfaller R., Sollner T., Griffiths G., Horstmann H., Pfanner N., and Neupert W. Identification of a mitochondrial receptor complex required for recognition and membrane insertion of precursor proteins Nature 348 1990 610 616
    • (1990) Nature , vol.348 , pp. 610-616
    • Kiebler, M.1    Pfaller, R.2    Sollner, T.3    Griffiths, G.4    Horstmann, H.5    Pfanner, N.6    Neupert, W.7
  • 11
    • 0024424988 scopus 로고
    • A 42K outer-membrane protein is a component of the yeast mitochondrial protein import site
    • Vestweber D., Brunner J., Baker A., and Schatz G. A 42K outer-membrane protein is a component of the yeast mitochondrial protein import site Nature 341 1989 205 209
    • (1989) Nature , vol.341 , pp. 205-209
    • Vestweber, D.1    Brunner, J.2    Baker, A.3    Schatz, G.4
  • 12
    • 0027434076 scopus 로고
    • Functional cooperation of mitochondrial protein import receptors in yeast
    • Ramage L., Junne T., Hahne K., Lithgow T., and Schatz G. Functional cooperation of mitochondrial protein import receptors in yeast EMBO J. 12 1993 4115 4123
    • (1993) EMBO J. , vol.12 , pp. 4115-4123
    • Ramage, L.1    Junne, T.2    Hahne, K.3    Lithgow, T.4    Schatz, G.5
  • 13
    • 0024801086 scopus 로고
    • MOM19, an import receptor for mitochondrial precursor proteins
    • Sollner T., Griffiths G., Pfaller R., Pfanner N., and Neupert W. MOM19, an import receptor for mitochondrial precursor proteins Cell 59 1989 1061 1070
    • (1989) Cell , vol.59 , pp. 1061-1070
    • Sollner, T.1    Griffiths, G.2    Pfaller, R.3    Pfanner, N.4    Neupert, W.5
  • 14
    • 0027164641 scopus 로고
    • The mitochondrial receptor complex: A central role of MOM22 in mediating preprotein transfer from receptors to the general insertion pore
    • Kiebler M., Keil P., Schneider H., van der Klei I.J., Pfanner N., and Neupert W. The mitochondrial receptor complex: a central role of MOM22 in mediating preprotein transfer from receptors to the general insertion pore Cell 74 1993 483 492
    • (1993) Cell , vol.74 , pp. 483-492
    • Kiebler, M.1    Keil, P.2    Schneider, H.3    Van Der Klei, I.J.4    Pfanner, N.5    Neupert, W.6
  • 15
    • 0028046512 scopus 로고
    • The mitochondrial outer membrane protein Mas22p is essential for protein import and viability of yeast
    • Lithgow T., Junne T., Suda K., Gratzer S., and Schatz G. The mitochondrial outer membrane protein Mas22p is essential for protein import and viability of yeast Proc. Natl Acad. Sci. USA 91 1994 11973 11977
    • (1994) Proc. Natl Acad. Sci. USA , vol.91 , pp. 11973-11977
    • Lithgow, T.1    Junne, T.2    Suda, K.3    Gratzer, S.4    Schatz, G.5
  • 16
    • 0029096887 scopus 로고
    • Reconstitution of the initial steps of mitochondrial protein import
    • Hachiya N., Mihara K., Suda K., Horst M., Schatz G., and Lithgow T. Reconstitution of the initial steps of mitochondrial protein import Nature 376 1995 705 709
    • (1995) Nature , vol.376 , pp. 705-709
    • Hachiya, N.1    Mihara, K.2    Suda, K.3    Horst, M.4    Schatz, G.5    Lithgow, T.6
  • 17
    • 0037428164 scopus 로고    scopus 로고
    • Molecular chaperones Hsp90 and Hsp70 deliver preproteins to the mitochondrial import receptor Tom70
    • Young J.C., Hoogenraad N.J., and Hartl F.U. Molecular chaperones Hsp90 and Hsp70 deliver preproteins to the mitochondrial import receptor Tom70 Cell 112 2003 41 50
    • (2003) Cell , vol.112 , pp. 41-50
    • Young, J.C.1    Hoogenraad, N.J.2    Hartl, F.U.3
  • 18
    • 0025035851 scopus 로고
    • Protein import into yeast mitochondria is accelerated by the outer membrane protein MAS70
    • Hines V., Brandt A., Griffiths G., Horstmann H., Brutsch H., and Schatz G. Protein import into yeast mitochondria is accelerated by the outer membrane protein MAS70 EMBO J. 9 1990 3191 3200
    • (1990) EMBO J. , vol.9 , pp. 3191-3200
    • Hines, V.1    Brandt, A.2    Griffiths, G.3    Horstmann, H.4    Brutsch, H.5    Schatz, G.6
  • 19
  • 20
    • 0040610676 scopus 로고    scopus 로고
    • Distribution of binding sequences for the mitochondrial import receptors Tom20, Tom22, and Tom70 in a presequence-carrying preprotein and a non-cleavable preprotein
    • Brix J., Rudiger S., Bukau B., Schneider-Mergener J., and Pfanner N. Distribution of binding sequences for the mitochondrial import receptors Tom20, Tom22, and Tom70 in a presequence-carrying preprotein and a non-cleavable preprotein J. Biol. Chem. 274 1999 16522 16530
    • (1999) J. Biol. Chem. , vol.274 , pp. 16522-16530
    • Brix, J.1    Rudiger, S.2    Bukau, B.3    Schneider-Mergener, J.4    Pfanner, N.5
  • 21
    • 3242761606 scopus 로고    scopus 로고
    • Tom22′, an 8-kDa trans-site receptor in plants and protozoans, is a conserved feature of the TOM complex that appeared early in the evolution of eukaryotes
    • Macasev D., Whelan J., Newbigin E., Silva-Filho M.C., Mulhern T.D., and Lithgow T. Tom22′, an 8-kDa trans-site receptor in plants and protozoans, is a conserved feature of the TOM complex that appeared early in the evolution of eukaryotes Mol. Biol. Evol. 21 2004 1557 1564
    • (2004) Mol. Biol. Evol. , vol.21 , pp. 1557-1564
    • MacAsev, D.1    Whelan, J.2    Newbigin, E.3    Silva-Filho, M.C.4    Mulhern, T.D.5    Lithgow, T.6
  • 22
    • 1642532372 scopus 로고    scopus 로고
    • A plant outer mitochondrial membrane protein with high amino acid sequence identity to a chloroplast protein import receptor
    • Chew O., Lister R., Qbadou S., Heazlewood J.L., Soll J., and Schleiff E. A plant outer mitochondrial membrane protein with high amino acid sequence identity to a chloroplast protein import receptor FEBS Lett. 557 2004 109 114
    • (2004) FEBS Lett. , vol.557 , pp. 109-114
    • Chew, O.1    Lister, R.2    Qbadou, S.3    Heazlewood, J.L.4    Soll, J.5    Schleiff, E.6
  • 23
    • 20044392656 scopus 로고    scopus 로고
    • Patterns that define the four domains conserved in known and novel isoforms of the protein import receptor Tom20
    • Likic V.A., Perry A., Hulett J., Derby M., Traven A., and Waller R.F. Patterns that define the four domains conserved in known and novel isoforms of the protein import receptor Tom20 J. Mol. Biol. 347 2005 81 93
    • (2005) J. Mol. Biol. , vol.347 , pp. 81-93
    • Likic, V.A.1    Perry, A.2    Hulett, J.3    Derby, M.4    Traven, A.5    Waller, R.F.6
  • 24
    • 31944448611 scopus 로고    scopus 로고
    • Convergent evolution of receptors for protein import into mitochondria
    • DOI 10.1016/j.cub.2005.12.034, PII S0960982205015964
    • Perry A.J., Hulett J.M., Likic V.A., Lithgow T., and Gooley P.R. Convergent evolution of receptors for protein import into mitochondria Curr. Biol. 16 2006 221 229 (Pubitemid 43190221)
    • (2006) Current Biology , vol.16 , Issue.3 , pp. 221-229
    • Perry, A.J.1    Hulett, J.M.2    Likic, V.A.3    Lithgow, T.4    Gooley, P.R.5
  • 25
    • 33644991350 scopus 로고    scopus 로고
    • Mitochondrial protein import: Convergent solutions for receptor structure
    • Lister R., and Whelan J. Mitochondrial protein import: convergent solutions for receptor structure Curr. Biol. 16 2006 R197 R199
    • (2006) Curr. Biol. , vol.16
    • Lister, R.1    Whelan, J.2
  • 26
    • 36248989141 scopus 로고    scopus 로고
    • Tom20 recognizes mitochondrial presequences through dynamic equilibrium among multiple bound states
    • Saitoh T., Igura M., Obita T., Ose T., Kojima R., and Maenaka K. Tom20 recognizes mitochondrial presequences through dynamic equilibrium among multiple bound states EMBO J. 26 2007 4777 4787
    • (2007) EMBO J. , vol.26 , pp. 4777-4787
    • Saitoh, T.1    Igura, M.2    Obita, T.3    Ose, T.4    Kojima, R.5    Maenaka, K.6
  • 27
    • 0029619088 scopus 로고
    • Acidic receptor domains on both sides of the outer membrane mediate translocation of precursor proteins into yeast mitochondria
    • Bolliger L., Junne T., Schatz G., and Lithgow T. Acidic receptor domains on both sides of the outer membrane mediate translocation of precursor proteins into yeast mitochondria EMBO J. 14 1995 6318 6326
    • (1995) EMBO J. , vol.14 , pp. 6318-6326
    • Bolliger, L.1    Junne, T.2    Schatz, G.3    Lithgow, T.4
  • 28
    • 0031741738 scopus 로고    scopus 로고
    • Preprotein translocase of the outer mitochondrial membrane: Molecular dissection and assembly of the general import pore complex
    • Dekker P.J., Ryan M.T., Brix J., Muller H., Honlinger A., and Pfanner N. Preprotein translocase of the outer mitochondrial membrane: molecular dissection and assembly of the general import pore complex Mol. Cell. Biol. 18 1998 6515 6524
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 6515-6524
    • Dekker, P.J.1    Ryan, M.T.2    Brix, J.3    Muller, H.4    Honlinger, A.5    Pfanner, N.6
  • 29
    • 0033619269 scopus 로고    scopus 로고
    • Tom22 is a multifunctional organizer of the mitochondrial preprotein translocase
    • van Wilpe S., Ryan M.T., Hill K., Maarse A.C., Meisinger C., and Brix J. Tom22 is a multifunctional organizer of the mitochondrial preprotein translocase Nature 401 1999 485 489
    • (1999) Nature , vol.401 , pp. 485-489
    • Van Wilpe, S.1    Ryan, M.T.2    Hill, K.3    Maarse, A.C.4    Meisinger, C.5    Brix, J.6
  • 30
    • 0029156778 scopus 로고
    • MOM22 is a receptor for mitochondrial targeting sequences and cooperates with MOM19
    • Mayer A., Nargang F.E., Neupert W., and Lill R. MOM22 is a receptor for mitochondrial targeting sequences and cooperates with MOM19 EMBO J. 14 1995 4204 4211
    • (1995) EMBO J. , vol.14 , pp. 4204-4211
    • Mayer, A.1    Nargang, F.E.2    Neupert, W.3    Lill, R.4
  • 31
    • 38649141822 scopus 로고    scopus 로고
    • The transmembrane segment of Tom20 is recognized by Mim1 for docking to the mitochondrial TOM complex
    • Hulett J.M., Lueder F., Chan N.C., Perry A.J., Wolynec P., and Likic V.A. The transmembrane segment of Tom20 is recognized by Mim1 for docking to the mitochondrial TOM complex J. Mol. Biol. 376 2008 694 704
    • (2008) J. Mol. Biol. , vol.376 , pp. 694-704
    • Hulett, J.M.1    Lueder, F.2    Chan, N.C.3    Perry, A.J.4    Wolynec, P.5    Likic, V.A.6
  • 32
    • 0031844305 scopus 로고    scopus 로고
    • Role of the negative charges in the cytosolic domain of TOM22 in the import of precursor proteins into mitochondria
    • Nargang F.E., Rapaport D., Ritzel R.G., Neupert W., and Lill R. Role of the negative charges in the cytosolic domain of TOM22 in the import of precursor proteins into mitochondria Mol. Cell. Biol. 18 1998 3173 3181
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 3173-3181
    • Nargang, F.E.1    Rapaport, D.2    Ritzel, R.G.3    Neupert, W.4    Lill, R.5
  • 33
    • 0035115121 scopus 로고    scopus 로고
    • Purification and characterization of the preprotein translocase of the outer mitochondrial membrane from Arabidopsis. Identification of multiple forms of TOM20
    • Werhahn W., Niemeyer A., Jansch L., Kruft V., Schmitz U.K., and Braun H. Purification and characterization of the preprotein translocase of the outer mitochondrial membrane from Arabidopsis. Identification of multiple forms of TOM20 Plant Physiol. 125 2001 943 954
    • (2001) Plant Physiol. , vol.125 , pp. 943-954
    • Werhahn, W.1    Niemeyer, A.2    Jansch, L.3    Kruft, V.4    Schmitz, U.K.5    Braun, H.6
  • 34
    • 0032169540 scopus 로고    scopus 로고
    • Mitochondrial protein import in plants. Signals, sorting, targeting, processing and regulation
    • Glaser E., Sjoling S., Tanudji M., and Whelan J. Mitochondrial protein import in plants. Signals, sorting, targeting, processing and regulation Plant Mol. Biol. 38 1998 311 338
    • (1998) Plant Mol. Biol. , vol.38 , pp. 311-338
    • Glaser, E.1    Sjoling, S.2    Tanudji, M.3    Whelan, J.4
  • 35
    • 1242317038 scopus 로고    scopus 로고
    • NMR solution structure of the mitochondrial F1beta presequence from Nicotiana plumbaginifolia
    • Moberg P., Nilsson S., Stahl A., Eriksson A.C., Glaser E., and Maler L. NMR solution structure of the mitochondrial F1beta presequence from Nicotiana plumbaginifolia J. Mol. Biol. 336 2004 1129 1140
    • (2004) J. Mol. Biol. , vol.336 , pp. 1129-1140
    • Moberg, P.1    Nilsson, S.2    Stahl, A.3    Eriksson, A.C.4    Glaser, E.5    Maler, L.6
  • 37
    • 0042622240 scopus 로고    scopus 로고
    • GlobPlot: Exploring protein sequences for globularity and disorder
    • Linding R., Russell R.B., Neduva V., and Gibson T.J. GlobPlot: exploring protein sequences for globularity and disorder Nucleic Acids Res. 31 2003 3701 3708
    • (2003) Nucleic Acids Res. , vol.31 , pp. 3701-3708
    • Linding, R.1    Russell, R.B.2    Neduva, V.3    Gibson, T.J.4
  • 38
    • 0035895431 scopus 로고    scopus 로고
    • NMR identification of the Tom20 binding segment in mitochondrial presequences
    • Muto T., Obita T., Abe Y., Shodai T., Endo T., and Kohda D. NMR identification of the Tom20 binding segment in mitochondrial presequences J. Mol. Biol. 306 2001 137 143
    • (2001) J. Mol. Biol. , vol.306 , pp. 137-143
    • Muto, T.1    Obita, T.2    Abe, Y.3    Shodai, T.4    Endo, T.5    Kohda, D.6
  • 39
    • 33751248768 scopus 로고    scopus 로고
    • Quantitative relation between intermolecular and intramolecular binding of Pro-rich peptides to SH3 domains
    • Zhou H.X. Quantitative relation between intermolecular and intramolecular binding of Pro-rich peptides to SH3 domains Biophys. J. 91 2006 3170 3181
    • (2006) Biophys. J. , vol.91 , pp. 3170-3181
    • Zhou, H.X.1
  • 40
    • 0034796437 scopus 로고    scopus 로고
    • Hydrophobic residues within the predicted N-terminal amphiphilic alpha-helix of a plant mitochondrial targeting presequence play a major role in in vivo import
    • Duby G., Oufattole M., and Boutry M. Hydrophobic residues within the predicted N-terminal amphiphilic alpha-helix of a plant mitochondrial targeting presequence play a major role in in vivo import Plant J. 27 2001 539 549
    • (2001) Plant J. , vol.27 , pp. 539-549
    • Duby, G.1    Oufattole, M.2    Boutry, M.3
  • 41
    • 0038832853 scopus 로고    scopus 로고
    • Signals required for the import and processing of the alternative oxidase into mitochondria
    • Tanudji M., Sjoling S., Glaser E., and Whelan J. Signals required for the import and processing of the alternative oxidase into mitochondria J. Biol. Chem. 274 1999 1286 1293
    • (1999) J. Biol. Chem. , vol.274 , pp. 1286-1293
    • Tanudji, M.1    Sjoling, S.2    Glaser, E.3    Whelan, J.4
  • 42
    • 0034214123 scopus 로고    scopus 로고
    • Protein sorting: Recognizing mitochondrial presequences
    • Pfanner N. Protein sorting: recognizing mitochondrial presequences Curr. Biol. 10 2000 R412 R415
    • (2000) Curr. Biol. , vol.10
    • Pfanner, N.1
  • 43
    • 42949139525 scopus 로고    scopus 로고
    • Tom20 and Tom22 share the common signal recognition pathway in mitochondrial protein import
    • Yamano K., Yatsukawa Y., Esaki M., Hobbs A.E., Jensen R.E., and Endo T. Tom20 and Tom22 share the common signal recognition pathway in mitochondrial protein import J. Biol. Chem. 283 2008 3799 3807
    • (2008) J. Biol. Chem. , vol.283 , pp. 3799-3807
    • Yamano, K.1    Yatsukawa, Y.2    Esaki, M.3    Hobbs, A.E.4    Jensen, R.E.5    Endo, T.6
  • 44
    • 35748930268 scopus 로고    scopus 로고
    • Domain stealing by receptors in a protein transport complex
    • Hulett J.M., Walsh P., and Lithgow T. Domain stealing by receptors in a protein transport complex Mol. Biol. Evol. 24 2007 1909 1911
    • (2007) Mol. Biol. Evol. , vol.24 , pp. 1909-1911
    • Hulett, J.M.1    Walsh, P.2    Lithgow, T.3
  • 45
    • 0035844870 scopus 로고    scopus 로고
    • Tom40, the pore-forming component of the protein-conducting TOM channel in the outer membrane of mitochondria
    • Ahting U., Thieffry M., Engelhardt H., Hegerl R., Neupert W., and Nussberger S. Tom40, the pore-forming component of the protein-conducting TOM channel in the outer membrane of mitochondria J. Cell Biol. 153 2001 1151 1160
    • (2001) J. Cell Biol. , vol.153 , pp. 1151-1160
    • Ahting, U.1    Thieffry, M.2    Engelhardt, H.3    Hegerl, R.4    Neupert, W.5    Nussberger, S.6
  • 46
    • 27144464893 scopus 로고    scopus 로고
    • Preprotein translocase of the outer mitochondrial membrane: Reconstituted Tom40 forms a characteristic TOM pore
    • Becker L., Bannwarth M., Meisinger C., Hill K., Model K., and Krimmer T. Preprotein translocase of the outer mitochondrial membrane: reconstituted Tom40 forms a characteristic TOM pore J. Mol. Biol. 353 2005 1011 1020
    • (2005) J. Mol. Biol. , vol.353 , pp. 1011-1020
    • Becker, L.1    Bannwarth, M.2    Meisinger, C.3    Hill, K.4    Model, K.5    Krimmer, T.6
  • 47
    • 0037566814 scopus 로고    scopus 로고
    • Tom40, the import channel of the mitochondrial outer membrane, plays an active role in sorting imported proteins
    • Gabriel K., Egan B., and Lithgow T. Tom40, the import channel of the mitochondrial outer membrane, plays an active role in sorting imported proteins EMBO J. 22 2003 2380 2386
    • (2003) EMBO J. , vol.22 , pp. 2380-2386
    • Gabriel, K.1    Egan, B.2    Lithgow, T.3
  • 48
    • 0030872409 scopus 로고    scopus 로고
    • Mitochondrial protein import. Tom40 plays a major role in targeting and translocation of preproteins by forming a specific binding site for the presequence
    • Rapaport D., Neupert W., and Lill R. Mitochondrial protein import. Tom40 plays a major role in targeting and translocation of preproteins by forming a specific binding site for the presequence J. Biol. Chem. 272 1997 18725 18731
    • (1997) J. Biol. Chem. , vol.272 , pp. 18725-18731
    • Rapaport, D.1    Neupert, W.2    Lill, R.3
  • 49
    • 0028017482 scopus 로고
    • Production, purification, and cleavage of tandem repeats of recombinant peptides
    • Kuliopulos A., and Walsh C.T. Production, purification, and cleavage of tandem repeats of recombinant peptides J. Am. Chem. Soc. 116 1994 4599 4607
    • (1994) J. Am. Chem. Soc. , vol.116 , pp. 4599-4607
    • Kuliopulos, A.1    Walsh, C.T.2
  • 52
    • 34249765651 scopus 로고
    • NMR VIEW-a computer-program for the visualization and analysis of NMR data
    • Johnson B.A., and Blevins R.A. NMR VIEW-a computer-program for the visualization and analysis of NMR data J. Biomol. NMR 4 1994 603 614
    • (1994) J. Biomol. NMR , vol.4 , pp. 603-614
    • Johnson, B.A.1    Blevins, R.A.2
  • 53
    • 63549111769 scopus 로고    scopus 로고
    • Probabilistic interaction network of evidence algorithm and its application to complete labeling of peak lists from protein NMR spectroscopy
    • Bahrami A., Assadi A.H., Markley J.L., and Eghbalnia H.R. Probabilistic interaction network of evidence algorithm and its application to complete labeling of peak lists from protein NMR spectroscopy PLoS Comput. Biol. 5 2009 e1000307
    • (2009) PLoS Comput. Biol. , vol.5 , pp. 1000307
    • Bahrami, A.1    Assadi, A.H.2    Markley, J.L.3    Eghbalnia, H.R.4
  • 54
    • 0036308102 scopus 로고    scopus 로고
    • Protein NMR structure determination with automated NOE assignment using the new software CANDID and the torsion angle dynamics algorithm DYANA
    • Herrmann T., Guntert P., and Wuthrich K. Protein NMR structure determination with automated NOE assignment using the new software CANDID and the torsion angle dynamics algorithm DYANA J. Mol. Biol. 319 2002 209 227
    • (2002) J. Mol. Biol. , vol.319 , pp. 209-227
    • Herrmann, T.1    Guntert, P.2    Wuthrich, K.3
  • 55
    • 0030339738 scopus 로고    scopus 로고
    • AQUA and PROCHECK-NMR: Programs for checking the quality of protein structures solved by NMR
    • Laskowski R.A., Rullmannn J.A., MacArthur M.W., Kaptein R., and Thornton J.M. AQUA and PROCHECK-NMR: programs for checking the quality of protein structures solved by NMR J. Biomol. NMR 8 1996 477 486
    • (1996) J. Biomol. NMR , vol.8 , pp. 477-486
    • Laskowski, R.A.1    Rullmannn, J.A.2    MacArthur, M.W.3    Kaptein, R.4    Thornton, J.M.5
  • 56
    • 23144437542 scopus 로고    scopus 로고
    • Protein energetic conformational analysis from NMR chemical shifts (PECAN) and its use in determining secondary structural elements
    • Eghbalnia H.R., Wang L., Bahrami A., Assadi A., and Markley J.L. Protein energetic conformational analysis from NMR chemical shifts (PECAN) and its use in determining secondary structural elements J. Biomol. NMR 32 2005 71 81
    • (2005) J. Biomol. NMR , vol.32 , pp. 71-81
    • Eghbalnia, H.R.1    Wang, L.2    Bahrami, A.3    Assadi, A.4    Markley, J.L.5
  • 57
    • 30844456535 scopus 로고    scopus 로고
    • SOFAST-HMQC experiments for recording two-dimensional heteronuclear correlation spectra of proteins within a few seconds
    • Schanda P., Kupce E., and Brutscher B. SOFAST-HMQC experiments for recording two-dimensional heteronuclear correlation spectra of proteins within a few seconds J. Biomol. NMR 33 2005 199 211
    • (2005) J. Biomol. NMR , vol.33 , pp. 199-211
    • Schanda, P.1    Kupce, E.2    Brutscher, B.3


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