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Volumn 61, Issue 3, 2005, Pages 642-648

Oligomerization states of Bowman-Birk inhibitor by atomic force microscopy and computational approaches

Author keywords

Accessible surface area; AFM; Atomic force microscopy; Docking; Proteinase inhibitor; Self assembly

Indexed keywords

BOWMAN BIRK INHIBITOR; DIMER; MONOMER; PROTEINASE INHIBITOR;

EID: 27544482791     PISSN: 08873585     EISSN: None     Source Type: Journal    
DOI: 10.1002/prot.20646     Document Type: Article
Times cited : (16)

References (39)
  • 1
    • 0036424666 scopus 로고    scopus 로고
    • Structural basis of macromolecular recognition
    • Wodak SJ, Janin J. Structural basis of macromolecular recognition. Adv Protein Chem 2003;61:9-73.
    • (2003) Adv Protein Chem , vol.61 , pp. 9-73
    • Wodak, S.J.1    Janin, J.2
  • 2
    • 0034254089 scopus 로고    scopus 로고
    • What are oligomerization domains good for?
    • Engel J, Kammerer RA. What are oligomerization domains good for? Matrix Biol 2000;19:283-288.
    • (2000) Matrix Biol , vol.19 , pp. 283-288
    • Engel, J.1    Kammerer, R.A.2
  • 3
    • 0032438190 scopus 로고    scopus 로고
    • The stability of proteins in extreme environments
    • Jaenicke R, Böhm G. The stability of proteins in extreme environments. Curr Opin Struct Biol 1998;8:738-748.
    • (1998) Curr Opin Struct Biol , vol.8 , pp. 738-748
    • Jaenicke, R.1    Böhm, G.2
  • 5
    • 0343777458 scopus 로고    scopus 로고
    • Observing single biomolecules at work with the atomic force microscope
    • Engel A, Muller DJ. Observing single biomolecules at work with the atomic force microscope. Nat Struct Biol 2000;7:715-718.
    • (2000) Nat Struct Biol , vol.7 , pp. 715-718
    • Engel, A.1    Muller, D.J.2
  • 7
    • 0036527014 scopus 로고    scopus 로고
    • Atomic force microscopy and proteins
    • Silva LP. Atomic force microscopy and proteins. Protein Peptide Lett 2002;9:117-125.
    • (2002) Protein Peptide Lett , vol.9 , pp. 117-125
    • Silva, L.P.1
  • 10
    • 0026700029 scopus 로고
    • Prediction of the structure of a receptor protein complex using a binary docking method
    • Stoddard BL, Koshland DE. Prediction of the structure of a receptor protein complex using a binary docking method. Nature 1992;358:774-776.
    • (1992) Nature , vol.358 , pp. 774-776
    • Stoddard, B.L.1    Koshland, D.E.2
  • 12
    • 0036099194 scopus 로고    scopus 로고
    • Computational simulation of the docking of Prochlorothrix hollandica plastocyanin to photosystem I: Modeling the electron transfer complex
    • Myshkin E, Leontis NB, Bullerjahn GS. Computational simulation of the docking of Prochlorothrix hollandica plastocyanin to photosystem I: Modeling the electron transfer complex. Biophys J 2002;82:3305-3313.
    • (2002) Biophys J , vol.82 , pp. 3305-3313
    • Myshkin, E.1    Leontis, N.B.2    Bullerjahn, G.S.3
  • 13
    • 0033587727 scopus 로고    scopus 로고
    • A systematic study of low-resolution recognition in protein-protein complexes
    • Vakser IA, Matar OG, Lam CF. A systematic study of low-resolution recognition in protein-protein complexes. Proc Natl Acad Sci USA 1999;96:8477-8482.
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 8477-8482
    • Vakser, I.A.1    Matar, O.G.2    Lam, C.F.3
  • 14
    • 0018873523 scopus 로고
    • Protein inhibitors of proteinases
    • Laskowski M, Kato I. Protein inhibitors of proteinases. Annu Rev Biochem 1980;49:593-626.
    • (1980) Annu Rev Biochem , vol.49 , pp. 593-626
    • Laskowski, M.1    Kato, I.2
  • 15
    • 0036678453 scopus 로고    scopus 로고
    • A clogged gutter mechanism for protease inhibitors
    • Radisky ES, Koshland, D. E. A clogged gutter mechanism for protease inhibitors. Proc Natl Acad Sci USA 2002;99:10316-10321.
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 10316-10321
    • Radisky, E.S.1    Koshland, D.E.2
  • 16
    • 0037117609 scopus 로고    scopus 로고
    • Modulation of protein-protein interactions by synthetic receptors: Design of molecules that disrupt serine protease-proteinaceous inhibitor interaction
    • Park HS, Lin Q, Hamilton AD. Modulation of protein-protein interactions by synthetic receptors: Design of molecules that disrupt serine protease-proteinaceous inhibitor interaction. Proc Natl Acad Sci USA 2002;99:5105-5109.
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 5105-5109
    • Park, H.S.1    Lin, Q.2    Hamilton, A.D.3
  • 18
    • 0023514883 scopus 로고
    • The complete amino-acid sequence of the Vigna-unguiculata (L) Walp seed trypsin and chymotrypsin inhibitor
    • Morhy L, Ventura MM. The complete amino-acid sequence of the Vigna-unguiculata (L) Walp seed trypsin and chymotrypsin inhibitor. An Acad Bras Cienc 1987;59:71-81.
    • (1987) An Acad Bras Cienc , vol.59 , pp. 71-81
    • Morhy, L.1    Ventura, M.M.2
  • 20
    • 0030983121 scopus 로고    scopus 로고
    • Analysis of the black-eyed pea trypsin and chymotrypsin inhibitor alpha-chymotrypsin complex
    • deFreitas SM, Mello LV, Silva MCM, Vriend G, Neshich G, Ventura MM. Analysis of the black-eyed pea trypsin and chymotrypsin inhibitor alpha-chymotrypsin complex. FEBS Lett 1997; 409:121-128.
    • (1997) FEBS Lett , vol.409 , pp. 121-128
    • DeFreitas, S.M.1    Mello, L.V.2    Silva, M.C.M.3    Vriend, G.4    Neshich, G.5    Ventura, M.M.6
  • 21
    • 0021444489 scopus 로고
    • Solvent perturbation and surface accessibility of the tryptophyl and tyrosyl groups in black-eyed pea trypsin and chymotrypsin inhibitor
    • Ventura MM, Mizuta K, Ikemoto H. Solvent perturbation and surface accessibility of the tryptophyl and tyrosyl groups in black-eyed pea trypsin and chymotrypsin inhibitor. An Acad Bras Cienc 1984;56:217-220.
    • (1984) An Acad Bras Cienc , vol.56 , pp. 217-220
    • Ventura, M.M.1    Mizuta, K.2    Ikemoto, H.3
  • 22
    • 0141984220 scopus 로고
    • Trypsin and chymotrypsin inhibitor from black-eyed pea (Vigna-sinensis L).6. Isolation and properties of complexes with trypsin and chymotrypsin
    • Ventura MM, OliveiraMartim CD, Morhy L. Trypsin and chymotrypsin inhibitor from black-eyed pea (Vigna-sinensis L).6. Isolation and properties of complexes with trypsin and chymotrypsin. An Acad Bras Cienc 1975;47:335-346.
    • (1975) An Acad Bras Cienc , vol.47 , pp. 335-346
    • Ventura, M.M.1    OliveiraMartim, C.D.2    Morhy, L.3
  • 23
    • 0008946673 scopus 로고
    • Self-association of the black-eyed pea trypsin and chymotrypsin inhibitor in solution - A study by light-scattering
    • Ventura MM, Mizuta K, Ikemoto H. Self-association of the black-eyed pea trypsin and chymotrypsin inhibitor in solution-a study by light-scattering. An Acad Bras Cienc 1981;53:195-201.
    • (1981) An Acad Bras Cienc , vol.53 , pp. 195-201
    • Ventura, M.M.1    Mizuta, K.2    Ikemoto, H.3
  • 24
    • 0038693409 scopus 로고    scopus 로고
    • Protein self-association in solution: The bovine pancreatic trypsin inhibitor decamer
    • Gottschalk M, Venu K, Halle B. Protein self-association in solution: The bovine pancreatic trypsin inhibitor decamer. Biophys J 2003;84:3941-3958.
    • (2003) Biophys J , vol.84 , pp. 3941-3958
    • Gottschalk, M.1    Venu, K.2    Halle, B.3
  • 25
    • 0004978724 scopus 로고
    • A trypsin and chymotrypsin inhibitor from black-eyed pea (Vigna sinensis). I. Purification and partial characterization
    • Ventura MM, Xavier-Filho J. A trypsin and chymotrypsin inhibitor from black-eyed pea (Vigna sinensis). I. Purification and partial characterization. An Acad Bras Cienc 1966;38:553-566.
    • (1966) An Acad Bras Cienc , vol.38 , pp. 553-566
    • Ventura, M.M.1    Xavier-Filho, J.2
  • 28
    • 0031473847 scopus 로고    scopus 로고
    • SWISS-MODEL and the Swiss-PdbViewer: An environment for comparative protein modeling
    • Guex N, Peitsch MC. SWISS-MODEL and the Swiss-PdbViewer: an environment for comparative protein modeling. Electrophoresis 1997;18:2714-2723.
    • (1997) Electrophoresis , vol.18 , pp. 2714-2723
    • Guex, N.1    Peitsch, M.C.2
  • 29
    • 0029881007 scopus 로고    scopus 로고
    • MOLMOL: A program for display and analysis of macromolecular structures
    • Koradi R, Billeter M, Wuthrich K. MOLMOL: a program for display and analysis of macromolecular structures. J Mol Graph 1996;14:51-55.
    • (1996) J Mol Graph , vol.14 , pp. 51-55
    • Koradi, R.1    Billeter, M.2    Wuthrich, K.3
  • 30
    • 0023645203 scopus 로고
    • Interior and surface of monomeric proteins
    • Miller S, Janin J, Lesk AM, Cyrus C. Interior and surface of monomeric proteins. J Mol Biol 1987;196:641-656.
    • (1987) J Mol Biol , vol.196 , pp. 641-656
    • Miller, S.1    Janin, J.2    Lesk, A.M.3    Cyrus, C.4
  • 31
    • 0024246956 scopus 로고
    • Surface, subunit interfaces and interior of oligomeric proteins
    • Janin J, Miller S, Chotia C. Surface, subunit interfaces and interior of oligomeric proteins. J Mol Biol 1988;204:155-164.
    • (1988) J Mol Biol , vol.204 , pp. 155-164
    • Janin, J.1    Miller, S.2    Chotia, C.3
  • 32
    • 12944331949 scopus 로고    scopus 로고
    • Predicting protein function from structure: Unique structural features of proteases
    • Stawiski EW, Baucom AE, Lohr SC, Gregoret LM. Predicting protein function from structure: Unique structural features of proteases. Proc Natl Acad Sci USA 2000;97:3954-3958.
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 3954-3958
    • Stawiski, E.W.1    Baucom, A.E.2    Lohr, S.C.3    Gregoret, L.M.4
  • 35
    • 0015222647 scopus 로고
    • Interpretation of protein structures-estimation of static accessibility
    • Lee BK, Richards FM. Interpretation of protein structures-estimation of static accessibility. J Mol Biol 1971;55:379-400.
    • (1971) J Mol Biol , vol.55 , pp. 379-400
    • Lee, B.K.1    Richards, F.M.2
  • 36
    • 0031951980 scopus 로고    scopus 로고
    • Molecular weights of individual proteins correlate with molecular volumes measured by atomic force microscopy
    • Schneider SW, Larmer J, Henderson RM, Oberleithner H. Molecular weights of individual proteins correlate with molecular volumes measured by atomic force microscopy. Pflug Arch Eur J Phys 1998;43:362-367.
    • (1998) Pflug Arch Eur J Phys , vol.43 , pp. 362-367
    • Schneider, S.W.1    Larmer, J.2    Henderson, R.M.3    Oberleithner, H.4
  • 37
    • 0037328523 scopus 로고    scopus 로고
    • Quantitative characterization of biomolecular assemblies and interactions using atomic force microscopy
    • Yang Y, Wang H, Eriea DA. Quantitative characterization of biomolecular assemblies and interactions using atomic force microscopy. Methods 2003;29:175-187.
    • (2003) Methods , vol.29 , pp. 175-187
    • Yang, Y.1    Wang, H.2    Eriea, D.A.3
  • 38
  • 39
    • 0037022821 scopus 로고    scopus 로고
    • A minimal exonuclease domain of WRN forms a hexamer on DNA and possesses both 3′-5′ exonuclease and 5′-protruding strand endonuclease activities
    • Xue Y, Ratcli GC, Wang H, Davis-Searles PR, Gray MD, Erie DA, Redinbo MR. A minimal exonuclease domain of WRN forms a hexamer on DNA and possesses both 3′-5′ exonuclease and 5′-protruding strand endonuclease activities. Biochemistry 2002; 41:2901-2912.
    • (2002) Biochemistry , vol.41 , pp. 2901-2912
    • Xue, Y.1    Ratcli, G.C.2    Wang, H.3    Davis-Searles, P.R.4    Gray, M.D.5    Erie, D.A.6    Redinbo, M.R.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.