SEARCH

SEARCH BY CITATION

References

  • 1
    Benchabane M, Schlüter U, Vorster J, Goulet MC & Michaud D (2010) Plant cystatins. Biochimie 92, 16571666.
  • 2
    Turk V, Stoka V & Turk D (2008) Cystatins: biochemical and structural properties, and medical relevance. Front Biosci 13, 54065420.
  • 3
    Oliveira JP, Magliarelli HF, Pereira FV, Gianotti A, Soares-Costa A, Henrique-Silva F, Wakamatsu A, Soares IC, Nonogaki S, Travassos LR, et al. (2011) Sugarcane cystatin CaneCPI-4 inhibits melanoma growth by angiogenesis disruption. J Cancer Sci Ther 3, 161167.
  • 4
    Nagata K, Kudo N, Abe K, Arai S & Tanokura M (2000) Three-dimensional solution structure of oryzacystatin-I, a cysteine proteinase inhibitor of the rice, Oryza sativa L. japonica. Biochemistry 39, 1475314760.
  • 5
    Bode W, Engh R, Musil D, Thiele U, Huber R, Karshikov A, Brzin J, Kos J & Turk V (1988) The 2.0 Å X-ray crystal structure of chicken egg white cystatin and its possible mode of interaction with cysteine proteinases. EMBO J 7, 25932599.
  • 6
    Stubbs MT, Laber B, Bode W, Huber R, Jerala R, Lenarcic B & Turk V (1990) The refined 2.4 Å X-ray crystal structure of recombinant human stefin B in complex with the cysteine proteinase papain: a novel type of proteinase inhibitor interaction. EMBO J 9, 19391947.
  • 7
    Jenko S, Dolenc I, Guncar G, Dobersek A, Podobnik M & Turk D (2003) Crystal structure of stefin A in complex with cathepsin H: N-terminal residues of inhibitors can adapt to the active sites of endo- and exopeptidases. J Mol Biol 326, 875885.
  • 8
    Renko M, Požgan U, Majera D & Turk D (2010) Stefin A displaces the occluding loop of cathepsin B only by as much as required to bind to the active site cleft. FEBS J 277, 43384345.
  • 9
    Chu MH, Liu KL, Wu HY, Yeh KW & Cheng YS (2011) Crystal structure of tarocystatin–papain complex: implications for the inhibition property of group-2 phytocystatins. Planta 234, 243254.
  • 10
    Mohamed MM & Sloane BF (2006) Cysteine cathepsins: multifunctional enzymes in cancer. Nat Rev Cancer 6, 764775.
  • 11
    Hook VY (2006) Unique neuronal functions of cathepsin L and cathepsin B in secretory vesicles: biosynthesis of peptides in neurotransmission and neurodegenerative disease. Biol Chem 387, 14291439.
  • 12
    Arai S, Matsumoto I, Emori Y & Abe K (2002) Plant seed cystatins and their target enzymes of endogenous and exogenous origin. J Agric Food Chem 50, 66126617.
  • 13
    Margis R, Reis EM & Villeret V (1998) Structural and phylogenetic relationships among plant and animal cystatins. Arch Biochem Biophys 359, 2430.
  • 14
    Hwang JE, Hong JK, Je JH, Lee KO, Kim DY, Lee SY & Lim CO (2009) Regulation of seed germination and seedling growth by an Arabidopsis phytocystatin isoform, AtCYS6. Plant Cell Rep 28, 16231632.
  • 15
    Neuteboom LW, Matsumoto KO & Christopher DA (2009) An extended AE-rich N-terminal trunk in secreted pineapple cystatin enhances inhibition of fruit bromelain and is posttranslationally removed during ripening. Plant Physiol 151, 515527.
  • 16
    Goulet MC, Dallaire C, Vaillancourt LP, Khalf M, Badri AM, Preradov A, Duceppe MO, Goulet C, Cloutier C & Michaud D (2008) Tailoring the specificity of a plant cystatin toward herbivorous insect digestive cysteine proteases by single mutations at positively selected amino acid sites. Plant Physiol 146, 10101019.
  • 17
    Carrillo L, Martinez M, Alvarez-Alfageme F, Castañera P, Smagghe G, Diaz I & Ortego F (2011) A barley cysteine-proteinase inhibitor reduces the performance of two aphid species in artificial diets and transgenic Arabidopsis plants. Transgenic Res 20, 305319.
  • 18
    Senthilkumar R, Cheng CP & Yeh KW (2010) Genetically pyramiding protease-inhibitor genes for dual broad-spectrum resistance against insect and phytopathogens in transgenic tobacco. Plant Biotechnol J 8, 6575.
  • 19
    Kiggundu A, Muchwezi J, Van der Vyver C, Viljoen A, Vorster J, Schlüter U, Kunert K & Michaud D (2010) Deleterious effects of plant cystatins against the banana weevil Cosmopolites sordidus. Arch Insect Biochem Physiol 73, 87105.
  • 20
    Samac DA & Smigocki AC (2003) Expression of oryzacystatin I and II in alfalfa increases resistance to the root-lesion nematode. Phytopathology 93, 799804.
  • 21
    Chan YL, Yang AH, Chen JT, Yeh KW & Chan MT (2010) Heterologous expression of taro cystatin protects transgenic tomato against Meloidogyne incognita infection by means of interfering sex determination and suppressing gall formation. Plant Cell Rep 29, 231238.
  • 22
    Cavini IA, de Oliveira-Silva R, de Almeida Marques I, Kalbitzer HR & Munte CE (2012) Chemical shift assignments of the canecystatin-1 from Saccharum officinarum. Biomol NMR Assign. doi:10.1007/s12104-012-9401-2.
  • 23
    Nissen MS, Kumar GN, Youn B, Knowles DB, Lam KS, Ballinger WJ, Knowles NR & Kang C (2009) Characterization of Solanum tuberosum multicystatin and its structural comparison with other cystatins. Plant Cell 21, 861975.
  • 24
    Irene D, Chen BJ, Lo SH, Liu TH, Tzen JT & Chyan CL (2012) Resonance assignments and secondary structure of a phytocystatin from Ananas comosus. Biomol NMR Assign 6, 99101.
  • 25
    Ekiel I & Abrahamson M (1996) Folding-related dimerization of human cystatin C. J Biol Chem 271, 13141321.
  • 26
    Ekiel I, Abrahamson M, Fulton DB, Lindahl P, Storer AC, Levadoux W, Lafrance M, Labelle S, Pomerleau Y, Groleau D, et al. (1997) NMR structural studies of human cystatin C dimers and monomers. J Mol Biol 271, 266277.
  • 27
    Janowski R, Kozak M, Abrahamson M, Grubb A & Jaskolski M (2005) 3D domain-swapped human cystatin C with amyloidlike intermolecular beta-sheets. Proteins 61, 570578.
  • 28
    Janowski R, Kozak M, Jankowska E, Grzonka Z, Grubb A, Abrahamson M & Jaskolski M (2001) Human cystatin C, an amyloidogenic protein, dimerizes through three-dimensional domain swapping. Nat Struct Biol 8, 316320.
  • 29
    Bennett MJ, Schlunegger MP & Eisenberg D (1995) 3D domain swapping: a mechanism for oligomer assembly. Protein Sci 4, 24552468.
  • 30
    Wishart DS, Sykes BD & Richards FM (1992) The chemical shift index: a fast and simple method for the assignment of protein secondary structure through NMR spectroscopy. Biochemistry 31, 16471651.
  • 31
    Barrientos LG, Louis JM, Botos I, Mori T, Han Z, O'Keefe BR, Boyd MR, Wlodawer A & Gronenborn AM (2002) The domain-swapped dimer of cyanovirin-N is in a metastable folded state: reconciliation of X-ray and NMR structures. Structure 10, 673686.
  • 32
    Schumann FH, Riepl H, Maurer T, Gronwald W, Neidig K-P & Kalbitzer HR (2007) Combined chemical shift changes and amino acid specific chemical shift mapping of protein–protein interactions. J Biomol NMR 39, 275289.
  • 33
    Jenko Kokalj S, Guncar G, Stern I, Morgan G, Rabzelj S, Kenig M, Staniforth RA, Waltho JP, Zerovnik E & Turk D (2007) Essential role of proline isomerization in stefin B tetramer formation. J Mol Biol 366, 15691579.
  • 34
    Salemme FR (1983) Structural properties of protein beta-sheets. Prog Biophys Mol Biol 42, 95133.
  • 35
    Richardson JS, Getzoff ED & Richardson DC (1978) The beta bulge: a common small unit of nonrepetitive protein structure. Proc Natl Acad Sci USA 75, 25742578.
  • 36
    Valadares NF, Dellamano M, Soares-Costa A, Henrique-Silva F & Garratt RC (2010) Molecular determinants of improved cathepsin B inhibition by new cystatins obtained by DNA shuffling. BMC Struct Biol 10, 30.
  • 37
    Palsdottir A, Abrahamson M, Thorsteinsson L, Arnason A, Olafsson I, Grubb A & Jensson O (1988) Mutation in cystatin C gene causes hereditary brain haemorrhage. Lancet 2, 603604.
  • 38
    Soares-Costa A, Beltramini LM, Thiemann OH & Henrique-Silva F (2002) A sugarcane cystatin: recombinant expression, purification, and antifungal activity. Biochem Biophys Res Commun 296, 11941199.
  • 39
    Leslie AGW & Powell HR (2007) Processing diffraction data with mosflm. In Evolving Methods for Macromolecular Crystallography (Read RJ & Sussman JL, eds), pp. 4151. Springer, Dordrecht, The Netherlands.
  • 40
    McCoy AJ, Grosse-Kunstleve RW, Adams PD, Winn MD, Storoni LC & Read RJ (2007) Phaser crystallographic software. J Appl Crystallogr 40, 658674.
  • 41
    Emsley P, Lohkamp B, Scott WG & Cowtan K (2010) Features and development of Coot. Acta Crystallogr D Biol Crystallogr D66, 486501.
  • 42
    Adams PD, Afonine PV, Bunkóczi G, Chen VB, Davis IW, Echols N, Headd JJ, Hung LW, Kapral GJ, Grosse-Kunstleve RW, et al. (2010) PHENIX: a comprehensive Python-based system for macromolecular structure solution. Acta Crystallogr D Biol Crystallogr D66, 213221.
  • 43
    Markley JL, Bax A, Arata Y, Hilbert CW, Kaptein R, Sykes BD, Wright PE & Wüthrich K (1998) Recommendations for the presentation of NMR structures of proteins and nucleic acids. Pure Appl Chem 70, 117142.