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Volumn 12, Issue 17, 2012, Pages 2641-2655

Natural intracellular peptides can modulate the interactions of mouse brain proteins and thimet oligopeptidase with 14-3-3ε and calmodulin

Author keywords

Biomedicine; Calcium; Interactome; Intracellular peptides; Peptide protein interaction; Protein target

Indexed keywords

BRAIN PROTEIN; CALCIUM ION; CALMODULIN; CELL PROTEIN; PROTEIN 14 3 3; PROTEIN 14 3 3 EPSILON; THIMET OLIGOPEPTIDASE; UNCLASSIFIED DRUG;

EID: 84865563623     PISSN: 16159853     EISSN: 16159861     Source Type: Journal    
DOI: 10.1002/pmic.201200032     Document Type: Article
Times cited : (40)

References (74)
  • 1
    • 67349200229 scopus 로고    scopus 로고
    • Interaction networks: from protein functions to drug discovery. A review
    • Chautard, E., Thierry-Mieg, N., Ricard-Blum, S., Interaction networks: from protein functions to drug discovery. A review. Pathol. Biol. 2009, 57, 324-333.
    • (2009) Pathol. Biol. , vol.57 , pp. 324-333
    • Chautard, E.1    Thierry-Mieg, N.2    Ricard-Blum, S.3
  • 2
    • 77956212938 scopus 로고    scopus 로고
    • Network bistability mediates spontaneous transitions between normal and pathological brain states
    • Frohlich, F., Sejnowski, T. J., Bazhenov, M., Network bistability mediates spontaneous transitions between normal and pathological brain states. J. Neurosci. 2010, 30, 10734-10743.
    • (2010) J. Neurosci. , vol.30 , pp. 10734-10743
    • Frohlich, F.1    Sejnowski, T.J.2    Bazhenov, M.3
  • 4
    • 59849125136 scopus 로고    scopus 로고
    • Dynamic modularity in protein interaction networks predicts breast cancer outcome
    • Taylor, I. W., Linding, R., Warde-Farley, D., Liu, Y. et al., Dynamic modularity in protein interaction networks predicts breast cancer outcome. Nat. Biotechnol. 2009, 27, 199-204.
    • (2009) Nat. Biotechnol. , vol.27 , pp. 199-204
    • Taylor, I.W.1    Linding, R.2    Warde-Farley, D.3    Liu, Y.4
  • 5
    • 79952674000 scopus 로고    scopus 로고
    • Interactome networks and human disease
    • Vidal, M., Cusick, M. E., Barabasi, A. L., Interactome networks and human disease. Cell 2011, 144, 986-998.
    • (2011) Cell , vol.144 , pp. 986-998
    • Vidal, M.1    Cusick, M.E.2    Barabasi, A.L.3
  • 6
    • 84860631021 scopus 로고    scopus 로고
    • The interaction network of the 14-3-3 protein in the ancient protozoan parasite Giardia duodenalis
    • Lalle, M., Camerini, S., Cecchetti, S., Sayadi, A. et al., The interaction network of the 14-3-3 protein in the ancient protozoan parasite Giardia duodenalis. J. Proteome. Res. 2012, 11, 2666-2683.
    • (2012) J. Proteome. Res. , vol.11 , pp. 2666-2683
    • Lalle, M.1    Camerini, S.2    Cecchetti, S.3    Sayadi, A.4
  • 7
    • 84858961199 scopus 로고    scopus 로고
    • Host-pathogen interactome mapping for HTLV-1 and 2 retroviruses
    • Simonis, N., Rual, J. F., Lemmens, I., Boxus, M. et al., Host-pathogen interactome mapping for HTLV-1 and 2 retroviruses. Retrovirology 2012, 9, 26.
    • (2012) Retrovirology , vol.9 , pp. 26
    • Simonis, N.1    Rual, J.F.2    Lemmens, I.3    Boxus, M.4
  • 8
    • 60849105400 scopus 로고    scopus 로고
    • Functional organization of the yeast proteome by a yeast interactome map
    • Valente, A. X., Roberts, S. B., Buck, G. A., Gao, Y., Functional organization of the yeast proteome by a yeast interactome map. Proc. Natl. Acad. Sci. USA 2009, 106, 1490-1495.
    • (2009) Proc. Natl. Acad. Sci. USA , vol.106 , pp. 1490-1495
    • Valente, A.X.1    Roberts, S.B.2    Buck, G.A.3    Gao, Y.4
  • 9
    • 84860721058 scopus 로고    scopus 로고
    • Functional versatility of a single protein surface in two protein: protein interactions
    • Adikaram, P., Beckett, D., Functional versatility of a single protein surface in two protein: protein interactions. J. Mol. Biol. 2012, 419, 223-233.
    • (2012) J. Mol. Biol. , vol.419 , pp. 223-233
    • Adikaram, P.1    Beckett, D.2
  • 10
    • 80053014109 scopus 로고    scopus 로고
    • Prediction of biological protein-protein interactions using atom-type and amino acid properties
    • Aziz, M. M., Maleki, M., Rueda, L., Raza, M. et al., Prediction of biological protein-protein interactions using atom-type and amino acid properties. Proteomics 2011, 11, 3802-3810.
    • (2011) Proteomics , vol.11 , pp. 3802-3810
    • Aziz, M.M.1    Maleki, M.2    Rueda, L.3    Raza, M.4
  • 11
    • 79959715936 scopus 로고    scopus 로고
    • Four-dimensional visualisation and analysis of protein-protein interaction networks
    • Goel, A., Li, S. S., Wilkins, M. R., Four-dimensional visualisation and analysis of protein-protein interaction networks. Proteomics 2011, 11, 2672-2682.
    • (2011) Proteomics , vol.11 , pp. 2672-2682
    • Goel, A.1    Li, S.S.2    Wilkins, M.R.3
  • 12
    • 84858685375 scopus 로고    scopus 로고
    • Coil-to-helix transitions in intrinsically disordered methyl CpG binding protein 2 and its isolated domains
    • Hite, K. C., Kalashnikova, A. A., Hansen, J. C., Coil-to-helix transitions in intrinsically disordered methyl CpG binding protein 2 and its isolated domains. Protein Sci. 2012, 21, 531-538.
    • (2012) Protein Sci. , vol.21 , pp. 531-538
    • Hite, K.C.1    Kalashnikova, A.A.2    Hansen, J.C.3
  • 13
    • 84055200396 scopus 로고    scopus 로고
    • Atomistic ensemble modeling and small-angle neutron scattering of intrinsically disordered protein complexes: applied to minichromosome maintenance protein
    • Krueger, S., Shin, J. H., Raghunandan, S., Curtis, J. E. et al., Atomistic ensemble modeling and small-angle neutron scattering of intrinsically disordered protein complexes: applied to minichromosome maintenance protein. Biophys. J. 2011, 101, 2999-3007.
    • (2011) Biophys. J. , vol.101 , pp. 2999-3007
    • Krueger, S.1    Shin, J.H.2    Raghunandan, S.3    Curtis, J.E.4
  • 14
    • 0037453510 scopus 로고    scopus 로고
    • Assembly of cell regulatory systems through protein interaction domains
    • Pawson, T., Nash, P., Assembly of cell regulatory systems through protein interaction domains. Science 2003, 300, 445-452.
    • (2003) Science , vol.300 , pp. 445-452
    • Pawson, T.1    Nash, P.2
  • 15
    • 33645316787 scopus 로고    scopus 로고
    • computing: can computers help to explain biology?
    • Brent, R., Bruck, J., computing: can computers help to explain biology? Nature 2006, 440, 416-417.
    • (2006) Nature , vol.440 , pp. 416-417
    • Brent, R.1    Bruck, J.2
  • 16
  • 17
    • 32344448382 scopus 로고    scopus 로고
    • Screening for peptide drugs from the natural repertoire of biodiverse protein folds
    • Watt, P. M., Screening for peptide drugs from the natural repertoire of biodiverse protein folds. Nat. Biotechnol. 2006, 24, 177-183.
    • (2006) Nat. Biotechnol. , vol.24 , pp. 177-183
    • Watt, P.M.1
  • 18
    • 0028274544 scopus 로고
    • Anchoring of protein kinase A is required for modulation of AMPA/kainate receptors on hippocampal neurons
    • Rosenmund, C., Carr, D. W., Bergeson, S. E., Nilaver, G. et al., Anchoring of protein kinase A is required for modulation of AMPA/kainate receptors on hippocampal neurons. Nature 1994, 368, 853-856.
    • (1994) Nature , vol.368 , pp. 853-856
    • Rosenmund, C.1    Carr, D.W.2    Bergeson, S.E.3    Nilaver, G.4
  • 19
    • 7044230885 scopus 로고    scopus 로고
    • Possible novel therapy for diabetes with cell-permeable JNK-inhibitory peptide
    • Kaneto, H., Nakatani, Y., Miyatsuka, T., Kawamori, D. et al., Possible novel therapy for diabetes with cell-permeable JNK-inhibitory peptide. Nat. Med. 2004, 10, 1128-1132.
    • (2004) Nat. Med. , vol.10 , pp. 1128-1132
    • Kaneto, H.1    Nakatani, Y.2    Miyatsuka, T.3    Kawamori, D.4
  • 20
    • 55949100580 scopus 로고    scopus 로고
    • Identification of a new JNK inhibitor targeting the JNK-JIP interaction site
    • Stebbins, J. L., De, S. K., Machleidt, T., Becattini, B. et al., Identification of a new JNK inhibitor targeting the JNK-JIP interaction site. Proc. Natl. Acad. Sci. USA 2008, 105, 16809-16813.
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 16809-16813
    • Stebbins, J.L.1    De, S.K.2    Machleidt, T.3    Becattini, B.4
  • 21
    • 33747372839 scopus 로고    scopus 로고
    • Protein kinase C delta (deltaPKC)-annexin V interaction: a required step in deltaPKC translocation and function
    • Kheifets, V., Bright, R., Inagaki, K., Schechtman, D. et al., Protein kinase C delta (deltaPKC)-annexin V interaction: a required step in deltaPKC translocation and function. J. Biol. Chem. 2006, 281, 23218-23226.
    • (2006) J. Biol. Chem. , vol.281 , pp. 23218-23226
    • Kheifets, V.1    Bright, R.2    Inagaki, K.3    Schechtman, D.4
  • 22
    • 84859136797 scopus 로고    scopus 로고
    • Protein quality control disruption by PKCbetaII in heart failure; rescue by the selective PKCetaII inhibitor, betaIIV5-3
    • Ferreira, J. C., Boer, B. N., Grinberg, M., Brum, P. C. et al., Protein quality control disruption by PKCbetaII in heart failure; rescue by the selective PKCetaII inhibitor, betaIIV5-3. PLoS One 2012, 7, e33175.
    • (2012) PLoS One , vol.7
    • Ferreira, J.C.1    Boer, B.N.2    Grinberg, M.3    Brum, P.C.4
  • 23
    • 80054116042 scopus 로고    scopus 로고
    • Rational design of peptides with anti-HCV/HIV activities and enhanced specificity
    • Li, G. R., He, L. Y., Liu, X. Y., Liu, A. P. et al., Rational design of peptides with anti-HCV/HIV activities and enhanced specificity. Chem. Biol. Drug Des. 2011, 78, 835-843.
    • (2011) Chem. Biol. Drug Des. , vol.78 , pp. 835-843
    • Li, G.R.1    He, L.Y.2    Liu, X.Y.3    Liu, A.P.4
  • 24
    • 80455143365 scopus 로고    scopus 로고
    • ALDH2 activator inhibits increased myocardial infarction injury by nitroglycerin tolerance
    • Sun, L., Ferreira, J. C., Mochly-Rosen, D., ALDH2 activator inhibits increased myocardial infarction injury by nitroglycerin tolerance. Sci. Transl. Med. 2011, 3, 107ra111.
    • (2011) Sci. Transl. Med. , vol.3
    • Sun, L.1    Ferreira, J.C.2    Mochly-Rosen, D.3
  • 25
    • 78649648123 scopus 로고    scopus 로고
    • Similar intracellular peptide profile of TAP1/beta2 microglobulin double-knockout mice and C57BL/6 wild-type mice as revealed by peptidomic analysis
    • Castro, L. M., Berti, D. A., Russo, L. C., Coelho, V. et al., Similar intracellular peptide profile of TAP1/beta2 microglobulin double-knockout mice and C57BL/6 wild-type mice as revealed by peptidomic analysis. AAPS J. 2010, 12, 608-616.
    • (2010) AAPS J. , vol.12 , pp. 608-616
    • Castro, L.M.1    Berti, D.A.2    Russo, L.C.3    Coelho, V.4
  • 26
    • 84857822899 scopus 로고    scopus 로고
    • Peptidomic analysis of HEK293T cells: effect of the proteasome inhibitor epoxomicin on intracellular peptides
    • Fricker, L. D., Gelman, J. S., Castro, L. M., Gozzo, F. C. et al., Peptidomic analysis of HEK293T cells: effect of the proteasome inhibitor epoxomicin on intracellular peptides. J. Proteome Res. 2012, 11, 1981-1990.
    • (2012) J. Proteome Res. , vol.11 , pp. 1981-1990
    • Fricker, L.D.1    Gelman, J.S.2    Castro, L.M.3    Gozzo, F.C.4
  • 28
    • 0037424492 scopus 로고    scopus 로고
    • Novel natural peptide substrates for endopeptidase 24.15, neurolysin, and angiotensin-converting enzyme
    • Rioli, V., Gozzo, F. C., Heimann, A. S., Linardi, A. et al., Novel natural peptide substrates for endopeptidase 24.15, neurolysin, and angiotensin-converting enzyme. J. Biol. Chem. 2003, 278, 8547-8555.
    • (2003) J. Biol. Chem. , vol.278 , pp. 8547-8555
    • Rioli, V.1    Gozzo, F.C.2    Heimann, A.S.3    Linardi, A.4
  • 29
    • 78649664752 scopus 로고    scopus 로고
    • Hemoglobin-derived peptides as novel type of bioactive signaling molecules
    • Gomes, I., Dale, C. S., Casten, K., Geigner, M. A. et al., Hemoglobin-derived peptides as novel type of bioactive signaling molecules. AAPS J. 2010, 12, 658-669.
    • (2010) AAPS J. , vol.12 , pp. 658-669
    • Gomes, I.1    Dale, C.S.2    Casten, K.3    Geigner, M.A.4
  • 30
    • 70349339642 scopus 로고    scopus 로고
    • Novel endogenous peptide agonists of cannabinoid receptors
    • Gomes, I., Grushko, J. S., Golebiewska, U., Hoogendoorn, S. et al., Novel endogenous peptide agonists of cannabinoid receptors. FASEB J. 2009, 23, 3020-3029.
    • (2009) FASEB J. , vol.23 , pp. 3020-3029
    • Gomes, I.1    Grushko, J.S.2    Golebiewska, U.3    Hoogendoorn, S.4
  • 31
    • 38049117749 scopus 로고    scopus 로고
    • Hemopressin is an inverse agonist of CB1 cannabinoid receptors
    • Heimann, A. S., Gomes, I., Dale, C. S., Pagano, R. L. et al., Hemopressin is an inverse agonist of CB1 cannabinoid receptors. Proc. Natl. Acad. Sci. USA 2007, 104, 20588-20593.
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , pp. 20588-20593
    • Heimann, A.S.1    Gomes, I.2    Dale, C.S.3    Pagano, R.L.4
  • 32
    • 8644245895 scopus 로고    scopus 로고
    • Intracellullar peptides as putative natural regulators of protein interactions
    • Ferro, E. S., Hyslop, S., Camargo, A. C., Intracellullar peptides as putative natural regulators of protein interactions. J. Neurochem. 2004, 91, 769-777.
    • (2004) J. Neurochem. , vol.91 , pp. 769-777
    • Ferro, E.S.1    Hyslop, S.2    Camargo, A.C.3
  • 33
    • 54049117647 scopus 로고    scopus 로고
    • Intracellular peptides as natural regulators of cell signaling
    • Cunha, F. M., Berti, D. A., Ferreira, Z. S., Klitzke, C. F. et al., Intracellular peptides as natural regulators of cell signaling. J. Biol. Chem. 2008, 283, 24448-24459.
    • (2008) J. Biol. Chem. , vol.283 , pp. 24448-24459
    • Cunha, F.M.1    Berti, D.A.2    Ferreira, Z.S.3    Klitzke, C.F.4
  • 34
    • 67649804558 scopus 로고    scopus 로고
    • Analysis of intracellular substrates and products of thimet oligopeptidase in human embryonic kidney 293 cells
    • Berti, D. A., Morano, C., Russo, L. C., Castro, L. M. et al., Analysis of intracellular substrates and products of thimet oligopeptidase in human embryonic kidney 293 cells. J. Biol. Chem. 2009, 284, 14105-14116.
    • (2009) J. Biol. Chem. , vol.284 , pp. 14105-14116
    • Berti, D.A.1    Morano, C.2    Russo, L.C.3    Castro, L.M.4
  • 35
    • 76849100919 scopus 로고    scopus 로고
    • The matrix peptide exporter HAF-1 signals a mitochondrial UPR by activating the transcription factor ZC376.7 in C. elegans
    • Haynes, C. M., Yang, Y., Blais, S. P., Neubert, T. A. et al., The matrix peptide exporter HAF-1 signals a mitochondrial UPR by activating the transcription factor ZC376.7 in C. elegans. Mol. Cell 2010, 37, 529-540.
    • (2010) Mol. Cell , vol.37 , pp. 529-540
    • Haynes, C.M.1    Yang, Y.2    Blais, S.P.3    Neubert, T.A.4
  • 36
    • 77954786287 scopus 로고    scopus 로고
    • Small peptides switch the transcriptional activity of Shavenbaby during Drosophila embryogenesis
    • Kondo, T., Plaza, S., Zanet, J., Benrabah, E. et al., Small peptides switch the transcriptional activity of Shavenbaby during Drosophila embryogenesis. Science 2010, 329, 336-339.
    • (2010) Science , vol.329 , pp. 336-339
    • Kondo, T.1    Plaza, S.2    Zanet, J.3    Benrabah, E.4
  • 39
    • 16244373008 scopus 로고    scopus 로고
    • 14-3-3 epsilon modulates the stimulated secretion of endopeptidase 24.15
    • Carreno, F. R., Goni, C. N., Castro, L. M., Ferro, E. S., 14-3-3 epsilon modulates the stimulated secretion of endopeptidase 24.15. J. Neurochem. 2005, 93, 10-25.
    • (2005) J. Neurochem. , vol.93 , pp. 10-25
    • Carreno, F.R.1    Goni, C.N.2    Castro, L.M.3    Ferro, E.S.4
  • 40
    • 68749107347 scopus 로고    scopus 로고
    • Interaction with calmodulin is important for the secretion of thimet oligopeptidase following stimulation
    • Russo, L. C., Goni, C. N., Castro, L. M., Asega, A. F. et al., Interaction with calmodulin is important for the secretion of thimet oligopeptidase following stimulation. FEBS J. 2009, 276, 4358-4371.
    • (2009) FEBS J. , vol.276 , pp. 4358-4371
    • Russo, L.C.1    Goni, C.N.2    Castro, L.M.3    Asega, A.F.4
  • 41
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M. M., A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 1976, 72, 248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 42
    • 23944492861 scopus 로고    scopus 로고
    • Surface plasmon resonance: applications in understanding receptor-ligand interaction
    • Pattnaik, P., Surface plasmon resonance: applications in understanding receptor-ligand interaction. Appl. Biochem. Biotechnol. 2005, 126, 79-92.
    • (2005) Appl. Biochem. Biotechnol. , vol.126 , pp. 79-92
    • Pattnaik, P.1
  • 43
    • 0346996861 scopus 로고    scopus 로고
    • Functional interactions between mu opioid and alpha 2A-adrenergic receptors
    • Jordan, B. A., Gomes, I., Rios, C., Filipovska, J. et al., Functional interactions between mu opioid and alpha 2A-adrenergic receptors. Mol. Pharmacol. 2003, 64, 1317-1324.
    • (2003) Mol. Pharmacol. , vol.64 , pp. 1317-1324
    • Jordan, B.A.1    Gomes, I.2    Rios, C.3    Filipovska, J.4
  • 44
    • 33745085564 scopus 로고    scopus 로고
    • mu opioid and CB1 cannabinoid receptor interactions: reciprocal inhibition of receptor signaling and neuritogenesis
    • Rios, C., Gomes, I., Devi, L. A., mu opioid and CB1 cannabinoid receptor interactions: reciprocal inhibition of receptor signaling and neuritogenesis. Br. J. Pharmacol. 2006, 148, 387-395.
    • (2006) Br. J. Pharmacol. , vol.148 , pp. 387-395
    • Rios, C.1    Gomes, I.2    Devi, L.A.3
  • 45
    • 0021061819 scopus 로고
    • Rapid colorimetric assay for cellular growth and survival: application to proliferation and cytotoxicity assays
    • Mosmann, T., Rapid colorimetric assay for cellular growth and survival: application to proliferation and cytotoxicity assays. J. Immunol. Methods 1983, 65, 55-63.
    • (1983) J. Immunol. Methods , vol.65 , pp. 55-63
    • Mosmann, T.1
  • 46
    • 42049119834 scopus 로고    scopus 로고
    • Kinin-B2 receptor expression and activity during differentiation of embryonic rat neurospheres
    • Martins, A. H., Alves, J. M., Trujillo, C. A., Schwindt, T. T. et al., Kinin-B2 receptor expression and activity during differentiation of embryonic rat neurospheres. Cytometry A. 2008, 73, 361-368.
    • (2008) Cytometry A. , vol.73 , pp. 361-368
    • Martins, A.H.1    Alves, J.M.2    Trujillo, C.A.3    Schwindt, T.T.4
  • 47
    • 26844518104 scopus 로고    scopus 로고
    • Quantitative neuropeptidomics of microwave-irradiated mouse brain and pituitary
    • Che, F. Y., Lim, J., Pan, H., Biswas, R. et al., Quantitative neuropeptidomics of microwave-irradiated mouse brain and pituitary. Mol. Cell Proteomics 2005, 4, 1391-1405.
    • (2005) Mol. Cell Proteomics , vol.4 , pp. 1391-1405
    • Che, F.Y.1    Lim, J.2    Pan, H.3    Biswas, R.4
  • 48
    • 38049037238 scopus 로고    scopus 로고
    • Optimization of neuropeptide extraction from the mouse hypothalamus
    • Che, F. Y., Zhang, X., Berezniuk, I., Callaway, M. et al., Optimization of neuropeptide extraction from the mouse hypothalamus. J. Proteome Res. 2007, 6, 4667-4676.
    • (2007) J. Proteome Res. , vol.6 , pp. 4667-4676
    • Che, F.Y.1    Zhang, X.2    Berezniuk, I.3    Callaway, M.4
  • 49
    • 57449116568 scopus 로고    scopus 로고
    • Multiple isotopic labels for quantitative mass spectrometry
    • Morano, C., Zhang, X., Fricker, L. D., Multiple isotopic labels for quantitative mass spectrometry. Anal. Chem. 2008, 80, 9298-9309.
    • (2008) Anal. Chem. , vol.80 , pp. 9298-9309
    • Morano, C.1    Zhang, X.2    Fricker, L.D.3
  • 50
    • 0032987473 scopus 로고    scopus 로고
    • Functional interaction of the K-Cl cotransporter (KCC1) with the Na-K-Cl cotransporter in HEK-293 cells
    • Gillen, C. M., Forbush, B., 3rd, Functional interaction of the K-Cl cotransporter (KCC1) with the Na-K-Cl cotransporter in HEK-293 cells. Am. J. Physiol. 1999, 276, C328-C336.
    • (1999) Am. J. Physiol. , vol.276
    • Gillen, C.M.1    Forbush 3rd, B.2
  • 51
    • 15244340432 scopus 로고    scopus 로고
    • ACE gene titration in mice uncovers a new mechanism for ACE on the control of body weight
    • Heimann, A. S., Favarato, M. H., Gozzo, F. C., Rioli, V. et al., ACE gene titration in mice uncovers a new mechanism for ACE on the control of body weight. Physiol. Genomics 2005, 20, 173-182.
    • (2005) Physiol. Genomics , vol.20 , pp. 173-182
    • Heimann, A.S.1    Favarato, M.H.2    Gozzo, F.C.3    Rioli, V.4
  • 52
    • 28444435236 scopus 로고    scopus 로고
    • Substrate phosphorylation affects degradation and interaction to endopeptidase 24.15, neurolysin, and angiotensin-converting enzyme
    • Machado, M. F., Cunha, F. M., Berti, D. A., Heimann, A. S. et al., Substrate phosphorylation affects degradation and interaction to endopeptidase 24.15, neurolysin, and angiotensin-converting enzyme. Biochem. Biophys. Res. Commun. 2006, 339, 520-525.
    • (2006) Biochem. Biophys. Res. Commun. , vol.339 , pp. 520-525
    • Machado, M.F.1    Cunha, F.M.2    Berti, D.A.3    Heimann, A.S.4
  • 53
    • 33747839468 scopus 로고    scopus 로고
    • ScanProsite: detection of PROSITE signature matches and ProRule-associated functional and structural residues in proteins
    • de Castro, E., Sigrist, C. J., Gattiker, A., Bulliard, V. et al., ScanProsite: detection of PROSITE signature matches and ProRule-associated functional and structural residues in proteins. Nucleic Acids Res. 2006, 34, W362-W365.
    • (2006) Nucleic Acids Res. , vol.34
    • de Castro, E.1    Sigrist, C.J.2    Gattiker, A.3    Bulliard, V.4
  • 54
    • 33748953868 scopus 로고    scopus 로고
    • Peptides mediating interaction networks: new leads at last
    • Neduva, V., Russell, R. B., Peptides mediating interaction networks: new leads at last. Curr. Opin. Biotechnol. 2006, 17, 465-471.
    • (2006) Curr. Opin. Biotechnol. , vol.17 , pp. 465-471
    • Neduva, V.1    Russell, R.B.2
  • 55
    • 49549083915 scopus 로고    scopus 로고
    • Peptide-mediated interactions in biological systems: new discoveries and applications
    • Petsalaki, E., Russell, R. B., Peptide-mediated interactions in biological systems: new discoveries and applications. Curr. Opin. Biotechnol. 2008, 19, 344-350.
    • (2008) Curr. Opin. Biotechnol. , vol.19 , pp. 344-350
    • Petsalaki, E.1    Russell, R.B.2
  • 56
    • 0345516047 scopus 로고    scopus 로고
    • Fast association rates suggest a conformational change in the MHC class I molecule H-2Db upon peptide binding
    • Springer, S., Doring, K., Skipper, J. C., Townsend, A. R. et al., Fast association rates suggest a conformational change in the MHC class I molecule H-2Db upon peptide binding. Biochemistry 1998, 37, 3001-3012.
    • (1998) Biochemistry , vol.37 , pp. 3001-3012
    • Springer, S.1    Doring, K.2    Skipper, J.C.3    Townsend, A.R.4
  • 58
    • 49749117432 scopus 로고    scopus 로고
    • Contextual specificity in peptide-mediated protein interactions
    • Stein, A., Aloy, P., Contextual specificity in peptide-mediated protein interactions. PLoS One 2008, 3, e2524.
    • (2008) PLoS One , vol.3
    • Stein, A.1    Aloy, P.2
  • 59
    • 0026571278 scopus 로고
    • The human class II MHC protein HLA-DR1 assembles as empty alpha beta heterodimers in the absence of antigenic peptide
    • Stern, L. J., Wiley, D. C., The human class II MHC protein HLA-DR1 assembles as empty alpha beta heterodimers in the absence of antigenic peptide. Cell 1992, 68, 465-477.
    • (1992) Cell , vol.68 , pp. 465-477
    • Stern, L.J.1    Wiley, D.C.2
  • 60
  • 61
    • 33644949935 scopus 로고    scopus 로고
    • Recapitulation and design of protein binding peptide structures and sequences
    • Sood, V. D., Baker, D., Recapitulation and design of protein binding peptide structures and sequences. J. Mol. Biol. 2006, 357, 917-927.
    • (2006) J. Mol. Biol. , vol.357 , pp. 917-927
    • Sood, V.D.1    Baker, D.2
  • 62
    • 84865563285 scopus 로고    scopus 로고
    • Identification of intracellular peptides in rat adipose tissue: insights into insulin resistance
    • Proteomics, DOI 10.1002/pmic.201200051.
    • Berti, D. A., Russo, L. C., Castro, L. M., Cruz, L. et al., Identification of intracellular peptides in rat adipose tissue: insights into insulin resistance. Proteomics 2012, DOI 10.1002/pmic.201200051.
    • (2012)
    • Berti, D.A.1    Russo, L.C.2    Castro, L.M.3    Cruz, L.4
  • 63
    • 0035117587 scopus 로고    scopus 로고
    • Association of GABA(B) receptors and members of the 14-3-3 family of signaling proteins
    • Couve, A., Kittler, J. T., Uren, J. M., Calver, A. R. et al., Association of GABA(B) receptors and members of the 14-3-3 family of signaling proteins. Mol. Cell Neurosci. 2001, 17, 317-328.
    • (2001) Mol. Cell Neurosci. , vol.17 , pp. 317-328
    • Couve, A.1    Kittler, J.T.2    Uren, J.M.3    Calver, A.R.4
  • 65
    • 0026726423 scopus 로고
    • Interaction between protein kinase C and Exo1 (14-3-3 protein) and its relevance to exocytosis in permeabilized adrenal chromaffin cells
    • Morgan, A., Burgoyne, R. D., Interaction between protein kinase C and Exo1 (14-3-3 protein) and its relevance to exocytosis in permeabilized adrenal chromaffin cells. Biochem. J. 1992, 286(Pt 3), 807-811.
    • (1992) Biochem. J. , vol.286 , Issue.PART 3 , pp. 807-811
    • Morgan, A.1    Burgoyne, R.D.2
  • 66
    • 0036479325 scopus 로고    scopus 로고
    • 14-3-3 proteins: active cofactors in cellular regulation by serine/threonine phosphorylation
    • Tzivion, G., Avruch, J., 14-3-3 proteins: active cofactors in cellular regulation by serine/threonine phosphorylation. J. Biol. Chem. 2002, 277, 3061-3064.
    • (2002) J. Biol. Chem. , vol.277 , pp. 3061-3064
    • Tzivion, G.1    Avruch, J.2
  • 67
    • 80054034515 scopus 로고    scopus 로고
    • Membrane proteins as 14-3-3 clients in functional regulation and intracellular transport
    • Smith, A. J., Daut, J., Schwappach, B., Membrane proteins as 14-3-3 clients in functional regulation and intracellular transport. Physiology 2011, 26, 181-191.
    • (2011) Physiology , vol.26 , pp. 181-191
    • Smith, A.J.1    Daut, J.2    Schwappach, B.3
  • 68
    • 0036844910 scopus 로고    scopus 로고
    • Exoenzyme S shows selective ADP-ribosylation and GTPase-activating protein (GAP) activities towards small GTPases in vivo
    • Henriksson, M. L., Sundin, C., Jansson, A. L., Forsberg, A. et al., Exoenzyme S shows selective ADP-ribosylation and GTPase-activating protein (GAP) activities towards small GTPases in vivo. Biochem. J. 2002, 367, 617-628.
    • (2002) Biochem. J. , vol.367 , pp. 617-628
    • Henriksson, M.L.1    Sundin, C.2    Jansson, A.L.3    Forsberg, A.4
  • 69
    • 0026748968 scopus 로고
    • Backbone dynamics of calmodulin studied by 15N relaxation using inverse detected two-dimensional NMR spectroscopy: the central helix is flexible
    • Barbato, G., Ikura, M., Kay, L. E., Pastor, R. W. et al., Backbone dynamics of calmodulin studied by 15N relaxation using inverse detected two-dimensional NMR spectroscopy: the central helix is flexible. Biochemistry 1992, 31, 5269-5278.
    • (1992) Biochemistry , vol.31 , pp. 5269-5278
    • Barbato, G.1    Ikura, M.2    Kay, L.E.3    Pastor, R.W.4
  • 70
    • 21344456360 scopus 로고    scopus 로고
    • Calcium modulates endopeptidase 24.15 (EC 3.4.24.15) membrane association, secondary structure and substrate specificity
    • Oliveira, V., Garrido, P. A., Rodrigues, C. C., Colquhoun, A. et al., Calcium modulates endopeptidase 24.15 (EC 3.4.24.15) membrane association, secondary structure and substrate specificity. FEBS J. 2005, 272, 2978-2992.
    • (2005) FEBS J. , vol.272 , pp. 2978-2992
    • Oliveira, V.1    Garrido, P.A.2    Rodrigues, C.C.3    Colquhoun, A.4
  • 74
    • 1542609485 scopus 로고    scopus 로고
    • Transduction peptides: from technology to physiology
    • Joliot, A., Prochiantz, A., Transduction peptides: from technology to physiology. Nat. Cell Biol. 2004, 6, 189-196.
    • (2004) Nat. Cell Biol. , vol.6 , pp. 189-196
    • Joliot, A.1    Prochiantz, A.2


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