메뉴 건너뛰기




Volumn 14, Issue 1, 2015, Pages 177-190

C-terminomics screen for natural substrates of cytosolic carboxypeptidase 1 reveals processing of acidic protein C termini

Author keywords

[No Author keywords available]

Indexed keywords

ASPARTIC ACID; CARBOXYPEPTIDASE; CYTOSOLIC CARBOXYPEPTIDASE 1; HIGH MOBILITY GROUP PROTEIN; MYOSIN LIGHT CHAIN KINASE; POLYGLUTAMIC ACID; RIBOSOME PROTEIN; TELOKIN; TUBULIN; UNCLASSIFIED DRUG; AGTPBP1 PROTEIN, HUMAN;

EID: 84920481806     PISSN: 15359476     EISSN: 15359484     Source Type: Journal    
DOI: 10.1074/mcp.M114.040360     Document Type: Article
Times cited : (27)

References (67)
  • 2
    • 84873439498 scopus 로고    scopus 로고
    • Functional segregation and emerging role of cilia-related cytosolic carboxypeptidases (CCPs)
    • Rodriguez de la Vega, M., Lorenzo, J., Tort, O., Aviles, F. X., and Bautista, J. M. (2012) Functional segregation and emerging role of cilia-related cytosolic carboxypeptidases (CCPs). FASEB J. 27, 424-431
    • (2012) FASEB J. , vol.27 , pp. 424-431
    • Rodriguez De La Vega, M.1    Lorenzo, J.2    Tort, O.3    Aviles, F.X.4    Bautista, J.M.5
  • 4
    • 33847661633 scopus 로고    scopus 로고
    • The purkinje cell degeneration (pcd) mouse: An unexpected molecular link between neuronal degeneration and regeneration
    • Wang, T., and Morgan, J. I. (2007) The Purkinje cell degeneration (pcd) mouse: an unexpected molecular link between neuronal degeneration and regeneration. Brain Res. 1140, 26-40
    • (2007) Brain Res. , vol.1140 , pp. 26-40
    • Wang, T.1    Morgan, J.I.2
  • 5
    • 0034533467 scopus 로고    scopus 로고
    • Regenerating motor neurons express nna1, a novel ATP/GTP-binding protein related to zinc carboxypeptidases
    • Harris, A., Morgan, J. I., Pecot, M., Soumare, A., Osborne, A., and Soares, H. D. (2000) Regenerating motor neurons express Nna1, a novel ATP/GTP-binding protein related to zinc carboxypeptidases. Mol. Cell. Neurosci. 16, 578-596
    • (2000) Mol. Cell. Neurosci. , vol.16 , pp. 578-596
    • Harris, A.1    Morgan, J.I.2    Pecot, M.3    Soumare, A.4    Osborne, A.5    Soares, H.D.6
  • 6
    • 84867725772 scopus 로고    scopus 로고
    • Kinesin-13 and tubulin posttranslational modifications regulate microtubule growth in axon regeneration
    • Ghosh-Roy, A., Goncharov, A., Jin, Y., and Chisholm, A. D. (2012) Kinesin-13 and tubulin posttranslational modifications regulate microtubule growth in axon regeneration. Dev. Cell 23, 716-728
    • (2012) Dev. Cell , vol.23 , pp. 716-728
    • Ghosh-Roy, A.1    Goncharov, A.2    Jin, Y.3    Chisholm, A.D.4
  • 8
    • 2042422363 scopus 로고
    • Purkinje cell degeneration, a new neurological mutation in the mouse
    • Mullen, R. J., Eicher, E. M., and Sidman, R. L. (1976) Purkinje cell degeneration, a new neurological mutation in the mouse. Proc. Natl. Acad. Sci. U.S.A. 73, 208-212
    • (1976) Proc. Natl. Acad. Sci. U.S.A. , vol.73 , pp. 208-212
    • Mullen, R.J.1    Eicher, E.M.2    Sidman, R.L.3
  • 9
    • 0020359828 scopus 로고
    • Retinal degeneration in the pcd cerebellar mutant mouse. II. Electron microscopic analysis
    • Blanks, J. C., Mullen, R. J., and LaVail, M. M. (1982) Retinal degeneration in the pcd cerebellar mutant mouse. II. Electron microscopic analysis. J. Comp. Neurol. 212, 231-246
    • (1982) J. Comp. Neurol. , vol.212 , pp. 231-246
    • Blanks, J.C.1    Mullen, R.J.2    LaVail, M.M.3
  • 10
    • 0020059026 scopus 로고
    • Mitral cell degeneration and sensory function in the neurological mutant mouse purkinje cell degeneration (PCD)
    • Greer, C. A., and Shepherd, G. M. (1982) Mitral cell degeneration and sensory function in the neurological mutant mouse Purkinje cell degeneration (PCD). Brain Res. 235, 156-161
    • (1982) Brain Res. , vol.235 , pp. 156-161
    • Greer, C.A.1    Shepherd, G.M.2
  • 11
    • 0021914258 scopus 로고
    • Degeneration of thalamic neurons in "Purkinje cell degeneration" mutant mice. I. Distribution of neuron loss
    • O'Gorman, S., and Sidman, R. L. (1985) Degeneration of thalamic neurons in "Purkinje cell degeneration" mutant mice. I. Distribution of neuron loss. J. Comp. Neurol. 234, 277-297
    • (1985) J. Comp. Neurol. , vol.234 , pp. 277-297
    • O'Gorman, S.1    Sidman, R.L.2
  • 12
    • 33244496230 scopus 로고    scopus 로고
    • Emergence of endoplasmic reticulum stress and activated microglia in purkinje cell degeneration mice
    • Kyuhou, S., Kato, N., and Gemba, H. (2006) Emergence of endoplasmic reticulum stress and activated microglia in Purkinje cell degeneration mice. Neurosci. Lett. 396, 91-96
    • (2006) Neurosci. Lett. , vol.396 , pp. 91-96
    • Kyuhou, S.1    Kato, N.2    Gemba, H.3
  • 13
    • 69249122087 scopus 로고    scopus 로고
    • Autophagy activation and enhanced mitophagy characterize the purkinje cells of pcd mice prior to neuronal death
    • Chakrabarti, L., Eng, J., Ivanov, N., Garden, G. A., and La Spada, A. R. (2009) Autophagy activation and enhanced mitophagy characterize the Purkinje cells of pcd mice prior to neuronal death. Mol. Brain 2, 24
    • (2009) Mol. Brain , vol.2 , pp. 24
    • Chakrabarti, L.1    Eng, J.2    Ivanov, N.3    Garden, G.A.4    La Spada, A.R.5
  • 16
    • 80051516014 scopus 로고    scopus 로고
    • Purkinje cell degeneration in pcd mice reveals large scale chromatin reorganization and gene silencing linked to defective DNA repair
    • Baltanas, F. C., Casafont, I., Lafarga, V., Weruaga, E., Alonso, J. R., Berciano, M. T., and Lafarga, M. (2011) Purkinje cell degeneration in pcd mice reveals large scale chromatin reorganization and gene silencing linked to defective DNA repair. J. Biol. Chem. 286, 28287-28302
    • (2011) J. Biol. Chem. , vol.286 , pp. 28287-28302
    • Baltanas, F.C.1    Casafont, I.2    Lafarga, V.3    Weruaga, E.4    Alonso, J.R.5    Berciano, M.T.6    Lafarga, M.7
  • 17
    • 79958793069 scopus 로고    scopus 로고
    • Nucleolar disruption and cajal body disassembly are nuclear hallmarks of DNA damage-induced neurodegeneration in purkinje cells
    • Baltanas, F. C., Casafont, I., Weruaga, E., Alonso, J. R., Berciano, M. T., and Lafarga, M. (2011) Nucleolar disruption and cajal body disassembly are nuclear hallmarks of DNA damage-induced neurodegeneration in purkinje cells. Brain Pathol. 21, 374-388
    • (2011) Brain Pathol. , vol.21 , pp. 374-388
    • Baltanas, F.C.1    Casafont, I.2    Weruaga, E.3    Alonso, J.R.4    Berciano, M.T.5    Lafarga, M.6
  • 18
    • 33750619522 scopus 로고    scopus 로고
    • Preneurodegeneration of mitral cells in the pcd mutant mouse is associated with DNA damage, transcriptional repression, and reorganization of nuclear speckles and cajal bodies
    • Valero, J., Berciano, M. T., Weruaga, E., Lafarga, M., and Alonso, J. R. (2006) Preneurodegeneration of mitral cells in the pcd mutant mouse is associated with DNA damage, transcriptional repression, and reorganization of nuclear speckles and Cajal bodies. Mol. Cell. Neurosci. 33, 283-295
    • (2006) Mol. Cell. Neurosci. , vol.33 , pp. 283-295
    • Valero, J.1    Berciano, M.T.2    Weruaga, E.3    Lafarga, M.4    Alonso, J.R.5
  • 21
    • 80054995650 scopus 로고    scopus 로고
    • The tubulin deglutamylase CCPP-1 regulates the function and stability of sensory cilia in C. Elegans
    • O'Hagan, R., Piasecki, B. P., Silva, M., Phirke, P., Nguyen, K. C., Hall, D. H., Swoboda, P., and Barr, M. M. (2011) The tubulin deglutamylase CCPP-1 regulates the function and stability of sensory cilia in C. elegans. Curr. Biol. 21, 1685-1694
    • (2011) Curr. Biol. , vol.21 , pp. 1685-1694
    • O'Hagan, R.1    Piasecki, B.P.2    Silva, M.3    Phirke, P.4    Nguyen, K.C.5    Hall, D.H.6    Swoboda, P.7    Barr, M.M.8
  • 24
    • 34250766201 scopus 로고    scopus 로고
    • The strep-tag system for one-step purification and high-affinity detection or capturing of proteins
    • Schmidt, T. G., and Skerra, A. (2007) The Strep-tag system for one-step purification and high-affinity detection or capturing of proteins. Nat. Protoc. 2, 1528-1535
    • (2007) Nat. Protoc. , vol.2 , pp. 1528-1535
    • Schmidt, T.G.1    Skerra, A.2
  • 25
    • 1842594546 scopus 로고
    • The mechanism of inhibition of carboxypeptidase A by 1,10-phenanthroline
    • Felber, J. P., Coombs, T. L., and Vallee, B. L. (1962) The mechanism of inhibition of carboxypeptidase A by 1,10-phenanthroline. Biochemistry 1, 231-238
    • (1962) Biochemistry , vol.1 , pp. 231-238
    • Felber, J.P.1    Coombs, T.L.2    Vallee, B.L.3
  • 26
    • 84868129951 scopus 로고    scopus 로고
    • Characterization of the proteolytic system present in vasconcellea quercifolia latex
    • Torres, M. J., Trejo, S. A., Obregon, W. D., Aviles, F. X., Lopez, L. M., and Natalucci, C. L. (2012) Characterization of the proteolytic system present in Vasconcellea quercifolia latex. Planta 236, 1471-1484
    • (2012) Planta , vol.236 , pp. 1471-1484
    • Torres, M.J.1    Trejo, S.A.2    Obregon, W.D.3    Aviles, F.X.4    Lopez, L.M.5    Natalucci, C.L.6
  • 28
    • 24144480557 scopus 로고    scopus 로고
    • DBToolkit: Processing protein databases for peptide-centric proteomics
    • Martens, L., Vandekerckhove, J., and Gevaert, K. (2005) DBToolkit: processing protein databases for peptide-centric proteomics. Bioinformatics 21, 3584-3585
    • (2005) Bioinformatics , vol.21 , pp. 3584-3585
    • Martens, L.1    Vandekerckhove, J.2    Gevaert, K.3
  • 29
    • 38649083118 scopus 로고    scopus 로고
    • Assigning significance to peptides identified by tandem mass spectrometry using decoy databases
    • Kall, L., Storey, J. D., MacCoss, M. J., and Noble, W. S. (2008) Assigning significance to peptides identified by tandem mass spectrometry using decoy databases. J. Proteome Res. 7, 29-34
    • (2008) J. Proteome Res. , vol.7 , pp. 29-34
    • Kall, L.1    Storey, J.D.2    MacCoss, M.J.3    Noble, W.S.4
  • 34
    • 0025259313 scopus 로고
    • Methods for assessing the statistical significance of molecular sequence features by using general scoring schemes
    • Karlin, S., and Altschul, S. F. (1990) Methods for assessing the statistical significance of molecular sequence features by using general scoring schemes. Proc. Natl. Acad. Sci. U.S.A. 87, 2264-2268
    • (1990) Proc. Natl. Acad. Sci. U.S.A. , vol.87 , pp. 2264-2268
    • Karlin, S.1    Altschul, S.F.2
  • 37
    • 84868300043 scopus 로고    scopus 로고
    • A structural and functional analysis of nna1 in purkinje cell degeneration (pcd) mice
    • Wu, H. Y., Wang, T., Li, L., Correia, K., and Morgan, J. I. (2012) A structural and functional analysis of Nna1 in Purkinje cell degeneration (pcd) mice. FASEB J. 26, 4468-4480
    • (2012) FASEB J. , vol.26 , pp. 4468-4480
    • Wu, H.Y.1    Wang, T.2    Li, L.3    Correia, K.4    Morgan, J.I.5
  • 38
    • 79951832417 scopus 로고    scopus 로고
    • Tumor suppressor RARRES1 interacts with cytoplasmic carboxypeptidase AGBL2 to regulate the alpha-tubulin tyrosination cycle
    • Sahab, Z. J., Hall, M. D., Me Sung, Y., Dakshanamurthy, S., Ji, Y., Kumar, D., and Byers, S. W. (2011) Tumor suppressor RARRES1 interacts with cytoplasmic carboxypeptidase AGBL2 to regulate the alpha-tubulin tyrosination cycle. Cancer Res. 71, 1219-1228
    • (2011) Cancer Res. , vol.71 , pp. 1219-1228
    • Sahab, Z.J.1    Hall, M.D.2    Me Sung, Y.3    Dakshanamurthy, S.4    Ji, Y.5    Kumar, D.6    Byers, S.W.7
  • 39
    • 0037144838 scopus 로고    scopus 로고
    • Tetrahymena thermophila contains a conventional gamma-tubulin that is differentially required for the maintenance of different microtubule-organizing centers
    • Shang, Y., Li, B., and Gorovsky, M. A. (2002) Tetrahymena thermophila contains a conventional gamma-tubulin that is differentially required for the maintenance of different microtubule-organizing centers. J. Cell Biol. 158, 1195-1206
    • (2002) J. Cell Biol. , vol.158 , pp. 1195-1206
    • Shang, Y.1    Li, B.2    Gorovsky, M.A.3
  • 40
    • 33947590948 scopus 로고    scopus 로고
    • Metallocar-boxypeptidases: Emerging drug targets in biomedicine
    • Arolas, J. L., Vendrell, J., Aviles, F. X., and Fricker, L. D. (2007) Metallocar-boxypeptidases: emerging drug targets in biomedicine. Curr. Pharm. Des. 13, 349-366
    • (2007) Curr. Pharm. Des. , vol.13 , pp. 349-366
    • Arolas, J.L.1    Vendrell, J.2    Aviles, F.X.3    Fricker, L.D.4
  • 41
    • 84874638077 scopus 로고    scopus 로고
    • Identification of CRM1-dependent nuclear export cargos using quantitative mass spectrometry
    • Thakar, K., Karaca, S., Port, S. A., Urlaub, H., and Kehlenbach, R. H. (2013) Identification of CRM1-dependent nuclear export cargos using quantitative mass spectrometry. Mol. Cell. Proteomics 12, 664-678
    • (2013) Mol. Cell. Proteomics , vol.12 , pp. 664-678
    • Thakar, K.1    Karaca, S.2    Port, S.A.3    Urlaub, H.4    Kehlenbach, R.H.5
  • 42
    • 0024469223 scopus 로고
    • Tissue specificity of nucleo-cytoplasmic distribution of HMG1 and HMG2 proteins and their probable functions
    • Mosevitsky, M. I., Novitskaya, V. A., Iogannsen, M. G., and Zabezhinsky, M. A. (1989) Tissue specificity of nucleo-cytoplasmic distribution of HMG1 and HMG2 proteins and their probable functions. Eur. J. Biochem. 185, 303-310
    • (1989) Eur. J. Biochem. , vol.185 , pp. 303-310
    • Mosevitsky, M.I.1    Novitskaya, V.A.2    Iogannsen, M.G.3    Zabezhinsky, M.A.4
  • 43
    • 0021285494 scopus 로고
    • Concentrations of high-mobility-group proteins in the nucleus and cytoplasm of several rat tissues
    • Kuehl, L., Salmond, B., and Tran, L. (1984) Concentrations of high-mobility-group proteins in the nucleus and cytoplasm of several rat tissues. J. Cell Biol. 99, 648-654
    • (1984) J. Cell Biol. , vol.99 , pp. 648-654
    • Kuehl, L.1    Salmond, B.2    Tran, L.3
  • 44
    • 74549226503 scopus 로고    scopus 로고
    • HMGB proteins: Interactions with DNA and chromatin
    • Stros, M. (2010) HMGB proteins: interactions with DNA and chromatin. Biochim. Biophys. Acta 1799, 101-113
    • (2010) Biochim. Biophys. Acta , vol.1799 , pp. 101-113
    • Stros, M.1
  • 45
    • 0018381702 scopus 로고
    • Antibodies against chromosomal HMG proteins stain the cytoplasm of mammalian cells
    • Bustin, M., and Neihart, N. K. (1979) Antibodies against chromosomal HMG proteins stain the cytoplasm of mammalian cells. Cell 16, 181-189
    • (1979) Cell , vol.16 , pp. 181-189
    • Bustin, M.1    Neihart, N.K.2
  • 46
    • 0034711421 scopus 로고    scopus 로고
    • The effect of the acidic tail on the DNA-binding properties of the HMG1,2 class of proteins: Insights from tail switching and tail removal
    • Lee, K. B., and Thomas, J. O. (2000) The effect of the acidic tail on the DNA-binding properties of the HMG1,2 class of proteins: insights from tail switching and tail removal. J. Mol. Biol. 304, 135-149
    • (2000) J. Mol. Biol. , vol.304 , pp. 135-149
    • Lee, K.B.1    Thomas, J.O.2
  • 47
    • 77954693076 scopus 로고    scopus 로고
    • Proteome-wide analysis of protein carboxy termini: C terminomics
    • Schilling, O., Barre, O., Huesgen, P. F., and Overall, C. M. (2010) Proteome-wide analysis of protein carboxy termini: C terminomics. Nat. Methods 7, 508-511
    • (2010) Nat. Methods , vol.7 , pp. 508-511
    • Schilling, O.1    Barre, O.2    Huesgen, P.F.3    Overall, C.M.4
  • 48
    • 80054992471 scopus 로고    scopus 로고
    • Chemoenzymatic labeling of protein C-termini for positive selection of C-terminal peptides
    • Xu, G., Shin, S. B., and Jaffrey, S. R. (2011) Chemoenzymatic labeling of protein C-termini for positive selection of C-terminal peptides. ACS Chem. Biol. 6, 1015-1020
    • (2011) ACS Chem. Biol. , vol.6 , pp. 1015-1020
    • Xu, G.1    Shin, S.B.2    Jaffrey, S.R.3
  • 49
    • 84888388524 scopus 로고    scopus 로고
    • Approach for identification and quantification of C-terminal peptides: Incorporation of isotopic arginine labeling based on oxazolone chemistry
    • Liu, M., Zhang, L., Yao, J., Yang, P., and Lu, H. (2013) Approach for identification and quantification of C-terminal peptides: incorporation of isotopic arginine labeling based on oxazolone chemistry. Anal. Chem. 85, 10745-10753
    • (2013) Anal. Chem. , vol.85 , pp. 10745-10753
    • Liu, M.1    Zhang, L.2    Yao, J.3    Yang, P.4    Lu, H.5
  • 50
    • 62549101653 scopus 로고    scopus 로고
    • The specific isolation of C-terminal peptides of proteins through a transamination reaction and its advantage for introducing functional groups into the peptide
    • Sonomura, K., Kuyama, H., Matsuo, E., Tsunasawa, S., and Nishimura, O. (2009) The specific isolation of C-terminal peptides of proteins through a transamination reaction and its advantage for introducing functional groups into the peptide. Rapid Commun. Mass Spectrom. 23, 611-618
    • (2009) Rapid Commun. Mass Spectrom. , vol.23 , pp. 611-618
    • Sonomura, K.1    Kuyama, H.2    Matsuo, E.3    Tsunasawa, S.4    Nishimura, O.5
  • 51
    • 0028283568 scopus 로고
    • Accumulation of delta 2-tubulin, a major tubulin variant that cannot be tyrosinated, in neuronal tissues and in stable microtubule assemblies
    • Paturle-Lafanechere, L., Manier, M., Trigault, N., Pirollet, F., Mazarguil, H., and Job, D. (1994) Accumulation of delta 2-tubulin, a major tubulin variant that cannot be tyrosinated, in neuronal tissues and in stable microtubule assemblies. J. Cell Sci. 107, 1529-1543
    • (1994) J. Cell Sci. , vol.107 , pp. 1529-1543
    • Paturle-Lafanechere, L.1    Manier, M.2    Trigault, N.3    Pirollet, F.4    Mazarguil, H.5    Job, D.6
  • 52
    • 81855196008 scopus 로고    scopus 로고
    • Post-translational regulation of the microtubule cytoskeleton: Mechanisms and functions
    • Janke, C., and Bulinski, J. C. (2011) Post-translational regulation of the microtubule cytoskeleton: mechanisms and functions. Nat. Rev. Mol. Cell Biol. 12, 773-786
    • (2011) Nat. Rev. Mol. Cell Biol. , vol.12 , pp. 773-786
    • Janke, C.1    Bulinski, J.C.2
  • 53
    • 84863264583 scopus 로고    scopus 로고
    • Analysis of tubulin alpha-1A/1B C-terminal tail post-translational poly-glutamylation reveals novel modification sites
    • Sahab, Z. J., Kirilyuk, A., Zhang, L., Khamis, Z. I., Pompach, P., Sung, Y., and Byers, S. W. (2012) Analysis of tubulin alpha-1A/1B C-terminal tail post-translational poly-glutamylation reveals novel modification sites. J. Proteome Res. 11, 1913-1923
    • (2012) J. Proteome Res. , vol.11 , pp. 1913-1923
    • Sahab, Z.J.1    Kirilyuk, A.2    Zhang, L.3    Khamis, Z.I.4    Pompach, P.5    Sung, Y.6    Byers, S.W.7
  • 54
    • 0032571398 scopus 로고    scopus 로고
    • Purification and characterization of a new eukaryotic protein translation factor. Eukaryotic initiation factor 4H
    • Richter-Cook, N. J., Dever, T. E., Hensold, J. O., and Merrick, W. C. (1998) Purification and characterization of a new eukaryotic protein translation factor. Eukaryotic initiation factor 4H. J. Biol. Chem. 273, 7579-7587
    • (1998) J. Biol. Chem. , vol.273 , pp. 7579-7587
    • Richter-Cook, N.J.1    Dever, T.E.2    Hensold, J.O.3    Merrick, W.C.4
  • 55
    • 0030809755 scopus 로고    scopus 로고
    • Characterization of the chicken telokin heterogeneity by time-offlight mass spectrometry
    • Rusconi, F., Potier, M. C., Le Caer, J. P., Schmitter, J. M., and Rossier, J. (1997) Characterization of the chicken telokin heterogeneity by time-offlight mass spectrometry. Biochemistry 36, 11021-11026
    • (1997) Biochemistry , vol.36 , pp. 11021-11026
    • Rusconi, F.1    Potier, M.C.2    Le Caer, J.P.3    Schmitter, J.M.4    Rossier, J.5
  • 56
    • 67649218816 scopus 로고    scopus 로고
    • HMGB1: The jack-of-all-trades protein is a master DNA repair mechanic
    • Lange, S. S., and Vasquez, K. M. (2009) HMGB1: the jack-of-all-trades protein is a master DNA repair mechanic. Mol. Carcinog. 48, 571-580
    • (2009) Mol. Carcinog. , vol.48 , pp. 571-580
    • Lange, S.S.1    Vasquez, K.M.2
  • 57
    • 0037295617 scopus 로고    scopus 로고
    • Priming the nucleosome: A role for HMGB proteins?
    • Travers, A. A. (2003) Priming the nucleosome: a role for HMGB proteins? EMBO Rep. 4, 131-136
    • (2003) EMBO Rep. , vol.4 , pp. 131-136
    • Travers, A.A.1
  • 58
    • 0027156630 scopus 로고
    • The specific interactions of HMG 1 and 2 with negatively supercoiled DNA are modulated by their acidic C-terminal domains and involve cysteine residues in their HMG 1/2 boxes
    • Sheflin, L. G., Fucile, N. W., and Spaulding, S. W. (1993) The specific interactions of HMG 1 and 2 with negatively supercoiled DNA are modulated by their acidic C-terminal domains and involve cysteine residues in their HMG 1/2 boxes. Biochemistry 32, 3238-3248
    • (1993) Biochemistry , vol.32 , pp. 3238-3248
    • Sheflin, L.G.1    Fucile, N.W.2    Spaulding, S.W.3
  • 59
    • 34547105307 scopus 로고    scopus 로고
    • Activation of poly(ADP)-ribose polymerase (PARP-1) induces release of the pro-inflammatory mediator HMGB1 from the nucleus
    • Ditsworth, D., Zong, W. X., and Thompson, C. B. (2007) Activation of poly(ADP)-ribose polymerase (PARP-1) induces release of the pro-inflammatory mediator HMGB1 from the nucleus. J. Biol. Chem. 282, 17845-17854
    • (2007) J. Biol. Chem. , vol.282 , pp. 17845-17854
    • Ditsworth, D.1    Zong, W.X.2    Thompson, C.B.3
  • 60
    • 0030922526 scopus 로고    scopus 로고
    • Nuclear accumulation of HMG2 protein is mediated by basic regions interspaced with a long DNA-binding sequence, and retention within the nucleus requires the acidic carboxyl terminus
    • Shirakawa, H., Tanigawa, T., Sugiyama, S., Kobayashi, M., Terashima, T., Yoshida, K., Arai, T., and Yoshida, M. (1997) Nuclear accumulation of HMG2 protein is mediated by basic regions interspaced with a long DNA-binding sequence, and retention within the nucleus requires the acidic carboxyl terminus. Biochemistry 36, 5992-5999
    • (1997) Biochemistry , vol.36 , pp. 5992-5999
    • Shirakawa, H.1    Tanigawa, T.2    Sugiyama, S.3    Kobayashi, M.4    Terashima, T.5    Yoshida, K.6    Arai, T.7    Yoshida, M.8
  • 61
    • 3342939967 scopus 로고    scopus 로고
    • Acidic C-tail of HMGB1 is required for its target binding to nucleosome linker DNA and transcription stimulation
    • Ueda, T., Chou, H., Kawase, T., Shirakawa, H., and Yoshida, M. (2004) Acidic C-tail of HMGB1 is required for its target binding to nucleosome linker DNA and transcription stimulation. Biochemistry 43, 9901-9908
    • (2004) Biochemistry , vol.43 , pp. 9901-9908
    • Ueda, T.1    Chou, H.2    Kawase, T.3    Shirakawa, H.4    Yoshida, M.5
  • 62
    • 0028580511 scopus 로고
    • Stimulation of transcription in cultured cells by high mobility group protein 1: Essential role of the acidic carboxyl-terminal region
    • Aizawa, S., Nishino, H., Saito, K., Kimura, K., Shirakawa, H., and Yoshida, M. (1994) Stimulation of transcription in cultured cells by high mobility group protein 1: essential role of the acidic carboxyl-terminal region. Biochemistry 33, 14690-14695
    • (1994) Biochemistry , vol.33 , pp. 14690-14695
    • Aizawa, S.1    Nishino, H.2    Saito, K.3    Kimura, K.4    Shirakawa, H.5    Yoshida, M.6
  • 63
    • 56949091228 scopus 로고    scopus 로고
    • The interaction of HMGB1 and linker histones occurs through their acidic and basic tails
    • Cato, L., Stott, K., Watson, M., and Thomas, J. O. (2008) The interaction of HMGB1 and linker histones occurs through their acidic and basic tails. J. Mol. Biol. 384, 1262-1272
    • (2008) J. Mol. Biol. , vol.384 , pp. 1262-1272
    • Cato, L.1    Stott, K.2    Watson, M.3    Thomas, J.O.4
  • 64
    • 4243824006 scopus 로고    scopus 로고
    • The DNA chaperone HMGB1 facilitates ACF/CHRAC-dependent nucleosome sliding
    • Bonaldi, T., Langst, G., Strohner, R., Becker, P. B., and Bianchi, M. E. (2002) The DNA chaperone HMGB1 facilitates ACF/CHRAC-dependent nucleosome sliding. EMBO J. 21, 6865-6873
    • (2002) EMBO J. , vol.21 , pp. 6865-6873
    • Bonaldi, T.1    Langst, G.2    Strohner, R.3    Becker, P.B.4    Bianchi, M.E.5
  • 65
    • 17144399922 scopus 로고    scopus 로고
    • The inhibitory effect of HMGB-1 protein on the repair of cisplatin-damaged DNA is accomplished through the acidic domain
    • Mitkova, E., Ugrinova, I., Pashev, I. G., and Pasheva, E. A. (2005) The inhibitory effect of HMGB-1 protein on the repair of cisplatin-damaged DNA is accomplished through the acidic domain. Biochemistry 44, 5893-5898
    • (2005) Biochemistry , vol.44 , pp. 5893-5898
    • Mitkova, E.1    Ugrinova, I.2    Pashev, I.G.3    Pasheva, E.A.4
  • 66
    • 43049124103 scopus 로고    scopus 로고
    • HMGB1 protein inhibits DNA replication in vitro: A role of the acetylation and the acidic tail
    • Topalova, D., Ugrinova, I., Pashev, I. G., and Pasheva, E. A. (2008) HMGB1 protein inhibits DNA replication in vitro: a role of the acetylation and the acidic tail. Int. J. Biochem. Cell Biol. 40, 1536-1542
    • (2008) Int. J. Biochem. Cell Biol. , vol.40 , pp. 1536-1542
    • Topalova, D.1    Ugrinova, I.2    Pashev, I.G.3    Pasheva, E.A.4
  • 67
    • 41149174663 scopus 로고    scopus 로고
    • Acidic C-terminal tail of the ssDNA-binding protein of bacteriophage T7 and ssDNA compete for the same binding surface
    • Marintcheva, B., Marintchev, A., Wagner, G., and Richardson, C. C. (2008) Acidic C-terminal tail of the ssDNA-binding protein of bacteriophage T7 and ssDNA compete for the same binding surface. Proc. Natl. Acad. Sci. U.S.A. 105, 1855-1860
    • (2008) Proc. Natl. Acad. Sci. U.S.A. , vol.105 , pp. 1855-1860
    • Marintcheva, B.1    Marintchev, A.2    Wagner, G.3    Richardson, C.C.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.