메뉴 건너뛰기




Volumn 11, Issue 3, 2012, Pages 1913-1923

Analysis of tubulin alpha-1A/1B C-terminal tail post-translational poly-glutamylation reveals novel modification sites

Author keywords

AGBL2; detyrosination; glutamylation; microtubule targetting drugs (MTTDs); nano LC; proteinase K; tandem hybrid mass spectrometry; tubulin C terminal tail; tubulin methylation; tubulin alpha

Indexed keywords

ALPHA 1A TUBULIN; ALPHA 1B TUBULIN; GLUTAMIC ACID; PROTEINASE K; TRYPSIN; TUBULIN; UNCLASSIFIED DRUG;

EID: 84863264583     PISSN: 15353893     EISSN: 15353907     Source Type: Journal    
DOI: 10.1021/pr2011044     Document Type: Conference Paper
Times cited : (13)

References (62)
  • 1
    • 77951737783 scopus 로고    scopus 로고
    • Mitochondrial fusion is required for mtDNA stability in skeletal muscle and tolerance of mtDNA mutations
    • Chen, H. C.; Vermulst, M.; Wang, Y. E.; Chomyn, A.; Prolla, T. A.; McCaffery, J. M.; Chan, D. C. Mitochondrial fusion is required for mtDNA stability in skeletal muscle and tolerance of mtDNA mutations Cell 2010, 141 (2) 280-289
    • (2010) Cell , vol.141 , Issue.2 , pp. 280-289
    • Chen, H.C.1    Vermulst, M.2    Wang, Y.E.3    Chomyn, A.4    Prolla, T.A.5    McCaffery, J.M.6    Chan, D.C.7
  • 2
    • 77953526521 scopus 로고    scopus 로고
    • OPA1 disease alleles causing dominant optic atrophy have defects in cardiolipin-stimulated GTP hydrolysis and membrane tubulation
    • Ban, T.; Heymann, J. A. W.; Song, Z. Y.; Hinshaw, J. E.; Chan, D. C. OPA1 disease alleles causing dominant optic atrophy have defects in cardiolipin-stimulated GTP hydrolysis and membrane tubulation Hum. Mol. Genet. 2010, 19 (11) 2113-2122
    • (2010) Hum. Mol. Genet. , vol.19 , Issue.11 , pp. 2113-2122
    • Ban, T.1    Heymann, J.A.W.2    Song, Z.Y.3    Hinshaw, J.E.4    Chan, D.C.5
  • 4
    • 78651103909 scopus 로고    scopus 로고
    • Lamin A variants that cause striated muscle disease are defective in anchoring transmembrane actin-associated nuclear lines for nuclear movement
    • Folker, E. S.; Ostlund, C.; Luxton, G. W. G.; Worman, H. J.; Gundersen, G. G. Lamin A variants that cause striated muscle disease are defective in anchoring transmembrane actin-associated nuclear lines for nuclear movement Proc. Natl. Acad. Sci. U. S. A. 2011, 108 (1) 131-136
    • (2011) Proc. Natl. Acad. Sci. U. S. A. , vol.108 , Issue.1 , pp. 131-136
    • Folker, E.S.1    Ostlund, C.2    Luxton, G.W.G.3    Worman, H.J.4    Gundersen, G.G.5
  • 5
    • 77955260357 scopus 로고    scopus 로고
    • The Yeast GRASP Grh1 colocalizes with COPII and is dispensable for organizing the secretory pathway
    • Levi, S. K.; Bhattacharyya, D.; Strack, R. L.; Austin, J. R.; Glick, B. S. The Yeast GRASP Grh1 colocalizes with COPII and is dispensable for organizing the secretory pathway Traffic 2010, 11 (9) 1168-1179
    • (2010) Traffic , vol.11 , Issue.9 , pp. 1168-1179
    • Levi, S.K.1    Bhattacharyya, D.2    Strack, R.L.3    Austin, J.R.4    Glick, B.S.5
  • 6
    • 77949489741 scopus 로고    scopus 로고
    • Kinesin-13s in mitosis: Key players in the spatial and temporal organization of spindle microtubules
    • Ems-McClung, S. C.; Walczak, C. E. Kinesin-13s in mitosis: Key players in the spatial and temporal organization of spindle microtubules Semin. Cell Dev. Biol. 2010, 21 (3) 276-282
    • (2010) Semin. Cell Dev. Biol. , vol.21 , Issue.3 , pp. 276-282
    • Ems-Mcclung, S.C.1    Walczak, C.E.2
  • 7
    • 77955927839 scopus 로고    scopus 로고
    • Nonmuscle myosin II is required for cell proliferation, cell sheet adhesion and wing hair morphology during wing morphogenesis
    • Franke, J. D.; Montague, R. A.; Kiehart, D. P. Nonmuscle myosin II is required for cell proliferation, cell sheet adhesion and wing hair morphology during wing morphogenesis Dev. Biol. 2010, 345 (2) 117-132
    • (2010) Dev. Biol. , vol.345 , Issue.2 , pp. 117-132
    • Franke, J.D.1    Montague, R.A.2    Kiehart, D.P.3
  • 8
    • 73649112814 scopus 로고    scopus 로고
    • Plasticity of telomere maintenance mechanisms in yeast
    • Lue, N. F. Plasticity of telomere maintenance mechanisms in yeast Trends Biochem. Sci. 2010, 35 (1) 8-17
    • (2010) Trends Biochem. Sci. , vol.35 , Issue.1 , pp. 8-17
    • Lue, N.F.1
  • 9
    • 78649685697 scopus 로고    scopus 로고
    • Defects in nuclear pore assembly lead to activation of an Aurora B-mediated abscission checkpoint
    • Mackay, D. R.; Makise, M.; Ullman, K. S. Defects in nuclear pore assembly lead to activation of an Aurora B-mediated abscission checkpoint J. Cell Biol. 2010, 191 (5) 923-931
    • (2010) J. Cell Biol. , vol.191 , Issue.5 , pp. 923-931
    • MacKay, D.R.1    Makise, M.2    Ullman, K.S.3
  • 10
  • 11
    • 79151475790 scopus 로고    scopus 로고
    • A nonmotor microtubule binding site in kinesin-5 is required for filament crosslinking and sliding
    • Weinger, J. S.; Qiu, M. H.; Yang, G.; Kapoor, T. M. A nonmotor microtubule binding site in kinesin-5 is required for filament crosslinking and sliding Curr. Biol. 2011, 21 (2) 154-160
    • (2011) Curr. Biol. , vol.21 , Issue.2 , pp. 154-160
    • Weinger, J.S.1    Qiu, M.H.2    Yang, G.3    Kapoor, T.M.4
  • 12
    • 79960816795 scopus 로고    scopus 로고
    • Putative biomarkers and targets of estrogen receptor negative human breast cancer
    • Sahab, Z. J.; Man, Y. G.; Byers, S. W.; Sang, Q. X. A. Putative biomarkers and targets of estrogen receptor negative human breast cancer Int. J. Mol. Sci. 2011, 12 (7) 4504-4521
    • (2011) Int. J. Mol. Sci. , vol.12 , Issue.7 , pp. 4504-4521
    • Sahab, Z.J.1    Man, Y.G.2    Byers, S.W.3    Sang, Q.X.A.4
  • 13
    • 0345169048 scopus 로고    scopus 로고
    • Post-translational modifications regulate microtubule function
    • Westermann, S.; Weber, K. Post-translational modifications regulate microtubule function Nat. Rev. Mol. Cell Biol. 2003, 4 (12) 938-947
    • (2003) Nat. Rev. Mol. Cell Biol. , vol.4 , Issue.12 , pp. 938-947
    • Westermann, S.1    Weber, K.2
  • 14
    • 75749117934 scopus 로고    scopus 로고
    • Mechanisms of force generation by end-on kinetochore-microtubule attachments
    • Joglekar, A. P.; Bloom, K. S.; Salmon, E. D. Mechanisms of force generation by end-on kinetochore-microtubule attachments Curr. Opin. Cell Biol. 2010, 22 (1) 57-67
    • (2010) Curr. Opin. Cell Biol. , vol.22 , Issue.1 , pp. 57-67
    • Joglekar, A.P.1    Bloom, K.S.2    Salmon, E.D.3
  • 15
    • 65249099634 scopus 로고    scopus 로고
    • PTC1 is required for vacuole inheritance and promotes the association of the myosin-V vacuole-specific receptor complex
    • Jin, Y.; Eves, P. T.; Tang, F.; Weisman, L. S. PTC1 is required for vacuole inheritance and promotes the association of the myosin-V vacuole-specific receptor complex Mol. Biol. Cell 2009, 20 (5) 1312-1323
    • (2009) Mol. Biol. Cell , vol.20 , Issue.5 , pp. 1312-1323
    • Jin, Y.1    Eves, P.T.2    Tang, F.3    Weisman, L.S.4
  • 16
    • 77649158939 scopus 로고    scopus 로고
    • Efficient spatiotemporal analysis of the flagellar waveform of Chlamydomonas reinhardtii
    • Bayly, P. V.; Lewis, B. L.; Kemp, P. S.; Pless, R. B.; Dutcher, S. K. Efficient spatiotemporal analysis of the flagellar waveform of Chlamydomonas reinhardtii Cytoskeleton 2010, 67 (1) 56-69
    • (2010) Cytoskeleton , vol.67 , Issue.1 , pp. 56-69
    • Bayly, P.V.1    Lewis, B.L.2    Kemp, P.S.3    Pless, R.B.4    Dutcher, S.K.5
  • 17
    • 77952920346 scopus 로고    scopus 로고
    • A ras signaling complex controls the RasC-TORC2 pathway and directed cell migration
    • Charest, P. G.; Shen, Z. X.; Lakoduk, A.; Sasaki, A. T.; Briggs, S. P.; Firtel, R. A. A ras signaling complex controls the RasC-TORC2 pathway and directed cell migration Dev. Cell 2010, 18 (5) 737-749
    • (2010) Dev. Cell , vol.18 , Issue.5 , pp. 737-749
    • Charest, P.G.1    Shen, Z.X.2    Lakoduk, A.3    Sasaki, A.T.4    Briggs, S.P.5    Firtel, R.A.6
  • 18
    • 79951554623 scopus 로고    scopus 로고
    • Mechanisms of aneuploidy
    • Compton, D. A. Mechanisms of aneuploidy Curr. Opin. Cell Biol. 2011, 23 (1) 109-113
    • (2011) Curr. Opin. Cell Biol. , vol.23 , Issue.1 , pp. 109-113
    • Compton, D.A.1
  • 19
    • 77958507493 scopus 로고    scopus 로고
    • Quantitative analysis of actin turnover in listeria comet tails: Evidence for catastrophic filament turnover
    • Kueh, H. Y.; Brieher, W. M.; Mitchison, T. J. Quantitative analysis of actin turnover in listeria comet tails: Evidence for catastrophic filament turnover Biophys. J. 2010, 99 (7) 2153-2162
    • (2010) Biophys. J. , vol.99 , Issue.7 , pp. 2153-2162
    • Kueh, H.Y.1    Brieher, W.M.2    Mitchison, T.J.3
  • 21
    • 78649566070 scopus 로고    scopus 로고
    • Assembly of Filopodia by the formin FRL2 (FMNL3)
    • Harris, E. S.; Gauvin, T. J.; Heimsath, E. G.; Higgs, H. N. Assembly of Filopodia by the formin FRL2 (FMNL3) Cytoskeleton 2010, 67 (12) 755-772
    • (2010) Cytoskeleton , vol.67 , Issue.12 , pp. 755-772
    • Harris, E.S.1    Gauvin, T.J.2    Heimsath, E.G.3    Higgs, H.N.4
  • 24
    • 82255195374 scopus 로고    scopus 로고
    • Tazarotene-induced gene 1 inhibits prostaglandin E2-stimulated HCT116 colon cancer cell growth
    • 10.1186/1423-0127-18-88
    • Tsai, F.-M.; Wu, C.-C.; Shyu, R.-Y.; Wang, C.-H.; Jiang, S.-Y. Tazarotene-induced gene 1 inhibits prostaglandin E2-stimulated HCT116 colon cancer cell growth. J. Biomed. Sci. 2011, 18 (88), 10.1186/1423-0127-18-88.
    • (2011) J. Biomed. Sci. , vol.18 , Issue.88
    • Tsai, F.-M.1    Wu, C.-C.2    Shyu, R.-Y.3    Wang, C.-H.4    Jiang, S.-Y.5
  • 25
    • 77957868249 scopus 로고    scopus 로고
    • Post-translational modifications of microtubules
    • Wloga, D.; Gaertig, J. Post-translational modifications of microtubules J. Cell Sci. 2010, 123 (20) 3447-3455
    • (2010) J. Cell Sci. , vol.123 , Issue.20 , pp. 3447-3455
    • Wloga, D.1    Gaertig, J.2
  • 27
    • 79951832417 scopus 로고    scopus 로고
    • Tumor suppressor RARRES1 interacts with cytoplasmic carboxypeptidase AGBL2 to regulate the a-tubulin tyrosination cycle
    • Sahab, Z. J.; Hall, M. D.; Sung, Y. M.; Dakshanamurthy, S.; Ji, Y.; Kumar, D.; Byers, S. W. Tumor suppressor RARRES1 interacts with cytoplasmic carboxypeptidase AGBL2 to regulate the a-tubulin tyrosination cycle Cancer Res. 2011, 71 (4) 1219-1228
    • (2011) Cancer Res. , vol.71 , Issue.4 , pp. 1219-1228
    • Sahab, Z.J.1    Hall, M.D.2    Sung, Y.M.3    Dakshanamurthy, S.4    Ji, Y.5    Kumar, D.6    Byers, S.W.7
  • 28
    • 0021154489 scopus 로고
    • Tyrosine incorporation in tubulin
    • Flavin, M.; Murofushi, H. Tyrosine incorporation in tubulin Methods Enzymol. 1984, 106, 223-237
    • (1984) Methods Enzymol. , vol.106 , pp. 223-237
    • Flavin, M.1    Murofushi, H.2
  • 29
    • 0028283568 scopus 로고
    • Accumulation of delta-2-Tubulin, a major tubulin variant that cannot be tyrosinated, in neuronal tissues and in stable microtubule assemblies
    • Paturlelafanechere, L.; Manier, M.; Trigault, N.; Pirollet, F.; Mazarguil, H.; Job, D. Accumulation of delta-2-Tubulin, a major tubulin variant that cannot be tyrosinated, in neuronal tissues and in stable microtubule assemblies J. Cell Sci. 1994, 107, 1529-1543
    • (1994) J. Cell Sci. , vol.107 , pp. 1529-1543
    • Paturlelafanechere, L.1    Manier, M.2    Trigault, N.3    Pirollet, F.4    Mazarguil, H.5    Job, D.6
  • 31
    • 0032553017 scopus 로고    scopus 로고
    • Posttranslational modifications of the C-terminus of alpha-tubulin in adult rat brain: Alpha 4 is glutamylated at two residues
    • Redeker, V.; Rossier, J.; Frankfurter, A. Posttranslational modifications of the C-terminus of alpha-tubulin in adult rat brain: Alpha 4 is glutamylated at two residues Biochemistry 1998, 37 (42) 14838-14844
    • (1998) Biochemistry , vol.37 , Issue.42 , pp. 14838-14844
    • Redeker, V.1    Rossier, J.2    Frankfurter, A.3
  • 32
    • 0038219598 scopus 로고    scopus 로고
    • Analysis of tubulin isotypes and mutations from taxol-resistant cells by combined isoelectrofocusing and mass spectrometry
    • Verdier-Pinard, P.; Wang, F.; Martello, L.; Burd, B.; Orr, G. A.; Horwitz, S. B. Analysis of tubulin isotypes and mutations from taxol-resistant cells by combined isoelectrofocusing and mass spectrometry Biochemistry 2003, 42 (18) 5349-5357
    • (2003) Biochemistry , vol.42 , Issue.18 , pp. 5349-5357
    • Verdier-Pinard, P.1    Wang, F.2    Martello, L.3    Burd, B.4    Orr, G.A.5    Horwitz, S.B.6
  • 33
    • 4644267074 scopus 로고    scopus 로고
    • Posttranslational modification of brain tubulins from the antarctic fish Notothenia coriiceps: Reduced C-terminal glutamylation correlates with efficient microtubule assembly at low temperatures
    • Redeker, V.; Frankfurter, A.; Parker, S. K.; Rossier, J.; Detrich, H. W. Posttranslational modification of brain tubulins from the antarctic fish Notothenia coriiceps: Reduced C-terminal glutamylation correlates with efficient microtubule assembly at low temperatures Biochemistry 2004, 43 (38) 12265-12274
    • (2004) Biochemistry , vol.43 , Issue.38 , pp. 12265-12274
    • Redeker, V.1    Frankfurter, A.2    Parker, S.K.3    Rossier, J.4    Detrich, H.W.5
  • 35
    • 0026338717 scopus 로고
    • Structure of the polyglutamyl side-chain posttranslationally added to alpha-tubulin
    • Redeker, V.; Lecaer, J. P.; Rossier, J.; Prome, J. C. Structure of the polyglutamyl side-chain posttranslationally added to alpha-tubulin J. Biol. Chem. 1991, 266 (34) 23461-23466
    • (1991) J. Biol. Chem. , vol.266 , Issue.34 , pp. 23461-23466
    • Redeker, V.1    Lecaer, J.P.2    Rossier, J.3    Prome, J.C.4
  • 36
    • 0028817534 scopus 로고
    • Characterization of posttranslational modifications of brain tubulin by matrix-assisted laser desorption/ionization mass-spectrometry - Direct one-step analysis of a limited subtilisin digest
    • Rudiger, A.; Rudiger, M.; Weber, K.; Schomburg, D. Characterization of posttranslational modifications of brain tubulin by matrix-assisted laser desorption/ionization mass-spectrometry - direct one-step analysis of a limited subtilisin digest Anal. Biochem. 1995, 224 (2) 532-537
    • (1995) Anal. Biochem. , vol.224 , Issue.2 , pp. 532-537
    • Rudiger, A.1    Rudiger, M.2    Weber, K.3    Schomburg, D.4
  • 37
    • 0038385497 scopus 로고    scopus 로고
    • Affinity mass spectrometry-based approaches for the analysis of protein-protein interaction and complex mixtures of peptide-ligands
    • Rudiger, A. H.; Rudiger, M.; Carl, U. D.; Chakraborty, T.; Roepstorff, P.; Wehland, J. Affinity mass spectrometry-based approaches for the analysis of protein-protein interaction and complex mixtures of peptide-ligands Anal. Biochem. 1999, 275 (2) 162-170
    • (1999) Anal. Biochem. , vol.275 , Issue.2 , pp. 162-170
    • Rudiger, A.H.1    Rudiger, M.2    Carl, U.D.3    Chakraborty, T.4    Roepstorff, P.5    Wehland, J.6
  • 39
    • 84857170028 scopus 로고    scopus 로고
    • Non-receptor tyrosine kinase 2 reaches its lowest expression levels in human breast cancer during regional nodal metastasis
    • Sang, Q.-X. A.; Man, Y.-G.; Sung, Y. M.; Khamis, Z. I.; Zhang, L.; Lee, M.-H.; Byers, S. W.; Sahab, Z. J. Non-receptor tyrosine kinase 2 reaches its lowest expression levels in human breast cancer during regional nodal metastasis Clin. Exp. Metastasis 2012, 29 (2) 143-53
    • (2012) Clin. Exp. Metastasis , vol.29 , Issue.2 , pp. 143-53
    • Sang, Q.-X.A.1    Man, Y.-G.2    Sung, Y.M.3    Khamis, Z.I.4    Zhang, L.5    Lee, M.-H.6    Byers, S.W.7    Sahab, Z.J.8
  • 40
    • 77957343443 scopus 로고    scopus 로고
    • Alteration in protein expression in estrogen receptor alpha-negative human breast cancer tissues indicates a malignant and metastatic phenotype
    • Sahab, Z. J.; Man, Y. G.; Semaan, S. M.; Newcomer, R. G.; Byers, S. W.; Sang, Q. X. A. Alteration in protein expression in estrogen receptor alpha-negative human breast cancer tissues indicates a malignant and metastatic phenotype Clin. Exp. Metastasis 2010, 27 (7) 493-503
    • (2010) Clin. Exp. Metastasis , vol.27 , Issue.7 , pp. 493-503
    • Sahab, Z.J.1    Man, Y.G.2    Semaan, S.M.3    Newcomer, R.G.4    Byers, S.W.5    Sang, Q.X.A.6
  • 41
    • 84855172843 scopus 로고    scopus 로고
    • Novel stromal biomarkers in human breast cancer tissues provide evidence for the more malignant phenotype of estrogen receptor-negative tumors
    • 10.1155/2011/723650
    • Khamis, Z. I.; Sahab, Z. J.; Byers, S. W.; Sang, Q. X. Novel stromal biomarkers in human breast cancer tissues provide evidence for the more malignant phenotype of estrogen receptor-negative tumors. J. Biomed. Biotech. 2011, 2011, 10.1155/2011/723650.
    • (2011) J. Biomed. Biotech. , vol.2011
    • Khamis, Z.I.1    Sahab, Z.J.2    Byers, S.W.3    Sang, Q.X.4
  • 42
    • 29144509592 scopus 로고    scopus 로고
    • Isoelectric point-based prefractionation of proteins from crude biological samples prior to two-dimensional gel electrophoresis
    • Sahab, Z. J.; Suh, Y.; Sang, Q. X. A. Isoelectric point-based prefractionation of proteins from crude biological samples prior to two-dimensional gel electrophoresis J. Proteome Res. 2005, 4 (6) 2266-2272
    • (2005) J. Proteome Res. , vol.4 , Issue.6 , pp. 2266-2272
    • Sahab, Z.J.1    Suh, Y.2    Sang, Q.X.A.3
  • 43
    • 79956279202 scopus 로고    scopus 로고
    • Protein profiling of isolated leukocytes, myofibroblasts, epithelial, basal, and endothelial cells from normal, hyperplastic, cancerous, and inflammatory human prostate tissues
    • Khamis, Z. I.; Iczkowski, K. A.; Sahab, Z. J.; Sang, Q. X. A. Protein profiling of isolated leukocytes, myofibroblasts, epithelial, basal, and endothelial cells from normal, hyperplastic, cancerous, and inflammatory human prostate tissues J. Cancer 2010, 1, 70-79
    • (2010) J. Cancer , vol.1 , pp. 70-79
    • Khamis, Z.I.1    Iczkowski, K.A.2    Sahab, Z.J.3    Sang, Q.X.A.4
  • 44
    • 79951845967 scopus 로고    scopus 로고
    • Tumor suppressor RARRES1 regulates DLG2, PP2A, VCP, EB1, and Ankrd26
    • Sahab, Z. J.; Hall, M. D.; Zhang, L.; Cheema, A.; Byers, S. W. Tumor suppressor RARRES1 regulates DLG2, PP2A, VCP, EB1, and Ankrd26 J. Cancer 2010, 1 (1) 14-22
    • (2010) J. Cancer , vol.1 , Issue.1 , pp. 14-22
    • Sahab, Z.J.1    Hall, M.D.2    Zhang, L.3    Cheema, A.4    Byers, S.W.5
  • 45
    • 80052178405 scopus 로고    scopus 로고
    • Mass spectrometry of peptides and proteins from human blood
    • Zhu, P.; Bowden, P.; Zhang, D.; Marshall, J. G. Mass spectrometry of peptides and proteins from human blood Mass Spectrom. Rev. 2011, 30 (5) 685-732
    • (2011) Mass Spectrom. Rev. , vol.30 , Issue.5 , pp. 685-732
    • Zhu, P.1    Bowden, P.2    Zhang, D.3    Marshall, J.G.4
  • 46
    • 80555150623 scopus 로고    scopus 로고
    • Depletion of highly abundant proteins in blood plasma by ammonium sulfate precipitation for 2D-PAGE analysis
    • Mahn, A.; Ismail, M. Depletion of highly abundant proteins in blood plasma by ammonium sulfate precipitation for 2D-PAGE analysis J. Chromatogr., B: Anal. Technol. Biomed. Life Sci. 2011, 879 (30) 3645-3648
    • (2011) J. Chromatogr., B: Anal. Technol. Biomed. Life Sci. , vol.879 , Issue.30 , pp. 3645-3648
    • Mahn, A.1    Ismail, M.2
  • 47
    • 77956181148 scopus 로고    scopus 로고
    • Enrichment of low-abundance proteins from bovine and porcine serum samples for proteomic studies
    • Marco-Ramell, A.; Bassols, A. Enrichment of low-abundance proteins from bovine and porcine serum samples for proteomic studies Res. Vet. Sci. 2010, 89 (3) 340-343
    • (2010) Res. Vet. Sci. , vol.89 , Issue.3 , pp. 340-343
    • Marco-Ramell, A.1    Bassols, A.2
  • 48
    • 79953278962 scopus 로고    scopus 로고
    • Microfluidic enrichment of small proteins from complex biological mixture on nanoporous silica chip
    • 10.1063/1.3528237
    • Hu, Y.; Gopal, A.; Lin, K.; Peng, Y.; Tasciotti, E.; Zhang, X.; Ferrari, M. Microfluidic enrichment of small proteins from complex biological mixture on nanoporous silica chip. Biomicrofluidics 2011, 5 (1), 10.1063/1.3528237.
    • (2011) Biomicrofluidics , vol.5 , Issue.1
    • Hu, Y.1    Gopal, A.2    Lin, K.3    Peng, Y.4    Tasciotti, E.5    Zhang, X.6    Ferrari, M.7
  • 49
    • 79960092663 scopus 로고    scopus 로고
    • Multiplexed protein analysis using encoded antibody-conjugated microbeads
    • Theilacker, N.; Roller, E. E.; Barbee, K. D.; Franzreb, M.; Huang, X. Multiplexed protein analysis using encoded antibody-conjugated microbeads J. R. Soc., Interface 2011, 8 (61) 1104-1113
    • (2011) J. R. Soc., Interface , vol.8 , Issue.61 , pp. 1104-1113
    • Theilacker, N.1    Roller, E.E.2    Barbee, K.D.3    Franzreb, M.4    Huang, X.5
  • 50
    • 80054032016 scopus 로고    scopus 로고
    • Monitoring protein distributions based on patterns generated by protein adsorption behavior in a microfluidic channel
    • Choi, S.; Huang, S.; Li, J.; Chae, J. Monitoring protein distributions based on patterns generated by protein adsorption behavior in a microfluidic channel Lab Chip 2011, 11 (21) 3681-3688
    • (2011) Lab Chip , vol.11 , Issue.21 , pp. 3681-3688
    • Choi, S.1    Huang, S.2    Li, J.3    Chae, J.4
  • 51
    • 79551486836 scopus 로고    scopus 로고
    • Microfluidic-based biosensors toward point-of-care detection of nucleic acids and proteins
    • Choi, S.; Goryll, M.; Sin, L. Y. M.; Wong, P. K.; Chae, J. Microfluidic-based biosensors toward point-of-care detection of nucleic acids and proteins Microfluid. Nanofluid. 2011, 10 (2) 231-247
    • (2011) Microfluid. Nanofluid. , vol.10 , Issue.2 , pp. 231-247
    • Choi, S.1    Goryll, M.2    Sin, L.Y.M.3    Wong, P.K.4    Chae, J.5
  • 53
    • 0029915410 scopus 로고    scopus 로고
    • Fragmentation reactions of protonated alpha-amino acids
    • Dookeran, N. N.; Yalcin, T.; Harrison, A. G. Fragmentation reactions of protonated alpha-amino acids J. Mass Spectrom. 1996, 31 (5) 500-508
    • (1996) J. Mass Spectrom. , vol.31 , Issue.5 , pp. 500-508
    • Dookeran, N.N.1    Yalcin, T.2    Harrison, A.G.3
  • 54
    • 0035860197 scopus 로고    scopus 로고
    • Ion chemistry of protonated glutamic acid derivatives
    • Harrison, A. G. Ion chemistry of protonated glutamic acid derivatives Int. J. Mass Spectrom. 2001, 210 (1-3) 361-370
    • (2001) Int. J. Mass Spectrom. , vol.210 , Issue.1-3 , pp. 361-370
    • Harrison, A.G.1
  • 55
    • 0033537641 scopus 로고    scopus 로고
    • Structural characterization by tandem mass spectrometry of the posttranslational polyglycylation of tubulin
    • Vinh, J.; Langridge, J. I.; Bre, M. H.; Levilliers, N.; Redeker, V.; Loyaux, D.; Rossier, J. Structural characterization by tandem mass spectrometry of the posttranslational polyglycylation of tubulin Biochemistry 1999, 38 (10) 3133-3139
    • (1999) Biochemistry , vol.38 , Issue.10 , pp. 3133-3139
    • Vinh, J.1    Langridge, J.I.2    Bre, M.H.3    Levilliers, N.4    Redeker, V.5    Loyaux, D.6    Rossier, J.7
  • 56
    • 77954656014 scopus 로고    scopus 로고
    • MALDI in-source decay of high mass protein lsoforms: Application to alpha- and beta-tubulin variants
    • Calligaris, D.; Villard, C.; Terras, L.; Braguer, D.; Verdier-Pinard, P.; Lafitte, D. MALDI in-source decay of high mass protein lsoforms: Application to alpha- and beta-tubulin variants Anal. Chem. 2010, 82 (14) 6176-6184
    • (2010) Anal. Chem. , vol.82 , Issue.14 , pp. 6176-6184
    • Calligaris, D.1    Villard, C.2    Terras, L.3    Braguer, D.4    Verdier-Pinard, P.5    Lafitte, D.6
  • 57
    • 0029800944 scopus 로고    scopus 로고
    • Structure of the C-terminal tail of alpha-tubulin: Increase of heterogeneity from newborn to adult
    • Redeker, V.; Rusconi, F.; Mary, J.; Prome, D.; Rossier, J. Structure of the C-terminal tail of alpha-tubulin: Increase of heterogeneity from newborn to adult J. Neurochem. 1996, 67 (5) 2104-2114
    • (1996) J. Neurochem. , vol.67 , Issue.5 , pp. 2104-2114
    • Redeker, V.1    Rusconi, F.2    Mary, J.3    Prome, D.4    Rossier, J.5
  • 58
    • 41149159170 scopus 로고    scopus 로고
    • Complications in the assignment of 14 and 28 da mass shift detected by mass spectrometry as in vivo methylation from endogenous proteins
    • Jung, S. Y.; Li, Y. H.; Wang, Y.; Chen, Y.; Zhao, Y. M.; Qin, J. Complications in the assignment of 14 and 28 Da mass shift detected by mass spectrometry as in vivo methylation from endogenous proteins Anal. Chem. 2008, 80 (5) 1721-1729
    • (2008) Anal. Chem. , vol.80 , Issue.5 , pp. 1721-1729
    • Jung, S.Y.1    Li, Y.H.2    Wang, Y.3    Chen, Y.4    Zhao, Y.M.5    Qin, J.6
  • 59
    • 0032495513 scopus 로고    scopus 로고
    • Structure of the alpha beta tubulin dimer by electron crystallography
    • Nogales, E.; Wolf, S. G.; Downing, K. H. Structure of the alpha beta tubulin dimer by electron crystallography Nature 1998, 391 (6663) 199-203
    • (1998) Nature , vol.391 , Issue.6663 , pp. 199-203
    • Nogales, E.1    Wolf, S.G.2    Downing, K.H.3
  • 60
    • 0017258851 scopus 로고
    • Effects of mitotic inhibitors on structure of vinblastine-induced tubulin paracrystals from sea-urchin eggs
    • Starling, D. Effects of mitotic inhibitors on structure of vinblastine-induced tubulin paracrystals from sea-urchin eggs J. of Cell Sci. 1976, 20 (1) 91-100
    • (1976) J. of Cell Sci. , vol.20 , Issue.1 , pp. 91-100
    • Starling, D.1
  • 61
    • 77958501821 scopus 로고    scopus 로고
    • Discovery of novel 2-aryl-4-benzoyl-imidazoles targeting the colchicines binding site in tubulin as potential anticancer agents
    • Chen, J. J.; Wang, Z.; Li, C. M.; Lu, Y.; Vaddady, P. K.; Meibohm, B.; Dalton, J. T.; Miller, D. D.; Li, W. Discovery of novel 2-aryl-4-benzoyl- imidazoles targeting the colchicines binding site in tubulin as potential anticancer agents J. Med. Chem. 2010, 53 (20) 7414-7427
    • (2010) J. Med. Chem. , vol.53 , Issue.20 , pp. 7414-7427
    • Chen, J.J.1    Wang, Z.2    Li, C.M.3    Lu, Y.4    Vaddady, P.K.5    Meibohm, B.6    Dalton, J.T.7    Miller, D.D.8    Li, W.9


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.