메뉴 건너뛰기




Volumn 75, Issue 1, 2011, Pages 145-159

Biomarkers of disease and post-mortem changes - Heat stabilization, a necessary tool for measurement of protein regulation

Author keywords

Degradation; Heat stabilization; Phosphorylation; Post sampling change; Quality

Indexed keywords

ALBUMIN; APOLIPOPROTEIN A1; BETA ACTIN; BETA TUBULIN; BIOLOGICAL MARKER; CATHEPSIN D; CHAPERONIN; COFILIN 1; COLLAPSIN RESPONSE MEDIATOR PROTEIN 2; COPPER ZINC SUPEROXIDE DISMUTASE; ELONGATION FACTOR; ENOLASE; FRUCTOSE BISPHOSPHATE ALDOLASE; GLUTATHIONE TRANSFERASE P1; GLYCERALDEHYDE 3 PHOSPHATE DEHYDROGENASE; HEAT SHOCK PROTEIN 27; HEAT SHOCK PROTEIN 70; HEMOGLOBIN; LAMIN A; LAMIN C; PEROXIREDOXIN 2; PHOSPHOGLYCERATE MUTASE; PROHIBITIN; PROTEIN 14 3 3; PROTEIN DISULFIDE ISOMERASE; PROTON TRANSPORTING ADENOSINE TRIPHOSPHATE SYNTHASE; PYRUVATE KINASE; STATHMIN; TROPOMYOSIN; VIMENTIN; PROTEIN;

EID: 84858744772     PISSN: 18743919     EISSN: 18767737     Source Type: Journal    
DOI: 10.1016/j.jprot.2011.06.009     Document Type: Review
Times cited : (21)

References (69)
  • 1
    • 70350215650 scopus 로고    scopus 로고
    • Tissue is alive: new technologies are needed to address the problems of protein biomarker pre-analytical variability
    • Espina V., Mueller C., Edmiston K., Sciro M., Petricoin E.F., Liotta L.A. Tissue is alive: new technologies are needed to address the problems of protein biomarker pre-analytical variability. Proteomics Clin Appl 2009, 3:874-882.
    • (2009) Proteomics Clin Appl , vol.3 , pp. 874-882
    • Espina, V.1    Mueller, C.2    Edmiston, K.3    Sciro, M.4    Petricoin, E.F.5    Liotta, L.A.6
  • 2
    • 0017101132 scopus 로고
    • Microwave applicator for in vivo rapid inactivation of enzymes in the central nervous system
    • Lenox R.H., Gandhi O.P., Meyerhoff J.L. Microwave applicator for in vivo rapid inactivation of enzymes in the central nervous system. IEEE Trans Microw Theory Tech 1976, 24:58-61.
    • (1976) IEEE Trans Microw Theory Tech , vol.24 , pp. 58-61
    • Lenox, R.H.1    Gandhi, O.P.2    Meyerhoff, J.L.3
  • 4
    • 0028784129 scopus 로고
    • Concurrent analysis of neuropeptides and biogenic amines in brain tissue of rats treated with electroconvulsive stimuli
    • Stenfors C., Bjellerupa P., Mathéb A.A., Theodorsson E. Concurrent analysis of neuropeptides and biogenic amines in brain tissue of rats treated with electroconvulsive stimuli. Brain Res 1995, 698:39-45.
    • (1995) Brain Res , vol.698 , pp. 39-45
    • Stenfors, C.1    Bjellerupa, P.2    Mathéb, A.A.3    Theodorsson, E.4
  • 5
    • 61849162815 scopus 로고    scopus 로고
    • Heat stabilization of the tissue proteome: a new technology for improved proteomics
    • Svensson M., Borén M., Skold K., Falth M., Sjogren B., Andersson M., et al. Heat stabilization of the tissue proteome: a new technology for improved proteomics. J Proteome Res 2009, 8:974-981.
    • (2009) J Proteome Res , vol.8 , pp. 974-981
    • Svensson, M.1    Borén, M.2    Skold, K.3    Falth, M.4    Sjogren, B.5    Andersson, M.6
  • 6
    • 38049025746 scopus 로고    scopus 로고
    • The significance of biochemical and molecular sample integrity in brain proteomics and peptidomics: stathmin 2-20 and peptides as sample quality indicators
    • Skold K., Svensson M., Norrman M., Sjogren B., Svenningsson P., Andren P.E. The significance of biochemical and molecular sample integrity in brain proteomics and peptidomics: stathmin 2-20 and peptides as sample quality indicators. Proteomics 2007, 7:4445-4456.
    • (2007) Proteomics , vol.7 , pp. 4445-4456
    • Skold, K.1    Svensson, M.2    Norrman, M.3    Sjogren, B.4    Svenningsson, P.5    Andren, P.E.6
  • 8
    • 33846262180 scopus 로고    scopus 로고
    • Neuropeptidomics: MS applied to the discovery of novel peptides from the brain
    • Svensson M., Skold K., Nilsson A., Falth M., Nydahl K., Svenningsson P., et al. Neuropeptidomics: MS applied to the discovery of novel peptides from the brain. Anal Chem 2007, 79:18-21.
    • (2007) Anal Chem , vol.79 , pp. 18-21
    • Svensson, M.1    Skold, K.2    Nilsson, A.3    Falth, M.4    Nydahl, K.5    Svenningsson, P.6
  • 9
    • 43549094212 scopus 로고    scopus 로고
    • Déjà vu in proteomics. A hit parade of repeatedly identified differentially expressed proteins
    • Petrak J., Ivanek R., Toman O., Cmejla R., Cmejlova J., Vyoral D., et al. Déjà vu in proteomics. A hit parade of repeatedly identified differentially expressed proteins. Proteomics 2008, 8:1744-1749.
    • (2008) Proteomics , vol.8 , pp. 1744-1749
    • Petrak, J.1    Ivanek, R.2    Toman, O.3    Cmejla, R.4    Cmejlova, J.5    Vyoral, D.6
  • 10
    • 67649184787 scopus 로고    scopus 로고
    • Generally detected proteins in comparative proteomics - a matter of cellular stress response?
    • Wang P., Bouwman F.G., Mariman E.C.M. Generally detected proteins in comparative proteomics - a matter of cellular stress response?. Proteomics 2009, 9:2955-2966.
    • (2009) Proteomics , vol.9 , pp. 2955-2966
    • Wang, P.1    Bouwman, F.G.2    Mariman, E.C.M.3
  • 11
    • 77952507597 scopus 로고    scopus 로고
    • Mass spectrometric imaging for biomedical tissue analysis
    • Chughtai K., Heeren R.M.A. Mass spectrometric imaging for biomedical tissue analysis. Chem Rev 2010, 110:3237-3277.
    • (2010) Chem Rev , vol.110 , pp. 3237-3277
    • Chughtai, K.1    Heeren, R.M.A.2
  • 14
    • 77952486235 scopus 로고    scopus 로고
    • A report on the ESF workshop on quality control in proteomics
    • Martens L. A report on the ESF workshop on quality control in proteomics. Mol Biosyst 2010, 6:935-938.
    • (2010) Mol Biosyst , vol.6 , pp. 935-938
    • Martens, L.1
  • 15
    • 0001778085 scopus 로고    scopus 로고
    • Neurotransmitters
    • E.R. Kandel, J.H. Schwartz, T.M. Jessel (Eds.)
    • Schwartz J.H. Neurotransmitters. Principles of Neural Science 2000, 280-297. 4th ed. E.R. Kandel, J.H. Schwartz, T.M. Jessel (Eds.).
    • (2000) Principles of Neural Science , pp. 280-297
    • Schwartz, J.H.1
  • 16
    • 61849098321 scopus 로고    scopus 로고
    • A quantitative peptidomic analysis of peptides related to the endogenous opioid and tachykinin systems in nucleus accumbens of rats following naloxone-precipitated morphine withdrawal
    • Rossbach U.L., Nilsson A., Falth M., Kultima K., Zhou Q., Hallberg M., et al. A quantitative peptidomic analysis of peptides related to the endogenous opioid and tachykinin systems in nucleus accumbens of rats following naloxone-precipitated morphine withdrawal. J Proteome Res 2009, 8:1091-1098.
    • (2009) J Proteome Res , vol.8 , pp. 1091-1098
    • Rossbach, U.L.1    Nilsson, A.2    Falth, M.3    Kultima, K.4    Zhou, Q.5    Hallberg, M.6
  • 17
    • 77956298568 scopus 로고    scopus 로고
    • Impact of temperature dependent sampling procedures in proteomics and peptidomics - a characterization of the liver and pancreas post mortem degradome
    • Scholz B., Skold K., Kultima K., Fernandez C., Waldemarson S., Savitski M.M., et al. Impact of temperature dependent sampling procedures in proteomics and peptidomics - a characterization of the liver and pancreas post mortem degradome. Mol Cell Proteomics 2011, 10.1074/mcp.M900229-MCP200.
    • (2011) Mol Cell Proteomics
    • Scholz, B.1    Skold, K.2    Kultima, K.3    Fernandez, C.4    Waldemarson, S.5    Savitski, M.M.6
  • 18
    • 71049194213 scopus 로고    scopus 로고
    • Development and evaluation of normalization methods for label-free relative quantification of endogenous peptides
    • Kultima K., Nilsson A., Scholz B., Rossbach U.L., Fälth M., Andrén P.E. Development and evaluation of normalization methods for label-free relative quantification of endogenous peptides. Mol Cell Proteomics 2009, 8:2285-2295.
    • (2009) Mol Cell Proteomics , vol.8 , pp. 2285-2295
    • Kultima, K.1    Nilsson, A.2    Scholz, B.3    Rossbach, U.L.4    Fälth, M.5    Andrén, P.E.6
  • 20
    • 79953032976 scopus 로고    scopus 로고
    • Neuropeptide profiling of the bovine hypothalamus: thermal stabilization is an effective tool in inhibiting post-mortem degradation
    • Colgrave M.L., Xi L., Lehnert S.A., Flatscher-Bader T., Wadensten H., Nilsson A., et al. Neuropeptide profiling of the bovine hypothalamus: thermal stabilization is an effective tool in inhibiting post-mortem degradation. Proteomics 2011, 11(7):1264-1276.
    • (2011) Proteomics , vol.11 , Issue.7 , pp. 1264-1276
    • Colgrave, M.L.1    Xi, L.2    Lehnert, S.A.3    Flatscher-Bader, T.4    Wadensten, H.5    Nilsson, A.6
  • 22
    • 77956401729 scopus 로고    scopus 로고
    • Stopping the clock on proteomic degradation by heat treatment at the point of tissue excision
    • Goodwin R.J.A., Lang A.M., Allingham H., Borén M., Pitt A.R. Stopping the clock on proteomic degradation by heat treatment at the point of tissue excision. Proteomics 2010, 10:1751-1761.
    • (2010) Proteomics , vol.10 , pp. 1751-1761
    • Goodwin, R.J.A.1    Lang, A.M.2    Allingham, H.3    Borén, M.4    Pitt, A.R.5
  • 23
    • 70350214790 scopus 로고    scopus 로고
    • Assessing the use of thermal treatment to preserve the intact proteomes of post-mortem heart and brain tissue
    • Robinson A.A., Westbrook J.A., English J.A., Borén M., Dunn M.J. Assessing the use of thermal treatment to preserve the intact proteomes of post-mortem heart and brain tissue. Proteomics 2009, 9:4433-4444.
    • (2009) Proteomics , vol.9 , pp. 4433-4444
    • Robinson, A.A.1    Westbrook, J.A.2    English, J.A.3    Borén, M.4    Dunn, M.J.5
  • 25
    • 53549083277 scopus 로고    scopus 로고
    • Time-dependent evolution of tissue markers by MALDI-MS imaging
    • Goodwin R.J.A., Dungworth J.C., Cobb S.R., Pitt A.R. Time-dependent evolution of tissue markers by MALDI-MS imaging. Proteomics 2008, 8:3801-3808.
    • (2008) Proteomics , vol.8 , pp. 3801-3808
    • Goodwin, R.J.A.1    Dungworth, J.C.2    Cobb, S.R.3    Pitt, A.R.4
  • 26
    • 53549134461 scopus 로고    scopus 로고
    • Protein and peptides in pictures: Imaging with MALDI mass spectrometry
    • Goodwin R.J.A., Pennington S.R., Pitt A.R. Protein and peptides in pictures: Imaging with MALDI mass spectrometry. Proteomics 2008, 8:3785-3800.
    • (2008) Proteomics , vol.8 , pp. 3785-3800
    • Goodwin, R.J.A.1    Pennington, S.R.2    Pitt, A.R.3
  • 28
    • 55049089416 scopus 로고    scopus 로고
    • A portrait of tissue phosphoprotein stability in the clinical tissue procurement process
    • Espina V., Edmiston K.H., Heiby M., Pierobon M., Sciro M., Merritt B., et al. A portrait of tissue phosphoprotein stability in the clinical tissue procurement process. Mol Cell Proteomics 2008, 7:1998-2018.
    • (2008) Mol Cell Proteomics , vol.7 , pp. 1998-2018
    • Espina, V.1    Edmiston, K.H.2    Heiby, M.3    Pierobon, M.4    Sciro, M.5    Merritt, B.6
  • 29
    • 79951552669 scopus 로고    scopus 로고
    • Preserving protein profiles in tissue samples: differing outcomes with and without heat stabilization
    • Ahmed M., Gardiner K.J. Preserving protein profiles in tissue samples: differing outcomes with and without heat stabilization. J Neurosci Methods 2011, 196:99-106.
    • (2011) J Neurosci Methods , vol.196 , pp. 99-106
    • Ahmed, M.1    Gardiner, K.J.2
  • 30
    • 78549284015 scopus 로고    scopus 로고
    • Clinical application for the preservation of phospho-proteins through in-situ tissue stabilization
    • Rountree B.C., Van Kirk C.A., You H., Ding W., Dang H., VanGuilder H.D., et al. Clinical application for the preservation of phospho-proteins through in-situ tissue stabilization. Proteome Sci 2010, 8:61.
    • (2010) Proteome Sci , vol.8 , pp. 61
    • Rountree, B.C.1    Van Kirk, C.A.2    You, H.3    Ding, W.4    Dang, H.5    VanGuilder, H.D.6
  • 33
    • 0037251963 scopus 로고    scopus 로고
    • SOURCE: a unified genomic resource of functional annotations, ontologies, and gene expression data
    • Diehn M., Sherlock G., Binkley G., Jin H., Matese J.C., Hernandez-Boussard T., et al. SOURCE: a unified genomic resource of functional annotations, ontologies, and gene expression data. Nucleic Acids Res 2003, 31:219-223.
    • (2003) Nucleic Acids Res , vol.31 , pp. 219-223
    • Diehn, M.1    Sherlock, G.2    Binkley, G.3    Jin, H.4    Matese, J.C.5    Hernandez-Boussard, T.6
  • 35
    • 84934440667 scopus 로고    scopus 로고
    • Detection of post-translational modifications by fluorescent staining of two-dimensional gels
    • Jacob A.M., Turck C.W. Detection of post-translational modifications by fluorescent staining of two-dimensional gels. Methods Mol Biol 2008, 446:21-32.
    • (2008) Methods Mol Biol , vol.446 , pp. 21-32
    • Jacob, A.M.1    Turck, C.W.2
  • 36
    • 77949829999 scopus 로고    scopus 로고
    • In vitro neurotoxicity of PBDE-99: immediate and concentration-dependent effects on protein expression in cerebral cortex cells
    • Alm H., Scholz B., Kultima K., Nilsson A., Andren P.E., Savitski M.M., et al. In vitro neurotoxicity of PBDE-99: immediate and concentration-dependent effects on protein expression in cerebral cortex cells. J Proteome Res 2010, 9:1226-1235.
    • (2010) J Proteome Res , vol.9 , pp. 1226-1235
    • Alm, H.1    Scholz, B.2    Kultima, K.3    Nilsson, A.4    Andren, P.E.5    Savitski, M.M.6
  • 39
    • 0015953734 scopus 로고
    • Phosphoglyceric acid mutase: rare genetic variants and tissue distribution
    • Chen S.H., Anderson J., Giblett E.R., Lewis M. Phosphoglyceric acid mutase: rare genetic variants and tissue distribution. Am J Hum Genet 1974, 26:73-77.
    • (1974) Am J Hum Genet , vol.26 , pp. 73-77
    • Chen, S.H.1    Anderson, J.2    Giblett, E.R.3    Lewis, M.4
  • 40
    • 33645824753 scopus 로고    scopus 로고
    • Identification of differentially expressed, tumor-associated proteins in oral squamous cell carcinoma by proteomic analysis
    • Turhani D., Krapfenbauer K., Thurnher D., Langen H., Fountoulakis M. Identification of differentially expressed, tumor-associated proteins in oral squamous cell carcinoma by proteomic analysis. Electrophoresis 2006, 27:1417-1423.
    • (2006) Electrophoresis , vol.27 , pp. 1417-1423
    • Turhani, D.1    Krapfenbauer, K.2    Thurnher, D.3    Langen, H.4    Fountoulakis, M.5
  • 41
    • 33747643543 scopus 로고    scopus 로고
    • Comparative proteome analysis of human lung squamous carcinoma tissue
    • Li C., Tang Ce, Duan C., Yi H., Xiao Z., Chen Z. Comparative proteome analysis of human lung squamous carcinoma tissue. Chin Ger J Clin Oncol 2006, 5:232-239.
    • (2006) Chin Ger J Clin Oncol , vol.5 , pp. 232-239
    • Li, C.1    Tang, C.2    Duan, C.3    Yi, H.4    Xiao, Z.5    Chen, Z.6
  • 42
    • 77950919036 scopus 로고    scopus 로고
    • Quantitative proteomics identification of phosphoglycerate mutase 1 as a novel therapeutic target in hepatocellular carcinoma
    • Ren F., Wu H., Lei Y., Zhang H., Liu R., Zhao Y., et al. Quantitative proteomics identification of phosphoglycerate mutase 1 as a novel therapeutic target in hepatocellular carcinoma. Mol Cancer 2010, 9:81.
    • (2010) Mol Cancer , vol.9 , pp. 81
    • Ren, F.1    Wu, H.2    Lei, Y.3    Zhang, H.4    Liu, R.5    Zhao, Y.6
  • 45
    • 70350569248 scopus 로고    scopus 로고
    • Overexpression of Annexin II affects the proliferation, apoptosis, invasion and production of proangiogenic factors in multiple myeloma
    • Bao H., Jiang M., Zhu M., Sheng F., Ruan J., Ruan C. Overexpression of Annexin II affects the proliferation, apoptosis, invasion and production of proangiogenic factors in multiple myeloma. Int J Hematol 2009, 90:177-185.
    • (2009) Int J Hematol , vol.90 , pp. 177-185
    • Bao, H.1    Jiang, M.2    Zhu, M.3    Sheng, F.4    Ruan, J.5    Ruan, C.6
  • 46
    • 77954146147 scopus 로고    scopus 로고
    • Identification of prohibitin as a potential biomarker for colorectal carcinoma based on proteomics technology
    • Chen D., Chen F., Lu X., Yang X., Xu Z., Pan J., et al. Identification of prohibitin as a potential biomarker for colorectal carcinoma based on proteomics technology. Int J Oncol 2010, 37:355-365.
    • (2010) Int J Oncol , vol.37 , pp. 355-365
    • Chen, D.1    Chen, F.2    Lu, X.3    Yang, X.4    Xu, Z.5    Pan, J.6
  • 47
    • 62249222525 scopus 로고    scopus 로고
    • Prohibitin is overexpressed in papillary thyroid carcinomas bearing the BRAF(V600E) mutation
    • Franzoni A., Dima M., D'Agostino M., Puppin C., Fabbro D., Loreto C.D., et al. Prohibitin is overexpressed in papillary thyroid carcinomas bearing the BRAF(V600E) mutation. Thyroid 2009, 19:247-255.
    • (2009) Thyroid , vol.19 , pp. 247-255
    • Franzoni, A.1    Dima, M.2    D'Agostino, M.3    Puppin, C.4    Fabbro, D.5    Loreto, C.D.6
  • 49
    • 79961156167 scopus 로고    scopus 로고
    • Prohibitin as a novel target protein of luteinizing hormone in ovarian epithelial carcinogenesis
    • Jia L., Yi X.F., Zhang Z.B., Zhuang Z.P., Li J., Chambers S.K., et al. Prohibitin as a novel target protein of luteinizing hormone in ovarian epithelial carcinogenesis. Neoplasma 2011, 58:104-109.
    • (2011) Neoplasma , vol.58 , pp. 104-109
    • Jia, L.1    Yi, X.F.2    Zhang, Z.B.3    Zhuang, Z.P.4    Li, J.5    Chambers, S.K.6
  • 50
    • 50349085895 scopus 로고    scopus 로고
    • Prohibitin: a potential biomarker for tissue-based detection of gastric cancer
    • Kang X., Zhang L., Sun J., Ni Z., Ma Y., Chen X., et al. Prohibitin: a potential biomarker for tissue-based detection of gastric cancer. J Gastroenterol 2008, 43:618-625.
    • (2008) J Gastroenterol , vol.43 , pp. 618-625
    • Kang, X.1    Zhang, L.2    Sun, J.3    Ni, Z.4    Ma, Y.5    Chen, X.6
  • 51
    • 78149411945 scopus 로고    scopus 로고
    • Increased expression of prohibitin and its relationship with poor prognosis in esophageal squamous cell carcinoma
    • Ren H.Z., Wang J.S., Wang P., Pan G.Q., Wen J.F., Fu H., et al. Increased expression of prohibitin and its relationship with poor prognosis in esophageal squamous cell carcinoma. Pathol Oncol Res 2010, 16:515-522.
    • (2010) Pathol Oncol Res , vol.16 , pp. 515-522
    • Ren, H.Z.1    Wang, J.S.2    Wang, P.3    Pan, G.Q.4    Wen, J.F.5    Fu, H.6
  • 52
    • 77958539005 scopus 로고    scopus 로고
    • Prohibitins are required for cancer cell proliferation and adhesion
    • Sievers C., Billig G., Gottschalk K., Rudel T. Prohibitins are required for cancer cell proliferation and adhesion. PLoS One 2010, 5:e12735.
    • (2010) PLoS One , vol.5
    • Sievers, C.1    Billig, G.2    Gottschalk, K.3    Rudel, T.4
  • 53
    • 33746913034 scopus 로고    scopus 로고
    • Prohibitin is a novel target gene of vitamin D involved in its antiproliferative action in breast cancer cells
    • Peng X., Mehta R., Wang S., Chellappan S., Mehta R.G. Prohibitin is a novel target gene of vitamin D involved in its antiproliferative action in breast cancer cells. Cancer Res 2006, 66:7361-7369.
    • (2006) Cancer Res , vol.66 , pp. 7361-7369
    • Peng, X.1    Mehta, R.2    Wang, S.3    Chellappan, S.4    Mehta, R.G.5
  • 54
    • 77249134537 scopus 로고    scopus 로고
    • Rescue of paclitaxel sensitivity by repression of Prohibitin1 in drug-resistant cancer cells
    • Patel N., Chatterjee S.K., Vrbanac V., Chung I., Mu C.J., Olsen R.R., et al. Rescue of paclitaxel sensitivity by repression of Prohibitin1 in drug-resistant cancer cells. Proc Natl Acad Sci USA 2010, 107:2503-2508.
    • (2010) Proc Natl Acad Sci USA , vol.107 , pp. 2503-2508
    • Patel, N.1    Chatterjee, S.K.2    Vrbanac, V.3    Chung, I.4    Mu, C.J.5    Olsen, R.R.6
  • 55
    • 0042704842 scopus 로고    scopus 로고
    • Cofilin phosphorylation and actin polymerization by NRK/NESK, a member of the germinal center kinase family
    • Nakano K., Kanai-Azuma M., Kanai Y., Moriyama K., Yazaki K., Hayashi Y., et al. Cofilin phosphorylation and actin polymerization by NRK/NESK, a member of the germinal center kinase family. Exp Cell Res 2003, 287:219-227.
    • (2003) Exp Cell Res , vol.287 , pp. 219-227
    • Nakano, K.1    Kanai-Azuma, M.2    Kanai, Y.3    Moriyama, K.4    Yazaki, K.5    Hayashi, Y.6
  • 56
    • 78549293961 scopus 로고    scopus 로고
    • The mitotic kinase Aurora-A induces mammary cell migration and breast cancer metastasis by activating the cofilin-F-actin pathway
    • Wang L.-h., Xiang J., Yan M., Zhang Y., Zhao Y., Yue C.-f., et al. The mitotic kinase Aurora-A induces mammary cell migration and breast cancer metastasis by activating the cofilin-F-actin pathway. Cancer Res 2010, 70:9118-9128.
    • (2010) Cancer Res , vol.70 , pp. 9118-9128
    • Wang, L.-H.1    Xiang, J.2    Yan, M.3    Zhang, Y.4    Zhao, Y.5    Yue, C.-F.6
  • 57
    • 77955367540 scopus 로고    scopus 로고
    • CFL1 expression levels as a prognostic and drug resistance marker in nonsmall cell lung cancer
    • Castro M.A.A., Dal-Pizzol F., Zdanov S., Soares M., Müller C.B., Lopes F.M., et al. CFL1 expression levels as a prognostic and drug resistance marker in nonsmall cell lung cancer. Cancer 2010, 116:3645-3655.
    • (2010) Cancer , vol.116 , pp. 3645-3655
    • Castro, M.A.A.1    Dal-Pizzol, F.2    Zdanov, S.3    Soares, M.4    Müller, C.B.5    Lopes, F.M.6
  • 58
    • 77953150632 scopus 로고    scopus 로고
    • Subcellular distribution and expression of cofilin and ezrin in human colon adenocarcinoma cell lines with different metastatic potential
    • e14-e.
    • Nowak D., Mazur A.J., Popow-Woźniak A., Radwańska A., Mannherz H.G., Malicka-Błaszkiewicz M. Subcellular distribution and expression of cofilin and ezrin in human colon adenocarcinoma cell lines with different metastatic potential. Eur J Histochem 2010, 54. e14-e.
    • (2010) Eur J Histochem , vol.54
    • Nowak, D.1    Mazur, A.J.2    Popow-Woźniak, A.3    Radwańska, A.4    Mannherz, H.G.5    Malicka-Błaszkiewicz, M.6
  • 59
    • 70349651926 scopus 로고    scopus 로고
    • Oxidant-induced apoptosis is mediated by oxidation of the actin-regulatory protein cofilin
    • Klamt F., Zdanov S., Levine R.L., Pariser A., Zhang Y., Zhang B., et al. Oxidant-induced apoptosis is mediated by oxidation of the actin-regulatory protein cofilin. Nat Cell Biol 2009, 11:1241-1246.
    • (2009) Nat Cell Biol , vol.11 , pp. 1241-1246
    • Klamt, F.1    Zdanov, S.2    Levine, R.L.3    Pariser, A.4    Zhang, Y.5    Zhang, B.6
  • 60
    • 34248574345 scopus 로고    scopus 로고
    • Deletion of the cruciform binding domain in CBP/14-3-3 displays reduced origin binding and initiation of DNA replication in budding yeast
    • Yahyaoui W., Callejo M., Price G.B., Zannis-Hadjopoulos M. Deletion of the cruciform binding domain in CBP/14-3-3 displays reduced origin binding and initiation of DNA replication in budding yeast. BMC Mol Biol 2007, 8:27.
    • (2007) BMC Mol Biol , vol.8 , pp. 27
    • Yahyaoui, W.1    Callejo, M.2    Price, G.B.3    Zannis-Hadjopoulos, M.4
  • 61
    • 71449102836 scopus 로고    scopus 로고
    • 14-3-3 proteins function in the initiation and elongation steps of DNA replication in Saccharomyces cerevisiae
    • Yahyaoui W., Zannis-Hadjopoulos M. 14-3-3 proteins function in the initiation and elongation steps of DNA replication in Saccharomyces cerevisiae. J Cell Sci 2009, 122:4419-4426.
    • (2009) J Cell Sci , vol.122 , pp. 4419-4426
    • Yahyaoui, W.1    Zannis-Hadjopoulos, M.2
  • 62
    • 77953645711 scopus 로고    scopus 로고
    • 14-3-3epsilon contributes to tumour suppression in laryngeal carcinoma by affecting apoptosis and invasion
    • Che X.H., Chen H., Xu Z.M., Shang C., Sun K.L., Fu W.N. 14-3-3epsilon contributes to tumour suppression in laryngeal carcinoma by affecting apoptosis and invasion. BMC Cancer 2010, 10:306.
    • (2010) BMC Cancer , vol.10 , pp. 306
    • Che, X.H.1    Chen, H.2    Xu, Z.M.3    Shang, C.4    Sun, K.L.5    Fu, W.N.6
  • 63
    • 29344452931 scopus 로고    scopus 로고
    • Protein kinase A phosphorylates and regulates dimerization of 14-3-3 epsilon
    • Gu Y.M., Jin Y.H., Choi J.K., Baek K.H., Yeo C.Y., Lee K.Y. Protein kinase A phosphorylates and regulates dimerization of 14-3-3 epsilon. FEBS Lett 2006, 580:305-310.
    • (2006) FEBS Lett , vol.580 , pp. 305-310
    • Gu, Y.M.1    Jin, Y.H.2    Choi, J.K.3    Baek, K.H.4    Yeo, C.Y.5    Lee, K.Y.6
  • 64
    • 2442429306 scopus 로고    scopus 로고
    • JNK promotes Bax translocation to mitochondria through phosphorylation of 14-3-3 proteins
    • Tsuruta F., Sunayama J., Mori Y., Hattori S., Shimizu S., Tsujimoto Y., et al. JNK promotes Bax translocation to mitochondria through phosphorylation of 14-3-3 proteins. EMBO J 2004, 23:1889-1899.
    • (2004) EMBO J , vol.23 , pp. 1889-1899
    • Tsuruta, F.1    Sunayama, J.2    Mori, Y.3    Hattori, S.4    Shimizu, S.5    Tsujimoto, Y.6
  • 65
    • 74849098583 scopus 로고    scopus 로고
    • Peroxiredoxin 1 and its role in cell signaling
    • Neumann C.A., Cao J., Manevich Y. Peroxiredoxin 1 and its role in cell signaling. Cell Cycle 2009, 8:4072-4078.
    • (2009) Cell Cycle , vol.8 , pp. 4072-4078
    • Neumann, C.A.1    Cao, J.2    Manevich, Y.3
  • 66
  • 67
    • 0042568938 scopus 로고    scopus 로고
    • Essential role for the peroxiredoxin Prdx1 in erythrocyte antioxidant defence and tumour suppression
    • Neumann C.A., Krause D.S., Carman C.V., Das S., Dubey D.P., Abraham J.L., et al. Essential role for the peroxiredoxin Prdx1 in erythrocyte antioxidant defence and tumour suppression. Nature 2003, 424:561-565.
    • (2003) Nature , vol.424 , pp. 561-565
    • Neumann, C.A.1    Krause, D.S.2    Carman, C.V.3    Das, S.4    Dubey, D.P.5    Abraham, J.L.6
  • 68
    • 0037067763 scopus 로고    scopus 로고
    • Regulation of peroxiredoxin I activity by Cdc2-mediated phosphorylation
    • Chang T.-S., Jeong W., Choi S.Y., Yu S., Kang S.W., Rhee S.G. Regulation of peroxiredoxin I activity by Cdc2-mediated phosphorylation. J Biol Chem 2002, 277:25370-25376.
    • (2002) J Biol Chem , vol.277 , pp. 25370-25376
    • Chang, T.-S.1    Jeong, W.2    Choi, S.Y.3    Yu, S.4    Kang, S.W.5    Rhee, S.G.6
  • 69
    • 79952231198 scopus 로고    scopus 로고
    • Peroxiredoxin 1 controls prostate cancer growth through toll-like receptor 4-dependent regulation of tumor vasculature
    • Riddell J.R., Bshara W., Moser M.T., Spernyak J.A., Foster B.A., Gollnick S.O. Peroxiredoxin 1 controls prostate cancer growth through toll-like receptor 4-dependent regulation of tumor vasculature. Cancer Res 2011, 71:1637-1646.
    • (2011) Cancer Res , vol.71 , pp. 1637-1646
    • Riddell, J.R.1    Bshara, W.2    Moser, M.T.3    Spernyak, J.A.4    Foster, B.A.5    Gollnick, S.O.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.