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Volumn , Issue , 2015, Pages 143-174

Proteomics and prostate cancer

Author keywords

Epitope tagging techniques; Expression proteomics; Flag Tag; Fluorescence resonance energy transfer; Functional proteomics; Glutathione S transferase pull down; Isotope tags for relative and absolute protein quantitation; Isotope coded affinity tag; Isotope tagged proteomics; Laser capture microdissection; Mass spectrometry; Multidimensional protein identification technology; Phage display; Prostate cancer; Prostate specific antigen; Protein arrays; Stable isotope labeling by amino acids in cell culture; Tandem affinity purification; Two dimensional difference gel electrophoresis; Two dimensional gel electrophoresis; Yeast two hybrid system

Indexed keywords


EID: 85052807745     PISSN: None     EISSN: None     Source Type: Book    
DOI: 10.1201/b18597     Document Type: Chapter
Times cited : (1)

References (189)
  • 1
    • 0037435030 scopus 로고    scopus 로고
    • Mass spectrometry-based proteomics
    • Aebersold, R.; Mann, M. Mass spectrometry-based proteomics. Nature 2003, 422, 198-207.
    • (2003) Nature , vol.422 , pp. 198-207
    • Aebersold, R.1    Mann, M.2
  • 3
    • 0032489015 scopus 로고    scopus 로고
    • The cell as a collection of protein machines: Preparing the next generation of molecular biologists
    • Alberts, B. The cell as a collection of protein machines: Preparing the next generation of molecular biologists. Cell 1998, 92, 291-294.
    • (1998) Cell , vol.92 , pp. 291-294
    • Alberts, B.1
  • 4
    • 33644550021 scopus 로고    scopus 로고
    • Structural systems biology: Modelling protein interactions
    • Aloy, P.; Russell, R. B. Structural systems biology: Modelling protein interactions. Nat Rev Mol Cell Biol 2006, 7, 188-197.
    • (2006) Nat Rev Mol Cell Biol , vol.7 , pp. 188-197
    • Aloy, P.1    Russell, R.B.2
  • 5
    • 33644675365 scopus 로고    scopus 로고
    • Stable isotope labeling with amino acids in cell culture (SILAC) for studying dynamics of protein abundance and posttranslational modifications
    • Amanchy, R.; Kalume, D. E.; Pandey, A. Stable isotope labeling with amino acids in cell culture (SILAC) for studying dynamics of protein abundance and posttranslational modifications. Sci STKE 2005, 267, l2.
    • (2005) Sci STKE , vol.267 , pp. l2
    • Amanchy, R.1    Kalume, D.E.2    Pandey, A.3
  • 6
    • 0001644020 scopus 로고    scopus 로고
    • The human plasma proteome: History, character, and diagnostic prospects
    • Anderson, N. L.; Anderson, N. G. The human plasma proteome: History, character, and diagnostic prospects. Mol Cell Proteomics 2002, 1, 845-867.
    • (2002) Mol Cell Proteomics , vol.1 , pp. 845-867
    • Anderson, N.L.1    Anderson, N.G.2
  • 7
    • 0036789265 scopus 로고    scopus 로고
    • Analyzing yeast protein-protein interaction data obtained from different sources
    • Bader, G. D.; Hogue, C. W. Analyzing yeast protein-protein interaction data obtained from different sources. Nat. Biotechnol 2002, 20, 991-997.
    • (2002) Nat. Biotechnol , vol.20 , pp. 991-997
    • Bader, G.D.1    Hogue, C.W.2
  • 9
    • 33645315510 scopus 로고    scopus 로고
    • Charting protein complexes, signaling pathways, and networks in the immune system
    • Bauch, A.; Superti-Furga, G. Charting protein complexes, signaling pathways, and networks in the immune system. Immunol Rev 2006, 210, 187-207.
    • (2006) Immunol Rev , vol.210 , pp. 187-207
    • Bauch, A.1    Superti-Furga, G.2
  • 10
    • 0035559449 scopus 로고    scopus 로고
    • Molecular profiling of tissue samples using laser capture microdissection
    • Best, C. J.; Emmert-Buck, M. R. Molecular profiling of tissue samples using laser capture microdissection. Expert Rev Mol Diagn 2001, 1, 53-60.
    • (2001) Expert Rev Mol Diagn , vol.1 , pp. 53-60
    • Best, C.J.1    Emmert-Buck, M.R.2
  • 11
    • 0037337310 scopus 로고    scopus 로고
    • A proteomics strategy to elucidate functional protein-protein interactions applied to EGF signaling
    • Blagoev, B.; Kratchmarova, I.; Ong, S. E.; Nielsen, M.; Foster, L. J.; Mann, M. A proteomics strategy to elucidate functional protein-protein interactions applied to EGF signaling. Nat Biotechnol 2003, 21, 315-318.
    • (2003) Nat Biotechnol , vol.21 , pp. 315-318
    • Blagoev, B.1    Kratchmarova, I.2    Ong, S.E.3    Nielsen, M.4    Foster, L.J.5    Mann, M.6
  • 12
    • 0026680845 scopus 로고
    • Interaction cloning: Identification of a helix-loop-helix zipper protein that interacts with c-fos
    • Blanar, M. A.; Rutter, W. J. Interaction cloning: Identification of a helix-loop-helix zipper protein that interacts with c-fos. Science 1992, 256, 1014-1018.
    • (1992) Science , vol.256 , pp. 1014-1018
    • Blanar, M.A.1    Rutter, W.J.2
  • 14
    • 0036023414 scopus 로고    scopus 로고
    • Normal, benign, preneoplastic, and malignant prostate cells have distinct protein expression profiles resolved by surface enhanced laser desorption/ionization mass spectrometry
    • Cazares, L. H.; Adam, B. L.; Ward, M. D.; Nasim, S.; Schellhammer, P. F.; Semmes, O. J.; Wright, G. L. Jr. Normal, benign, preneoplastic, and malignant prostate cells have distinct protein expression profiles resolved by surface enhanced laser desorption/ionization mass spectrometry. Clin Cancer Res 2002, 8, 2541-2552.
    • (2002) Clin Cancer Res , vol.8 , pp. 2541-2552
    • Cazares, L.H.1    Adam, B.L.2    Ward, M.D.3    Nasim, S.4    Schellhammer, P.F.5    Semmes, O.J.6    Wright, G.L.7
  • 15
  • 16
    • 0033649916 scopus 로고    scopus 로고
    • High-resolution two-dimensional gel electrophoresis and protein identification using western blotting and ECL detection
    • Celis, J. E.; Gromov, P. High-resolution two-dimensional gel electrophoresis and protein identification using western blotting and ECL detection. Exs 2000, 88, 55-67.
    • (2000) Exs , vol.88 , pp. 55-67
    • Celis, J.E.1    Gromov, P.2
  • 17
    • 0037487233 scopus 로고    scopus 로고
    • Proteomics in translational cancer research: Toward an integrated approach
    • Celis, J. E.; Gromov, P. Proteomics in translational cancer research: Toward an integrated approach. Cancer Cell 2003, 3, 9-15.
    • (2003) Cancer Cell , vol.3 , pp. 9-15
    • Celis, J.E.1    Gromov, P.2
  • 19
    • 0032757296 scopus 로고    scopus 로고
    • Natural poly-histidine affinity tag for purification of recombinant proteins on cobalt(II)-carboxymethylaspartate crosslinked agarose
    • Chaga, G.; Bochkariov, D. E.; Jokhadze, G. G.; Hopp, J.; Nelson, P. Natural poly-histidine affinity tag for purification of recombinant proteins on cobalt(II)-carboxymethylaspartate crosslinked agarose. J Chromatogr A 1999, 864, 247-256.
    • (1999) J Chromatogr A , vol.864 , pp. 247-256
    • Chaga, G.1    Bochkariov, D.E.2    Jokhadze, G.G.3    Hopp, J.4    Nelson, P.5
  • 21
    • 11844292771 scopus 로고    scopus 로고
    • High level expression and single-step purification of hexahistidine-tagged l-2-hydroxyisocaproate dehydrogenase making use of a versatile expression vector set
    • Chatterjee, S.; Schoepe, J.; Lohmer, S.; Schomburg, D. High level expression and single-step purification of hexahistidine-tagged l-2-hydroxyisocaproate dehydrogenase making use of a versatile expression vector set. Protein Expr Purif 2005, 39, 137-143.
    • (2005) Protein Expr Purif , vol.39 , pp. 137-143
    • Chatterjee, S.1    Schoepe, J.2    Lohmer, S.3    Schomburg, D.4
  • 23
    • 0025940629 scopus 로고
    • The two-hybrid system: A method to identify and clone genes for proteins that interact with a protein of interest
    • Chien, C. T.; Bartel, P. L.; Sternglanz, R.; Fields, S. The two-hybrid system: A method to identify and clone genes for proteins that interact with a protein of interest. Proc Natl Acad Sci USA 1991, 88, 9578-9582.
    • (1991) Proc Natl Acad Sci USA , vol.88 , pp. 9578-9582
    • Chien, C.T.1    Bartel, P.L.2    Sternglanz, R.3    Fields, S.4
  • 24
    • 0033611663 scopus 로고    scopus 로고
    • Identification of a protein kinase cascade of major importance in insulin signal transduction
    • Cohen, P. The Croonian Lecture 1998. Identification of a protein kinase cascade of major importance in insulin signal transduction. Philos Trans R Soc Lond B Biol Sci 1999, 354, 485-495.
    • (1999) Philos Trans R Soc Lond B Biol Sci , vol.354 , pp. 485-495
    • Cohen, P.1
  • 25
    • 8844280078 scopus 로고    scopus 로고
    • Integrating a functional proteomic approach into the target discovery process
    • Colland, F.; Daviet, L. Integrating a functional proteomic approach into the target discovery process. Biochimie 2004, 86, 625-632.
    • (2004) Biochimie , vol.86 , pp. 625-632
    • Colland, F.1    Daviet, L.2
  • 26
    • 34547693897 scopus 로고    scopus 로고
    • Proteomic analyses to identify novel therapeutic targets for the treatment of advanced prostate cancer
    • Comuzzi, B.; Sadar, M. D. Proteomic analyses to identify novel therapeutic targets for the treatment of advanced prostate cancer. Cell Science 2006, 3, 61-81.
    • (2006) Cell Science , vol.3 , pp. 61-81
    • Comuzzi, B.1    Sadar, M.D.2
  • 28
    • 0033022342 scopus 로고    scopus 로고
    • A mechanism for hormone-independent prostate cancer through modulation of androgen receptor signaling by the HER-2/neu tyrosine kinase
    • Craft, N.; Shostak, Y.; Carey, M.; Sawyers, C. L. A mechanism for hormone-independent prostate cancer through modulation of androgen receptor signaling by the HER-2/neu tyrosine kinase. Nat Med 1999, 5, 280-285.
    • (1999) Nat Med , vol.5 , pp. 280-285
    • Craft, N.1    Shostak, Y.2    Carey, M.3    Sawyers, C.L.4
  • 29
    • 0028113415 scopus 로고
    • Androgen receptor activation in prostatic tumor cell lines by insulin-like growth factor-I, keratinocyte growth factor and epidermal growth factor
    • Culig, Z.; Hobisch, A.; Cronauer, M. V.; Radmayr, C.; Trapman, J.; Hittmair, A.; Bartsch, G.; Klocker, H. Androgen receptor activation in prostatic tumor cell lines by insulin-like growth factor-I, keratinocyte growth factor and epidermal growth factor. Cancer Res 1994, 54, 5474-5478.
    • (1994) Cancer Res , vol.54 , pp. 5474-5478
    • Culig, Z.1    Hobisch, A.2    Cronauer, M.V.3    Radmayr, C.4    Trapman, J.5    Hittmair, A.6    Bartsch, G.7    Klocker, H.8
  • 30
    • 0032161918 scopus 로고    scopus 로고
    • Visualization of Pit-1 transcription factor interactions in the living cell nucleus by fluorescence resonance energy transfer microscopy
    • Day, R. N. Visualization of Pit-1 transcription factor interactions in the living cell nucleus by fluorescence resonance energy transfer microscopy. Mol Endocrinol 1998, 12, 1410-1419.
    • (1998) Mol Endocrinol , vol.12 , pp. 1410-1419
    • Day, R.N.1
  • 31
    • 3342986727 scopus 로고    scopus 로고
    • Selective capture of prostatic basal cells and secretory epithelial cells for proteomic and genomic analysis
    • Diaz, J. I.; Cazares, L. H.; Corica, A.; John Semmes, O. Selective capture of prostatic basal cells and secretory epithelial cells for proteomic and genomic analysis. Urol Oncol 2004, 22, 329-336.
    • (2004) Urol Oncol , vol.22 , pp. 329-336
    • Diaz, J.I.1    Cazares, L.H.2    Corica, A.3    John Semmes, O.4
  • 33
    • 0346094408 scopus 로고    scopus 로고
    • Recent developments in the analysis of protein complexes
    • Dziembowski, A.; Séraphin, B. Recent developments in the analysis of protein complexes. FEBS Lett 2004, 556, 1-6.
    • (2004) FEBS Lett , vol.556 , pp. 1-6
    • Dziembowski, A.1    Séraphin, B.2
  • 35
    • 0036805329 scopus 로고    scopus 로고
    • Bridging structural biology and genomics: Assessing protein interaction data with known complexes
    • Edwards, A. M.; Kus, B.; Jansen, R.; Greenbaum, D.; Greenblatt, J.; Gerstein, M. Bridging structural biology and genomics: Assessing protein interaction data with known complexes. Trends Genet 2002, 18, 529-536.
    • (2002) Trends Genet , vol.18 , pp. 529-536
    • Edwards, A.M.1    Kus, B.2    Jansen, R.3    Greenbaum, D.4    Greenblatt, J.5    Gerstein, M.6
  • 36
    • 0035975859 scopus 로고    scopus 로고
    • The FLAG peptide, a versatile fusion tag for the purification of recombinant proteins
    • Einhauer, A.; Jungbauer, A. The FLAG peptide, a versatile fusion tag for the purification of recombinant proteins. J. Biochem. Biophys. Methods 2001,49, 455-465.
    • (2001) J. Biochem. Biophys. Methods , vol.49 , pp. 455-465
    • Einhauer, A.1    Jungbauer, A.2
  • 37
    • 2642576786 scopus 로고    scopus 로고
    • High-yield expression and purification of p18 form of Bax as an MBP-fusion protein
    • Eliseev, R.; Alexandrov, A.; Gunter, T. High-yield expression and purification of p18 form of Bax as an MBP-fusion protein. Protein Expr Purif 2004, 35, 206-209.
    • (2004) Protein Expr Purif , vol.35 , pp. 206-209
    • Eliseev, R.1    Alexandrov, A.2    Gunter, T.3
  • 39
    • 0037014792 scopus 로고    scopus 로고
    • Overdiagnosis due to prostate-specific antigen screening: Lessons from U.S. prostate cancer incidence trends
    • Etzioni, R.; Penson, D. F.; Legler, J. M.; di Tommaso, D.; Boer, R.; Gann, P. H.; Feuer, E. J. Overdiagnosis due to prostate-specific antigen screening: Lessons from U.S. prostate cancer incidence trends. J Natl Cancer Inst 2002, 94, 981-990.
    • (2002) J Natl Cancer Inst , vol.94 , pp. 981-990
    • Etzioni, R.1    Penson, D.F.2    Legler, J.M.3    di Tommaso, D.4    Boer, R.5    Gann, P.H.6    Feuer, E.J.7
  • 40
    • 4043141477 scopus 로고    scopus 로고
    • Quantitative cancer proteomics: Stable isotope labeling with amino acids in cell culture (SILAC) as a tool for prostate cancer research
    • Everley, P. A.; Krijgsveld, J.; Zetter, B. R.; Gygi, S. P. Quantitative cancer proteomics: Stable isotope labeling with amino acids in cell culture (SILAC) as a tool for prostate cancer research. Mol Cell Proteomics 2004, 3, 729-735.
    • (2004) Mol Cell Proteomics , vol.3 , pp. 729-735
    • Everley, P.A.1    Krijgsveld, J.2    Zetter, B.R.3    Gygi, S.P.4
  • 41
    • 15244360113 scopus 로고    scopus 로고
    • Expression of the murine leukemia virus protease in fusion with maltose-binding protein in Escherichia coli
    • Feher, A.; Boross, P.; Sperka, T.; Oroszlan, S.; Tozser, J. Expression of the murine leukemia virus protease in fusion with maltose-binding protein in Escherichia coli. Protein Expr Purif 2004, 35, 62-68.
    • (2004) Protein Expr Purif , vol.35 , pp. 62-68
    • Feher, A.1    Boross, P.2    Sperka, T.3    Oroszlan, S.4    Tozser, J.5
  • 42
    • 0035496220 scopus 로고    scopus 로고
    • The development of androgen-independent prostate cancer
    • Feldman, B. J.; Feldman, D. The development of androgen-independent prostate cancer. Nat. Rev Cancer 2001, 1, 34-45.
    • (2001) Nat. Rev Cancer , vol.1 , pp. 34-45
    • Feldman, B.J.1    Feldman, D.2
  • 43
    • 0024406857 scopus 로고
    • A novel genetic system to detect protein-protein interactions
    • Fields, S.; Song, O. A novel genetic system to detect protein-protein interactions. Nature 1989, 340, 245-246.
    • (1989) Nature , vol.340 , pp. 245-246
    • Fields, S.1    Song, O.2
  • 44
    • 84981779372 scopus 로고
    • Intermolecular energy migration and fluorescence
    • Forster, T. Intermolecular energy migration and fluorescence. Ann Physik 1948, 2, 55-75.
    • (1948) Ann Physik , vol.2 , pp. 55-75
    • Forster, T.1
  • 45
    • 22544475902 scopus 로고    scopus 로고
    • Plasma chromogranin A in patients with prostate cancer improves the diagnostic efficacy of free/total prostate-specific antigen determination
    • Fracalanza, S.; Prayer-Galetti, T.; Pinto, F.; Navaglia, F.; Sacco, E.; Ciaccia, M.; Plebani, M.; Pagano, F.; Basso, D. Plasma chromogranin A in patients with prostate cancer improves the diagnostic efficacy of free/total prostate-specific antigen determination. Urol Int 2005, 75, 57-61.
    • (2005) Urol Int , vol.75 , pp. 57-61
    • Fracalanza, S.1    Prayer-Galetti, T.2    Pinto, F.3    Navaglia, F.4    Sacco, E.5    Ciaccia, M.6    Plebani, M.7    Pagano, F.8    Basso, D.9
  • 46
    • 0034581171 scopus 로고    scopus 로고
    • Epitope tagging: General method for tracking recombinant proteins
    • Fritze, C. E.; Anderson, T. R. Epitope tagging: General method for tracking recombinant proteins. Methods Enzymol 2000, 327, 3-16.
    • (2000) Methods Enzymol , vol.327 , pp. 3-16
    • Fritze, C.E.1    Anderson, T.R.2
  • 47
    • 4143114765 scopus 로고    scopus 로고
    • Acetylation of nuclear receptors in cellular growth and apoptosis
    • Fu, M.; Wang, C.; Zhang, X.; Pestell, R. G. Acetylation of nuclear receptors in cellular growth and apoptosis. Biochem Pharmacol 2004, 68, 1199-1208.
    • (2004) Biochem Pharmacol , vol.68 , pp. 1199-1208
    • Fu, M.1    Wang, C.2    Zhang, X.3    Pestell, R.G.4
  • 48
    • 0033583033 scopus 로고    scopus 로고
    • Cloning and characterization of androgen receptor coactivator, ARA55, in human prostate
    • Fujimoto, N.; Yeh, S.; Kang, H. Y.; Inui, S.; Chang, H. C.; Mizokami, A.; Chang, C. Cloning and characterization of androgen receptor coactivator, ARA55, in human prostate. J Biol Chem 1999, 274:8316-8321.
    • (1999) J Biol Chem , vol.274 , pp. 8316-8321
    • Fujimoto, N.1    Yeh, S.2    Kang, H.Y.3    Inui, S.4    Chang, H.C.5    Mizokami, A.6    Chang, C.7
  • 49
  • 51
    • 0036645414 scopus 로고    scopus 로고
    • Molecular biology of the androgen receptor
    • Gelmann, E. P. Molecular biology of the androgen receptor. J Clin Oncol 2002, 20, 3001-3015.
    • (2002) J Clin Oncol , vol.20 , pp. 3001-3015
    • Gelmann, E.P.1
  • 52
    • 0347407794 scopus 로고    scopus 로고
    • Akt in prostate cancer: Possible role in androgen-independence
    • Ghosh, P. M.; Malik, S.; Bedolla, R.; Kreisberg, J. I. Akt in prostate cancer: Possible role in androgen-independence. Curr Drug Metab 2003, 4, 487-496.
    • (2003) Curr Drug Metab , vol.4 , pp. 487-496
    • Ghosh, P.M.1    Malik, S.2    Bedolla, R.3    Kreisberg, J.I.4
  • 56
    • 35848931437 scopus 로고    scopus 로고
    • The use of isobaric tag peptide labeling (iTRAQ) and mass spectrometry to examine rare, primitive hematopoietic cells from patients with chronic myeloid leukemia
    • Griffiths, S. D.; Burthem, J.; Unwin, R. D.; Holyoake, T. L.; Melo, J. V.; Lucas, G. S.; Whetton, A. D. The use of isobaric tag peptide labeling (iTRAQ) and mass spectrometry to examine rare, primitive hematopoietic cells from patients with chronic myeloid leukemia. Mol Biotechnol 2007, 36, 81-89.
    • (2007) Mol Biotechnol , vol.36 , pp. 81-89
    • Griffiths, S.D.1    Burthem, J.2    Unwin, R.D.3    Holyoake, T.L.4    Melo, J.V.5    Lucas, G.S.6    Whetton, A.D.7
  • 60
  • 61
    • 0034527640 scopus 로고    scopus 로고
    • Baltimore Longitudinal Study on Aging. Serum levels of insulin-like growth factor I (IGF-I), IGF-II, IGF-binding protein-3, and prostate-specific antigen as predictors of clinical prostate cancer
    • Harman, S. M.; Metter, E. J.; Landis, P. K.; Carter, H. B. Baltimore Longitudinal Study on Aging. Serum levels of insulin-like growth factor I (IGF-I), IGF-II, IGF-binding protein-3, and prostate-specific antigen as predictors of clinical prostate cancer. J Clin Endocrinol Metab 2000, 85, 4258-4265.
    • (2000) J Clin Endocrinol Metab , vol.85 , pp. 4258-4265
    • Harman, S.M.1    Metter, E.J.2    Landis, P.K.3    Carter, H.B.4
  • 62
    • 0037155790 scopus 로고    scopus 로고
    • The FXXLF motif mediates androgen receptor-specific interactions with coregulators
    • He, B.; Minges, J. T.; Lee, L. W.; Wilson, E. M. The FXXLF motif mediates androgen receptor-specific interactions with coregulators. J Biol Chem 2002, 277, 10226-10235.
    • (2002) J Biol Chem , vol.277 , pp. 10226-10235
    • He, B.1    Minges, J.T.2    Lee, L.W.3    Wilson, E.M.4
  • 63
    • 37349118115 scopus 로고    scopus 로고
    • Androgen receptor (AR) coregulators: A diversity of functions converging on and regulating the AR transcriptional complex
    • Heemers, H. V.; Tindall, D. J. Androgen receptor (AR) coregulators: A diversity of functions converging on and regulating the AR transcriptional complex. Endocr Rev 2007, 28, 778-808.
    • (2007) Endocr Rev , vol.28 , pp. 778-808
    • Heemers, H.V.1    Tindall, D.J.2
  • 64
    • 0035997269 scopus 로고    scopus 로고
    • Proteomics and its trends facing nature’s complexity
    • Hochstrasser, D. F.; Sanchez, J. C.; Appel, R. D. Proteomics and its trends facing nature’s complexity. Proteomics 2002, 2, 807-812.
    • (2002) Proteomics , vol.2 , pp. 807-812
    • Hochstrasser, D.F.1    Sanchez, J.C.2    Appel, R.D.3
  • 66
    • 1842690558 scopus 로고    scopus 로고
    • Androgens negatively regulate forkhead transcription factor FKHR (FOXO1) through a proteolytic mechanism in prostate cancer cells
    • Huang, H.; Muddiman, D. C.; Tindall, D. J. Androgens negatively regulate forkhead transcription factor FKHR (FOXO1) through a proteolytic mechanism in prostate cancer cells. J Biol Chem 2004, 279, 138, 66-13877.
    • (2004) J Biol Chem , vol.279 , Issue.138 , pp. 66-13877
    • Huang, H.1    Muddiman, D.C.2    Tindall, D.J.3
  • 67
    • 0036421180 scopus 로고    scopus 로고
    • Expression of the class 1 outer-membrane protein of Neisseria meningitidis in Escherichia coli and purification using a self-cleavable affinity tag
    • Humphries, H. E.; Christodoulides, M.; Heckels, J. E. Expression of the class 1 outer-membrane protein of Neisseria meningitidis in Escherichia coli and purification using a self-cleavable affinity tag. Protein Expr Purif 2002, 26, 243-248.
    • (2002) Protein Expr Purif , vol.26 , pp. 243-248
    • Humphries, H.E.1    Christodoulides, M.2    Heckels, J.E.3
  • 68
    • 10344248945 scopus 로고    scopus 로고
    • Microdissection techniques for molecular testing in surgical pathology
    • Hunt, J. L.; Finkelstein, S. D. Microdissection techniques for molecular testing in surgical pathology. Arch Pathol Lab Med 2004, 128, 1372-1378.
    • (2004) Arch Pathol Lab Med , vol.128 , pp. 1372-1378
    • Hunt, J.L.1    Finkelstein, S.D.2
  • 69
    • 0242569349 scopus 로고    scopus 로고
    • A proteomic approach for quantitation of phosphorylation using stable isotope labeling in cell culture
    • Ibarrola, N.; Kalume, D. E.; Gronborg, M.; Iwahori, A.; Pandey, A. A proteomic approach for quantitation of phosphorylation using stable isotope labeling in cell culture. Anal Chem 2003, 75, 6043-6049.
    • (2003) Anal Chem , vol.75 , pp. 6043-6049
    • Ibarrola, N.1    Kalume, D.E.2    Gronborg, M.3    Iwahori, A.4    Pandey, A.5
  • 70
  • 72
    • 17044415362 scopus 로고    scopus 로고
    • Single-step Strep-tag purification for the isolation and identification of protein complexes from mammalian cells
    • Junttila, M. R.; Saarinen, S.; Schmidt, T.; Kast, J.; Westermarck, J. Single-step Strep-tag purification for the isolation and identification of protein complexes from mammalian cells. Proteomics 2005, 5, 1199-1203.
    • (2005) Proteomics , vol.5 , pp. 1199-1203
    • Junttila, M.R.1    Saarinen, S.2    Schmidt, T.3    Kast, J.4    Westermarck, J.5
  • 73
    • 0036279153 scopus 로고    scopus 로고
    • Protein interaction verification and functional annotation by integrated analysis of genome-scale data
    • Kemmeren, P.; van Berkum, N. L.; Vilo, J.; Bijma, T.; Donders, R.; Brazma, A.; Holstege, F. C. Protein interaction verification and functional annotation by integrated analysis of genome-scale data. Mol Cell 2002, 9, 1133-1143.
    • (2002) Mol Cell , vol.9 , pp. 1133-1143
    • Kemmeren, P.1    van Berkum, N.L.2    Vilo, J.3    Bijma, T.4    Donders, R.5    Brazma, A.6    Holstege, F.C.7
  • 75
    • 0028073310 scopus 로고
    • An improved affinity tag based on the FLAG peptide for the detection and purification of recombinant antibody fragments
    • Knappik, A.; Plückthun, A. An improved affinity tag based on the FLAG peptide for the detection and purification of recombinant antibody fragments. Biotechniques 1994, 17, 754-761.
    • (1994) Biotechniques , vol.17 , pp. 754-761
    • Knappik, A.1    Plückthun, A.2
  • 76
    • 15944422816 scopus 로고    scopus 로고
    • Double standards in quantitative proteomics: Direct comparative assessment of difference in gel electrophoresis and metabolic stable isotope labeling
    • Kolkman, A.; Dirksen, E. H.; Slijper, M.; Heck, A. J. Double standards in quantitative proteomics: Direct comparative assessment of difference in gel electrophoresis and metabolic stable isotope labeling. Mol Cell Proteomics 2005, 4, 255-266.
    • (2005) Mol Cell Proteomics , vol.4 , pp. 255-266
    • Kolkman, A.1    Dirksen, E.H.2    Slijper, M.3    Heck, A.J.4
  • 77
    • 0026801193 scopus 로고
    • The human leukocyte platelet activating factor receptor
    • Kunz, D.; Gerad, N. P.; Gerad, C. The human leukocyte platelet activating factor receptor. J Biol Chem 1992, 267, 9101-9106.
    • (1992) J Biol Chem , vol.267 , pp. 9101-9106
    • Kunz, D.1    Gerad, N.P.2    Gerad, C.3
  • 78
    • 4444269507 scopus 로고    scopus 로고
    • Prognostic value of combined “triple”-reverse transcription-PCR analysis for prostate-specific antigen, human kallikrein 2, and prostate-specific membrane antigen mRNA in peripheral blood and lymph nodes of prostate cancer patients
    • Kurek, R.; Nunez, G.; Tselis, N.; Konrad, L.; Martin, T.; Roeddiger, S.; Aumüller, G.; Zamboglou, N.; Lin, D. W.; Tunn, U. W.; Renneberg, H. Prognostic value of combined “triple”-reverse transcription-PCR analysis for prostate-specific antigen, human kallikrein 2, and prostate-specific membrane antigen mRNA in peripheral blood and lymph nodes of prostate cancer patients. Clin Cancer Res 2004, 10, 5808-5814.
    • (2004) Clin Cancer Res , vol.10 , pp. 5808-5814
    • Kurek, R.1    Nunez, G.2    Tselis, N.3    Konrad, L.4    Martin, T.5    Roeddiger, S.6    Aumüller, G.7    Zamboglou, N.8    Lin, D.W.9    Tunn, U.W.10    Renneberg, H.11
  • 79
    • 16244390914 scopus 로고    scopus 로고
    • Identification of serum amyloid A as a biomarker to distinguish prostate cancer patients with bone lesions
    • Le, L.; Chi, K.; Tyldesley, S.; Flibotte, S.; Diamond, D. L.; Kuzyk, M. A.; Sadar, M. D. Identification of serum amyloid A as a biomarker to distinguish prostate cancer patients with bone lesions. Clin Chem 2005, 51, 695-707.
    • (2005) Clin Chem , vol.51 , pp. 695-707
    • Le, L.1    Chi, K.2    Tyldesley, S.3    Flibotte, S.4    Diamond, D.L.5    Kuzyk, M.A.6    Sadar, M.D.7
  • 80
    • 3242671815 scopus 로고    scopus 로고
    • Mammalian two-hybrid assay for detecting protein-protein interactions in vivo
    • Lee, J. W.; Lee, S. K. Mammalian two-hybrid assay for detecting protein-protein interactions in vivo. Methods Mol Biol 2004, 261, 327-336.
    • (2004) Methods Mol Biol , vol.261 , pp. 327-336
    • Lee, J.W.1    Lee, S.K.2
  • 82
    • 34147112806 scopus 로고    scopus 로고
    • Regulation of SRC family coactivators by post-translational modifications
    • Li, S.; Shang, Y. Regulation of SRC family coactivators by post-translational modifications. Cell Signal 2007, 19, 1101-1112.
    • (2007) Cell Signal , vol.19 , pp. 1101-1112
    • Li, S.1    Shang, Y.2
  • 83
    • 31544475135 scopus 로고    scopus 로고
    • Proteasome mediated degradation of Id-1 is associated with TNFalpha-induced apoptosis in prostate cancer cells
    • Ling, M. T.; Kwok, W. K.; Fung, M. K.; Xianghong, W.; Wong, Y. C. Proteasome mediated degradation of Id-1 is associated with TNFalpha-induced apoptosis in prostate cancer cells. Carcinogenesis 2006, 27, 205-215.
    • (2006) Carcinogenesis , vol.27 , pp. 205-215
    • Ling, M.T.1    Kwok, W.K.2    Fung, M.K.3    Xianghong, W.4    Wong, Y.C.5
  • 85
    • 0034622925 scopus 로고    scopus 로고
    • Printing proteins as microarrays for high-throughput function determination
    • MacBeath, G.; Schreiber, S. L. Printing proteins as microarrays for high-throughput function determination. Science 2000, 289, 1760-1763.
    • (2000) Science , vol.289 , pp. 1760-1763
    • MacBeath, G.1    Schreiber, S.L.2
  • 87
    • 0033618555 scopus 로고    scopus 로고
    • Detecting protein function and protein-protein interactions from genome sequences
    • Marcotte, E. M.; Pellegrini, M.; Ng, H. L.; Rice, D. W.; Yeates, T. O.; Eisenberg, D. Detecting protein function and protein-protein interactions from genome sequences. Science 1999, 285, 751-753.
    • (1999) Science , vol.285 , pp. 751-753
    • Marcotte, E.M.1    Pellegrini, M.2    Ng, H.L.3    Rice, D.W.4    Yeates, T.O.5    Eisenberg, D.6
  • 88
    • 20644457711 scopus 로고    scopus 로고
    • Insulin-like growth factor 1, chromogranin A and prostate specific antigen serum levels in prostate cancer patients and controls
    • Marszalek, M.; Wachter, J.; Ponholzer, A.; Leitha, T.; Rauchenwald, M.; Madersbacher, S. Insulin-like growth factor 1, chromogranin A and prostate specific antigen serum levels in prostate cancer patients and controls. Eur Urol 2005, 48, 34-39.
    • (2005) Eur Urol , vol.48 , pp. 34-39
    • Marszalek, M.1    Wachter, J.2    Ponholzer, A.3    Leitha, T.4    Rauchenwald, M.5    Madersbacher, S.6
  • 90
    • 1842476014 scopus 로고    scopus 로고
    • Quantitative profiling of LNCaP prostate cancer cells using isotope-coded affinity tags and mass spectrometry
    • Meehan, K. L.; Sadar, M. D. Quantitative profiling of LNCaP prostate cancer cells using isotope-coded affinity tags and mass spectrometry. Proteomics 2004, 4, 1116-1134.
    • (2004) Proteomics , vol.4 , pp. 1116-1134
    • Meehan, K.L.1    Sadar, M.D.2
  • 91
    • 0033915395 scopus 로고    scopus 로고
    • Quantitation of peptides and proteins by matrix-assisted laser desorption/ionization mass spectrometry using (18)O-labeled internal standards
    • Mirgorodskaya, O. A.; Kozmin, Y. P.; Titov, M. I.; Körner, R.; Sönksen, C. P.; Roepstorff, P. Quantitation of peptides and proteins by matrix-assisted laser desorption/ionization mass spectrometry using (18)O-labeled internal standards. Rapid Commun. Mass Spectrom 2000, 14, 1226-1232.
    • (2000) Rapid Commun. Mass Spectrom , vol.14 , pp. 1226-1232
    • Mirgorodskaya, O.A.1    Kozmin, Y.P.2    Titov, M.I.3    Körner, R.4    Sönksen, C.P.5    Roepstorff, P.6
  • 93
    • 0742269685 scopus 로고    scopus 로고
    • Molecular oncology in the post-genomic era: The challenge of proteomics
    • Mocellin, S.; Rossi, C. R.; Traldi, P.; Nitti, D.; Lise, M. Molecular oncology in the post-genomic era: The challenge of proteomics. Trends Mol Med 2004, 10, 24-32.
    • (2004) Trends Mol Med , vol.10 , pp. 24-32
    • Mocellin, S.1    Rossi, C.R.2    Traldi, P.3    Nitti, D.4    Lise, M.5
  • 94
    • 0031812159 scopus 로고    scopus 로고
    • Identification of a novel RING finger protein as a coregulator in steroid receptor-mediated gene transcription
    • Moilanen, A. M.; Poukka, H.; Karvonen, U.; Häkli, M.; Jänne, O. A.; Palvimo, J. J. Identification of a novel RING finger protein as a coregulator in steroid receptor-mediated gene transcription. Mol Cell Biol 1998, 18, 5128-5139.
    • (1998) Mol Cell Biol , vol.18 , pp. 5128-5139
    • Moilanen, A.M.1    Poukka, H.2    Karvonen, U.3    Häkli, M.4    Jänne, O.A.5    Palvimo, J.J.6
  • 95
    • 0002532058 scopus 로고    scopus 로고
    • Current trends in differential expression proteomics: Isotopically coded tags
    • Moseley, M. A. Current trends in differential expression proteomics: Isotopically coded tags. Trends in Biotechnology 2001, 19, S10-16.
    • (2001) Trends in Biotechnology , vol.19 , pp. S10-S16
    • Moseley, M.A.1
  • 96
    • 0035212065 scopus 로고    scopus 로고
    • Is there a bias in proteome research?
    • Mrowka, R.; Patzak, A.; Herzel, H. Is there a bias in proteome research? Genome Res 2001, 11, 1971-1973.
    • (2001) Genome Res , vol.11 , pp. 1971-1973
    • Mrowka, R.1    Patzak, A.2    Herzel, H.3
  • 97
    • 0029814415 scopus 로고    scopus 로고
    • Activation of the human androgen receptor through a protein kinase A signaling pathway
    • Nazareth, L. V.; Weigel, N. L. Activation of the human androgen receptor through a protein kinase A signaling pathway. J Biol Chem 1996, 271, 19900-19907.
    • (1996) J Biol Chem , vol.271 , pp. 19900-19907
    • Nazareth, L.V.1    Weigel, N.L.2
  • 98
    • 33846958453 scopus 로고    scopus 로고
    • Biologic agents as adjunctive therapy for prostate cancer: A rationale for use with androgen deprivation
    • Nelson, E. C.; Cambio, A. J.; Yang, J. C.; Lara, P. N. J.; Evans, C. P. Biologic agents as adjunctive therapy for prostate cancer: A rationale for use with androgen deprivation. Nat Clin Pract Urol 2007, 4, 82-94.
    • (2007) Nat Clin Pract Urol , vol.4 , pp. 82-94
    • Nelson, E.C.1    Cambio, A.J.2    Yang, J.C.3    Lara, P.N.J.4    Evans, C.P.5
  • 99
    • 0016711037 scopus 로고
    • High resolution two-dimensional electrophoresis of proteins
    • O’Farrell, P. H. High resolution two-dimensional electrophoresis of proteins. J Biol Chem 1975, 250, 4007-4021.
    • (1975) J Biol Chem , vol.250 , pp. 4007-4021
    • O’Farrell, P.H.1
  • 100
    • 0036583926 scopus 로고    scopus 로고
    • Stable isotope labeling by amino acids in cell culture, SILAC, as a simple and accurate approach to expression proteomics
    • Ong, S. E.; Blagoev, B.; Kratchmarova, I.; Kristensen, D. B.; Steen, H.; Pandey, A.; Mann, M. Stable isotope labeling by amino acids in cell culture, SILAC, as a simple and accurate approach to expression proteomics. Mol Cell Proteomics 2002, 1, 376-386.
    • (2002) Mol Cell Proteomics , vol.1 , pp. 376-386
    • Ong, S.E.1    Blagoev, B.2    Kratchmarova, I.3    Kristensen, D.B.4    Steen, H.5    Pandey, A.6    Mann, M.7
  • 101
    • 34250372908 scopus 로고    scopus 로고
    • Stable isotope labeling by amino acids in cell culture for quantitative proteomics
    • Ong, S. E.; Mann, M. Stable isotope labeling by amino acids in cell culture for quantitative proteomics. Methods Mol Biol 2007, 359, 37-52.
    • (2007) Methods Mol Biol , vol.359 , pp. 37-52
    • Ong, S.E.1    Mann, M.2
  • 102
    • 0033975643 scopus 로고    scopus 로고
    • Characterization of intracellular prostate-specific antigen from laser capture microdissected benign and malignant prostatic epithelium
    • Ornstein, D. K.; Englert, C.; Gillespie, J. W.; Paweletz, C. P.; Linehan, W. M.; Emmert-Buck, M. R.; Petricoin, E. F. 3rd. Characterization of intracellular prostate-specific antigen from laser capture microdissected benign and malignant prostatic epithelium. Clin Cancer Res 2000, 6, 353-356.
    • (2000) Clin Cancer Res , vol.6 , pp. 353-356
    • Ornstein, D.K.1    Englert, C.2    Gillespie, J.W.3    Paweletz, C.P.4    Linehan, W.M.5    Emmert-Buck, M.R.6    Petricoin, E.F.7
  • 104
    • 33846347711 scopus 로고    scopus 로고
    • The androgen receptor T877A mutant recruits LXXLL and FXXLF peptides differently than wild-type androgen receptor in a time-resolved fluorescence resonance energy transfer assay
    • Ozers, M. S.; Marks, B. D.; Gowda, K.; Kupcho, K. R.; Ervin, K. M.; De Rosier, T.; Qadir, N.; Eliason, H. C.; Riddle, S. M.; Shekhani, M. S. The androgen receptor T877A mutant recruits LXXLL and FXXLF peptides differently than wild-type androgen receptor in a time-resolved fluorescence resonance energy transfer assay. Biochemistry 2007, 46, 683-695.
    • (2007) Biochemistry , vol.46 , pp. 683-695
    • Ozers, M.S.1    Marks, B.D.2    Gowda, K.3    Kupcho, K.R.4    Ervin, K.M.5    De Rosier, T.6    Qadir, N.7    Eliason, H.C.8    Riddle, S.M.9    Shekhani, M.S.10
  • 105
    • 0024780688 scopus 로고
    • Filamentous fusion phage cloning vectors for the study of epitopes and design of vaccines
    • Parmley, S. F.; Smith, G. P. Filamentous fusion phage cloning vectors for the study of epitopes and design of vaccines. Adv Exp Med Biol 1989, 251, 215-218.
    • (1989) Adv Exp Med Biol , vol.251 , pp. 215-218
    • Parmley, S.F.1    Smith, G.P.2
  • 106
    • 20144375228 scopus 로고    scopus 로고
    • Detection of prostate cancer with a blood-based assay for early prostate cancer antigen
    • Paul, B.; Dhir, R.; Landsittel, D.; Hitchens, M. R.; Getzenberg, R. H. Detection of prostate cancer with a blood-based assay for early prostate cancer antigen. Cancer Res 2005, 65, 4097-4100.
    • (2005) Cancer Res , vol.65 , pp. 4097-4100
    • Paul, B.1    Dhir, R.2    Landsittel, D.3    Hitchens, M.R.4    Getzenberg, R.H.5
  • 107
    • 0034969901 scopus 로고    scopus 로고
    • New technologies for biomarker analysis of prostate cancer progression: Laser capture microdissection and tissue proteomics
    • Paweletz, C. P.; Liotta, L. A.; Petricoin, E. F. 3rd. New technologies for biomarker analysis of prostate cancer progression: Laser capture microdissection and tissue proteomics. Urology 2001, 57, 160-163.
    • (2001) Urology , vol.57 , pp. 160-163
    • Paweletz, C.P.1    Liotta, L.A.2    Petricoin, E.F.3
  • 110
    • 13844277017 scopus 로고    scopus 로고
    • New methodologies for measuring protein interactions in vivo and in vitro
    • Piehler, J. New methodologies for measuring protein interactions in vivo and in vitro. Curr Opin Struct Biol 2005, 15, 4-14.
    • (2005) Curr Opin Struct Biol , vol.15 , pp. 4-14
    • Piehler, J.1
  • 112
    • 0034687807 scopus 로고    scopus 로고
    • Covalent modification of the androgen receptor by small ubiquitin-like modifier 1 (SUMO-1)
    • Poukka, H.; Karvonen, U.; Janne, O. A.; Palvimo, J. J. Covalent modification of the androgen receptor by small ubiquitin-like modifier 1 (SUMO-1). Proc Natl Acad Sci USA 2000, 97, 14145-14150.
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 14145-14150
    • Poukka, H.1    Karvonen, U.2    Janne, O.A.3    Palvimo, J.J.4
  • 113
    • 33846000674 scopus 로고    scopus 로고
    • Epidemiology and pathophysiology of prostate cancer in African-American men
    • Powell, I. J. Epidemiology and pathophysiology of prostate cancer in African-American men. J Urol 2007, 177, 444-449.
    • (2007) J Urol , vol.177 , pp. 444-449
    • Powell, I.J.1
  • 114
    • 15244343201 scopus 로고    scopus 로고
    • GST fusion vector with caspase-6 cleavage site for removal of fusion tag during column purification
    • Purbey, P. K.; Jayakumar, P. C.; Deepalakshmi, P. D.; Patole, M. S.; Galande, S. GST fusion vector with caspase-6 cleavage site for removal of fusion tag during column purification. Biotechniques 2005, 38, 360-364.
    • (2005) Biotechniques , vol.38 , pp. 360-364
    • Purbey, P.K.1    Jayakumar, P.C.2    Deepalakshmi, P.D.3    Patole, M.S.4    Galande, S.5
  • 115
    • 23844446718 scopus 로고    scopus 로고
    • Chromatofocusing fractionation and two-dimensional difference gel electrophoresis for low abundance serum proteins
    • Qin, S.; Ferdinand, A. S.; Richie, J. P.; O’Leary, M. P.; Mok, S. C.; Liu, B. C. Chromatofocusing fractionation and two-dimensional difference gel electrophoresis for low abundance serum proteins. Proteomics 2005, 5, 3183-3192.
    • (2005) Proteomics , vol.5 , pp. 3183-3192
    • Qin, S.1    Ferdinand, A.S.2    Richie, J.P.3    Mok, S.C.4    Liu, B.C.5
  • 116
    • 0036791428 scopus 로고    scopus 로고
    • Boosted decision tree analysis of surface-enhanced laser desorption/ion ization mass spectral serum profiles discriminates prostate cancer from noncancer patients
    • Qu, Y.; Adam, B. L.; Yasui, Y.; Ward, M. D.; Cazares, L. H.; Schellhammer, P. F.; Feng, Z.; Semmes, O. J.; Wright, G. L. Jr. Boosted decision tree analysis of surface-enhanced laser desorption/ion ization mass spectral serum profiles discriminates prostate cancer from noncancer patients. Clin Chem 2002, 48, 1835-1843.
    • (2002) Clin Chem , vol.48 , pp. 1835-1843
    • Qu, Y.1    Adam, B.L.2    Yasui, Y.3    Ward, M.D.4    Cazares, L.H.5    Schellhammer, P.F.6    Feng, Z.7    Semmes, O.J.8    Wright, G.L.9
  • 117
    • 33846609681 scopus 로고    scopus 로고
    • Decoy molecules of the androgen receptor block the growth of prostate cancer
    • Quayle, S. N.; Mawji, N. R.; Wang, J.; Sadar, M. D. Decoy molecules of the androgen receptor block the growth of prostate cancer. Proc Natl Acad Sci USA 2007, 104, 1331-1336.
    • (2007) Proc Natl Acad Sci USA , vol.104 , pp. 1331-1336
    • Quayle, S.N.1    Mawji, N.R.2    Wang, J.3    Sadar, M.D.4
  • 118
    • 3242665953 scopus 로고    scopus 로고
    • Cancer proteomics: Serum diagnostics for tumor marker discovery
    • Rai, A. J.; Chan, D. W. Cancer proteomics: Serum diagnostics for tumor marker discovery. Ann N Y Acad Sci 2004, 1022, 286-294.
    • (2004) Ann N Y Acad Sci , vol.1022 , pp. 286-294
    • Rai, A.J.1    Chan, D.W.2
  • 119
    • 3042802392 scopus 로고    scopus 로고
    • Large-scale overproduction, functional purification and ligand affinities of the His-tagged human histamine H1 receptor
    • Ratnala, V. R.; Swarts, H. G.; Van Oostrum, J.; Leurs, R.; De Groot, H. J.; Bakker, R. A.; De Grip, W. J. Large-scale overproduction, functional purification and ligand affinities of the His-tagged human histamine H1 receptor. Eur J Biochem 2004, 271, 2636-2646.
    • (2004) Eur J Biochem , vol.271 , pp. 2636-2646
    • Ratnala, V.R.1    Swarts, H.G.2    Van Oostrum, J.3    Leurs, R.4    De Groot, H.J.5    Bakker, R.A.6    De Grip, W.J.7
  • 120
    • 0037205522 scopus 로고    scopus 로고
    • Conformational analysis of the androgen receptor amino-terminal domain involved in transactivation. Influence of structure-stabilizing solutes and protein-protein interactions
    • Reid, J.; Kelly, S. M.; Watt, K.; Price, N. C.; Mc Ewan, I. J. Conformational analysis of the androgen receptor amino-terminal domain involved in transactivation. Influence of structure-stabilizing solutes and protein-protein interactions. J Biol Chem 2002, 277, 20079-20086.
    • (2002) J Biol Chem , vol.277 , pp. 20079-20086
    • Reid, J.1    Kelly, S.M.2    Watt, K.3    Price, N.C.4    Mc Ewan, I.J.5
  • 123
    • 0035371218 scopus 로고    scopus 로고
    • Phage display selection of peptides that affect prostate carcinoma cells attachment and invasion
    • Romanov, V. I.; Durand, D. B.; Petrenko, V. A. Phage display selection of peptides that affect prostate carcinoma cells attachment and invasion. Prostate 2001, 47, 239-251.
    • (2001) Prostate , vol.47 , pp. 239-251
    • Romanov, V.I.1    Durand, D.B.2    Petrenko, V.A.3
  • 125
    • 33846589692 scopus 로고    scopus 로고
    • Evaluation of an in vitro model of androgen ablation and identification of the androgen responsive proteome in LNCaP cells
    • Rowland, J. G.; Robson, J. L.; Simon, W. J.; Leung, H. Y.; Slabas, A. R. Evaluation of an in vitro model of androgen ablation and identification of the androgen responsive proteome in LNCaP cells. Proteomics 2007, 7, 47-63.
    • (2007) Proteomics , vol.7 , pp. 47-63
    • Rowland, J.G.1    Robson, J.L.2    Simon, W.J.3    Leung, H.Y.4    Slabas, A.R.5
  • 126
    • 0033583317 scopus 로고    scopus 로고
    • Androgen-independent induction of prostate-specific antigen gene expression via cross-talk between the androgen receptor and protein kinase A signal transduction pathways
    • Sadar, M. D. Androgen-independent induction of prostate-specific antigen gene expression via cross-talk between the androgen receptor and protein kinase A signal transduction pathways. J Biol Chem 1999, 274, 7777-7783.
    • (1999) J Biol Chem , vol.274 , pp. 7777-7783
    • Sadar, M.D.1
  • 127
    • 0034667457 scopus 로고    scopus 로고
    • Ligand-independent activation of the androgen receptor by the differentiation agent butyrate in human prostate cancer cells
    • Sadar, M. D.; Gleave, M. E. Ligand-independent activation of the androgen receptor by the differentiation agent butyrate in human prostate cancer cells. Cancer Res 2000, 60, 5825-5831.
    • (2000) Cancer Res , vol.60 , pp. 5825-5831
    • Sadar, M.D.1    Gleave, M.E.2
  • 128
    • 0021320171 scopus 로고
    • A polypeptide fusion designed for purification of recombinant proteins
    • Sassenfeld, H. M.; Brewer, S. J. A polypeptide fusion designed for purification of recombinant proteins. Bio/Technology 1984, 2, 76-81.
    • (1984) Bio/Technology , vol.2 , pp. 76-81
    • Sassenfeld, H.M.1    Brewer, S.J.2
  • 129
    • 0025112794 scopus 로고
    • Searching for peptide ligands with an epitope library
    • Scott, J. K.; Smith, G. P. Searching for peptide ligands with an epitope library. Science 1990, 249, 386-390.
    • (1990) Science , vol.249 , pp. 386-390
    • Scott, J.K.1    Smith, G.P.2
  • 130
    • 3042566944 scopus 로고    scopus 로고
    • An automated method for highthroughput protein purification applied to a comparison of His-tag and GST-tag affinity chromatography
    • Scheich, C.; Sievert, V.; Bussow, K. An automated method for highthroughput protein purification applied to a comparison of His-tag and GST-tag affinity chromatography. BMC. Biotechnol 2003, 3, 12.
    • (2003) BMC. Biotechnol , vol.3 , pp. 12
    • Scheich, C.1    Sievert, V.2    Bussow, K.3
  • 131
    • 0024402266 scopus 로고
    • Two-dimensional protein profiles of cultured stromal and epithelial cells from hyperplastic human prostate
    • Sherwood, E. R.; Berg, L. A.; Mc Ewan, R. N.; Pasciak, R. M.; Kozlowski, J. M.; Lee, C. Two-dimensional protein profiles of cultured stromal and epithelial cells from hyperplastic human prostate. J Cell Biochem 1989, 40, 201-214.
    • (1989) J Cell Biochem , vol.40 , pp. 201-214
    • Sherwood, E.R.1    Berg, L.A.2    Mc Ewan, R.N.3    Pasciak, R.M.4    Kozlowski, J.M.5    Lee, C.6
  • 134
    • 23944463921 scopus 로고    scopus 로고
    • Simulation of large-scale production of a soluble recombinant protein expressed in Escherichia coli using an intein-mediated purification system
    • Sharma, S. S.; Chong, S.; Harcum, S. W. Simulation of large-scale production of a soluble recombinant protein expressed in Escherichia coli using an intein-mediated purification system. Appl Biochem Biotechnol 2005, 126, 93-118.
    • (2005) Appl Biochem Biotechnol , vol.126 , pp. 93-118
    • Sharma, S.S.1    Chong, S.2    Harcum, S.W.3
  • 135
    • 0033814033 scopus 로고    scopus 로고
    • Use of the Strep-tag and streptavidin for detection and purification of recombinant proteins
    • Skerra, A.; Schmidt, T. G. M. Use of the Strep-tag and streptavidin for detection and purification of recombinant proteins. Methods Enzymol 2000, 326, 271-304.
    • (2000) Methods Enzymol , vol.326 , pp. 271-304
    • Skerra, A.1    Schmidt, T.G.M.2
  • 136
    • 33847659368 scopus 로고    scopus 로고
    • Identification of new tag sequences with differential and selective recognition properties for the anti-FLAG monoclonal antibodies M1, M2 and M5
    • Slootstra, J. W.; Kuperus, D.; Pluckthun, A.; Meloen, R. H. Identification of new tag sequences with differential and selective recognition properties for the anti-FLAG monoclonal antibodies M1, M2 and M5. Mol Divers 1997, 2, 156-164.
    • (1997) Mol Divers , vol.2 , pp. 156-164
    • Slootstra, J.W.1    Kuperus, D.2    Pluckthun, A.3    Meloen, R.H.4
  • 139
    • 13944264638 scopus 로고    scopus 로고
    • Three-dimensional structure-activity relationships of nonsteroidal ligands in complex with androgen receptor ligand-binding domain
    • Söderholm, A. A.; Lehtovuori, P. T.; Nyrönen, T. H. Three-dimensional structure-activity relationships of nonsteroidal ligands in complex with androgen receptor ligand-binding domain. J Med Chem 2005, 48, 917-925.
    • (2005) J Med Chem , vol.48 , pp. 917-925
    • Söderholm, A.A.1    Lehtovuori, P.T.2    Nyrönen, T.H.3
  • 142
    • 26244443933 scopus 로고    scopus 로고
    • Two-dimensional gel isoelectric focusing
    • Stastná, M.; Slais, K. Two-dimensional gel isoelectric focusing. Electrophoresis 2005, 26, 3586-3591.
    • (2005) Electrophoresis , vol.26 , pp. 3586-3591
    • Stastná, M.1    Slais, K.2
  • 143
    • 0033730301 scopus 로고    scopus 로고
    • Molecular forms of prostate-specific antigen and human kallikrein 2 as promising tools for early diagnosis of prostate cancer
    • Stephan, C.; Jung, K.; Lein, M.; Sinha, P.; Schnorr, D.; Loening, S. A. Molecular forms of prostate-specific antigen and human kallikrein 2 as promising tools for early diagnosis of prostate cancer. Cancer Epidemiol Biomarkers Prev 2000, 9, 1133-1147.
    • (2000) Cancer Epidemiol Biomarkers Prev , vol.9 , pp. 1133-1147
    • Stephan, C.1    Jung, K.2    Lein, M.3    Sinha, P.4    Schnorr, D.5    Loening, S.A.6
  • 144
    • 33645458299 scopus 로고    scopus 로고
    • Serum human glandular kallikrein 2 (hK2) for distinguishing stage and grade of prostate cancer
    • Stephan, C.; Jung, K.; Nakamura, T.; Yousef, G. M.; Kristiansen, G.; Diamandis, E. P. Serum human glandular kallikrein 2 (hK2) for distinguishing stage and grade of prostate cancer. Int J Urol 2006, 13, 238-243.
    • (2006) Int J Urol , vol.13 , pp. 238-243
    • Stephan, C.1    Jung, K.2    Nakamura, T.3    Yousef, G.M.4    Kristiansen, G.5    Diamandis, E.P.6
  • 145
    • 0034303493 scopus 로고    scopus 로고
    • The use of yeast two-hybrid screens in studies of protein: Protein interactions involved in trafficking
    • Stephens, D. J.; Banting, G. The use of yeast two-hybrid screens in studies of protein:protein interactions involved in trafficking. Traffic 2000, 1, 763-768.
    • (2000) Traffic , vol.1 , pp. 763-768
    • Stephens, D.J.1    Banting, G.2
  • 147
    • 0026577811 scopus 로고
    • A single step purification for recombinant proteins
    • Stofko-Hahn, R. E.; Carr, D. W.; Scott, J. D. A single step purification for recombinant proteins. FEBS Lett 1992, 302, 274-278.
    • (1992) FEBS Lett , vol.302 , pp. 274-278
    • Stofko-Hahn, R.E.1    Carr, D.W.2    Scott, J.D.3
  • 148
    • 33748763282 scopus 로고    scopus 로고
    • Structural basis for androgen receptor agonists and antagonists: Interaction of SPEED 98-listed chemicals and related compounds with the androgen receptor based on an in vitro reporter gene assay and 3D-QSAR
    • Tamura, H.; Ishimoto, Y.; Fujikawa, T.; Aoyama, H.; Yoshikawa, H.; Akamatsu, M. Structural basis for androgen receptor agonists and antagonists: Interaction of SPEED 98-listed chemicals and related compounds with the androgen receptor based on an in vitro reporter gene assay and 3D-QSAR. Bioorg Med Chem 2006, 14, 7160-7174.
    • (2006) Bioorg Med Chem , vol.14 , pp. 7160-7174
    • Tamura, H.1    Ishimoto, Y.2    Fujikawa, T.3    Aoyama, H.4    Yoshikawa, H.5    Akamatsu, M.6
  • 149
    • 0037255597 scopus 로고    scopus 로고
    • Overview of tag protein fusions: From molecular and biochemical fundamentals to commercial systems
    • Terpe, K. Overview of tag protein fusions: From molecular and biochemical fundamentals to commercial systems. Appl Microbiol Biotechnol 2003, 60, 523-533.
    • (2003) Appl Microbiol Biotechnol , vol.60 , pp. 523-533
    • Terpe, K.1
  • 151
    • 0034847625 scopus 로고    scopus 로고
    • Using the yeast interaction trap and other two-hybrid-based approaches to study protein-protein interactions
    • Toby, G. G.; Golemis, E. A. Using the yeast interaction trap and other two-hybrid-based approaches to study protein-protein interactions. Methods 2001, 24, 201-217.
    • (2001) Methods , vol.24 , pp. 201-217
    • Toby, G.G.1    Golemis, E.A.2
  • 152
    • 0029154151 scopus 로고
    • Detection and characterization of the prostate-specific membrane antigen (PSMA) in tissue extracts and body fluids
    • Troyer, J. K.; Beckett, M. L.; Wright, G. L. Jr. Detection and characterization of the prostate-specific membrane antigen (PSMA) in tissue extracts and body fluids. Int J Cancer 1995, 62, 552-558.
    • (1995) Int J Cancer , vol.62 , pp. 552-558
    • Troyer, J.K.1    Beckett, M.L.2    Wright, G.L.3
  • 153
    • 0034597674 scopus 로고    scopus 로고
    • Combined transformation and genetic technique verification of protein-protein interactions in the yeast two-hybrid system
    • Tyagi, S.; Lal, S. K. Combined transformation and genetic technique verification of protein-protein interactions in the yeast two-hybrid system. Biochem Biophys Res Commun 2000, 277, 589-593.
    • (2000) Biochem Biophys Res Commun , vol.277 , pp. 589-593
    • Tyagi, S.1    Lal, S.K.2
  • 154
    • 0037064106 scopus 로고    scopus 로고
    • Ligand-independent activation of the androgen receptor by interleukin-6 and the role of steroid receptor coactivator-1 in prostate cancer cells
    • Ueda, T.; Mawji, N. R.; Bruchovsky, N.; Sadar, M. D. Ligand-independent activation of the androgen receptor by interleukin-6 and the role of steroid receptor coactivator-1 in prostate cancer cells. J Biol Chem 2002a, 277, 38087-38094.
    • (2002) J Biol Chem , vol.277 , pp. 38087-38094
    • Ueda, T.1    Mawji, N.R.2    Bruchovsky, N.3    Sadar, M.D.4
  • 155
    • 0036510548 scopus 로고    scopus 로고
    • Activation of the androgen receptor N-terminal domain by interleukin-6 via MAPK and STAT3 signal transduction pathways
    • Ueda, T.; Bruchovsky, N.; Sadar, M. D. Activation of the androgen receptor N-terminal domain by interleukin-6 via MAPK and STAT3 signal transduction pathways. J Biol Chem 2002b, 277, 7076-7085.
    • (2002) J Biol Chem , vol.277 , pp. 7076-7085
    • Ueda, T.1    Bruchovsky, N.2    Sadar, M.D.3
  • 157
    • 0343376097 scopus 로고    scopus 로고
    • Difference gel electrophoresis: A single gel method for detecting changes in protein extracts
    • Unlü, M.; Morgan, M. E.; Minden, J. S. Difference gel electrophoresis: A single gel method for detecting changes in protein extracts. Electrophoresis 1997, 18, 2071-2077.
    • (1997) Electrophoresis , vol.18 , pp. 2071-2077
    • Unlü, M.1    Morgan, M.E.2    Minden, J.S.3
  • 159
    • 0036632368 scopus 로고    scopus 로고
    • The phosphatidylinositol 3-kinase AKT pathway in human cancer
    • Vivanco, I.; Sawyers, C. L. The phosphatidylinositol 3-kinase AKT pathway in human cancer. Nat Rev Cancer 2002, 2, 489-501.
    • (2002) Nat Rev Cancer , vol.2 , pp. 489-501
    • Vivanco, I.1    Sawyers, C.L.2
  • 160
    • 33645986960 scopus 로고    scopus 로고
    • Amino-terminus domain of the androgen receptor as a molecular target to prevent the hormonal progression of prostate cancer
    • Wang, G.; Sadar, M. D. Amino-terminus domain of the androgen receptor as a molecular target to prevent the hormonal progression of prostate cancer. J Cell Biochem 2006, 98, 36-53.
    • (2006) J Cell Biochem , vol.98 , pp. 36-53
    • Wang, G.1    Sadar, M.D.2
  • 162
    • 0035413269 scopus 로고    scopus 로고
    • Inverse 18O labeling mass spectrometry for the rapid identification of marker/target proteins
    • Wang, Y. K.; Ma, Z.; Quinn, D. F.; Fu, E. W. Inverse 18O labeling mass spectrometry for the rapid identification of marker/target proteins. Anal Chem 2001, 73, 3742-3750.
    • (2001) Anal Chem , vol.73 , pp. 3742-3750
    • Wang, Y.K.1    Ma, Z.2    Quinn, D.F.3    Fu, E.W.4
  • 163
    • 0035106351 scopus 로고    scopus 로고
    • Large-scale analysis of the yeast proteome by multidimensional protein identification technology
    • Washburn, M. P.; Wolters, D.; Yates, J. R. 3rd. Large-scale analysis of the yeast proteome by multidimensional protein identification technology. Nat Biotechnol 2001, 19, 242-247.
    • (2001) Nat Biotechnol , vol.19 , pp. 242-247
    • Washburn, M.P.1    Wolters, D.2    Yates, J.R.3
  • 165
    • 0035957374 scopus 로고    scopus 로고
    • The use of mRNA display to select high-affinity protein-binding peptides
    • Wilson, D. S.; Keefe, A. D.; Szostak, J. W. The use of mRNA display to select high-affinity protein-binding peptides. Proc Natl Acad Sci USA 2001, 98, 3750-3755.
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 3750-3755
    • Wilson, D.S.1    Keefe, A.D.2    Szostak, J.W.3
  • 166
    • 7044279162 scopus 로고    scopus 로고
    • Rapid one step protein purification from plant material using the eight-amino acid StrepII epitope
    • Witte, C. P.; Noel, L. D.; Gielbert, J.; Parker, J. E.; Romeis, T. Rapid one step protein purification from plant material using the eight-amino acid StrepII epitope. Plant Mol Biol 2004, 55, 135-147.
    • (2004) Plant Mol Biol , vol.55 , pp. 135-147
    • Witte, C.P.1    Noel, L.D.2    Gielbert, J.3    Parker, J.E.4    Romeis, T.5
  • 167
    • 33947608608 scopus 로고    scopus 로고
    • A novel variant of the putative demethylase gene, s-JMJD1C, is a coactivator of the AR
    • Wolf, S. S.; Patchev, V. K.; Obendorf, M. A novel variant of the putative demethylase gene, s-JMJD1C, is a coactivator of the AR. Arch Biochem Biophys 2007, 460, 56-66.
    • (2007) Arch Biochem Biophys , vol.460 , pp. 56-66
    • Wolf, S.S.1    Patchev, V.K.2    Obendorf, M.3
  • 168
    • 0035582244 scopus 로고    scopus 로고
    • An automated multidimensional protein identification technology for shotgun proteomics
    • Wolters, D. A.; Washburn, M. P.; Yates, J. R. 3rd. An automated multidimensional protein identification technology for shotgun proteomics. Anal Chem 2001, 73, 5683-5690.
    • (2001) Anal Chem , vol.73 , pp. 5683-5690
    • Wolters, D.A.1    Washburn, M.P.2    Yates, J.R.3
  • 170
    • 0011063449 scopus 로고    scopus 로고
    • Proteinchip(R) surface enhanced laser desorption/ionization (SELDI) mass spectrometry: A novel protein biochip technology for detection of prostate cancer biomarkers in complex protein mixtures
    • Wright, G. W.; Cazares, L. H.; Leung, S. M.; Nasim, S.; Adam, B. L.; Yip, T. T.; Schellhammer, P. F.; Gong, L.; Vlahou, A. Proteinchip(R) surface enhanced laser desorption/ionization (SELDI) mass spectrometry: A novel protein biochip technology for detection of prostate cancer biomarkers in complex protein mixtures. Prostate Cancer Prostatic Dis 1999, 2, 264-276.
    • (1999) Prostate Cancer Prostatic Dis , vol.2 , pp. 264-276
    • Wright, G.W.1    Cazares, L.H.2    Leung, S.M.3    Nasim, S.4    Adam, B.L.5    Yip, T.T.6    Schellhammer, P.F.7    Gong, L.8    Vlahou, A.9
  • 171
    • 1442329650 scopus 로고    scopus 로고
    • Identification of androgen-coregulated protein networks from the microsomes of human prostate cancer cells
    • Wright, M. E.; Eng, J.; Sherman, J.; Hockenbery, D. M.; Nelson, P. S.; Galitski, T.; Aebersold, R. Identification of androgen-coregulated protein networks from the microsomes of human prostate cancer cells. Genome Biol 2003, 5, R4.
    • (2003) Genome Biol , vol.5 , pp. R4
    • Wright, M.E.1    Eng, J.2    Sherman, J.3    Hockenbery, D.M.4    Nelson, P.S.5    Galitski, T.6    Aebersold, R.7
  • 172
    • 34249796386 scopus 로고    scopus 로고
    • Ubiquitin-like protein modifications in prostate and breast cancer
    • Wu, F.; Mo, Y. Y. Ubiquitin-like protein modifications in prostate and breast cancer. Front Biosci 2007, 12, 700-711.
    • (2007) Front Biosci , vol.12 , pp. 700-711
    • Wu, F.1    Mo, Y.Y.2
  • 173
    • 0033776083 scopus 로고    scopus 로고
    • Identification of novel prostate-specific antigen-binding peptides modulating its enzyme activity
    • Wu, P.; Leinonen, J.; Koivunen, E.; Lankinen, H.; Stenman, U. H. Identification of novel prostate-specific antigen-binding peptides modulating its enzyme activity. Eur J Biochem 2000, 267, 6212-6220.
    • (2000) Eur J Biochem , vol.267 , pp. 6212-6220
    • Wu, P.1    Leinonen, J.2    Koivunen, E.3    Lankinen, H.4    Stenman, U.H.5
  • 174
    • 0034564363 scopus 로고    scopus 로고
    • Androgen receptor isoforms in human and rat prostate
    • Xia, S. J.; Hao, G. Y.; Tang, X. D. Androgen receptor isoforms in human and rat prostate. Asian J Androl 2000, 2, 307-310.
    • (2000) Asian J Androl , vol.2 , pp. 307-310
    • Xia, S.J.1    Hao, G.Y.2    Tang, X.D.3
  • 175
    • 21744455695 scopus 로고    scopus 로고
    • Role of mitogen-activated protein kinases in phenethyl isothiocyanate-induced apoptosis in human prostate cancer cells
    • Xiao, D.; Choi, S.; Lee, Y. J.; Singh, S. V. Role of mitogen-activated protein kinases in phenethyl isothiocyanate-induced apoptosis in human prostate cancer cells. Mol Carcinog 2005, 43, 130-140.
    • (2005) Mol Carcinog , vol.43 , pp. 130-140
    • Xiao, D.1    Choi, S.2    Lee, Y.J.3    Singh, S.V.4
  • 176
    • 0034042053 scopus 로고    scopus 로고
    • Generation of a baculovirus recombinant prostate-specific membrane antigen and its use in the development of a novel protein biochip quantitative immunoassay
    • Xiao, Z.; Jiang, X.; Beckett, M.; Wright, G. L. Jr. Generation of a baculovirus recombinant prostate-specific membrane antigen and its use in the development of a novel protein biochip quantitative immunoassay. Prot Expression Purif 2000, 19, 12-21.
    • (2000) Prot Expression Purif , vol.19 , pp. 12-21
    • Xiao, Z.1    Jiang, X.2    Beckett, M.3    Wright, G.L.4
  • 177
    • 0036261635 scopus 로고    scopus 로고
    • Heavy metal removal by novel CBD-EC20 sorbents immobilized on cellulose
    • Xu, Z.; Bae, W.; Mulchandani, A.; Mehra, R. K.; Chen, W. Heavy metal removal by novel CBD-EC20 sorbents immobilized on cellulose. Biomacromolecules 2002, 3, 462-465.
    • (2002) Biomacromolecules , vol.3 , pp. 462-465
    • Xu, Z.1    Bae, W.2    Mulchandani, A.3    Mehra, R.K.4    Chen, W.5
  • 178
    • 19444363756 scopus 로고    scopus 로고
    • Mass spectrometry-based quantitative proteomic profiling
    • Yan, W.; Chen, S. S. Mass spectrometry-based quantitative proteomic profiling. Brief Funct Genomic Proteomic 2005, 4, 27-38.
    • (2005) Brief Funct Genomic Proteomic , vol.4 , pp. 27-38
    • Yan, W.1    Chen, S.S.2
  • 179
    • 0035384687 scopus 로고    scopus 로고
    • Proteolytic 18O labeling for comparative proteomics: Model studies with two serotypes of adenovirus
    • Yao, X.; Freas, A.; Ramirez, J.; Demirev, P. A.; Fenselau, C. Proteolytic 18O labeling for comparative proteomics: Model studies with two serotypes of adenovirus. Anal Chem 2004, 73, 2836-2842.
    • (2004) Anal Chem , vol.73 , pp. 2836-2842
    • Yao, X.1    Freas, A.2    Ramirez, J.3    Demirev, P.A.4    Fenselau, C.5
  • 180
    • 0029951486 scopus 로고    scopus 로고
    • Cloning and characterization of a specific coactivator, ARA70, for the androgen receptor in human prostate cells
    • Yeh, S.; Chang, C. Cloning and characterization of a specific coactivator, ARA70, for the androgen receptor in human prostate cells. Proc Natl Acad Sci USA 1996, 93, 5517-5521.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 5517-5521
    • Yeh, S.1    Chang, C.2
  • 181
    • 0032551749 scopus 로고    scopus 로고
    • Retinoblastoma, a tumor suppressor, is a coactivator for the androgen receptor in human prostate cancer DU145 cells
    • Yeh, S.; Miyamoto, H.; Nishimura, K.; Kang, H.; Ludlow, J.; Hsiao, P.; Wang, C.; Su, C.; Chang, C. Retinoblastoma, a tumor suppressor, is a coactivator for the androgen receptor in human prostate cancer DU145 cells. Biochem Biophys Res Commun 1998, 248, 361-367.
    • (1998) Biochem Biophys Res Commun , vol.248 , pp. 361-367
    • Yeh, S.1    Miyamoto, H.2    Nishimura, K.3    Kang, H.4    Ludlow, J.5    Hsiao, P.6    Wang, C.7    Su, C.8    Chang, C.9
  • 182
    • 20944444686 scopus 로고    scopus 로고
    • Increased quantitative proteome coverage with (13)C/(12)C-based, acid-cleavable isotope-coded affinity tag reagent and modified data acquisition scheme
    • Yi, E. C.; Li, X. J.; Cooke, K.; Lee, H.; Raught, B.; Page, A.; Aneliunas, V.; Hieter, P.; Goodlett, D. R.; Aebersold, R. Increased quantitative proteome coverage with (13)C/(12)C-based, acid-cleavable isotope-coded affinity tag reagent and modified data acquisition scheme. Proteomics 2005, 5, 380-387.
    • (2005) Proteomics , vol.5 , pp. 380-387
    • Yi, E.C.1    Li, X.J.2    Cooke, K.3    Lee, H.4    Raught, B.5    Page, A.6    Aneliunas, V.7    Hieter, P.8    Goodlett, D.R.9    Aebersold, R.10
  • 183
  • 184
    • 0034735569 scopus 로고    scopus 로고
    • Akt regulates cell survival and apoptosis at a postmitochondrial level
    • Zhou, H.; Li, X. M.; Meinkoth, J.; Pittman, R. N. Akt regulates cell survival and apoptosis at a postmitochondrial level. J Cell Biol 2000, 151, 483-494.
    • (2000) J Cell Biol , vol.151 , pp. 483-494
    • Zhou, H.1    Li, X.M.2    Meinkoth, J.3    Pittman, R.N.4
  • 185
    • 0029041681 scopus 로고
    • Identification of three proline-directed phosphorylation sites in the human androgen receptor
    • Zhou, Z. X.; Kemppainen, J. A.; Wilson, E. M. Identification of three proline-directed phosphorylation sites in the human androgen receptor. Mol Endocrinol 1995, 9, 605-615.
    • (1995) Mol Endocrinol , vol.9 , pp. 605-615
    • Zhou, Z.X.1    Kemppainen, J.A.2    Wilson, E.M.3
  • 187


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