메뉴 건너뛰기




Volumn 45, Issue 6, 2006, Pages 643-661

Frozen tissue biobanks. Tissue handling, cryopreservation, extraction, and use for proteomic analysis

Author keywords

[No Author keywords available]

Indexed keywords

PROTEOME;

EID: 33748636268     PISSN: 0284186X     EISSN: 1651226X     Source Type: Journal    
DOI: 10.1080/02841860600818047     Document Type: Review
Times cited : (43)

References (95)
  • 2
    • 0344306381 scopus 로고    scopus 로고
    • Proteomic applications for differential diagnosis of histologically identical tumors
    • Vortmeyer AO, Weil RJ, Zhuang Z. Proteomic applications for differential diagnosis of histologically identical tumors. Neurology 2003;61:1626-7.
    • (2003) Neurology , vol.61 , pp. 1626-1627
    • Vortmeyer, A.O.1    Weil, R.J.2    Zhuang, Z.3
  • 3
    • 33748667390 scopus 로고    scopus 로고
    • Oncogenic pathway signatures in human cancers as a guide to targeted therapies
    • Bild AH, Yao G, Chang JT, Wang Q, Potti A, Chasse D, et al. Oncogenic pathway signatures in human cancers as a guide to targeted therapies. Nature 2005.
    • (2005) Nature
    • Bild, A.H.1    Yao, G.2    Chang, J.T.3    Wang, Q.4    Potti, A.5    Chasse, D.6
  • 4
    • 0001644020 scopus 로고    scopus 로고
    • The human plasma proteome: History, character, and diagnostic prospects
    • Anderson NL, Anderson NG. The human plasma proteome: History, character, and diagnostic prospects. Mol Cell Proteomics 2002;1:845-67.
    • (2002) Mol Cell Proteomics , vol.1 , pp. 845-867
    • Anderson, N.L.1    Anderson, N.G.2
  • 5
    • 0036408225 scopus 로고    scopus 로고
    • Use of laser capture microdissection to selectively obtain distinct populations of cells for proteomic analysis
    • Craven RA, Banks RE. Use of laser capture microdissection to selectively obtain distinct populations of cells for proteomic analysis. Methods Enzymol 2002;356:33-49.
    • (2002) Methods Enzymol , vol.356 , pp. 33-49
    • Craven, R.A.1    Banks, R.E.2
  • 6
    • 0027485292 scopus 로고
    • Nonenzymatic extraction of cells from clinical tumor material for analysis of gene expression by two-dimensional polyacrylamide gel electrophoresis
    • Franzen B, Linder S, Okuzawa K, Kato H, Auer G. Nonenzymatic extraction of cells from clinical tumor material for analysis of gene expression by two-dimensional polyacrylamide gel electrophoresis. Electrophoresis 1993; 14:1045-53.
    • (1993) Electrophoresis , vol.14 , pp. 1045-1053
    • Franzen, B.1    Linder, S.2    Okuzawa, K.3    Kato, H.4    Auer, G.5
  • 7
    • 1642579024 scopus 로고    scopus 로고
    • The Human Proteome Organization Plasma Proteome Project pilot phase: Reference specimens, technology platform comparisons, and standardized data submissions and analyses
    • Omenn GS. The Human Proteome Organization Plasma Proteome Project pilot phase: Reference specimens, technology platform comparisons, and standardized data submissions and analyses. Proteomics 2004;4:1235-40.
    • (2004) Proteomics , vol.4 , pp. 1235-1240
    • Omenn, G.S.1
  • 8
    • 23944492134 scopus 로고    scopus 로고
    • Overview of the HUPO Plasma Proteome Project: Results from the pilot phase with 35 collaborating laboratories and multiple analytical groups, generating a core dataset of 3020 proteins and a publicly-available database
    • Omenn GS, States DJ, Adamski M, Blackwell TW, Menon R, Hermjakob H, et al. Overview of the HUPO Plasma Proteome Project: Results from the pilot phase with 35 collaborating laboratories and multiple analytical groups, generating a core dataset of 3020 proteins and a publicly-available database. Proteomics 2005;5:3226-45.
    • (2005) Proteomics , vol.5 , pp. 3226-3245
    • Omenn, G.S.1    States, D.J.2    Adamski, M.3    Blackwell, T.W.4    Menon, R.5    Hermjakob, H.6
  • 9
    • 24144432109 scopus 로고    scopus 로고
    • Influences of blood sample processing on low-molecular-weight proteome identified by surface-enhanced laser desorption/ionization mass spectrometry
    • Banks RE, Stanley AJ, Cairns DA, Barret JH, Clarke PC, Thompson D, et al. Influences of blood sample processing on low-molecular-weight proteome identified by surface-enhanced laser desorption/ionization mass spectrometry. Clin Chem 2005;51:1637-49.
    • (2005) Clin Chem , vol.51 , pp. 1637-1649
    • Banks, R.E.1    Stanley, A.J.2    Cairns, D.A.3    Barret, J.H.4    Clarke, P.C.5    Thompson, D.6
  • 10
    • 4344576101 scopus 로고    scopus 로고
    • An investigation of plasma collection, stabilization, and storage procedures for proteomic analysis of clinical samples
    • Hulmes JD, Bethea D, Ho K, Huang S-P, Ricci DL, Opiteck GJ, et al. An investigation of plasma collection, stabilization, and storage procedures for proteomic analysis of clinical samples. Clin Proteomics J 2004;1:17-31.
    • (2004) Clin Proteomics J , vol.1 , pp. 17-31
    • Hulmes, J.D.1    Bethea, D.2    Ho, K.3    Huang, S.-P.4    Ricci, D.L.5    Opiteck, G.J.6
  • 11
    • 23944520883 scopus 로고    scopus 로고
    • HUPO Plasma Proteome Project specimen collection and handling: Towards the standardization of parameters for plasma proteome samples
    • Rai AJ, Gelfand CA, Haywood BC, Warunek DJ, Yi J, Schuchard MD, et al. HUPO Plasma Proteome Project specimen collection and handling: Towards the standardization of parameters for plasma proteome samples. Proteomics 2005;5:3262-77.
    • (2005) Proteomics , vol.5 , pp. 3262-3277
    • Rai, A.J.1    Gelfand, C.A.2    Haywood, B.C.3    Warunek, D.J.4    Yi, J.5    Schuchard, M.D.6
  • 12
    • 23944470664 scopus 로고    scopus 로고
    • Peptidomic analysis of human blood specimens: Comparison between plasma specimens and serum by differential peptide display
    • Tammen H, Schulte I, Hess R, Menzel C, Kellmann M, Mohring T, et al. Peptidomic analysis of human blood specimens: Comparison between plasma specimens and serum by differential peptide display. Proteomics 2005;5:3414-22.
    • (2005) Proteomics , vol.5 , pp. 3414-3422
    • Tammen, H.1    Schulte, I.2    Hess, R.3    Menzel, C.4    Kellmann, M.5    Mohring, T.6
  • 14
    • 12444339443 scopus 로고    scopus 로고
    • The human serum proteome: Display of nearly 3700 chromatographically separated protein spots on two-dimensional electrophoresis gels and identification of 325 distinct proteins
    • Pieper R, Gatlin CL, Makusky AJ, Russo PS, Schatz CR, Miller SS, et al. The human serum proteome: Display of nearly 3700 chromatographically separated protein spots on two-dimensional electrophoresis gels and identification of 325 distinct proteins. Proteomics 2003;3:1345-64.
    • (2003) Proteomics , vol.3 , pp. 1345-1364
    • Pieper, R.1    Gatlin, C.L.2    Makusky, A.J.3    Russo, P.S.4    Schatz, C.R.5    Miller, S.S.6
  • 19
    • 0035106351 scopus 로고    scopus 로고
    • Large-scale analysis of the yeast proteome by multidimensional protein identification technology
    • rd. Large-scale analysis of the yeast proteome by multidimensional protein identification technology. Nat Biotechnol 2001;19:242-7.
    • (2001) Nat Biotechnol , vol.19 , pp. 242-247
    • Washburn, M.P.1    Wolters, D.2    Yates III, J.R.3
  • 20
    • 0037277179 scopus 로고    scopus 로고
    • Evaluation of multidimensional chromatography coupled with tandem mass spectrometry (LC/LC-MS/MS) for large-scale protein analysis: The yeast proteome
    • Peng J, Elias JE, Thoreen CC, Licklider LJ, Gygi SP. Evaluation of multidimensional chromatography coupled with tandem mass spectrometry (LC/LC-MS/MS) for large-scale protein analysis: The yeast proteome. J Proteome Res 2003;2:43-50.
    • (2003) J Proteome Res , vol.2 , pp. 43-50
    • Peng, J.1    Elias, J.E.2    Thoreen, C.C.3    Licklider, L.J.4    Gygi, S.P.5
  • 23
    • 4444311058 scopus 로고    scopus 로고
    • A human proteome project with a beginning and an end
    • Humphery-Smith I. A human proteome project with a beginning and an end. Proteomics 2004;4:2519-21.
    • (2004) Proteomics , vol.4 , pp. 2519-2521
    • Humphery-Smith, I.1
  • 24
    • 28444433078 scopus 로고    scopus 로고
    • Towards a human proteome atlas: High-throughput generation of mono-specific antibodies for tissue profiling
    • Nilsson P, Paavilainen L, Larsson K, Odling J, Sundberg M, Andersson AC, et al. Towards a human proteome atlas: High-throughput generation of mono-specific antibodies for tissue profiling. Proteomics 2005.
    • (2005) Proteomics
    • Nilsson, P.1    Paavilainen, L.2    Larsson, K.3    Odling, J.4    Sundberg, M.5    Andersson, A.C.6
  • 25
    • 17844396912 scopus 로고    scopus 로고
    • Antibody-based proteomics for human tissue profiling
    • Uhlen M, Ponten F. Antibody-based proteomics for human tissue profiling. Mol Cell Proteomics 2005;4:384-93.
    • (2005) Mol Cell Proteomics , vol.4 , pp. 384-393
    • Uhlen, M.1    Ponten, F.2
  • 29
    • 0037647196 scopus 로고    scopus 로고
    • An overview of the protein tyrosine phosphatase superfamily
    • Wang WQ, Sun JP, Zhang ZY. An overview of the protein tyrosine phosphatase superfamily. Curr Top Med Chem 2003;3:739-48.
    • (2003) Curr Top Med Chem , vol.3 , pp. 739-748
    • Wang, W.Q.1    Sun, J.P.2    Zhang, Z.Y.3
  • 30
    • 0037075845 scopus 로고    scopus 로고
    • Serine-threonine protein phosphatase inhibitors: Development of potential therapeutic strategies
    • McCluskey A, Sim AT, Sakoff JA. Serine-threonine protein phosphatase inhibitors: Development of potential therapeutic strategies. J Med Chem 2002;45:1151-75.
    • (2002) J Med Chem , vol.45 , pp. 1151-1175
    • McCluskey, A.1    Sim, A.T.2    Sakoff, J.A.3
  • 31
    • 0036032778 scopus 로고    scopus 로고
    • Regulators of serine/threonine protein phosphatases at the dawn of a clinical era?
    • Honkanen RE, Golden T. Regulators of serine/threonine protein phosphatases at the dawn of a clinical era? Curr Med Chem 2002;9:2055-75.
    • (2002) Curr Med Chem , vol.9 , pp. 2055-2075
    • Honkanen, R.E.1    Golden, T.2
  • 32
    • 0142040631 scopus 로고    scopus 로고
    • Phosphoprotein isotope-coded solid-phase tag approach for enrichment and quantitative analysis of phosphopeptides from complex mixtures
    • Qian WJ, Goshe MB, Camp DG, 2nd, Yu LR, Tang K, Smith RD. Phosphoprotein isotope-coded solid-phase tag approach for enrichment and quantitative analysis of phosphopeptides from complex mixtures. Anal Chem 2003;75:5441-50.
    • (2003) Anal Chem , vol.75 , pp. 5441-5450
    • Qian, W.J.1    Goshe, M.B.2    Camp II, D.G.3    Yu, L.R.4    Tang, K.5    Smith, R.D.6
  • 34
    • 0028232354 scopus 로고
    • Analysis of cellular phosphoproteins by two-dimensional gel electrophoresis: Applications for cell signaling in normal and cancer cells
    • Guy GR, Philip R, Tan YH. Analysis of cellular phosphoproteins by two-dimensional gel electrophoresis: Applications for cell signaling in normal and cancer cells. Electrophoresis 1994;15:417-40.
    • (1994) Electrophoresis , vol.15 , pp. 417-440
    • Guy, G.R.1    Philip, R.2    Tan, Y.H.3
  • 35
    • 0242608354 scopus 로고    scopus 로고
    • Signal pathway profiling of ovarian cancer from human tissue specimens using reverse-phase protein microarrays
    • Wulfkuhle JD, Aquino JA, Calvert VS, Fishman DA, Coukos G, Liotta LA, et al. Signal pathway profiling of ovarian cancer from human tissue specimens using reverse-phase protein microarrays. Proteomics 2003;3:2085-90.
    • (2003) Proteomics , vol.3 , pp. 2085-2090
    • Wulfkuhle, J.D.1    Aquino, J.A.2    Calvert, V.S.3    Fishman, D.A.4    Coukos, G.5    Liotta, L.A.6
  • 37
    • 0003206867 scopus 로고    scopus 로고
    • Toward a human blood serum proteome: Analysis by multidimensional separation coupled with mass spectrometry
    • Adkins JN, Varnum SM, Auberry KJ, Moore RJ, Angell NH, Smith RD, et al. Toward a human blood serum proteome: Analysis by multidimensional separation coupled with mass spectrometry. Mol Cell Proteomics 2002;1:947-55.
    • (2002) Mol Cell Proteomics , vol.1 , pp. 947-955
    • Adkins, J.N.1    Varnum, S.M.2    Auberry, K.J.3    Moore, R.J.4    Angell, N.H.5    Smith, R.D.6
  • 38
    • 23944459569 scopus 로고    scopus 로고
    • Efficient prefractionation of low-abundance proteins in human plasma and construction of a two-dimensional map
    • Cho SY, Lee EY, Lee JS, Kim HY, Park JM, Kwon MS, et al. Efficient prefractionation of low-abundance proteins in human plasma and construction of a two-dimensional map. Proteomics 2005;5:3386-96.
    • (2005) Proteomics , vol.5 , pp. 3386-3396
    • Cho, S.Y.1    Lee, E.Y.2    Lee, J.S.3    Kim, H.Y.4    Park, J.M.5    Kwon, M.S.6
  • 39
    • 23944434470 scopus 로고    scopus 로고
    • A novel four-dimensional strategy combining protein and peptide separation methods enables detection of low-abundance proteins in human plasma and serum proteomes
    • Tang HY, Ali-Khan N, Echan LA, Levenkova N, Rux JJ, Speicher DW. A novel four-dimensional strategy combining protein and peptide separation methods enables detection of low-abundance proteins in human plasma and serum proteomes. Proteomics 2005;5:3329-42.
    • (2005) Proteomics , vol.5 , pp. 3329-3342
    • Tang, H.Y.1    Ali-Khan, N.2    Echan, L.A.3    Levenkova, N.4    Rux, J.J.5    Speicher, D.W.6
  • 40
    • 8844233567 scopus 로고    scopus 로고
    • Mass spectrometric quantitation of peptides and proteins using Stable Isotope Standards and Capture by Anti-Peptide Antibodies (SISCAPA)
    • Anderson NL, Anderson NG, Haines LR, Hardie DB, Olafson RW, Pearson TW. Mass spectrometric quantitation of peptides and proteins using Stable Isotope Standards and Capture by Anti-Peptide Antibodies (SISCAPA). J Proteome Res 2004;3:235-44.
    • (2004) J Proteome Res , vol.3 , pp. 235-244
    • Anderson, N.L.1    Anderson, N.G.2    Haines, L.R.3    Hardie, D.B.4    Olafson, R.W.5    Pearson, T.W.6
  • 43
    • 0036645099 scopus 로고    scopus 로고
    • Serum protein fingerprinting coupled with a pattern-matching algorithm distinguishes prostate cancer from benign prostate hyperplasia and healthy men
    • Adam BL, Qu Y, Davis JW, Ward MD, Clements MA, Cazares LH, et al. Serum protein fingerprinting coupled with a pattern-matching algorithm distinguishes prostate cancer from benign prostate hyperplasia and healthy men. Cancer Res 2002;62:3609-14.
    • (2002) Cancer Res , vol.62 , pp. 3609-3614
    • Adam, B.L.1    Qu, Y.2    Davis, J.W.3    Ward, M.D.4    Clements, M.A.5    Cazares, L.H.6
  • 44
    • 0142027764 scopus 로고    scopus 로고
    • Identification of biomarkers for ovarian cancer using strong anion-exchange ProteinChips: Potential use in diagnosis and prognosis
    • Kozak KR, Amneus MW, Pusey SM, Su F, Luong MN, Luong SA, et al. Identification of biomarkers for ovarian cancer using strong anion-exchange ProteinChips: Potential use in diagnosis and prognosis. Proc Natl Acad Sci USA 2003;100:12343-8.
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 12343-12348
    • Kozak, K.R.1    Amneus, M.W.2    Pusey, S.M.3    Su, F.4    Luong, M.N.5    Luong, S.A.6
  • 46
    • 1542378202 scopus 로고    scopus 로고
    • Analysis of serum proteomic patterns for early cancer diagnosis: Drawing attention to potential problems
    • Diamandis EP. Analysis of serum proteomic patterns for early cancer diagnosis: Drawing attention to potential problems. J Natl Cancer Inst 2004;96:353-6.
    • (2004) J Natl Cancer Inst , vol.96 , pp. 353-356
    • Diamandis, E.P.1
  • 49
    • 0035107435 scopus 로고    scopus 로고
    • The effect of protease inhibitors on the two-dimensional electrophoresis pattern of red blood cell membranes
    • Olivieri E, Herbert B, Righetti PG. The effect of protease inhibitors on the two-dimensional electrophoresis pattern of red blood cell membranes. Electrophoresis 2001; 22:560-5.
    • (2001) Electrophoresis , vol.22 , pp. 560-565
    • Olivieri, E.1    Herbert, B.2    Righetti, P.G.3
  • 50
    • 33846835489 scopus 로고    scopus 로고
    • Proteinase families and their inhibitors
    • Mykles DL. Proteinase families and their inhibitors. Methods Cell Biol 2001;66:247-87.
    • (2001) Methods Cell Biol , vol.66 , pp. 247-287
    • Mykles, D.L.1
  • 52
    • 0032569674 scopus 로고    scopus 로고
    • Decreases in mouse brain NAD+ and ATP induced by 1-methyl-4-phenyl-1, 2,3,6-tetrahydropyridine (MPTP): Prevention by the poly(ADP-ribose) polymerase inhibitor, benzamide
    • Cosi C, Marien M. Decreases in mouse brain NAD+ and ATP induced by 1-methyl-4-phenyl-1, 2,3,6-tetrahydropyridine (MPTP): Prevention by the poly(ADP-ribose) polymerase inhibitor, benzamide. Brain Res 1998;809:58-67.
    • (1998) Brain Res , vol.809 , pp. 58-67
    • Cosi, C.1    Marien, M.2
  • 53
    • 0017145306 scopus 로고
    • Qualitative and quantitative studies on human myelin basic protein in situ with respect to time interval between death and autopsy
    • Ansari KA, Rand A, Hendrickson H, Bentley MD. Qualitative and quantitative studies on human myelin basic protein in situ with respect to time interval between death and autopsy. J Neuropathol Exp Neurol 1976;35:180-90.
    • (1976) J Neuropathol Exp Neurol , vol.35 , pp. 180-190
    • Ansari, K.A.1    Rand, A.2    Hendrickson, H.3    Bentley, M.D.4
  • 54
    • 0019142891 scopus 로고
    • Studies of human myelin proteins during old age
    • Berlet HH, Volk B. Studies of human myelin proteins during old age. Mech Ageing Dev 1980;14:211-22.
    • (1980) Mech Ageing Dev , vol.14 , pp. 211-222
    • Berlet, H.H.1    Volk, B.2
  • 55
    • 0031836730 scopus 로고    scopus 로고
    • Regional differences in protein carboxymethylation in post-mortem human brain
    • Goggins M, Scott JM, Weir DG. Regional differences in protein carboxymethylation in post-mortem human brain. Clin Sci (Lond) 1998;94:677-85.
    • (1998) Clin Sci (Lond) , vol.94 , pp. 677-685
    • Goggins, M.1    Scott, J.M.2    Weir, D.G.3
  • 57
    • 28544446695 scopus 로고    scopus 로고
    • Biomarkers in cancer staging, prognosis and treatment selection
    • Ludwig JA, Weinstein JN. Biomarkers in cancer staging, prognosis and treatment selection. Nat Rev Cancer 2005;5:845-56.
    • (2005) Nat Rev Cancer , vol.5 , pp. 845-856
    • Ludwig, J.A.1    Weinstein, J.N.2
  • 58
    • 0024594943 scopus 로고
    • Isolation of human platelets from plasma by centrifugation and washing
    • Mustard JF, Kinlough-Rathbone RL, Packham MA. Isolation of human platelets from plasma by centrifugation and washing. Methods Enzymol 1989;169:3-11.
    • (1989) Methods Enzymol , vol.169 , pp. 3-11
    • Mustard, J.F.1    Kinlough-Rathbone, R.L.2    Packham, M.A.3
  • 59
    • 0035652393 scopus 로고    scopus 로고
    • Longitudinal stability of coagulation, fibrinolysis, and inflammation factors in stored plasma samples
    • Lewis MR, Callas PW, Jenny NS, Tracy RP. Longitudinal stability of coagulation, fibrinolysis, and inflammation factors in stored plasma samples. Thromb Haemost 2001;86:1495-500.
    • (2001) Thromb Haemost , vol.86 , pp. 1495-1500
    • Lewis, M.R.1    Callas, P.W.2    Jenny, N.S.3    Tracy, R.P.4
  • 61
    • 24744457360 scopus 로고    scopus 로고
    • Proteomic-based prognosis of brain tumor patients using direct-tissue matrix-assisted laser desorption ionization mass spectrometry
    • Schwartz SA, Weil RJ, Thompson RC, Shyr Y, Moore JH, Toms SA, et al. Proteomic-based prognosis of brain tumor patients using direct-tissue matrix-assisted laser desorption ionization mass spectrometry. Cancer Res 2005;65:7674-81.
    • (2005) Cancer Res , vol.65 , pp. 7674-7681
    • Schwartz, S.A.1    Weil, R.J.2    Thompson, R.C.3    Shyr, Y.4    Moore, J.H.5    Toms, S.A.6
  • 62
    • 1042290316 scopus 로고    scopus 로고
    • Protein profiling in brain tumors using mass spectrometry: Feasibility of a new technique for the analysis of protein expression
    • Schwartz SA,Weil RJ, Johnson MD, Toms SA, Caprioli RM. Protein profiling in brain tumors using mass spectrometry: Feasibility of a new technique for the analysis of protein expression. Clin Cancer Res 2004;10:981-7.
    • (2004) Clin Cancer Res , vol.10 , pp. 981-987
    • Schwartz, S.A.1    Weil, R.J.2    Johnson, M.D.3    Toms, S.A.4    Caprioli, R.M.5
  • 63
    • 0025370815 scopus 로고
    • Dominant forces in protein folding
    • Dill KA. Dominant forces in protein folding. Biochemistry 1990;29:7133-55.
    • (1990) Biochemistry , vol.29 , pp. 7133-7155
    • Dill, K.A.1
  • 64
    • 0008863560 scopus 로고
    • Some factors in the interpretation of protein denaturation
    • Kauzmann W. Some factors in the interpretation of protein denaturation. Adv Protein Chem 1959;14:1-63.
    • (1959) Adv Protein Chem , vol.14 , pp. 1-63
    • Kauzmann, W.1
  • 66
    • 0025261680 scopus 로고
    • Preparation of extracts from higher eukaryotes
    • Dignam JD. Preparation of extracts from higher eukaryotes. Methods Enzymol 1990;182:194-203.
    • (1990) Methods Enzymol , vol.182 , pp. 194-203
    • Dignam, J.D.1
  • 67
    • 0003924086 scopus 로고
    • New York, Chichester, Brisbane, Toronto, Singapore: Wiley-Liss
    • Bollag DM, Edelstein SJ. Protein Methods. New York, Chichester, Brisbane, Toronto, Singapore: Wiley-Liss; 1991.
    • (1991) Protein Methods
    • Bollag, D.M.1    Edelstein, S.J.2
  • 68
    • 0025208204 scopus 로고
    • Maintaining protein stability
    • Deutscher MP. Maintaining protein stability. Methods Enzymol 1990;182:83-9.
    • (1990) Methods Enzymol , vol.182 , pp. 83-89
    • Deutscher, M.P.1
  • 70
    • 0032935808 scopus 로고    scopus 로고
    • Comparison of yeast cell protein solubilization procedures for two-dimensional electrophoresis
    • Harder A, Wildgruber R, Nawrocki A, Fey SJ, Larsen PM, Gorg A. Comparison of yeast cell protein solubilization procedures for two-dimensional electrophoresis. Electrophoresis 1999;20:826-9.
    • (1999) Electrophoresis , vol.20 , pp. 826-829
    • Harder, A.1    Wildgruber, R.2    Nawrocki, A.3    Fey, S.J.4    Larsen, P.M.5    Gorg, A.6
  • 72
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli UK. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 1970; 227(259):680-5.
    • (1970) Nature , vol.227 , Issue.259 , pp. 680-685
    • Laemmli, U.K.1
  • 73
    • 0015853344 scopus 로고
    • Maturation of the head of bacteriophage T4. I. DNA packaging events
    • Laemmli UK, Favre M. Maturation of the head of bacteriophage T4. I. DNA packaging events. J Mol Biol 1973;80:575-99.
    • (1973) J Mol Biol , vol.80 , pp. 575-599
    • Laemmli, U.K.1    Favre, M.2
  • 74
    • 0030218803 scopus 로고    scopus 로고
    • SYPRO orange and SYPRO red protein gel stains: One-step fluorescent staining of denaturing gels for detection of nanogram levels of protein
    • Steinberg TH, Jones LJ, Haugland RP, Singer VL. SYPRO orange and SYPRO red protein gel stains: One-step fluorescent staining of denaturing gels for detection of nanogram levels of protein. Anal Biochem 1996;239:223-37.
    • (1996) Anal Biochem , vol.239 , pp. 223-237
    • Steinberg, T.H.1    Jones, L.J.2    Haugland, R.P.3    Singer, V.L.4
  • 75
    • 0030219531 scopus 로고    scopus 로고
    • Applications of SYPRO orange and SYPRO red protein gel stains
    • Steinberg TH, Haugland RP, Singer VL. Applications of SYPRO orange and SYPRO red protein gel stains. Anal Biochem 1996;239:238-45.
    • (1996) Anal Biochem , vol.239 , pp. 238-245
    • Steinberg, T.H.1    Haugland, R.P.2    Singer, V.L.3
  • 76
    • 0346256833 scopus 로고    scopus 로고
    • A fluorescent natural product for ultra sensitive detection of proteins in one-dimensional and two-dimensional gel electrophoresis
    • Mackintosh JA, Choi HY, Bae SH, Veal DA, Bell PJ, Ferrari BC, et al. A fluorescent natural product for ultra sensitive detection of proteins in one-dimensional and two-dimensional gel electrophoresis. Proteomics 2003;3:2273-88.
    • (2003) Proteomics , vol.3 , pp. 2273-2288
    • Mackintosh, J.A.1    Choi, H.Y.2    Bae, S.H.3    Veal, D.A.4    Bell, P.J.5    Ferrari, B.C.6
  • 77
    • 0035408680 scopus 로고    scopus 로고
    • Rapid and simple single nanogram detection of glycoproteins in polyacrylamide gels and on electroblots
    • Steinberg TH, Pretty On Top K, Berggren KN, Kemper C, Jones L, Diwu Z, et al. Rapid and simple single nanogram detection of glycoproteins in polyacrylamide gels and on electroblots. Proteomics 2001;1:841-55.
    • (2001) Proteomics , vol.1 , pp. 841-855
    • Steinberg, T.H.1    Pretty On Top, K.2    Berggren, K.N.3    Kemper, C.4    Jones, L.5    Diwu, Z.6
  • 78
    • 0019551730 scopus 로고
    • "Western blotting": Electrophoretic transfer of proteins from sodium dodecyl sulfate-polyacrylamide gels to unmodified nitrocellulose and radiographic detection with antibody and radioiodinated protein A
    • Burnette WN. "Western blotting": Electrophoretic transfer of proteins from sodium dodecyl sulfate-polyacrylamide gels to unmodified nitrocellulose and radiographic detection with antibody and radioiodinated protein A. Anal Biochem 1981;112:195-203.
    • (1981) Anal Biochem , vol.112 , pp. 195-203
    • Burnette, W.N.1
  • 80
    • 0016711037 scopus 로고
    • High resolution two-dimensional electrophoresis of proteins
    • O'Farrell PH. High resolution two-dimensional electrophoresis of proteins. J Biol Chem 1975;250:4007-21.
    • (1975) J Biol Chem , vol.250 , pp. 4007-4021
    • O'Farrell, P.H.1
  • 81
    • 0017696571 scopus 로고
    • High resolution two-dimensional electrophoresis of basic as well as acidic proteins
    • O'Farrell PZ, Goodman HM, O'Farrell PH. High resolution two-dimensional electrophoresis of basic as well as acidic proteins. Cell 1977;12:1133-41.
    • (1977) Cell , vol.12 , pp. 1133-1141
    • O'Farrell, P.Z.1    Goodman, H.M.2    O'Farrell, P.H.3
  • 83
    • 0036324715 scopus 로고    scopus 로고
    • Proteomics and bioinformatics approaches for identification of serum biomarkers to detect breast cancer
    • Li J, Zhang Z, Rosenzweig J, Wang YY, Chan DW. Proteomics and bioinformatics approaches for identification of serum biomarkers to detect breast cancer. Clin Chem 2002;48:1296-304.
    • (2002) Clin Chem , vol.48 , pp. 1296-1304
    • Li, J.1    Zhang, Z.2    Rosenzweig, J.3    Wang, Y.Y.4    Chan, D.W.5
  • 85
    • 0042233694 scopus 로고    scopus 로고
    • Liquid chromatography-Fourier transform ion cyclotron resonance mass spectrometric characterization of protein kinase C phosphorylation
    • Chalmers MJ, Quinn JP, Blakney GT, Emmett MR, Mischak H, Gaskell SJ, et al. Liquid chromatography-Fourier transform ion cyclotron resonance mass spectrometric characterization of protein kinase C phosphorylation. J Proteome Res 2003;2:373-82.
    • (2003) J Proteome Res , vol.2 , pp. 373-382
    • Chalmers, M.J.1    Quinn, J.P.2    Blakney, G.T.3    Emmett, M.R.4    Mischak, H.5    Gaskell, S.J.6
  • 86
    • 0036468952 scopus 로고    scopus 로고
    • Phosphoprotein isotope-coded affinity tags: Application to the enrichment and identification of lowabundance phosphoproteins
    • Goshe MB, Veenstra TD, Panisko EA, Conrads TP, Angell NH, Smith RD. Phosphoprotein isotope-coded affinity tags: Application to the enrichment and identification of lowabundance phosphoproteins. Anal Chem 2002;74:607-16.
    • (2002) Anal Chem , vol.74 , pp. 607-616
    • Goshe, M.B.1    Veenstra, T.D.2    Panisko, E.A.3    Conrads, T.P.4    Angell, N.H.5    Smith, R.D.6
  • 87
    • 0035072715 scopus 로고    scopus 로고
    • A systematic approach to the analysis of protein phosphorylation
    • Zhou H, Watts JD, Aebersold R. A systematic approach to the analysis of protein phosphorylation. Nat Biotechnol 2001;19:375-8.
    • (2001) Nat Biotechnol , vol.19 , pp. 375-378
    • Zhou, H.1    Watts, J.D.2    Aebersold, R.3
  • 88
    • 0037253267 scopus 로고    scopus 로고
    • A novel experimental design for comparative two-dimensional gel analysis: Two-dimensional difference gel electrophoresis incorporating a pooled internal standard
    • Alban A, David SO, Bjorkesten L, Andersson C, Sloge E, Lewis S, et al. A novel experimental design for comparative two-dimensional gel analysis: Two-dimensional difference gel electrophoresis incorporating a pooled internal standard. Proteomics 2003;3:36-44.
    • (2003) Proteomics , vol.3 , pp. 36-44
    • Alban, A.1    David, S.O.2    Bjorkesten, L.3    Andersson, C.4    Sloge, E.5    Lewis, S.6
  • 89
    • 0346874342 scopus 로고    scopus 로고
    • Proteomic characterization of the human centrosome by protein correlation profiling
    • Andersen JS, Wilkinson CJ, Mayor T, Mortensen P, Nigg EA, Mann M. Proteomic characterization of the human centrosome by protein correlation profiling. Nature 2003; 426(6966):570-4.
    • (2003) Nature , vol.426 , Issue.6966 , pp. 570-574
    • Andersen, J.S.1    Wilkinson, C.J.2    Mayor, T.3    Mortensen, P.4    Nigg, E.A.5    Mann, M.6
  • 90
    • 0037337310 scopus 로고    scopus 로고
    • A proteomics strategy to elucidate functional protein-protein interactions applied to EGF signaling
    • Blagoev B, Kratchmarova I, Ong SE, Nielsen M, Foster LJ, Mann M. A proteomics strategy to elucidate functional protein-protein interactions applied to EGF signaling. Nat Biotechnol 2003;21:315-8.
    • (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
  • 92
    • 0036391454 scopus 로고    scopus 로고
    • Proteome analysis of low-abundance proteins using multidimensional chromatography and isotope-coded affinity tags
    • Gygi SP, Rist B, Griffin TJ, Eng J, Aebersold R. Proteome analysis of low-abundance proteins using multidimensional chromatography and isotope-coded affinity tags. J Proteome Res 2002;1:47-54.
    • (2002) J Proteome Res , vol.1 , pp. 47-54
    • Gygi, S.P.1    Rist, B.2    Griffin, T.J.3    Eng, J.4    Aebersold, R.5
  • 95
    • 0037795741 scopus 로고    scopus 로고
    • Absolute quantification of proteins and phosphoproteins from cell lysates by tandem MS
    • Gerber SA, Rush J, Stemman O, Kirschner MW, Gygi SP. Absolute quantification of proteins and phosphoproteins from cell lysates by tandem MS. Proc Natl Acad Sci USA 2003;100:6940-5.
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 6940-6945
    • Gerber, S.A.1    Rush, J.2    Stemman, O.3    Kirschner, M.W.4    Gygi, S.P.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.