Proteomics of blood and derived products: what’s next?

References

• Hess JR, Grazzini G. Blood proteomics and transfusion safety. J. Proteomics73(3), 365–367 (2010).
   PubMed Web of Science ®Google Scholar
• Liumbruno G, D’Alessandro A, Grazzini G, Zolla L. Blood-related proteomics. J. Proteomics73(3), 483–507 (2010).
   PubMed Web of Science ®Google Scholar
• Tissot JD. Blood proteomics. J. Proteomics73(3), 466–467 (2010).
   PubMed Web of Science ®Google Scholar
• Aebersold R, Mann M. Mass spectrometry-based proteomics. Nature422(6928), 198–207 (2003).
   PubMed Web of Science ®Google Scholar
• Walther TC, Mann M. Mass spectrometry-based proteomics in cell biology. J. Cell Biol.190(4), 491–500 (2010).
   PubMed Web of Science ®Google Scholar
• Walsh GM, Rogalski JC, Klockenbusch C, Kast J. Mass spectrometry-based proteomics in biomedical research: emerging technologies and future strategies. Expert Rev. Mol. Med.12, e30 (2010).
   Google Scholar
• Lion N, Prudent M, Crettaz D, Tissot J-D. Proteomics and transfusion medicine. Trans. Clin. Biol.18(2), 79–96 (2011).
   PubMed Web of Science ®Google Scholar
• Ong SE, Mann M. Mass spectrometry-based proteomics turns quantitative. Nat. Chem. Biol.1(5), 252–262 (2005).
   PubMed Web of Science ®Google Scholar
• Elliott MH, Smith DS, Parker CE, Borchers C. Current trends in quantitative proteomics. J. Mass Spectrom.44(12), 1637–1660 (2009).
   PubMed Web of Science ®Google Scholar
• Boja E, Hiltke T, Rivers R et al. Evolution of clinical proteomics and its role in medicine. J. Proteome Res.10(1), 66–84 (2011).
   PubMed Web of Science ®Google Scholar
• Choudhary C, Mann M. Decoding signalling networks by mass spectrometry-based proteomics. Nat. Rev. Mol. Cell Biol.11(6), 427–439 (2010).
   PubMed Web of Science ®Google Scholar
• D’Alessandro A, Zolla L. Proteomics for quality-control processes in transfusion medicine. Anal. Bioanal. Chem.398(1), 111–124 (2010).
   PubMed Web of Science ®Google Scholar
• Devine DV, Schubert P. Proteomic applications in blood transfusion: working the jigsaw puzzle. Vox. Sang.100(1), 84–91 (2011).
   PubMed Web of Science ®Google Scholar
• Lion N, Crettaz D, Rubin O, Tissot JD. Stored red blood cells: a changing universe waiting for its map(s). J. Proteomics73(3), 374–385 (2010).
   PubMed Web of Science ®Google Scholar
• Lion N, Tissot JD. Application of proteomics to hematology: the revolution is starting. Expert Rev. Proteomics5(3), 375–379 (2008).
   PubMed Web of Science ®Google Scholar
• Liumbruno G, D’Alessandro A, Grazzini G, Zolla L. How has proteomics informed transfusion biology so far? Crit. Rev. Oncol. Hematol.76(3), 153–172 (2010).
   PubMed Web of Science ®Google Scholar
• Schubert P, Devine DV. Proteomics meets blood banking: identification of protein targets for the improvement of platelet quality. J. Proteomics73(3), 436–444 (2010).
   PubMed Web of Science ®Google Scholar
• Low TY, Seow TK, Chung MC. Separation of human erythrocyte membrane associated proteins with one-dimensional and two-dimensional gel electrophoresis followed by identification with matrix-assisted laser desorption/ionization-time of flight mass spectrometry. Proteomics2(9), 1229–1239 (2002).
   PubMed Web of Science ®Google Scholar
• Kakhniashvili DG, Bulla LA Jr, Goodman SR. The human erythrocyte proteome: analysis by ion trap mass spectrometry. Mol. Cell. Proteomics3(5), 501–509 (2004).
   PubMed Web of Science ®Google Scholar
• Pasini EM, Kirkegaard M, Mortensen P, Lutz HU, Thomas AW, Mann M. In-depth analysis of the membrane and cytosolic proteome of red blood cells. Blood108(3), 791–801 (2006).
   PubMed Web of Science ®Google Scholar
• Ringrose JH, van Solinge WW, Mohammed S et al. Highly efficient depletion strategy for the two most abundant erythrocyte soluble proteins improves proteome coverage dramatically. J. Proteome Res.7(7), 3060–3063 (2008).
   PubMed Web of Science ®Google Scholar
• Roux-Dalvai F, Gonzalez de Peredo A, Simo C et al. Extensive analysis of the cytoplasmic proteome of human erythrocytes using the peptide ligand library technology and advanced mass spectrometry. Mol. Cell. Proteomics7(11), 2254–2269 (2008).
   PubMed Web of Science ®Google Scholar
• van Gestel RA, van Solinge WW, van der Toorn HW et al. Quantitative erythrocyte membrane proteome analysis with Blue-native/SDS PAGE. J. Proteomics73(3), 456–465 (2010).
   PubMed Web of Science ®Google Scholar
• Harrison ML, Rathinavelu P, Arese P, Geahlen RL, Low PS. Role of band-3 tyrosine phosphorylation in the regulation of erythrocyte glycolysis. J. Biol. Chem.266(7), 4106–4111 (1991).
   PubMed Web of Science ®Google Scholar
• Low PS, Allen DP, Zioncheck TF et al. Tyrosine phosphorylation of band-3 inhibits peripheral protein-binding. J. Biol. Chem.262(10), 4592–4596 (1987).
   PubMed Web of Science ®Google Scholar
• Low PS, Rathinavelu P, Harrison ML. Regulation of glycolysis via reversible enzyme binding to the membrane-protein, band-3. J. Biol. Chem.268(20), 14627–14631 (1993).
   PubMed Web of Science ®Google Scholar
• Yannoukakos D, Vasseur C, Piau JP, Wajcman H, Bursaux E. Phosphorylation sites in human erythrocyte band-3 protein. Biochim. Biophys. Acta1066(2), 253–266 (1991).
   Google Scholar
• Ferru E, Giger K, Pantaleo A et al. Regulation of membrane-cytoskeletal interactions by tyrosine phosphorylation of erythrocyte band 3. Blood117(22), 5998–6006 (2011).
   PubMed Web of Science ®Google Scholar
• De Franceschi L, Biondani A, Carta F et al. PTP epsilon has a critical role in signaling transduction pathways and phosphoprotein network topology in red cells. Proteomics8(22), 4695–4708 (2008).
   PubMed Web of Science ®Google Scholar
• Siciliano A, Turrini F, Bertoldi M et al. Deoxygenation affects tyrosine phosphoproteome of red cell membrane from patients with sickle cell disease. Blood Cells Mol. Dis.44(4), 233–242 (2010).
   PubMed Web of Science ®Google Scholar
• Bessos H, Seghatchian J. Red cell storage lesion: the potential impact of storage-induced CD47 decline on immunomodulation and the survival of leucofiltered red cells. Transfus. Apher. Sci.32(2), 227–232 (2005).
   PubMed Web of Science ®Google Scholar
• Chin-Yee I, Arya N, d’Almeida MS. The red cell storage lesion and its implication for transfusion. Transfus. Sci.18(3), 447–458 (1997).
   PubMedGoogle Scholar
• Gladwin MT, Kim-Shapiro DB. Storage lesion in banked blood due to hemolysis-dependent disruption of nitric oxide homeostasis. Curr. Opin. Hematol.16(6), 515–523 (2009).
   PubMed Web of Science ®Google Scholar
• Glynn SA. The red blood cell storage lesion: a method to the madness. Transfusion50(6), 1164–1169 (2010).
   PubMed Web of Science ®Google Scholar
• Schrier SL, Hardy B, Bensch K, Junga I, Krueger J. Red blood cell membrane storage lesion. Transfusion19(2), 158–165 (1979).
   PubMed Web of Science ®Google Scholar
• Tinmouth A, Chin-Yee I. The clinical consequences of the red cell storage lesion. Transfus. Med. Rev.15(2), 91–107 (2001).
   PubMed Web of Science ®Google Scholar
• Wolfe L. The red cell membrane and the storage lesion. Clin. Haematol.14(1), 259–276 (1985).
   PubMedGoogle Scholar
• Rubin O, Crettaz D, Canellini G, Tissot JD, Lion N. Microparticles in stored red blood cells: an approach using flow cytometry and proteomic tools. Vox. Sang.95(4), 288–297 (2008).
   PubMed Web of Science ®Google Scholar
• Rubin O, Crettaz D, Tissot JD, Lion N. Microparticles in stored red blood cells: submicron clotting bombs? Blood. Transfus.8(Suppl. 3), S31–S38 (2010).
   Google Scholar
• Tissot JD, Rubin O, Canellini G. Analysis and clinical relevance of microparticles from red blood cells. Curr. Opin. Hematol.17(6), 571–577 (2010).
   PubMed Web of Science ®Google Scholar
• Bosman G, Lasonder E, Groenen-Dopp YAM, Willekens FLA, Werre JM, Novotny VMJ. Comparative proteomics of erythrocyte aging in vivo and in vitro. J. Proteomics73(3), 396–402 (2010).
   PubMed Web of Science ®Google Scholar
• Bosman G, Werre JM, Willekens FLA, Novotny VMJ. Erythrocyte ageing in vivo and in vitro: structural aspects and implications for transfusion. Transfus. Med.18(6), 335–347 (2008).
   PubMed Web of Science ®Google Scholar
• D’Amici GM, Rinalducci S, Zolla L. Proteomic analysis of RBC membrane protein degradation during blood storage. J. Proteome Res.6(8), 3242–3255 (2007).
   PubMed Web of Science ®Google Scholar
• Rubin O, Crettaz D, Tissot JD, Lion N. Pre-analytical and methodological challenges in red blood cell microparticle proteomics. Talanta82(1), 1–8 (2010).
   PubMed Web of Science ®Google Scholar
• Bosman GJ, Lasonder E, Luten M et al. The proteome of red cell membranes and vesicles during storage in blood bank conditions. Transfusion48(5), 827–835 (2008).
   PubMed Web of Science ®Google Scholar
• Rinalducci S, D’Amici GM, Blasi B, Zolla L. Oxidative stress-dependent oligomeric status of erythrocyte peroxiredoxin II (PrxII) during storage under standard blood banking conditions. Biochimie93, 845–853 (2011).
   PubMed Web of Science ®Google Scholar
• Antonelou MH, Kriebardis AG, Stamoulis KE, Economou-Petersen E, Margaritis LH, Papassideri IS. Red blood cell aging markers during storage in citrate-phosphate-dextrose-saline-adenine-glucose-mannitol. Transfusion50(2), 376–389 (2010).
   PubMed Web of Science ®Google Scholar
• Rinalducci S, D’Amici GM, Blasi B, Vaglio S, Grazzini G, Zolla L. Peroxiredoxin-2 as a candidate biomarker to test oxidative stress levels of stored red blood cells under blood bank conditions. Transfusion51(7), 1439–1449 (2011).
   PubMed Web of Science ®Google Scholar
• Finamore F, Pieroni L, Ronci M et al. Proteomics investigation of human platelets by shotgun nUPLC-MSE and 2DE experimental strategies: a comparative study. Blood Transfus.8(Suppl. 3), S140–S148 (2010).
   Web of Science ®Google Scholar
• Senzel L, Gnatenko DV, Bahou WF. The platelet proteome. Curr. Opin. Hematol.16(5), 329–333 (2009).
   PubMed Web of Science ®Google Scholar
• Simon O, Wortelkamp S, Sickmann A. Characterization of platelet proteins using peptide centric proteomics. Methods Mol. Biol.564, 155–171 (2009).
   PubMedGoogle Scholar
• Yin W, Czuchlewski D, Peerschke EI. Development of proteomic signatures of platelet activation using surface-enhanced laser desorption/ionization technology in a clinical setting. Am. J. Clin. Pathol.129(6), 862–869 (2008).
   PubMed Web of Science ®Google Scholar
• Foy M, Maguire PB. Recent advances in the characterisation of the platelet membrane system by proteomics. Curr. Pharm. Des.13(26), 2647–2655 (2007).
   PubMed Web of Science ®Google Scholar
• Greening DW, Glenister KM, Sparrow RL, Simpson RJ. Enrichment of human platelet membranes for proteomic analysis. Methods Mol. Biol.528, 245–258 (2009).
   PubMedGoogle Scholar
• Lewandrowski U, Wortelkamp S, Lohrig K et al. Platelet membrane proteomics: a novel repository for functional research. Blood114(1), e10–e19 (2009).
   PubMed Web of Science ®Google Scholar
• Miller JL. Glycoprotein analysis for the diagnostic evaluation of platelet disorders. Semin. Thromb. Hemost.35(2), 224–232 (2009).
   PubMed Web of Science ®Google Scholar
• Maguire PB, Wynne KJ, Harney DF, O’Donoghue NM, Stephens G, Fitzgerald DJ. Identification of the phosphotyrosine proteome from thrombin activated platelets. Proteomics2(6), 642–648 (2002).
   PubMed Web of Science ®Google Scholar
• Qureshi AH, Chaoji V, Maiguel D et al. Proteomic and phospho-proteomic profile of human platelets in basal, resting state: insights into integrin signaling. PLoS One4(10), e7627 (2009).
   PubMed Web of Science ®Google Scholar
• Zahedi RP, Lewandrowski U, Wiesner J et al. Phosphoproteome of resting human platelets. J. Proteome Res.7(2), 526–534 (2008).
   PubMed Web of Science ®Google Scholar
• Maynard DM, Heijnen HF, Horne MK, White JG, Gahl WA. Proteomic analysis of platelet alpha-granules using mass spectrometry. J. Thromb. Haemost.5(9), 1945–1955 (2007).
   PubMed Web of Science ®Google Scholar
• Majek P, Reicheltova Z, Stikarova J, Suttnar J, Sobotkova A, Dyr JE. Proteome changes in platelets activated by arachidonic acid, collagen, and thrombin. Proteome Sci.8, 56 (2010).
   PubMed Web of Science ®Google Scholar
• Tucker KL, Kaiser WJ, Bergeron AL et al. Proteomic analysis of resting and thrombin-stimulated platelets reveals the translocation and functional relevance of HIP-55 in platelets. Proteomics9(18), 4340–4354 (2009).
   PubMed Web of Science ®Google Scholar
• Davi G, Patrono C. Mechanisms of disease: platelet activation and atherothrombosis. N. Engl. J. Med.357(24), 2482–2494 (2007).
   PubMed Web of Science ®Google Scholar
• Siess W. Molecular mechanisms of platelet activation. Physiol. Rev.69(1), 58–178 (1989).
   PubMed Web of Science ®Google Scholar
• Senis YA, Tomlinson MG, Garcia A et al. A comprehensive proteomics and genomics analysis reveals novel transmembrane proteins in human platelets and mouse megakaryocytes including G6b-B, a novel immunoreceptor tyrosine-based inhibitory motif protein. Mol. Cell. Proteomics6(3), 548–564 (2007).
   PubMed Web of Science ®Google Scholar
• Suzuki-Inoue K, Fuller GLJ, Garcia A et al. A novel Syk-dependent mechanism of platelet activation by the C-type lectin receptor CLEC-2. Blood107(2), 542–549 (2006).
   PubMed Web of Science ®Google Scholar
• Kaiser WJ, Holbrook LM, Tucker KL, Stanley RG, Gibbins JM. A functional proteomic method for the enrichment of peripheral membrane proteins reveals the collagen binding protein Hsp47 is exposed on the surface of activated human platelets. J. Proteome Res.8(6), 2903–2914 (2009).
   PubMed Web of Science ®Google Scholar
• Marcus K, Immler D, Sternberger J, Meyer HE. Identification of platelet proteins separated by two-dimensional gel electrophoresis and analyzed by matrix assisted laser desorption/ioniztion-time of flight-mass spectrometry and detection of tyrosine-phosphorylated proteins. Electrophoresis21(13), 2622–2636 (2000).
   PubMed Web of Science ®Google Scholar
• Marcus K, Moebius J, Meyer HE. Differential analysis of phosphorylated proteins in resting and thrombin-stimulated human platelets. Anal. Bioanal. Chem.376(7), 973–993 (2003).
   PubMed Web of Science ®Google Scholar
• García A, Senis YA, Antrobus R et al. A global proteomics approach identifies novel phosphorylated signaling proteins in GPVI-activated platelets: involvement of G6f, a novel platelet Grb2-binding membrane adapter. Proteomics6(19), 5332–5343 (2006).
   PubMed Web of Science ®Google Scholar
• Seghatchian J, Krailadsiri P. Platelet storage lesion and apoptosis: are they related? Transfus. Apher. Sci.24(1), 103–105 (2001).
   PubMed Web of Science ®Google Scholar
• Shrivastava M. The platelet storage lesion. Transfus. Apher. Sci.41(2), 105–113 (2009).
   PubMed Web of Science ®Google Scholar
• Seghatchian J, Krailadsiri P. The platelet storage lesion. Transf. Med. Rev.11(2), 130–144 (1997).
   PubMed Web of Science ®Google Scholar
• Thon JN, Schubert P, Duguay M et al. Comprehensive proteomic analysis of protein changes during platelet storage requires complementary proteomic approaches. Transfusion48(3), 425–435 (2008).
   PubMed Web of Science ®Google Scholar
• Kulkarni S, Kannan M, Atreya CD. Omic approaches to quality biomarkers for stored platelets: are we there yet? Transfus. Med. Rev.24(3), 211–217 (2010).
   PubMed Web of Science ®Google Scholar
• Thiele T, Steil L, Gebhard S et al. Profiling of alterations in platelet proteins during storage of platelet concentrates. Transfusion47(7), 1221–1233 (2007).
   PubMed Web of Science ®Google Scholar
• Thon JN, Schubert P, Devine DV. Platelet storage lesion: a new understanding from a proteomic perspective. Transfus. Med. Rev.22(4), 268–279 (2008).
   PubMed Web of Science ®Google Scholar
• Glenister KM, Payne KA, Sparrow RL. Proteomic analysis of supernatant from pooled buffy-coat platelet concentrates throughout 7-day storage. Transfusion48(1), 99–107 (2008).
   PubMed Web of Science ®Google Scholar
• Egidi MG, Rinalducci S, Marrocco C, Vaglio S, Zolla L. Proteomic analysis of plasma derived from platelet buffy coats during storage at room temperature. An application of ProteoMiner(™) technology. Platelets22(4), 252–269 (2011).
   PubMed Web of Science ®Google Scholar
• Lemaitre D, Vericel E, Polette A, Lagarde M. Effects of fatty acids on human platelet glutathione peroxidase: possible role of oxidative stress. Biochem. Pharmacol.53(4), 479–486 (1997).
   PubMed Web of Science ®Google Scholar
• Alexandru N, Constantin A, Popov D. Carbonylation of platelet proteins occurs as consequence of oxidative stress and thrombin activation, and is stimulated by ageing and Type 2 diabetes. Clin. Chem. Lab. Med.46(4), 528–536 (2008).
   PubMed Web of Science ®Google Scholar
• Hayashi T, Tanaka S, Hori Y, Hirayama F, Sato EF, Inoue M. Role of mitochondria in the maintenance of platelet function during in vitro storage. Transfus. Med.21(3), 166–174 (2011).
   PubMed Web of Science ®Google Scholar
• Allet N, Barrillat N, Baussant T et al. In vitro and in silico processes to identify differentially expressed proteins. Proteomics4(8), 2333–2351 (2004).
   PubMed Web of Science ®Google Scholar
• Goldknopf IL. Blood-based proteomics for personalized medicine: examples from neurodegenerative disease. Expert Rev. Proteomics5(1), 1–8 (2008).
   PubMed Web of Science ®Google Scholar
• Huijbers A, Velstra B, Dekker TJA et al. Proteomic serum biomarkers and their potential application in cancer screening programs. Int. J. Mol. Sci.11(11), 4175–4193 (2010).
   PubMed Web of Science ®Google Scholar
• Schneider P, Hampel H, Buerger K. Biological marker candidates of Alzheimer’s disease in blood, plasma, and serum. CNS Neurosci. Ther.15(4), 358–374 (2009).
   PubMed Web of Science ®Google Scholar
• Simpson KL, Whetton AD, Dive C. Quantitative mass spectrometry-based techniques for clinical use: biomarker identification and quantification. J. Chromatogr. B.877(13), 1240–1249 (2009).
   PubMed Web of Science ®Google Scholar
• Omenn GS. The HUPO human plasma proteome project. Proteomics Clin. Appl.1(8), 769–779 (2007).
   PubMed Web of Science ®Google Scholar
• Omenn GS. Data management and data integration in the HUPO plasma proteome project. Methods Mol. Biol.696, 247–257 (2011).
   PubMedGoogle Scholar
• Cottingham K. HUPO Plasma Proteome Project: challenges and future directions. J. Proteome Res5(6), 1298 (2006).
   PubMedGoogle Scholar
• Crettaz D, Sensebe L, Vu DH et al. Proteomics of methylene blue photo-treated plasma before and after removal of the dye by an absorbent filter. Proteomics4(3), 881–891 (2004).
   PubMed Web of Science ®Google Scholar
• Brigulla M, Thiele T, Scharf C et al. Proteomics as a tool for assessment of therapeutics in transfusion medicine: evaluation of prothrombin complex concentrates. Transfusion46(3), 377–385 (2006).
   PubMed Web of Science ®Google Scholar
• Ohlmann P, Cazenave J-P, Isola H, Gachet C. Photochemical pathogen inactivation treatment of human plasma (amotosalen plus UVA) has no major impact on the protein expression pattern assessed by a 2-DIGE proteomic assay. Presented at: 24th Congress of the French Society of Blood Transfusion. Strasbourg, France, 23–25 June 2009.
   Google Scholar
• Steil L, Thiele T, Hammer E et al. Proteomic characterization of freeze-dried human plasma: providing treatment of bleeding disorders without the need for a cold chain. Transfusion48(11), 2356–2363 (2008).
   PubMed Web of Science ®Google Scholar
• Hsieh SY, Chen RK, Pan YH, Lee HL. Systematical evaluation of the effects of sample collection procedures on low-molecular-weight serum/plasma proteome profiling. Proteomics6(10), 3189–3198 (2006).
   PubMed Web of Science ®Google Scholar
• Ettinger A, Miklauz MM, Hendrix BK, Bihm DJ, Maldonado-Codina G, Goodrich RP. Protein stability of previously frozen plasma, riboflavin and UV light-treated, refrozen and stored for up to 2 years at -30 degrees C. Transfus. Apher. Sci.44(1), 25–31 (2011).
   PubMed Web of Science ®Google Scholar
• Thiele T, Steil L, Volker U, Greinacher A. Transfusion medicine and proteomics. Alliance or coexistence? Blood Transfus.8(Suppl. 3), S16–S25 (2010).
   Google Scholar
• Delobel J, Rubin O, Prudent M, Crettaz D, Tissot JD, Lion N. Biomarker analysis of stored blood products: emphasis on pre-analytical issues. Int. J. Mol. Sci.11(11), 4601–4617 (2010).
   PubMed Web of Science ®Google Scholar
• Salomao M, Zhang XH, Yang Y et al. Protein 4.1R-dependent multiprotein complex: new insights into the structural organization of the red blood cell membrane. Proc. Natl Acad. Sci. USA105(23), 8026–8031 (2008).
   PubMed Web of Science ®Google Scholar
• van den Akker E, Satchwell TJ, Williamson RC, Toye AM. Band 3 multiprotein complexes in the red cell membrane; of mice and men. Blood Cells Mol. Dis.45(1), 1–8 (2010).
   PubMed Web of Science ®Google Scholar
• Burton NM, Bruce LJ. Modelling the structure of the red cell membrane. Biochem. Cell Biol.89(2), 200–215 (2011).
   PubMed Web of Science ®Google Scholar
• Bruce LJ, Beckmann R, Ribeiro ML et al. A band 3-based macrocomplex of integral and peripheral proteins in the RBC membrane. Blood101(10), 4180–4188 (2003).
   PubMed Web of Science ®Google Scholar
• Goodman SR, Kurdia A, Ammann L, Kakhniashvili D, Daescu O. The human red blood cell proteome and interactome. Exp. Biol. Med.232(11), 1391–1408 (2007).
   PubMed Web of Science ®Google Scholar
• Chaurasia G, Iqbal Y, Hanig C, Herzel H, Wanker EE, Futschik ME. UniHI: an entry gate to the human protein interactome. Nucleic Acids Res.35, D590–D594 (2007).
   Google Scholar
• Balasubramanian R, LaFramboise T, Scholtens D, Gentleman R. A graph-theoretic approach to testing associations between disparate sources of functional genomics data. Bioinformatics20(18), 3353–3362 (2004).
   PubMed Web of Science ®Google Scholar
• D’Alessandro A, Righetti PG, Zolla L. The red blood cell proteome and interactome: an update. J. Proteome Res.9(1), 144–163 (2010).
   PubMed Web of Science ®Google Scholar
• Bianchi P, Fermo E, Vercellati C et al. Congenital dyserythropoietic anemia Type II (CDAII) is caused by mutations in the SEC23B Gene. Hum. Mutat.30(9), 1292–1298 (2009).
   PubMed Web of Science ®Google Scholar
• Kakhniashvili DG, Griko NB, Bulla LA, Goodman SR. The proteomics of sickle cell disease: profiling of erythrocyte membrane proteins by 2D-DIGE and tandem mass spectrometry. Exp. Biol. Med.230(11), 787–792 (2005).
   PubMed Web of Science ®Google Scholar
• Ghatpande SS, Choudhary PK, Quinn CT, Goodman SR. Pharmaco-proteomic study of hydroxyurea-induced modifications in the sickle red blood cell membrane proteome. Exp. Biol. Med.233(12), 1510–1517 (2008).
   PubMed Web of Science ®Google Scholar
• Fibach E, Burke LP, Schechter AN, Noguchi CT, Rodgers GP. Hydroxyurea increases fetal hemoglobin in cultured erythroid-cells derived from normal individuals and patients with sickle-cell-anemia or beta-thalassemia. Blood81(6), 1630–1635 (1993).
   PubMed Web of Science ®Google Scholar
• Ghatpande SS, Choudhary PK, Quinn CT, Goodman SR. In vivo pharmaco-proteomic analysis of hydroxyurea induced changes in the sickle red blood cell membrane proteome. J. Proteomics73(3), 619–626 (2010).
   PubMed Web of Science ®Google Scholar
• Bhattacharya D, Saha S, Basu S et al. Differential regulation of redox proteins and chaperones in HbE beta-thalassemia erythrocyte proteome. Proteomics Clin. Appl.4(5), 480–488 (2010).
   PubMed Web of Science ®Google Scholar
• Chakrabarti A, Bhattacharya D, Basu A, Basu S, Saha S, Halder S. Differential expression of red cell proteins in hemoglobinopathy. Proteomics Clin. Appl.5(1–2), 98–108 (2011).
   PubMed Web of Science ®Google Scholar
• Florens L, Washburn MP, Raine JD et al. A proteomic view of the Plasmodium falciparum life cycle. Nature419(6906), 520–526 (2002).
   PubMed Web of Science ®Google Scholar
• Lasonder E, Ishihama Y, Andersen JS et al. Analysis of the Plasmodium falciparum proteome by high-accuracy mass spectrometry. Nature419(6906), 537–542 (2002).
   PubMed Web of Science ®Google Scholar
• Sims PFG, Hyde JE. Proteomics of the human malaria parasite Plasmodium falciparum. Expert Rev. Proteomics3(1), 87–95 (2006).
   PubMed Web of Science ®Google Scholar
• Wu Y, Craig A. Comparative proteomic analysis of metabolically labelled proteins from Plasmodium falciparum isolates with different adhesion properties. Malar. J.5, 67 (2006).
   PubMed Web of Science ®Google Scholar
• Fried M, Hixson KK, Anderson L, Ogata Y, Mutabingwa TK, Duffy PE. The distinct proteome of placental malaria parasites. Mol. Biochem. Parasitol.155(1), 57–65 (2007).
   PubMed Web of Science ®Google Scholar
• Seghatchian J, de Sousa G. Pathogen-reduction systems for blood components: the current position and future trends. Transfus. Apher. Sci.35(3), 189–196 (2006).
   PubMed Web of Science ®Google Scholar
• Benjamin RJ, McCullough J, Mintz PD et al. Therapeutic efficacy and safety of red blood cells treated with a chemical process (S-303) for pathogen inactivation: a Phase III clinical trial in cardiac surgery patients. Transfusion45(11), 1739–1749 (2005).
   PubMed Web of Science ®Google Scholar
• Henschler R, Seifried E, Mufti N. Development of the S-303 pathogen inactivation technology for red blood cell concentrates. Transfus. Med. Hemother.38(1), 33–42 (2011).
   PubMed Web of Science ®Google Scholar
• Anniss AM, Glenister KM, Killian JJ, Sparrow RL. Proteomic analysis of supernatants of stored red blood cell products. Transfusion45(9), 1426–1433 (2005).
   PubMed Web of Science ®Google Scholar
• Koch CG, Li L, Sessler DI et al. Duration of red-cell storage and complications after cardiac surgery. N. Engl. J. Med.358(12), 1229–1239 (2008).
   PubMed Web of Science ®Google Scholar
• Rüesch M, Jutzi M. Annual haemovigilance report 2009. SwissMedic, Bern, Switzerland (2010).
   Google Scholar
• McCullough J, Vesole D, Benjamin RJ et al. Pathogen inactivated platelets (pit) using helinx technology (INTERCEPT plt) are hemostatically effective in thrombocytopenic patients (tcp pts): the SPRINT trial. Blood98(11 PART I), 450A (2001).
   PubMed Web of Science ®Google Scholar
• Osselaer JC, Cazenave JP, Lambermont M et al. An active haemovigilance programme characterizing the safety profile of 7437 platelet transfusions prepared with amotosalen photochemical treatment. Vox Sang.94(4), 315–323 (2008).
   PubMed Web of Science ®Google Scholar
• Osselaer JC, Messe N, Hervig T et al. A prospective observational cohort safety study of 5106 platelet transfusions with components prepared with photochemical pathogen inactivation treatment. Transfusion48(6), 1061–1071 (2008).
   PubMed Web of Science ®Google Scholar
• AuBuchon JP, Herschel L, Roger J et al. Efficacy of apheresis platelets treated with riboflavin and ultraviolet light for pathogen reduction. Transfusion45(8), 1335–1341 (2005).
   PubMed Web of Science ®Google Scholar
• Goodrich RP, Edrich RA, Li J, Seghatchian J. The Mirasol PRT system for pathogen reduction of platelets and plasma: an overview of current status and future trends. Transfus. Apher. Sci.35(1), 5–17 (2006).
   PubMed Web of Science ®Google Scholar
• Perez-Pujol S, Tonda R, Lozano M et al. Effects of a new pathogen-reduction technology (Mirasol PRT) on functional aspects of platelet concentrates. Transfusion45(6), 911–919 (2005).
   PubMed Web of Science ®Google Scholar
• Mohr H, Gravemann U, Bayer A, Müller TH. Sterilization of platelet concentrates at production scale by irradiation with short-wave ultraviolet light. Transfusion49(9), 1956–1963 (2009).
   PubMed Web of Science ®Google Scholar
• Mohr H, Steil L, Gravemann U et al. A novel approach to pathogen reduction in platelet concentrates using short-wave ultraviolet light. Transfusion49(12), 2612–2624 (2009).
   PubMed Web of Science ®Google Scholar
• Terpstra FG, Van’t Wout AB, Schuitemaker H et al. Potential and limitation of UVC irradiation for the inactivation of pathogens in platelet concentrates. Transfusion48(2), 304–313 (2008).
   PubMed Web of Science ®Google Scholar
• Springer DL, Miller JH, Spinelli SL et al. Platelet proteome changes associated with diabetes and during platelet storage for transfusion. J. Proteome Res.8(5), 2261–2272 (2009).
   PubMed Web of Science ®Google Scholar
• Wurtz V, Hechler B, Ohlmann P, Isola H, Schaeffer-Reiss C, Cazenave JP. Identification of platelet factor 4 and β-thromboglobulin by profiling and liquid chromatography tandem mass spectrometry of supernatant peptides in stored apheresis and buffy-coat platelet concentrates. Transfusion47(6), 1099–1101 (2007).
   PubMed Web of Science ®Google Scholar
• Kluter H, Bubel S, Kirchner H, Wilhelm D. Febrile and allergic transfusion reactions after the transfusion of white cell-poor platelet preparations. Transfusion39(11–12), 1179–1184 (1999).
   PubMed Web of Science ®Google Scholar
• Dittrich M, Birschmann I, Mietner S, Sickmann A, Walter U, Dandekar T. Platelet protein interactions – map, signaling components, and phosphorylation groundstate. Arterioscler. Thromb. Vasc. Biol.28(7), 1326–1331 (2008).
   PubMed Web of Science ®Google Scholar
• Zhang CC, Rogalski JC, Evans DM, Klockenbusch C, Beavis RC, Kast J. In silico protein interaction analysis using the global proteome machine database. J. Proteome Res.10(2), 656–668 (2011).
   PubMed Web of Science ®Google Scholar
• Hellstern P, Solheim BG. The use of solvent/detergent treatment in pathogen reduction of plasma. Transfus. Med. Hemother.38(1), 65–70 (2011).
   PubMed Web of Science ®Google Scholar
• Rock G. A comparison of methods of pathogen inactivation of FFP. Vox Sang.100(2), 169–178 (2011).
   PubMed Web of Science ®Google Scholar
• Singh Y, Sawyer LS, Pinkoski LS et al. Photochemical treatment of plasma with amotosalen and long-wavelength ultraviolet light inactivates pathogens while retaining coagulation function. Transfusion46(7), 1168–1177 (2006).
   PubMed Web of Science ®Google Scholar
• Seghatchian J, Struff WG, Reichenberg S. Main properties of the THERAFLEX MB-plasma system for pathogen reduction. Transfus. Med. Hemother.38(1), 55–64 (2011).
   PubMed Web of Science ®Google Scholar
• Seltsam A, Muller TH. UVC irradiation for pathogen reduction of platelet concentrates and plasma. Transfus. Med. Hemother.38(1), 43–54 (2011).
   PubMed Web of Science ®Google Scholar
• Dewachter P, Castro S, Nicaise-Roland P et al. Anaphylactic reaction after methylene blue-treated plasma transfusion. Br. J. Anaesth.106(5), 687–689 (2011).
   PubMed Web of Science ®Google Scholar
• Nubret K, Delhoume M, Orsel I, Laudy JS, Sellami M, Nathan N. Anaphylactic shock to fresh-frozen plasma inactivated with methylene blue. Transfusion51(1), 125–128 (2011).
   PubMed Web of Science ®Google Scholar
• Gaso-Sokac D, Josic D. The role of proteomics in plasma fractionation and quality control of plasma-derived therapeutic proteins. Blood Transf.8, S86–S91 (2010).
   Google Scholar
• Yang XL, Clifton JG, Huang FL, Kovac S, Hixson DC, Josic D. Proteomic analysis for process development and control of therapeutic protein separation from human plasma. Electrophoresis30(7), 1185–1193 (2009).
   PubMed Web of Science ®Google Scholar
• Clifton JG, Huang FL, Kovac S, Yang XL, Hixson DC, Josic D. Proteomic characterization of plasma-derived clotting factor VIII-von Willebrand factor concentrates. Electrophoresis30(20), 3636–3646 (2009).
   PubMed Web of Science ®Google Scholar
• Clifton JG, Huang FL, Gaso-Sokac D, Brilliant K, Hixson D, Josic D. Use of proteomics for validation of the isolation process of clotting factor IX from human plasma. J. Proteomics73(3), 678–688 (2010).
   PubMed Web of Science ®Google Scholar
• Basilico F, Nardini I, Mori F et al. Characterization of factor VIII pharmaceutical preparations by means of MudPIT proteomic approach. J. Pharm. Biomed. Anal.53(1), 50–57 (2010).
   PubMed Web of Science ®Google Scholar
• Custer B, Agapova M, Martinez RH. The cost–effectiveness of pathogen reduction technology as assessed using a multiple risk reduction model. Transfusion50(11), 2461–2473 (2010).
   PubMed Web of Science ®Google Scholar
• Hirth RA, Chernew ME, Miller E, Fendrick AM, Weissert WG. Willingness to pay for a quality-adjusted life year: in search of a standard. Med. Decis. Mak.20(3), 332–342 (2000).
   PubMed Web of Science ®Google Scholar
• Davidson T, Ekermo B, Gaines H, Lesko B, Akerlind B. The cost–effectiveness of introducing nucleic acid testing to test for hepatitis B, hepatitis C, and human immunodeficiency virus among blood donors in Sweden. Transfusion51(2), 421–429 (2011).
   PubMed Web of Science ®Google Scholar
• AuBuchon JP. Update on the status of pathogen inactivation methods. ISBT Science Series6(1), 181–188 (2011).
   Google Scholar
• Janssen MP, van der Poel CL, Buskens E, Bonneux L, Bonsel GJ, van Hout BA. Costs and benefits of bacterial culturing and pathogen reduction in The Netherlands. Transfusion46(6), 956–965 (2006).
   PubMed Web of Science ®Google Scholar
• Feuchtbaum L, Cunningham G. Economic evaluation of tandem mass spectrometry screening in California. Pediatrics117(5), S280–S286 (2006).
   PubMed Web of Science ®Google Scholar
• Borman SA. New Year, new instruments. Chemical and Engineering News89(14), 37–40 (2011).
   Google Scholar
• Martens L, Vizcaino JA, Banks R. Quality control in proteomics. Proteomics11(6), 1015–1016 (2011).
   PubMed Web of Science ®Google Scholar
• Burkhart JM, Vaudel M, Zahedi RP, Martens L, Sickmann A. iTRAQ protein quantification: a quality-controlled workflow. Proteomics11(6), 1125–1134 (2011).
   PubMed Web of Science ®Google Scholar
• Köcher T, Pichler P, Swart R, Mechtler K. Quality control in LC-MS/MS. Proteomics11(6), 1026–1030 (2011).
   PubMed Web of Science ®Google Scholar
• Campbell J, Rezai T, Prakash A et al. Evaluation of absolute peptide quantitation strategies using slected reaction monitoring. Proteomics11(6), 1148–1152 (2011).
   PubMed Web of Science ®Google Scholar
• Barelli S, Crettaz D, Thadikkaran L, Rubin O, Tissot JD. Plasma/serum proteomics: pre-analytical issues. Expert Rev. Proteomics4(3), 363–370 (2007).
   PubMed Web of Science ®Google Scholar
• Dugo P, Cacciola F, Kumm T, Dugo G, Mondello L. Comprehensive multidimensional liquid chromatography: theory and applications. J. Chromatogr. A1184(1–2), 353–368 (2008).
   PubMed Web of Science ®Google Scholar
• Tang J, Gao M, Deng C, Zhang X. Recent development of multi-dimensional chromatography strategies in proteome research. J. Chromatogr. B Analyt. Technol. Biomed. Life Sci.866(1–2), 123–132 (2008).
   PubMed Web of Science ®Google Scholar
• Wei J, Sun J, Yu W et al. Global proteome discovery using an online three-dimensional LC-MS/MS. J. Proteome Res.4(3), 801–808 (2005).
   PubMed Web of Science ®Google Scholar
• Thompson A, Schafer J, Kuhn K et al. Tandem mass tags: a novel quantification strategy for comparative analysis of complex protein mixtures by MS/MS. Anal. Chem.75(8), 1895–1904 (2003).
   PubMed Web of Science ®Google Scholar
• Timms JF, Cramer R. Difference gel electrophoresis. Proteomics8(23–24), 4886–4897 (2008).
   PubMed Web of Science ®Google Scholar
• Minden JS, Dowd SR, Meyer HE, Stuhler K. Difference gel electrophoresis. Electrophoresis30(Suppl. 1), S156–S161 (2009).
   PubMed Web of Science ®Google Scholar
• Kitteringham NR, Jenkins RE, Lane CS, Elliott VL, Park BK. Multiple reaction monitoring for quantitative biomarker analysis in proteomics and metabolomics. J. Chromatogr. B Analyt. Technol. Biomed. Life Sci.877(13), 1229–1239 (2009).
   PubMed Web of Science ®Google Scholar
• Lange V, Picotti P, Domon B, Aebersold R. Selected reaction monitoring for quantitative proteomics: a tutorial. Mol. Syst. Biol.4, 222 (2008).
   PubMed Web of Science ®Google Scholar
• 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. USA100(12), 6940–6945 (2003).
   PubMed Web of Science ®Google Scholar
• Kirkpatrick DS, Gerber SA, Gygi SP. The absolute quantification strategy: a general procedure for the quantification of proteins and post-translational modifications. Methods35(3), 265–273 (2005).
   PubMed Web of Science ®Google Scholar
• Ong SE, Blagoev B, Kratchmarova I et al. Stable isotope labeling by amino acids in cell culture, SILAC, as a simple and accurate approach to expression proteomics. Mol. Cell Proteomics1(5), 376–386 (2002).
   PubMed Web of Science ®Google Scholar
• Gygi SP, Rist B, Gerber SA, Turecek F, Gelb MH, Aebersold R. Quantitative analysis of complex protein mixtures using isotope-coded affinity tags. Nat. Biotechnol.17(10), 994–999 (1999).
   PubMed Web of Science ®Google Scholar
• Ross PL, Huang YN, Marchese JN et al. Multiplexed protein quantitation in Saccharomyces cerevisiae using amine-reactive isobaric tagging reagents. Mol. Cell Proteomics3(12), 1154–1169 (2004).
   PubMed Web of Science ®Google Scholar
• Anderson NL, Anderson NG. The human plasma proteome – history, character, and diagnostic prospects. Mol. Cell. Proteomics1(11), 845–867 (2002).
   PubMed Web of Science ®Google Scholar
• Ly L, Wasinger VC. Protein and peptide fractionation, enrichment and depletion: tools for the complex proteome. Proteomics11(4), 513–534 (2011).
   PubMed Web of Science ®Google Scholar
• Fitzgerald A, Walsh BJ. New method for prefractionation of plasma for proteomic analysis. Electrophoresis31(21), 3580–3585 (2010).
   PubMed Web of Science ®Google Scholar
• Boschetti E, Righetti PG. The ProteoMiner in the proteomic arena: a non-depleting tool for discovering low-abundance species. J. Proteomics71(3), 255–264 (2008).
   PubMed Web of Science ®Google Scholar
• Righetti PG, Boschetti E, Lomas L, Citterio A. Protein Equalizer™ technology: the quest for a ‘democratic proteome’. Proteomics6(14), 3980–3992 (2006).
   PubMed Web of Science ®Google Scholar
• Righetti PG, Boschetti E. Blood proteomics and the dynamic range: some light at the end of the tunnel? J. Proteomics73(3), 627–628 (2010).
   PubMed Web of Science ®Google Scholar