|
1.Seo J and Lee KJ, Post-translational modifications and their biological functions: proteomic analysis and systematic approaches. J Biochem Mol Biol, 2004. 37, 35-44.
2.Yarema KJ and Bertozzi CR, Characterizing glycosylation pathways. Genome Biol, 2001. 2, REVIEWS0004.
3.Marquardt T and Denecke J, Congenital disorders of glycosylation: review of their molecular bases, clinical presentations and specific therapies. Eur J Pediatr, 2003. 162, 359-379.
4.Zhang Y and Reinberg D, Transcription regulation by histone methylation: interplay between different covalent modifications of the core histone tails. Genes Dev, 2001. 15, 2343-2360.
5.Eberharter A, and Becker PB, Histone acetylation: a switch between repressive and permissive chromatin. Second in review series on chromatin dynamics. EMBO Rep, 2002. 3, 224-229.
6.Hunter T, Signaling--2000 and beyond. Cell, 2000. 100, 113-127.
7.Posada J and Cooper JA, Molecular signal integration. Interplay between serine, threonine, and tyrosine phosphorylation. Mol Biol Cell, 1992. 3, 583-592.
8.Siegel GJ, Agranoff BW, Albers RW, Fisher SK, and Uhler MD, Basic neurochemistry: molecular, cellular, and medical aspects. 6th edition, 1999. Philadelphia: Lippincott-Raven.
9. http://nobelprize.org/nobel_prizes/medicine/laureates/1992/
press.html
10.Everett CJ, Frithsen I, and Player M, Relationship of polychlorinated biphenyls with type 2 diabetes and hypertension. J Environ Monit, 2011. 13, 241-251.
11.Borai A, Livingstone C, Ghayour-Mobarhan M, Abuosa A, Shafi S, Mehta S, Heidari A, Emadzadeh A, Wark G, and Ferns G, Serum insulin-like growth factor binding protein-1 (IGFBP-1) phosphorylation status in subjects with and without ischaemic heart disease. Atherosclerosis, 2010. 208, 593-598.
12.Waseem A, Karsten U, Leigh IM, Purkis P, Waseem NH, and Lane E, Conformational changes in the rod domain of human keratin 8 following heterotypic association with keratin 18 and its implication for filament stability. Biochemistry, 2004. 43, 1283-1295.
13.Ku NO and Omary MB, A disease- and phosphorylation-related nonmechanical function for keratin 8. J Cell Biol, 2006. 174, 115-125.
14.Hoffert JD, Pisitkun T, Wang G, Shen RF, Knepper MA, Quantitative phosphoproteomics of vasopressin-sensitive renal cells: regulation of aquaporin-2 phosphorylation at two sites. Proc Natl Acad Sci U S A, 2006. 103, 7159-7164.
15.Fenton RA, Moeller HB, Hoffert JD, Yu MJ, Nielsen S, and Knepper MA, Acute regulation of aquaporin-2 phosphorylation at Ser-264 by vasopressin. Proc Natl Acad Sci U S A, 2008. 105, 3134-3139.
16.Karin M and Hunter T, Transcriptional control by protein phosphorylation: signal transmission from the cell surface to the nucleus. Curr Biol, 1995. 5, 747-757.
17.Karin M, Signal transduction from the cell surface to the nucleus through the phosphorylation of transcription factors. Curr Opin Cell Biol, 1994. 6, 415-424.
18.Lane RF, Gatson JW, Small SA, Ehrlich ME, and Gandy S, Protein kinase C and rho activated coiled coil protein kinase 2 (ROCK2) modulate Alzheimer''s APP metabolism and phosphorylation of the Vps10-domain protein, SorL1. Mol Neurodegener, 2010. 5, 62.
19.Maillet M, Purcell NH, Sargent MA, York AJ, Bueno OF, and Molkentin JD, DUSP6 (MKP3) null mice show enhanced ERK1/2 phosphorylation at baseline and increased myocyte proliferation in the heart affecting disease susceptibility. J Biol Chem, 2008. 283, 31246-31255.
20.Tanaka T, Halicka D, Traganos F, and Darzynkiewicz Z, Cytometric analysis of DNA damage: phosphorylation of histone H2AX as a marker of DNA double-strand breaks (DSBs). Methods Mol Biol, 2009. 523, 161-168.
21.Khromov A, Choudhury N, Stevenson AS, Somlyo AV, and Eto M, Phosphorylation-dependent autoinhibition of myosin light chain phosphatase accounts for Ca2+ sensitization force of smooth muscle contraction. The J Biol Chem, 2009. 284, 21569-21579.
22.Dhanasekaran DN, Kashef K, Lee CM, Xu H, and Reddy EP, Scaffold proteins of MAP-kinase modules. Oncogene, 2007. 26, 3185-3202.
23.van Amerongen R and Nusse R, Towards an integrated view of Wnt signaling in development. Development, 2009. 136, 3205-3214.
24. Joussen AM, Doehmen S, Le ML, Koizumi K, Radetzky S, Krohne TU, Poulaki V, Semkova I, and Kociok N, TNF-α mediated apoptosis plays an important role in the development of early diabetic retinopathy and long-term histopathological alterations. Mol Vis, 2009. 15, 1418-1428.
25.O'' Reilly LA, Tai L, Lee L, Kruse EA, Grabow S, Fairlie WD, Haynes NM, Tarlinton DM, Zhang JG, Belz GT, Smyth MJ, Bouillet P, Robb L, and Strasser A, Membrane-bound Fas ligand only is essential for Fas-induced apoptosis. Nature, 2009. 461, 659-663.
26.Kufe DW, Pollock RE, Weichselbaum RR, Bast RC Jr, Gansler TS, Holland JF, and Frei E, Holland-Frei Cancer Medicine. 6th edition, 2003. Hamilton: BC Decker.
27.Thornton TM and Rincon M, Non-classical p38 map kinase functions: cell cycle checkpoints and survival. International Int J Biol Sci, 2009. 5, 44-51.
28.Luo H, Li Y, Mu JJ, Zhang J, Tonaka T, Hamamori Y, Jung SY, Wang Y, and Qin J, Regulation of intra-S phase checkpoint by ionizing radiation (IR)-dependent and IR-independent phosphorylation of SMC3. The J Biol Chem, 2008. 283, 19176-19183.
29.Nair JS, Ho AL, Tse AN, Coward J, Cheema H, Ambrosini G, Keen N, and Schwartz GK, Aurora B kinase regulates the postmitotic endoreduplication checkpoint via phosphorylation of the retinoblastoma protein at serine 780. Mol Biol Cell, 2009. 20, 2218-2228.
30.van Vugt MA, Gardino AK, Linding R, Ostheimer GJ, Reinhardt HC, Ong SE, Tan CS, Miao H, Keezer SM, Li J, Pawson T, Lewis TA, Carr SA, Smerdon SJ, Brummelkamp TR, and Yaffe MB, A mitotic phosphorylation feedback network connects Cdk1, Plk1, 53BP1, and Chk2 to inactivate the G(2)/M DNA damage checkpoint. PLoS Biol, 2010. 8, e1000287.
31.Whibley C, Pharoah PD, and Hollstein M, p53 polymorphisms: cancer implications. Nat Rev Cancer, 2009. 9, 95-107.
32.Liu DP, Song H, and Xu Y, A common gain of function of p53 cancer mutants in inducing genetic instability. Oncogene, 2010. 29, 949-956.
33.Sluss HK, Gannon H, Coles AH, Shen Q, Eischen CM, and Jones SN, Phosphorylation of p53 serine 18 upregulates apoptosis to suppress Myc-induced tumorigenesis. Mol Cancer Res, 2010. 8, 216-222.
34.Demidenko ZN, Kalurupalle S, Hanko C, Lim CU, Broude E, and Blagosklonny MV, Mechanism of G1-like arrest by low concentrations of paclitaxel: next cell cycle p53-dependent arrest with sub G1 DNA content mediated by prolonged mitosis. Oncogene, 2008. 27, 4402-4410.
35.Bourougaa K, Naski N, Boularan C, Mlynarczyk C, Candeias MM, Marullo S, and Fåhraeus R, Endoplasmic reticulum stress induces G2 cell-cycle arrest via mRNA translation of the p53 isoform p53/47. Mol Cell, 2010. 38, 78-88.
36.Hanger DP, Anderton BH, and Noble W, Tau phosphorylation: the therapeutic challenge for neurodegenerative disease. Trends Mol Med, 2009. 15, 112-119.
37.Ittner LM and Götz J, Amyloid-beta and tau--a toxic pas de deux in Alzheimer''s disease. Nat Rev Neurosci, 2011. 12, 65-72.
38.Grimsrud PA, Swaney DL, Wenger CD, Beauchene NA, and Coon JJ, Phosphoproteomics for the masses. ACS Chem Biol, 2010. 5, 105-119.
39.Guo D, Jia Q, Song HY, Warren RS, and Donner DB, Vascular endothelial cell growth factor promotes tyrosine phosphorylation of mediators of signal transduction that contain SH2 domains. Association with endothelial cell proliferation. J Biol Chem, 1995. 270, 6729-6733.
40.Barria A, Muller D, Derkach V, Griffith LC, and Soderling TR, Regulatory phosphorylation of AMPA-type glutamate receptors by CaM-KII during long-term potentiation. Science, 1997. 276, 2042-2045.
41.Palkowitsch L, Leidner J, Ghosh S, and Marienfeld RB, Phosphorylation of serine 68 in the IkappaB kinase (IKK)-binding domain of NEMO interferes with the structure of the IKK complex and tumor necrosis factor-alpha-induced NF-kappaB activity. J Biol Chem, 2008. 283, 76-86.
42.Hillenkamp F, Karas M, Beavis RC, and Chait BT, Matrix-assisted laser desorption/ionization mass spectrometry of biopolymers. Anal Chem, 1991. 63, 1193-1203.
43.Siegel MM, Hollander IJ, Hamann PR, James JP, Hinman L, Smith BJ, Farnsworth AP, Phipps A, King DJ, Karas M, Ingendoh A, and Hillenkamp F, Matrix-assisted UV-laser desorption/ionization mass spectrometric analysis of monoclonal antibodies for the determination of carbohydrate, conjugated chelator, and conjugated drug content. Anal Chem, 1991. 63, 2470-2481.
44.Smith RD, Loo JA, Edmonds CG, Barinaga CJ, and Udseth HR, New developments in biochemical mass spectrometry: electrospray ionization. Anal Chem, 1990. 62, 882-899.
45.Loo JA, Studying noncovalent protein complexes by electrospray ionization mass spectrometry. Mass Spectrom Rev, 1997. 16, 1-23.
46.Schlosser A, Pipkorn R, Bossemeyer D, and Lehmann WD, Analysis of protein phosphorylation by a combination of elastase digestion and neutral loss tandem mass spectrometry. Anal Chem, 2001. 73, 170-176.
47.Sweet SM, Creese AJ, and Cooper HJ, Strategy for the identification of sites of phosphorylation in proteins: neutral loss triggered electron capture dissociation. Anal Chem, 2006. 78, 7563-7569.
48.Gafken PR and Lampe PD, Methodologies for characterizing phosphoproteins by mass spectrometry. Cell Commun Adhes, 2006. 13, 249-262.
49.del Peso L, González-García M, Page C, Herrera R, and Nuñez G, Interleukin-3-induced phosphorylation of BAD through the protein kinase Akt. Science, 1997. 278, 687-689.
50.Zheng-Fischhöfer Q, Biernat J, Mandelkow EM, Illenberger S, Godemann R, and Mandelkow E, Sequential phosphorylation of Tau by glycogen synthase kinase-3beta and protein kinase A at Thr212 and Ser214 generates the Alzheimer-specific epitope of antibody AT100 and requires a paired-helical-filament-like conformation. Eur J Biochem, 1998. 252, 542-552.
51.Beausoleil SA, Villén J, Gerber SA, Rush J, and Gygi SP, A probability-based approach for high-throughput protein phosphorylation analysis and site localization. Nat Biotechnol, 2006. 24, 1285-1292.
52.Blacken GR, Gelb MH, and Turecek F, Metal affinity capture tandem mass spectrometry for the selective detection of phosphopeptides. Anal Chem, 2006. 78, 6065-6073.
53.Dunn JD, Watson JT, and Bruening ML, Detection of phosphopeptides using Fe(III)-nitrilotriacetate complexes immobilized on a MALDI plate. Anal Chem, 2006. 78, 1574-1580.
54.Dai J, Jin WH, Sheng QH, Shieh CH, Wu JR, and Zeng R, Protein phosphorylation and expression profiling by Yin-yang multidimensional liquid chromatography (Yin-yang MDLC) mass spectrometry. J Proteome Res, 2007. 6, 250-262.
55.Xu S, Whitin JC, Yu TT, Zhou H, Sun D, Sue HJ, Zou H, Cohen HJ, and Zare RN, Capture of phosphopeptides using alpha-zirconium phosphate nanoplatelets. Anal Chem, 2008. 80, 5542-5549.
56.Thingholm TE, Jensen ON, Robinson PJ, and Larsen MR, SIMAC (sequential elution from IMAC), a phosphoproteomics strategy for the rapid separation of monophosphorylated from multiply phosphorylated peptides. Mol Cell Proteomics, 2008. 7, 661-671.
57.Pinkse MW, Mohammed S, Gouw JW, van Breukelen B, Vos HR, and Heck AJ, Highly robust, automated, and sensitive online TiO2-based phosphoproteomics applied to study endogenous phosphorylation in Drosophila melanogaster. J Proteome Res, 2008. 7, 687-697.
58.Yu LR, Zhu Z, Chan KC, Issaq HJ, Dimitrov DS, and Veenstra TD, Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra. J Proteome Res, 2007. 6, 4150-4162.
59.Imanishi SY, Kochin V, Ferraris SE, de Thonel A, Pallari HM, Corthals GL, and Eriksson JE, Reference-facilitated phosphoproteomics: fast and reliable phosphopeptide validation by microLC-ESI-Q-TOF MS/MS. Mol Cell Proteomics, 2007. 6, 1380-1391.
60.Villén J and Gygi SP, The SCX/IMAC enrichment approach for global phosphorylation analysis by mass spectrometry. Nat Protoc, 2008. 3, 1630-1638.
61.Thingholm TE, Jensen ON, and Larsen MR, Analytical strategies for phosphoproteomics. Proteomics, 2009. 9, 1451-1468.
62.Aggarwal K, Choe LH, and Lee KH, Shotgun proteomics using the iTRAQ isobaric tags. Brief Funct Genomic Proteomic, 2006. 5, 112-120.
63.Wiese S, Reidegeld KA, Meyer HE, and Warscheid B, Protein labeling by iTRAQ: a new tool for quantitative mass spectrometry in proteome research. Proteomics, 2007. 7, 340-350.
64.Zieske LR, A perspective on the use of iTRAQ reagent technology for protein complex and profiling studies. J Exp Bot, 2006. 57, 1501-1518.
65.Matthias M, Functional and quantitative proteomics using SILAC. Nat Rev Mol Cell Biol, 2006. 7, 952-958.
66.Everley PA, Krijgsveld J, Zetter BR, and Gygi SP, 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.
67.Kirkpatrick DS, Gerber SA, and Gygi SP, The absolute quantification strategy: a general procedure for the quantification of proteins and post-translational modifications. Methods, 2005. 35, 265-273.
68.O Turapov OA, Mukamolova GV, Bottrill AR, and Pangburn MK, Digestion of native proteins for proteomics using a thermocycler. Anal Chem, 2008. 80, 6093-6099.
69.López-Ferrer D, Capelo JL, and Vázquez J, Ultra fast trypsin digestion of proteins by high intensity focused ultrasound. J Proteome Res, 2005. 4, 1569-1574.
70.López-Ferrer D, Petritis K, Lourette NM, Clowers B, Hixson KK, Heibeck T, Prior DC, Pasa-Tolić L, Camp DG 2nd, Belov ME, and Smith RD, On-line digestion system for protein characterization and proteome analysis. Anal Chem, 2008. 80, 8930-8936.
71.Wang S, Bao H, Liu T, Zhang L, Yang P, and Chen G, Accelerated proteolysis in alternating electric fields for peptide mapping. Rapid Commun Mass Spectrom, 2008. 22, 3225-3232.
72. Chen CC, Chen CF, Chen CM, and Chuang FT, Modification of multi-walled carbon nanotubes by microwave digestion method as electrocatalyst supports for direct methanol fuel cell applications. Electrochem commun, 2007. 9, 159-163
73.Pramanik BN, Mirza UA, Ing YH, Liu YH, Bartner PL, Weber PC, and Bose AK, Microwave-enhanced enzyme reaction for protein mapping by mass spectrometry: a new approach to protein digestion in minutes. Protein Sci, 2002. 11, 2676-2687.
74.Juan HF, Chang SC, Huang HC, and Chen ST, A new application of microwave technology to proteomics. Proteomics, 2005. 5, 840-842.
75.Vesper HW, Mi L, Enada A, and Myers GL, Assessment of microwave-assisted enzymatic digestion by measuring glycated hemoglobin A1c by mass spectrometry. Rapid Commun Mass Spectrom, 2005. 19, 2865-2870.
76.Lill JR, Ingle ES, Liu PS, Pham V, and Sandoval WN, Microwave-assisted proteomics. Mass Spectrom Rev, 2007. 26, 657-671.
77.Capelo JL, Carreira R, Diniz M, Fernandes L, Galesio M, Lodeiro C, Santos HM, and Vale G, Overview on modern approaches to speed up protein identification workflows relying on enzymatic cleavage and mass spectrometry-based techniques. Anal Chim Acta, 2009. 650, 151-159.
78.Thaler F, Valsasina B, Baldi R, Xie J, Stewart A, Isacchi A, Kalisz HM, and Rusconi L, A new approach to phosphoserine and phosphothreonine analysis in peptides and proteins: chemical modification, enrichment via solid-phase reversible binding, and analysis by mass spectrometry. Anal Bioanal Chem, 2003. 376, 366-373.
79.Riedel M, Goldbaum O, and Richter-Landsberg C, Alpha-Synuclein promotes the recruitment of tau to protein inclusions in oligodendroglial cells: effects of oxidative and proteolytic stress. J Mol Neurosci, 2009. 39, 226-234.
80.Magliaro BC, and Saldanha CJ, Clozapine protects PC-12 cells from death due to oxidative stress induced by hydrogen peroxide via a cell-type specific mechanism involving inhibition of extracellular signal-regulated kinase phosphorylation. Brain Res, 2009. 1283, 14-24.
81. Castegna A, Aksenov M, Thongboonkerd V, Klein JB, Pierce WM, Booze R, Markesbery WR, and Butterfield DA, Proteomic identification of oxidatively modified proteins in Alzheimer’s disease brain. Part II: dihydropyrimidinase-related protein 2, a-enolase and heat shock cognate 71. J Neurochem, 2002. 82, 1524-1532.
82. Dastoor Z and Dreyer J, Nuclear translocation and aggregate formation of heat shock cognate protein 70 (Hsc70) in oxidative stress and apoptosis. J Cell Sci, 2000. 113, 2845-2854.
83. Haase H, Ahnak, a new player in β-adrenergic regulation of the cardiac L-type Ca2+ channel. Cardiovasc Res, 2007. 73, 19–25.
84. Sussman J, Stokoe D, Ossina N, and Shtivelman E, Protein kinase B phosphorylates AHNAK and regulates its subcellular localization. J Cell Biol, 2001. 154, 1019-1030.
85. Lee IH, Lim HJ, Yoon S, Seong JK, Bae DS, Rhee SG, and Bae YS, Ahnak protein activates protein kinase c (pkc) through dissociation of the pkc-protein phosphatase 2a complex. J Biol Chem, 2008. 283, 6312-6320.
86. Shatunov A, Olivé M, Odgerel Z, Stadelmann-Nessler C, Irlbacher K, van Landeghem F, Bayarsaikhan M, Lee HS, Goudeau B, Chinnery PF, Straub V, Hilton-Jones D, Damian MS, Kaminska A, Vicart P, Bushby K, Dalakas MC, Sambuughin N, Ferrer I, Goebel HH, and Goldfarb LG, In-frame deletion in the seventh immunoglobulin-like repeat of filamin C in a family with myofibrillar myopathy. Eur J Hum Genet, 2009. 17, 656-663.
87. Grünblatt E, Mandel S, Jacob-Hirsch J, Zeligson S, Amariglo N, Rechavi G, Li J, Ravid R, Roggendorf W, Riederer P, and Youdim MB, Gene expression profiling of parkinsonian substantia nigra pars compacta; alterations in ubiquitin-proteasome, heat shock protein, iron and oxidative stress regulated proteins, cell adhesion/cellular matrix and vesicle trafficking genes. J Neural Transm, 2004. 111, 1543-1573.
88. Benjamin IJ and McMillan DR, Stress (heat shock) proteins molecular chaperones in cardiovascular biology and disease. Circ Res, 1998. 83, 117-132.
89. Walker MB, Miller CT, Swartz ME, Eberhart JK, and Kimmel CB, Phospholipase C, beta 3 is required for Endothelin1 regulation of pharyngeal arch patterning in zebrafish. Dev Biol, 2007. 304, 194-207.
90. Roach TI, Rebres RA, Fraser ID, Decamp DL, Lin KM, Sternweis PC, Simon MI, and Seaman WE, Signaling and cross-talk by C5a and UDP in macrophages selectively use PLCβ3 to regulate intracellular fFree calcium. J Biol Chem, 2008. 283, 17351-17361.
91. Frankowski H, Castro-Obregon S, del Rio G, Rao RV, and Bredesen DE, PLAIDD, a type II death domain protein that interacts with p75 neurotrophin receptor. Neuromolecular Med, 2002. 1, 153-170.
92. Sarek G, Järviluoma A, Moore HM, Tojkander S, Vartia S, Biberfeld P, Laiho M, and Ojala PM, Nucleophosmin phosphorylation by v-cyclin-CDK6 controls KSHV latency. PLoS Pathog, 2010. 6, e1000818.
93. Brady SN, Maggi LB Jr, Winkeler CL, Toso EA, Gwinn AS, Pelletier CL, and Weber JD, Nucleophosmin protein expression level, but not threonine 198 phosphorylation, is essential in growth and proliferation. Oncogene, 2009. 28, 3209-3220.
94. Lin CY, Tan BC, Liu H, Shih CJ, Chien KY, Lin CL, and Yung BY, Dephosphorylation of nucleophosmin by PP1 facilitates pRB binding and consequent E2F1-dependent DNA repair. Mol Biol Cell, 2010. 21, 4409-4417.
95. Lee SM, Kim JH, Cho EJ, and Youn HD, A nucleocytoplasmic malate dehydrogenase regulates p53 transcriptional activity in response to metabolic stress. Cell Death Differ, 2009. 16, 738-748.
96. Christofk HR, Vander Heiden MG, Harris MH, Ramanathan A, Gerszten RE, Wei R, Fleming MD, Schreiber SL, and Cantley LC, The M2 splice isoformof pyruvate kinase is important for cancer metabolism and tumour growth. Nature, 2008. 452, 230-234.
97. Christofk HR, Vander Heiden MG, Wu N, Asara JM, and Cantley LC, Pyruvate kinase M2 is a phosphotyrosine-binding protein. Nature, 2008. 452, 181-188.
98. Clower CV, Chatterjee D, Wang Z, Cantley LC, Vander Heiden MG, and Krainer AR, The alternative splicing repressors hnRNP A1/A2 and PTB influence pyruvate kinase isoform expression and cell metabolism. Proc Natl Acad Sci U S A, 2010. 107, 1894-1899.
99. Zhao P, Zhang L, Zhong W, Ying X, Huang H, Yao B, Yuan Z, Fu J, Wang Y, and Zhou Z, Antigen-subtracted 2-DE/MS strategy, a novel proteomic analysis platform. Arch Toxicol, 2011. 85, 35–41
100. Eltoweissy M, Müller GA, Bibi A, Nguye PV, Dihazi GH, Müller CA, and Dihazi H, Proteomics analysis identifies PARK7 as an important player for renal cell resistance and survival under oxidative stress. Mol Biosyst, 2011. 7, 1277-1288.
101. Liu X, Ren Z, Zhan R, Wang X, Wang X, Zhang Z, Leng X, Yang Z, and Qian L, Prohibitin protects against oxidative stress-induced cell injury in cultured neonatal cardiomyocyte. Cell Stress Chaperones, 2009. 14, 311-319.
102. Theiss AL, Idell RD, Srinivasan S, Klapproth JM, Jones DP, Merlin D, and Sitaraman SV, Prohibitin protects against oxidative stress in intestinal epithelial cells. FASEB J, 2007. 21, 197-206.
103. Gin P, Hsu AY, Rothman SC, Jonassen T, Lee PT, Tzagoloff A, and Clarke CF, The saccharomyces cerevisiae COQ6 gene encodes a mitochondrial flavin-dependent monooxygenase required for coenzyme Q biosynthesis. J Biol Chem, 2003. 278, 25308-25316.
104. Bhattacharjee A, Majumdar U, Maity D, Sarkar TS, Goswami AM, Sahoo R, and Ghosh S, In vivo protein tyrosine nitration in S. cerevisiae: Identification of tyrosine-nitrated proteins in mitochondria. Biochem Biophys Res Commun, 2009. 388, 612-617.
105.Zhu W, Smith JW, and Huang CM, Mass spectrometry-based label-free quantitative proteomics. J Biomed Biotechnol, 2010. 2010, 1-6.
|