{"database":"JPOST Repository","file_versions":[{"headers":{"Content-Type":["application/json"]},"body":{"files":{"Raw":["https://storage.jpostdb.org/JPST001186/files/181107QE_OVA_titamag_1.raw","https://storage.jpostdb.org/JPST001186/files/181107QE_OVA_titamag_3.raw","https://storage.jpostdb.org/JPST001186/files/190514QE_HEK_PTM_2.raw","https://storage.jpostdb.org/JPST001186/files/180912QE_OVA_mag_1.raw","https://storage.jpostdb.org/JPST001186/files/190514QE_HEK_PTA_2.raw","https://storage.jpostdb.org/JPST001186/files/180912QE_OVA_aga_1.raw","https://storage.jpostdb.org/JPST001186/files/180912QE_OVA_tita_1.raw","https://storage.jpostdb.org/JPST001186/files/180912QE_OVA_mag_2.raw","https://storage.jpostdb.org/JPST001186/files/190514QE_HEK_Tita_2.raw","https://storage.jpostdb.org/JPST001186/files/190514QE_HEK_PTM_1.raw","https://storage.jpostdb.org/JPST001186/files/190514QE_HEK_PTM_3.raw","https://storage.jpostdb.org/JPST001186/files/181107QE_OVA_titamag_2.raw","https://storage.jpostdb.org/JPST001186/files/180912QE_OVA_tita_3.raw","https://storage.jpostdb.org/JPST001186/files/190514QE_HEK_PTA_3.raw","https://storage.jpostdb.org/JPST001186/files/180912QE_OVA_aga_2.raw","https://storage.jpostdb.org/JPST001186/files/190514QE_HEK_Tita_3.raw","https://storage.jpostdb.org/JPST001186/files/180912QE_OVA_aga_3.raw","https://storage.jpostdb.org/JPST001186/files/190514QE_HEK_PTA_1.raw","https://storage.jpostdb.org/JPST001186/files/180912QE_OVA_tita_2.raw","https://storage.jpostdb.org/JPST001186/files/180912QE_OVA_mag_3.raw"]},"type":"primary"},"statusCodeValue":200,"statusCode":"OK"}],"scores":null,"additional":{"omics_type":["Proteomics"],"submitter":["Yayoi Kimura"],"species":["Homo Sapiens (human)","Cellular Organisms"],"full_dataset_link":["https://repository.jpostdb.org/entry/JPST001186"],"submitter_affiliation":["Yokohama City University"],"sample_protocol":[""],"repository":["jPOST"],"data_protocol":[""],"pubmed_abstract":["Information about phosphorylation status can be used to prioritize and characterize biological processes in the cell. Various analytical strategies have been proposed to address the complexity of phosphorylation status and comprehensively identify phosphopeptides. In this study, we evaluated four strategies for phosphopeptide enrichment, using titanium dioxide (TiO<sub>2</sub> ) and Phos-tag ligand particles from in-gel or in-solution digests prior to mass spectrometry-based analysis. Using TiO<sub>2</sub> and Phos-tag magnetic beads, it was possible to enrich phosphopeptides from in-gel digests of phosphorylated ovalbumin separated by Phos-tag SDS-PAGE or in-solution serum digests, while minimizing non-specific adsorption. The tip-column strategy with TiO<sub>2</sub> particles enabled enrichment of phosphopeptides from in-solution digests of whole-cell lysates with high efficiency and selectivity. However, the tip-column strategy with Phos-tag agarose beads yielded the greatest number of identified phosphopeptides. The strategies using both types of tip columns had a high degree of overlap, although there were differences in selectivity between the identified phosphopeptides. Together, our results indicate that multi-enrichment strategies using TiO<sub>2</sub> particles and Phos-tag agarose beads are useful for comprehensive phosphoproteomic analysis."],"pubmed_title":["Evaluation of four phosphopeptide enrichment strategies for mass spectrometry-based proteomic analysis."],"pubmed_authors":["Ino Yoko Y, Kinoshita Eiji E, Kinoshita-Kikuta Emiko E, Akiyama Tomoko T, Nakai Yusuke Y, Nishino Kohei K, Osada Makoto M, Ryo Akihide A, Hirano Hisashi H, Koike Tohru T, Kimura Yayoi Y"],"name_synonyms":["Mass Spectrum Analysis, Spectroscopy, Mass Spectrum, MS, Phosphopeptide, Analyses, Mass, proteomic analysis., Spectrometry, Analysis, Spectrum Analyses, Mass Spectrum Analyses, Spectrum Analysis, Mass Spectroscopy"],"pubmed_abstract_synonyms":["Spi3, Nup32D, nebb, PLIP, degree (angle), CG10718, determination, Spi9, Spi8, Spi7, Spi6, brookite, Blood, Sepharose C1 4B, Addresses, SPIC, Serum, phosphorylation, Type 2A-interacting protein, EIC, EIB, SUB, dmTAF[[II]]230, nano-TiO2, DmelCG12298, dJ69E11.3, sl(2)ry, DGS, SDS-PAGE, titanium white, SCRAMBLED, Analysis, KIF20A, HTATIP, nup154, Mass Spectrum Analysis, Sepharose, Divorced, Polyacrylamide, TFIID TAF250, SDS-PAGE electrophoresis, Analyses, cel, SPI3C, Titania, SPI3B, BC052216, klp38B, chemical analysis., Divorces, C76174, C76171, rutile, AT2, C1 4B, Spi13, cPLA2, column, Spi14, DmelCG1106, Spi12, SPI-CI, Spi10, nano-anatase, NK21L1, KLP 38B, high efficiency, TIP, AW540195, dTAF[[II]]230, Ligand, anatomical protrusion, KIF14, ZC2HC5, 4B, STRUBBELIG, TAF200, ovalbumin, NK21, HTATIP1, TAFII-250, Blood Serum, TAF250/230, tip, tio, ANAC091, Spectrum Analysis, results, Spectroscopy, Putative MAPK-activating protein PM10, TAFII250, [4)-3, Sepharose C1, overlap, TIP60, NK10, NK13, Sodium Dodecyl Sulfate-PAGE, anatase titanium dioxide, OTTMUSG00000000720, R86, Spectrometry, SDS polyacrylamide gel electrophoresis, LNKN-1, CG17603, TAF[[II]], CG1106, CAP3, CAP2, NK26, Taf250, spine, SR3-5, 1600019A21Rik, Sepharose 4B, AI462524, Mot, Sodium Dodecyl Sulfate-PAGEs, tlp, TIP41, TAF230, 4930482L21Rik, bis-bisPMAP, AT1G11140, Maspin, d230, 38B.12, 38B.10, DmKlp38B, number, dTAFII250, CAP-3, Gel Electrophoresis, Spectrum Analyses, CAP-2, SDS polyacrylamide gel electrophoresis of proteins, EfW1, DmelCG10718, ESA1, KLP-38B, CG12298, protrusion, Sodium Dodecyl Sulfate PAGE, dmTAF1, Taf230, anatase, Serpin1b1, Arabidopsis NAC domain containing protein 91, Klp38B, Polyacrylamide Gel Electrophoresis, Mass, zk, l(2)k00802, Separated, Mass Spectroscopy, TAF250, PI-9, KLP38B, study, Taf200, PI-5, l(2)10432, dTAF[[II]]250, PI-6, BB283241, cell, mei-1794, ligand, gel, Taf1p, food additive E171, Solution, PI9, dTAF250, DmelCG4579, ms(2)zk, Neb, D330015H01Rik, Agarose, SRF9, l(2)01501, D8Wsu49e, TAF, 6-An-alpha-L-Galp-(1->3)-beta-D-Galp-(1->]n, SDS PAGE, Serpin B14, TAF[[II]]250, 1110036M19Rik, Gm11396, BcDNA:LD21772, Phosphorylations, Serpinb6, l(3)84Ab, titanium oxide, BG:DS00004.13, Cell, dTAF230, Ovalbumins, STRUBBELIG-RECEPTOR FAMILY 9, l(2)03552, MS, Phosphopeptide, p230, chemical analysis, TAF[[II]]250/230, TFIID, Mass Spectrum Analyses, Taf[[II]]250, Mass Spectrum, Separation, nup32D, l(2)k07614, TAF[[II]]230, phos-tag, Separations, sodium dodecyl sulphate–polyacrylamide gel electrophoresis, Dub, 6330533H24Rik, CG4579, Magnetic, TAF[II]250, arc degree, CDA08, DmelCG17603, Klp38, Dm0332, AI646751, cardinality, TCV-interacting protein, assay, sl(2)ry3, Adsorptions, T19D16.8, SCM, Serums, TAF1"],"pubmed_title_synonyms":["Mass Spectrum Analysis, Spectroscopy, Mass Spectrum, MS, Phosphopeptide, Analyses, Mass, proteomic analysis., Spectrometry, Analysis, Spectrum Analyses, Mass Spectrum Analyses, Spectrum Analysis, Mass Spectroscopy"],"description_synonyms":["Mass Spectrum Analysis, Mass Spectrum, Ligand, phos-tag, Analyses, Titania, brookite, anatase titanium dioxide, ligand, gel, proteomic analysis., Spectrometry, titanium oxide, food additive E171, Spectrum Analyses, Spectrum Analysis, rutile, Solution, CG1106, Spectroscopy, nano-TiO2, MS, Phosphopeptide, DmelCG1106, anatase, Mass, nano-anatase, DGS, titanium white, Analysis, Mass Spectrum Analyses, Mass Spectroscopy, bis-bisPMAP"],"additional_accession":[]},"is_claimable":false,"name":"Characterization of phosphopeptide enrichment strategy for mass spectrometry-based proteomic analysis","description":"We attempted to evaluate four strategies for phosphopeptide enrichment, using the titanium dioxide (TiO2) and Phos-tag ligand particles, from in-solution or in-gel digests prior to mass spectrometry-based proteomic analysis. ","dates":{"publication":"Fri Dec 24 00:00:00 GMT 2021"},"accession":"PXD026295","cross_references":{"TAXONOMY":["131567","9606"],"pubmed":["34932266"]}}