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Kosaku Shinoda, Kana Ohyama, Yutaka Hasegawa, Hsin-Yi Chang, David W. Scheel, Louis Z. Sharp, Haemin Hong, Takashi Hosono, Mayu Ogura, Ayaka Sato, Yasushi Ishihama, and Shingo Kajimura. Phosphoproteomics Identifies CK2 As a Negative Regulator of Beige Adipocyte Thermogenesis and Energy Expenditure. ...
ORGANISM(S): Mus Musculus (ncbitaxon:10090) 
2015-08-28 | MSV000079278 | MassIVE
Wild-type and talA talB double knockout cells were grown in 50 ml of MOPS medium supplemented with 0.2% glucose or xylose in 500 ml Erlenmeyer flasks until the OD600 reached 1. At the sampling RNA was stabilized by mixing with RNAprotect Bacteria regent (Qiagen) and total RNA were isolated, by RNeas...
ORGANISM(S): Escherichia coli 
In-depth membrane proteomic study of breast cancer tissues
ORGANISM(S): Homo Sapiens (human) 
2013-12-31 | PAe004084 | PeptideAtlas
Pol II(G) is a novel form of RNA polymerase II that contains a tightly associated Gdown1 polypeptide. Whereas Pol II suffices for robust activator-dependent transcription in the absence of Mediator, Pol II(G) is highly dependent upon Mediator in a biochemically defined in vitro system. However, the ...
ORGANISM(S): Homo sapiens 
Protein tyrosine phosphatases (PTPs) cooperate with protein tyrosine kinases to regulate intracellular tyrosine phosphorylation levels, and their dysfunction is associated with various diseases. However, due to the low abundance of PTPs in cells, comprehensive analysis requires an enrichment step pr...
ORGANISM(S): Homo Sapiens (human) 
Kinase -networks are important for cellular signal transduction. Despite tremendous efforts to uncover these signaling pathways, huge numbers of uncharacterized phosphosites still remain in the human proteome. Because of the transient nature of kinase-substrate interactions in vivo, it is almost imp...
ORGANISM(S): Homo Sapiens (human) 
Identifying cellular phosphorylation pathways based on kinase-substrate relationships is a critical step to understanding the regulation of physiological functions in cells. Mass spectrometry-based phosphoproteomics workflows have made it possible to comprehensively collect information on individual...
ORGANISM(S): Homo Sapiens (human) 
We have developed a one-step method to isolate protein C-terminal peptides from V8-digested proteins by metal oxide-based ligand-exchange (MOLEX) chromatography. V8 protease cleaves the C-terminal side of Asp and Glu, and the resulting digested peptide has two carboxy groups at the C-terminus, where...
ORGANISM(S): Homo Sapiens (human) 
PXD ID: PXD000071. Experiment: 120206ry_aHDF1419-P10_3, data file: 120206ry_aHDF1419-P10_3_1-120206ry011.mgf. Data published as part of J Proteome Res. 2013 Jan 4;12(1):214-21 [[PubMed]]. From the Abstract: {{i}}Proteome analyses of human induced pluripotent stem cells (iPSC) were carried out on a l...
ORGANISM(S): Human, Human_adenovirus_54, Human_adenovirus_a, Human_adenovirus_b, Human_adenovirus_c, Human_adenovirus_d, Human_adenovirus_e, Human_adenovirus_f, Human_adenovirus_g, Human_astrovirus, Human_bocavirus, Human_bocavirus_2, Human_bocavirus_3, Human_bocavirus_4, Human_coronavirus_229e, Human_coronavirus_hku1, Human_coronavirus_nl63, Human_coronavirus_oc43, Human_cosavirus_a, Human_cosavirus_b, Human_cosavirus_d, Human_cosavirus_e, Human_enteric_coronavirus_4408, Human_enterovirus_100, Human_enterovirus_a, Human_enterovirus_b, Human_enterovirus_c, Human_enterovirus_d, Human_erythrovirus_v9, Human_herpesvirus_1, Human_herpesvirus_2, Human_herpesvirus_3, Human_herpesvirus_4_type_1, Human_herpesvirus_4_type_2, Human_herpesvirus_5, Human_herpesvirus_6a, Human_herpesvirus_6b, Human_herpesvirus_7, Human_herpesvirus_8_type_p, Human_immunodeficiency_virus_1, Human_immunodeficiency_virus_2, Human_metapneumovirus, Human_papillomavirus_fa75_ki88_03, Human_papillomavirus_rtrx7, Human_papillomavirus_type_10, Human_papillomavirus_type_100, Human_papillomavirus_type_101, Human_papillomavirus_type_103, Human_papillomavirus_type_104, Human_papillomavirus_type_105, Human_papillomavirus_type_108, Human_papillomavirus_type_109, Human_papillomavirus_type_112, Human_papillomavirus_type_113, Human_papillomavirus_type_16, Human_papillomavirus_type_24, Human_papillomavirus_type_26, Human_papillomavirus_type_32, Human_papillomavirus_type_34, Human_papillomavirus_type_4, Human_papillomavirus_type_41, Human_papillomavirus_type_48, Human_papillomavirus_type_49, Human_papillomavirus_type_5, Human_papillomavirus_type_50, Human_papillomavirus_type_53, Human_papillomavirus_type_60, Human_papillomavirus_type_63, Human_papillomavirus_type_6b, Human_papillomavirus_type_7, Human_papillomavirus_type_71, Human_papillomavirus_type_88, Human_papillomavirus_type_9, Human_papillomavirus_type_92, Human_papillomavirus_type_96, Human_papillomavirus_type_98, Human_papillomavirus_type_99, Human_papillomavirus___1, Human_papillomavirus___18, Human_papillomavirus___2, Human_papillomavirus___54, Human_papillomavirus___61, Human_papillomavirus___cand90, Human_parainfluenza_virus_1, Human_parainfluenza_virus_2, Human_parainfluenza_virus_3, Human_parechovirus, Human_parvovirus_4, Human_parvovirus_b19, Human_picobirnavirus, Human_respiratory_syncytial_virus, Human_rhinovirus_a, Human_rhinovirus_b, Human_rhinovirus_c, Human_tmev_like_cardiovirus, Human_t_lymphotropic_virus_1, Human_t_lymphotropic_virus_2, Human_t_lymphotropic_virus_4 
There is a need for robust phosphopeptide enrichment methods to allow signaling network analysis in cancer cell lines and tissues with minimal fractionation. With recent instrument developments thousands of unique phosphopeptides can be detected by single-shot LC-MS/MS. However, successful phosphopr...
ORGANISM(S): Homo Sapiens (ncbitaxon:9606) 
2017-03-28 | MSV000080715 | MassIVE
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