Quantitative proteomics analysis of platelet-derived microparticles reveals distinct protein signatures when stimulated by different physiological agonists (2015)
- Authors:
- Autor USP: PALMISANO, GIUSEPPE - ICB
- Unidade: ICB
- DOI: 10.1016/j.jprot.2015.03.01
- Subjects: PARASITOLOGIA; PROTEINAS
- Language: Inglês
- Imprenta:
- Source:
- Título: Journal of Proteomics
- ISSN: 1876-7737
- Volume/Número/Paginação/Ano: v. 121, p. 56-66, 2015
- Este periódico é de acesso aberto
- Este artigo NÃO é de acesso aberto
-
ABNT
MILIOLI, Marco et al. Quantitative proteomics analysis of platelet-derived microparticles reveals distinct protein signatures when stimulated by different physiological agonists. Journal of Proteomics, v. 121, p. 56-66, 2015Tradução . . Disponível em: https://doi.org/10.1016/j.jprot.2015.03.01. Acesso em: 28 dez. 2025. -
APA
Milioli, M., Ibáñez-Vea, M., Sidoli, S., Palmisano, G., Careri, M., & Larsen, M. R. (2015). Quantitative proteomics analysis of platelet-derived microparticles reveals distinct protein signatures when stimulated by different physiological agonists. Journal of Proteomics, 121, 56-66. doi:10.1016/j.jprot.2015.03.01 -
NLM
Milioli M, Ibáñez-Vea M, Sidoli S, Palmisano G, Careri M, Larsen MR. Quantitative proteomics analysis of platelet-derived microparticles reveals distinct protein signatures when stimulated by different physiological agonists [Internet]. Journal of Proteomics. 2015 ; 121 56-66.[citado 2025 dez. 28 ] Available from: https://doi.org/10.1016/j.jprot.2015.03.01 -
Vancouver
Milioli M, Ibáñez-Vea M, Sidoli S, Palmisano G, Careri M, Larsen MR. Quantitative proteomics analysis of platelet-derived microparticles reveals distinct protein signatures when stimulated by different physiological agonists [Internet]. Journal of Proteomics. 2015 ; 121 56-66.[citado 2025 dez. 28 ] Available from: https://doi.org/10.1016/j.jprot.2015.03.01 - Battle through signalling between weat and the fungal pathogen Septoria tritici revealed by proteomics and phosphoproteomics
- Simultaneous enrichment of cysteine-containing peptides and phosphopeptides using a cysteine-specific phosphonate adaptable Tag (CysPAT) in combination with titanium dioxide (TiO2) chromatography
- Trypanosoma cruzi pathogenicity involves virulence factor expression and upregulation of bioenergetic and biosynthetic pathways
- TiCPG - a strategy for the simultaneous enrichment of reversibly modified cysteine peptides, phosphopeptides, and sialylated N-Glycopeptides to study cytokines stimulated beta-cells
- Structural analysis of glycoprotein sialylation – part II: LC-MS based detection
- Structural analysis of glycoprotein sialylation – Part I: pre-LC-MS analytical strategies
- Community evaluation of glycoproteomics informatics solutions reveals high-performance search strategies for serum glycopeptide analysis
- Direct identification of trypanosomatids by matrix-assisted laser desorption ionization-time of flight mass spectrometry (DIT MALDI-TOF MS)
- Extracellular vesicles in brain tumors and neurodegenerative diseases
- A novel mass spectrometric strategy “BEMAP” reveals Extensive O-linked protein glycosylation in Enterotoxigenic Escherichia coli
Informações sobre o DOI: 10.1016/j.jprot.2015.03.01 (Fonte: oaDOI API)
How to cite
A citação é gerada automaticamente e pode não estar totalmente de acordo com as normas
