Zobrazeno 1 - 10
of 35
pro vyhledávání: '"Christophe Masselon"'
Publikováno v:
Analyst
Analyst, Royal Society of Chemistry, 2017, 142 (11), pp.2054-2054. ⟨10.1039/c7an90034a⟩
Analyst, 2017, 142 (11), pp.2054-2054. ⟨10.1039/c7an90034a⟩
Analyst, Royal Society of Chemistry, 2017, 142 (11), pp.2054-2054. ⟨10.1039/c7an90034a⟩
Analyst, 2017, 142 (11), pp.2054-2054. ⟨10.1039/c7an90034a⟩
Correction for ‘Predictive chromatography of peptides and proteins as a complementary tool for proteomics’ by Irina A. Tarasova et al., Analyst, 2016, 141, 4816–4832.
Publikováno v:
Analyst
Analyst, Royal Society of Chemistry, 2017, 142 (11), pp.2052-2053. ⟨10.1039/c7an00627f⟩
Analyst, 2017, 142 (11), pp.2052-2053. ⟨10.1039/c7an00627f⟩
Analyst, Royal Society of Chemistry, 2017, 142 (11), pp.2052-2053. ⟨10.1039/c7an00627f⟩
Analyst, 2017, 142 (11), pp.2052-2053. ⟨10.1039/c7an00627f⟩
On the applicability of peptide retention time prediction software for data acquired using different LC conditions.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e8715dcfd32f730788e39eaa24bbf752
https://hal.archives-ouvertes.fr/hal-02191336
https://hal.archives-ouvertes.fr/hal-02191336
Autor:
Dong Gi Mun, Sang Won Lee, Hangyeore Lee, Christophe Masselon, Hokeun Kim, Jeong Eun So, Jingi Bae
Publikováno v:
Analytical Chemistry
Analytical Chemistry, American Chemical Society, 2016, 88 (23), pp.11734-11741. ⟨10.1021/acs.analchem.6b03366⟩
Analytical Chemistry, 2016, 88 (23), pp.11734-11741. ⟨10.1021/acs.analchem.6b03366⟩
Analytical Chemistry, American Chemical Society, 2016, 88 (23), pp.11734-11741. ⟨10.1021/acs.analchem.6b03366⟩
Analytical Chemistry, 2016, 88 (23), pp.11734-11741. ⟨10.1021/acs.analchem.6b03366⟩
Proteomics aims to achieve complete profiling of the protein content and protein modifications in cells, tissues, and biofluids and to quantitatively determine changes in their abundances. This information serves to elucidate cellular processes and s
Autor:
Vilém Guryča, Irina A. Tarasova, Lev I. Levitsky, V. V. Evreinov, A. V. Gorshkov, Anton Goloborodko, Marina L. Pridatchenko, Mikhail V. Gorshkov, T. Yu. Perlova, Christophe Masselon
Publikováno v:
Journal of Analytical Chemistry. 67:1014-1025
Inversion of the order of peptide elution in reversed-phase liquid chromatography under changing separation conditions, such as gradient slope has been considered. Using a six-protein proteolytic peptide standard and available literature data, the oc
Publikováno v:
Analyst
Analyst, Royal Society of Chemistry, 2016, 141 (16), pp.4816-4832. ⟨10.1039/c6an00919k⟩
Analyst, 2016, 141 (16), pp.4816-4832. ⟨10.1039/c6an00919k⟩
Analyst, Royal Society of Chemistry, 2016, 141 (16), pp.4816-4832. ⟨10.1039/c6an00919k⟩
Analyst, 2016, 141 (16), pp.4816-4832. ⟨10.1039/c6an00919k⟩
In the last couple of decades, considerable effort has been focused on developing methods for quantitative and qualitative proteome characterization. The method of choice in this characterization is mass spectrometry used in combination with sample s
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d28126eeba051e7b36463c6b39790aca
https://hal.archives-ouvertes.fr/hal-02084726
https://hal.archives-ouvertes.fr/hal-02084726
Publikováno v:
Clinical Proteomics Methods and Protocols-Methods in Molecular Biology vol 1243
Clinical Proteomics Methods and Protocols-Methods in Molecular Biology vol 1243, pp.175-186, 2015, ⟨10.1007/978-1-4939-1872-0_10⟩
Methods in Molecular Biology ISBN: 9781493918713
Clinical Proteomics Methods and Protocols-Methods in Molecular Biology vol 1243, pp.175-186, 2015, ⟨10.1007/978-1-4939-1872-0_10⟩
Methods in Molecular Biology ISBN: 9781493918713
Urine has garnered tremendous interest over the past decade as a potential source of protein biomarkers for various pathologies. However, due to its low protein concentration and the presence of interfering compounds, urine constitutes a challenging
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::79c51d2f790037fec4618c379f97d835
https://hal.archives-ouvertes.fr/hal-02084741
https://hal.archives-ouvertes.fr/hal-02084741
Publikováno v:
Journal of Proteomics. 72:740-749
The development of mass spectrometry (MS)-based methodologies for high-throughput protein identification has generated a concomitant need for protein quantification. Numerous MS-based relative quantification methodologies have been dedicated to the e
Autor:
Irina A. Tarasova, V. V. Evreinov, Marina L. Pridatchenko, A. V. Gorshkov, Christophe Masselon, Mikhail V. Gorshkov, Sylvie Kieffer-Jaquinod, Vilém Guryča
Publikováno v:
Journal of Chromatography B. 877:433-440
The combination of liquid chromatography (LC) with mass spectrometry (MS) has become a mainstream proteome analysis strategy. In LC-MS, measured masses possess their "universal" scale derived from atomic mass tables. In contrast, the observed LC rete
Publikováno v:
Mass Spectrometry Reviews
Mass Spectrometry Reviews, Wiley, 2014, 33 (6), pp.452-470. ⟨10.1002/mas.21400⟩
Mass Spectrometry Reviews, 2014, 33 (6), pp.452-470. ⟨10.1002/mas.21400⟩
Mass Spectrometry Reviews, Wiley, 2014, 33 (6), pp.452-470. ⟨10.1002/mas.21400⟩
Mass Spectrometry Reviews, 2014, 33 (6), pp.452-470. ⟨10.1002/mas.21400⟩
One of the most important early developments in the field of proteomics was the advent of automated data acquisition routines that allowed high-throughput unattended data acquisition during HPLC introduction of peptide mixtures to a tandem mass spect
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::65922f07a5eff023aa144b6f102d1557
https://hal.archives-ouvertes.fr/hal-02084749
https://hal.archives-ouvertes.fr/hal-02084749
Autor:
Bogdan Bogdanov, Richard D. Smith, Yufeng Shen, Rui Zhao, Mary S. Lipton, Gordon A. Anderson, Christophe Masselon, Wei-Jun Qian, Andrey N. Vilkov, David G. Camp, Liljiana Pasa-Tolic, Nikola Tolić
Publikováno v:
Analytical Chemistry. 77:400-406
In proteomics, effective methods are needed for identifying the relatively limited subset of proteins displaying significant changes in abundance between two samples. One way to accomplish this task is to target for identification by MS/MS only the "