Zobrazeno 1 - 10
of 79
pro vyhledávání: '"M. Solovyeva"'
Autor:
Chengxin Dai, Anja Füllgrabe, Julianus Pfeuffer, Elizaveta M. Solovyeva, Jingwen Deng, Pablo Moreno, Selvakumar Kamatchinathan, Deepti Jaiswal Kundu, Nancy George, Silvie Fexova, Björn Grüning, Melanie Christine Föll, Johannes Griss, Marc Vaudel, Enrique Audain, Marie Locard-Paulet, Michael Turewicz, Martin Eisenacher, Julian Uszkoreit, Tim Van Den Bossche, Veit Schwämmle, Henry Webel, Stefan Schulze, David Bouyssié, Savita Jayaram, Vinay Kumar Duggineni, Patroklos Samaras, Mathias Wilhelm, Meena Choi, Mingxun Wang, Oliver Kohlbacher, Alvis Brazma, Irene Papatheodorou, Nuno Bandeira, Eric W. Deutsch, Juan Antonio Vizcaíno, Mingze Bai, Timo Sachsenberg, Lev I. Levitsky, Yasset Perez-Riverol
Publikováno v:
Nature Communications, Vol 12, Iss 1, Pp 1-8 (2021)
The number of publicly available proteomics datasets is growing rapidly, but a standardized approach for describing the associated metadata is lacking. Here, the authors propose a format and a software pipeline to present and validate metadata, and i
Externí odkaz:
https://doaj.org/article/33519ff7742042fb963af4bf5ef059fa
Autor:
Lev I. Levitsky, Mark V. Ivanov, Anton O. Goncharov, Anna A. Kliuchnikova, Julia A. Bubis, Anna A. Lobas, Elizaveta M. Solovyeva, Mikhail A. Pyatnitskiy, Ruslan K. Ovchinnikov, Mikhail S. Kukharsky, Tatiana E. Farafonova, Svetlana E. Novikova, Victor G. Zgoda, Irina A. Tarasova, Mikhail V. Gorshkov, Sergei A. Moshkovskii
Publikováno v:
Journal of Proteome Research.
The proteogenomic search pipeline developed in this work has been applied for re-analysis of 40 publicly available shotgun proteomic datasets from various human tissues comprising more than 8,000 individual LC-MS/MS runs, of which 5442 .raw data file
Akademický článek
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Akademický článek
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Autor:
Adriano Mazzini, E. N. Poludetkina, Evgeniya Egoshina, A. A. Kudaev, O. Vidishcheva, Dmitry Korost, K. A. Grigorev, Nikita Morozov, Grigorii Akhmanov, O. Khlystov, M. Solovyeva
Publikováno v:
Moscow University Bulletin. Series 4. Geology. 1:3-16
The Gydratny Fault extends in the SW–NE direction for over 60 km in the central basin of Lake Baikal. During the Class@Baikal-2019 expedition we conducted a multidisciplinary study coupling seismic and gas sampling obtained from bottom sediment pro
Autor:
Anna A. Lobas, Elizaveta M. Solovyeva, Lev I. Levitsky, Anton O. Goncharov, Elena Y. Lyssuk, Sergey S. Larin, Sergei A. Moshkovskii, Mikhail V. Gorshkov
Publikováno v:
International Journal of Molecular Sciences
Volume 24
Issue 3
Pages: 2466
Volume 24
Issue 3
Pages: 2466
Alternative splicing is one of the main regulation pathways in living cells beyond simple changes in the level of protein expression. Most of the approaches proposed in proteomics for the identification of specific splicing isoforms require a prelimi
Autor:
Elizaveta M. Solovyeva, Julia A. Bubis, Irina A. Tarasova, Anna A. Lobas, Mark V. Ivanov, Alexey A. Nazarov, Ilya A. Shutkov, Mikhail V. Gorshkov
Publikováno v:
Biochemistry. Biokhimiia. 87(11)
Abstract Protein quantitation in tissue cells or physiological fluids based on liquid chromatography/mass spectrometry is one of the key sources of information on the mechanisms of cell functioning during chemotherapeutic treatment. Information on si
Autor:
Julian A. Dowdeswell, M. Solovyeva, Grigorii Akhmanov, M. Tokarev, Aleksandr Montelli, Y.E. Terekhina, Sergey Mironyuk
Publikováno v:
Geology. 49:1484-1488
The locations and orientations of more than 1000 late Quaternary subglacial and ice-marginal landforms, including streamlined sedimentary bed forms, glacitectonic hill-hole pairs, meltwater channels, and eskers, were mapped from blocks of multibeam d
Autor:
Mark V. Ivanov, Julia A. Bubis, Vladimir Gorshkov, Irina A. Tarasova, Lev I. Levitsky, Elizaveta M. Solovyeva, Anastasiya V. Lipatova, Frank Kjeldsen, Mikhail V. Gorshkov
Publikováno v:
Analytical chemistry. 94(38)
Recently, we presented the DirectMS1 method of ultrafast proteome-wide analysis based on minute-long LC gradients and MS1-only mass spectra acquisition. Currently, the method provides the depth of human cell proteome coverage of 2500 proteins at 1% f
Publikováno v:
Biochemistry (Moscow), Supplement Series B: Biomedical Chemistry. 14:204-215