Zobrazeno 1 - 10
of 49
pro vyhledávání: '"Melvin A. Park"'
Autor:
Andreas‐David Brunner, Marvin Thielert, Catherine Vasilopoulou, Constantin Ammar, Fabian Coscia, Andreas Mund, Ole B Hoerning, Nicolai Bache, Amalia Apalategui, Markus Lubeck, Sabrina Richter, David S Fischer, Oliver Raether, Melvin A Park, Florian Meier, Fabian J Theis, Matthias Mann
Publikováno v:
Molecular Systems Biology, Vol 18, Iss 3, Pp 1-15 (2022)
Abstract Single‐cell technologies are revolutionizing biology but are today mainly limited to imaging and deep sequencing. However, proteins are the main drivers of cellular function and in‐depth characterization of individual cells by mass spect
Externí odkaz:
https://doaj.org/article/ac8470a27f154fe790c1489104ae340a
Publikováno v:
Analyst
Ion mobility spectrometry/mass spectrometry (IMS/MS) is widely used to study various levels of protein structure. Here, we review the current state of affairs in tandem-trapped ion mobility spectrometry/mass spectrometry (tTIMS/MS). Two different tTI
Autor:
Kevin Jeanne Dit Fouque, Samuel A. Miller, Khoa Pham, Natarajan V. Bhanu, Yarixa L. Cintron-Diaz, Dennys Leyva, Desmond Kaplan, Valery G. Voinov, Mark E. Ridgeway, Melvin A. Park, Benjamin A. Garcia, Francisco Fernandez-Lima
Publikováno v:
Analytical chemistry. 94(44)
Post-translational modifications (PTMs) on intact histones play a major role in regulating chromatin dynamics and influence biological processes such as DNA transcription, replication, and repair. The nature and position of each histone PTM is crucia
Publikováno v:
Journal of the American Society for Mass Spectrometry. 32:2241-2250
Blanc's Law has served as a way to predict the mobilities of ions in mixed drift gases for over 100 years yet has remained largely unexplored using newer ion mobility spectrometry (IMS) configurations, including traveling wave and trapped IMS (TIMS)
Autor:
Samuel A. Miller, Kevin Jeanne Dit Fouque, Mark E. Ridgeway, Melvin A. Park, Francisco Fernandez-Lima
Publikováno v:
J Am Soc Mass Spectrom
Trapped ion mobility spectrometry (TIMS) when coupled with mass spectrometry (MS) offers great advantages for the separation of isobaric, isomeric and/or conformeric species. In the present work, we report the advantages of coupling TIMS with a low-c
Autor:
Yuk-Ching Tse-Dinh, Francisco Fernandez-Lima, Alyssa Garabedian, Mark E. Ridgeway, Melvin A. Park, Kevin Jeanne Dit Fouque, Fenfei Leng
Publikováno v:
Anal Chem
The structural elucidation of native macromolecular assemblies has been a subject of considerable interest in native mass spectrometry (MS), and more recently in tandem with ion mobility spectrometry (IMS-MS), for a better understanding of their bioc
Publikováno v:
Anal Chem
Glycoproteins play a central role in many biological processes including disease mechanisms. Nevertheless, because glycoproteins are heterogeneous entities, it remains unclear how glycosylation modulates the protein structure and function. Here, we a
Autor:
Nicolai Bache, Melvin A. Park, Ole Bjeld Horning, Constantin Ammar, Florian Meier, Andreas Mund, Fabian Coscia, David S. Fischer, Marvin Thielert, Matthias Mann, Oliver Raether, Amalia Apalategui, Catherine G. Vasilopoulou, Andreas-David Brunner, Markus Lubeck, Fabian J. Theis, Sabrina Richter
Publikováno v:
bioRxiv
Mol. Syst. Biol. 18:e10798 (2022)
Brunner, A-D, Thielert, M, Vasilopoulou, C, Ammar, C, Coscia, F, Mund, A, Hoerning, O B, Bache, N, Apalategui, A, Lubeck, M, Richter, S, Fischer, D S, Raether, O, Park, M A, Meier, F, Theis, F J & Mann, M 2022, ' Ultra-high sensitivity mass spectrometry quantifies single-cell proteome changes upon perturbation ', Molecular Systems Biology, vol. 18, no. 3, e10798 . https://doi.org/10.15252/msb.202110798
Mol. Syst. Biol. 18:e10798 (2022)
Brunner, A-D, Thielert, M, Vasilopoulou, C, Ammar, C, Coscia, F, Mund, A, Hoerning, O B, Bache, N, Apalategui, A, Lubeck, M, Richter, S, Fischer, D S, Raether, O, Park, M A, Meier, F, Theis, F J & Mann, M 2022, ' Ultra-high sensitivity mass spectrometry quantifies single-cell proteome changes upon perturbation ', Molecular Systems Biology, vol. 18, no. 3, e10798 . https://doi.org/10.15252/msb.202110798
Single-cell technologies are revolutionizing biology but are today mainly limited to imaging and deep sequencing1–3. However, proteins are the main drivers of cellular function and in-depth characterization of individual cells by mass spectrometry
Autor:
Mark E. Ridgeway, Melvin A. Park, Christian Bleiholder, Christopher A. Wootton, Fanny C. Liu, Alina Theisen, J. S. Raaj Vellore Winfred, Jusung Lee, Nick C. Polfer
Publikováno v:
Rapid Commun Mass Spectrom
RATIONALE Tandem-ion mobility spectrometry/mass spectrometry methods have recently gained traction for the structural characterization of proteins and protein complexes. However, ion activation techniques currently coupled with tandem-ion mobility sp
Publikováno v:
Molecular & Cellular Proteomics : MCP
Recent advances in efficiency and ease of implementation have rekindled interest in ion mobility spectrometry, a technique that separates gas phase ions by their size and shape and that can be hybridized with conventional LC and MS. Here, we review t