Mass Spectrometric Analysis of Post-translational Modifications (PTMs) and Protein–Protein Interactions (PPIs)

2014 ◽  
pp. 205-235 ◽  
Author(s):  
Armand G. Ngounou Wetie ◽  
Alisa G. Woods ◽  
Costel C. Darie
Keyword(s):  
Protein Interactions ◽  
Mass Spectrometric ◽  
Mass Spectrometric Analysis ◽  
Spectrometric Analysis ◽  
Protein Protein Interactions ◽  
Post Translational Modifications

scholarly journals SECAT: Quantifying differential protein-protein interaction states by network-centric analysis

2019 ◽  
Author(s):  
George Rosenberger ◽  
Moritz Heusel ◽  
Isabell Bludau ◽  
Ben Collins ◽  
Claudia Martelli ◽  
...  
Keyword(s):  
Protein Interaction ◽  
Protein Interactions ◽  
Molecular Mechanisms ◽  
Protein Complexes ◽  
Mass Spectrometric ◽  
Mass Spectrometric Analysis ◽  
Size Exclusion ◽  
Spectrometric Analysis ◽  
Differential Analysis ◽  
Ppi Networks

AbstractProtein-protein interactions (PPIs) play critical functional and regulatory roles in virtually all cellular processes. They are essential for the formation of macromolecular complexes, which in turn constitute the basis for extended protein interaction networks that determine the functional state of a cell. We and others have previously shown that chromatographic fractionation of native protein complexes in combination with bottom-up mass spectrometric analysis of consecutive fractions supports the multiplexed characterization and detection of state-specific changes of protein complexes.In this study, we describe a computational approach that extends the analysis of data from the co-fractionation / mass spectrometric analysis of native complexes to the level of PPI networks, thus enabling a qualitative and quantitative comparison of the proteome organization between samples and states. The Size-Exclusion Chromatography Algorithmic Toolkit (SECAT) implements a novel, network-centric strategy for the scalable and robust differential analysis of PPI networks. SECAT and its underlying statistical framework elucidate differential quantitative abundance and stoichiometry attributes of proteins in the context of their PPIs. We validate algorithm predictions using publicly available datasets and demonstrate that SECAT represents a more scalable and effective methodology to assess protein-network state and that our approach thus obviates the need to explicitly infer individual protein complexes. Further, by differential analysis of PPI networks of HeLa cells in interphase and mitotic state, respectively, we demonstrate the ability of the algorithm to detect PPI network differences and to thus suggest molecular mechanisms that differentiate cellular states.

Mass spectrometric analysis of protein interactions

2005 ◽  
Vol 9 (5) ◽  
pp. 509-516 ◽  
Author(s):  
Jonas Borch ◽  
Thomas JD Jørgensen ◽  
Peter Roepstorff
Keyword(s):  
Protein Interactions ◽  
Mass Spectrometric ◽  
Mass Spectrometric Analysis ◽  
Spectrometric Analysis

A Questionnaire Survey on General Status and Opinions about Clinical Mass Spectrometric Analysis in Korea (2018)

2019 ◽  
Vol 9 (3) ◽  
pp. 161
Author(s):  
Sung-Eun Cho ◽  
Hyojin Chae ◽  
Hyung-Doo Park ◽  
Sail Chun ◽  
Yong-Wha Lee ◽  
...  
Keyword(s):  
Questionnaire Survey ◽  
Mass Spectrometric ◽  
Mass Spectrometric Analysis ◽  
Spectrometric Analysis ◽  
General Status

Mechanisms of Dopant Depth Profile Modification During Mass Spectrometric Analysis of Multilayer Structure

2015 ◽  
Vol 60 (6) ◽  
pp. 511-520 ◽  
Author(s):  
A.A. Efremov ◽  
◽  
V.G. Litovchenko ◽  
V.P. Melnik ◽  
O.S. Oberemok ◽  
...  
Keyword(s):  
Depth Profile ◽  
Multilayer Structure ◽  
Mass Spectrometric ◽  
Mass Spectrometric Analysis ◽  
Spectrometric Analysis ◽  
Profile Modification

Mass Spectrometric Analysis of Porcine Rhodopsin¶

2002 ◽  
Vol 75 (3) ◽  
pp. 316 ◽  
Author(s):  
Zsolt Ablonczy ◽  
Patrice Goletz ◽  
Daniel R. Knapp ◽  
Rosalie K. Crouch
Keyword(s):  
Mass Spectrometric ◽  
Mass Spectrometric Analysis ◽  
Spectrometric Analysis
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