Mass spectrometry-based proteomics

Aebersold, Ruedi; Mann, Matthias

doi:10.1038/nature01511

Cited by 6,298 publications

(5,004 citation statements)

References 90 publications

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“…Studying these events is a challenging area because of the dynamics of the cellular proteome and the sensitivity of the molecules of interest to fluctuations in their natural surroundings. Recently, imaging mass spectrometry (IMS) has been recognized as a proteomic tool for in situ spatial analysis of (diseased) tissue [9,10]. Matrixassisted laser desorption/ionization (MALDI) MS has been shown to be able to determine the localization of native biomolecular components like proteins and peptides in tissue [11][12][13][14][15].…”

mentioning

confidence: 99%

Imaging of peptides in the rat brain using MALDI-FTICR mass spectrometry

Taban

Altelaar

Burgt

et al. 2007

J. Am. Soc. Mass Spectrom.

148

136

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Analytical methods are pursued to measure the identity and location of biomolecules down to the subcellular ( m) level. Available mass spectrometric imaging methods either compromise localization accuracy or identification accuracy in their analysis of surface biomolecules. In this study, imaging FTICR-MS is applied for the spatially resolved mass analysis of rat brain tissue with the aim to optimize protein identification by the high mass accuracy and online MS/MS capabilities of the technique. Mass accuracies up to 6 ppm were obtained in the direct MALDI-analysis of the tissue together with a spatial resolution of 200 m. The spatial distributions of biomolecules differing in mass by less than 0.1 Da could be resolved, and are shown to differ significantly. Online MS/MS analysis of selected ions was demonstrated. A comparison of the FTICR-MS imaging results with stigmatic TOF imaging on the same sample is presented. To reduce the extended measuring times involved, it is recommended to restrict the FTICR-MS analyses to areas of interest as can be preselected by other, faster imaging methods. (J Am Soc Mass Spectrom 2007, 18, 145-151)

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mentioning

confidence: 99%

Imaging of peptides in the rat brain using MALDI-FTICR mass spectrometry

Taban

Altelaar

Burgt

et al. 2007

J. Am. Soc. Mass Spectrom.

148

136

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“…They are the most common variations (Aebersold and Mann 2003) used for the analysis of biomolecules and have been used in proteomic profiling for the diagnosis, prognosis, and therapeutic monitoring of cancer.…”

Section: Mass Spectrometrymentioning

confidence: 99%

A review of novel analytical diagnostics for liquid biopsies: spectroscopic and spectrometric serum profiling of primary and secondary brain tumors

Spalding

Board²,

Dawson

et al. 2016

Brain and Behavior

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IntroductionSpectroscopic and spectrometric analysis of biological samples is regarded as quick, cost effective, easy to operate, and spectroscopic sample preparation involves minimal sample preparation.ResultsTechniques like infrared (IR) spectroscopy, surface‐enhanced laser desorption/ionization (SELDI)‐mass spectroscopy (MS), and matrix‐assisted laser desorption/ionization (MALDI) ‐MS could enable early diagnosis of cancer, disease monitoring, and assessment of treatment responses allowing refinement, if required.DiscussionCarrying out analytical testing within outpatient clinics would dramatically cut the time spent by patients attending different appointments, at different locations, save hospital time and resources but importantly would theoretically enable a reduction in mortality and morbidity. While the advantages of such a prospect seem obvious, this review aims to evaluate the use of human serum spectroscopic and spectrometric analysis as a diagnostic tool for brain cancers, creating a platform for the future of cancer diagnostics.

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“…Rather, they operate in a large number of biological contexts, spatial, and temporal scales and functional states exemplified by protein‐specific properties such as reaction mechanisms, substrate/ motif binding and complex formation. In addition, properties of protein networks such as information processing, noise, adaptability, robustness, and even seemingly paradoxical arrangement of components and functions, such as enzyme promiscuity 19, 20, 21, 22, 23, 24, 25, 26. Moreover, a protein can exist with different variant sequences due to splicing or mutations, and be subject to different PTMs at different sites, resulting in a vast number of theoretical combination of PTMs, known as “mod‐forms”, see for example the histone‐code 18.…”

Section: Introductionmentioning

confidence: 99%

Applications of targeted proteomics in systems biology and translational medicine

et al. 2015

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Biological systems are composed of numerous components of which proteins are of particularly high functional significance. Network models are useful abstractions for studying these components in context. Network representations display molecules as nodes and their interactions as edges. Because they are difficult to directly measure, functional edges are frequently inferred from suitably structured datasets consisting of the accurate and consistent quantification of network nodes under a multitude of perturbed conditions. For the precise quantification of a finite list of proteins across a wide range of samples, targeted proteomics exemplified by selected/multiple reaction monitoring (SRM, MRM) mass spectrometry has proven useful and has been applied to a variety of questions in systems biology and clinical studies. Here, we survey the literature of studies using SRM‐MS in systems biology and clinical proteomics. Systems biology studies frequently examine fundamental questions in network biology, whereas clinical studies frequently focus on biomarker discovery and validation in a variety of diseases including cardiovascular disease and cancer. Targeted proteomics promises to advance our understanding of biological networks and the phenotypic significance of specific network states and to advance biomarkers into clinical use.

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Mass spectrometry-based proteomics

Cited by 6,298 publications

References 90 publications

Imaging of peptides in the rat brain using MALDI-FTICR mass spectrometry

Imaging of peptides in the rat brain using MALDI-FTICR mass spectrometry

A review of novel analytical diagnostics for liquid biopsies: spectroscopic and spectrometric serum profiling of primary and secondary brain tumors

Applications of targeted proteomics in systems biology and translational medicine

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