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Journal ArticleDOI

Stable isotope-coded proteomic mass spectrometry

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TLDR
The ability to quantify differences in protein expression and post-translational modifications using stable isotope labeling has been achieved, but insights into the biochemical mechanisms that will contribute to the development of new biotechnologies have yet to be realized.
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This article is published in Current Opinion in Biotechnology.The article was published on 2003-02-01. It has received 184 citations till now. The article focuses on the topics: Stable isotope ratio & Proteomics.

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Citations
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Journal ArticleDOI

Multiplexed Protein Quantitation in Saccharomyces cerevisiae Using Amine-reactive Isobaric Tagging Reagents

TL;DR: It is found that inactivation of Upf1p and Xrn1p causes common as well as unique effects on protein expression, and the use of 4-fold multiplexing to enable relative protein measurements simultaneously with determination of absolute levels of a target protein using synthetic isobaric peptide standards.
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Interpretation of Shotgun Proteomic Data The Protein Inference Problem

TL;DR: The difficulties of interpreting shotgun proteomic data are illustrated and the need for common nomenclature and transparent informatic approaches are discussed and related issues such as the state of protein sequence databases and their role in shotgun proteomics analysis, interpretation of relative peptide quantification data in the presence of multiple protein isoforms, and the integration of proteomic and transcriptional data are discussed.
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Stable-isotope dimethyl labeling for quantitative proteomics.

TL;DR: A novel, stable-isotope labeling strategy for quantitative proteomics that uses a simple reagent, formaldehyde, to globally label the N-terminus and epsilon-amino group of Lys through reductive amination is reported.
Journal ArticleDOI

Analysis and validation of proteomic data generated by tandem mass spectrometry.

TL;DR: This review discusses critical issues related to data processing and analysis in proteomics and describes available methods and tools and places special emphasis on the elaboration of results that are supported by sound statistical arguments.
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Modification-specific proteomics: characterization of post-translational modifications by mass spectrometry

TL;DR: Combinations of affinity-based enrichment and extraction methods, multidimensional separation technologies and mass spectrometry are particularly attractive for systematic investigation of post-translationally modified proteins in proteomics.
References
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Journal ArticleDOI

Stable isotope labeling by amino acids in cell culture, SILAC, as a simple and accurate approach to expression proteomics.

TL;DR: SILAC is a simple, inexpensive, and accurate procedure that can be used as a quantitative proteomic approach in any cell culture system and is applied to the relative quantitation of changes in protein expression during the process of muscle cell differentiation.
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Quantitative analysis of complex protein mixtures using isotope-coded affinity tags

TL;DR: An approach for the accurate quantification and concurrent sequence identification of the individual proteins within complex mixtures based on isotope-coded affinity tags and tandem mass spectrometry is described.
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Phosphoproteome analysis by mass spectrometry and its application to Saccharomyces cerevisiae

TL;DR: In this article, a methodology was proposed to characterize most, if not all, phosphoproteins from a whole-cell lysate in a single experiment, and a total of 216 peptide sequences defining 383 sites of phosphorylation were determined.
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Accurate quantitation of protein expression and site-specific phosphorylation

TL;DR: The present method is general and affords a quantitative description of cellular differences at the level of protein expression and modification, thus providing information that is critical to the understanding of complex biological phenomena.
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Quantitative profiling of differentiation-induced microsomal proteins using isotope-coded affinity tags and mass spectrometry.

TL;DR: The method and the new software tools to support it are well suited to the large-scale, quantitative analysis of membrane proteins and other classes of proteins that have been refractory to standard proteomics technology.
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