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The speciation of the proteome.

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The speciation of the proteome. / Jungblut, Peter R; Holzhütter, Hermann G; Apweiler, Rolf; Schlüter, Hartmut.

in: CHEM CENT J, Jahrgang 2, 2008, S. 16.

Publikationen: SCORING: Beitrag in Fachzeitschrift/Zeitung › SCORING: Zeitschriftenaufsatz › Forschung › Begutachtung

Harvard

Jungblut, PR, Holzhütter, HG, Apweiler, R & Schlüter, H 2008, 'The speciation of the proteome.', CHEM CENT J, Jg. 2, S. 16. https://doi.org/10.1186/1752-153X-2-16

APA

Jungblut, P. R., Holzhütter, H. G., Apweiler, R., & Schlüter, H. (2008). The speciation of the proteome. CHEM CENT J, 2, 16. https://doi.org/10.1186/1752-153X-2-16

Vancouver

Jungblut PR, Holzhütter HG, Apweiler R, Schlüter H. The speciation of the proteome. CHEM CENT J. 2008;2:16. https://doi.org/10.1186/1752-153X-2-16

Bibtex

@article{9683d6fbce1b46fb97a88d193f0c0b6d,
title = "The speciation of the proteome.",
abstract = "ABSTRACT: INTRODUCTION: In proteomics a paradox situation developed in the last years. At one side it is basic knowledge that proteins are post-translationally modified and occur in different isoforms. At the other side the protein expression concept disclaims post-translational modifications by connecting protein names directly with function. DISCUSSION: Optimal proteome coverage is today reached by bottom-up liquid chromatography/mass spectrometry. But quantification at the peptide level in shotgun or bottom-up approaches by liquid chromatography and mass spectrometry is completely ignoring that a special peptide may exist in an unmodified form and in several-fold modified forms. The acceptance of the protein species concept is a basic prerequisite for meaningful quantitative analyses in functional proteomics. In discovery approaches only top-down analyses, separating the protein species before digestion, identification and quantification by two-dimensional gel electrophoresis or protein liquid chromatography, allow the correlation between changes of a biological situation and function. CONCLUSION: To obtain biological relevant information kinetics and systems biology have to be performed at the protein species level, which is the major challenge in proteomics today.",
author = "Jungblut, {Peter R} and Holzh{\"u}tter, {Hermann G} and Rolf Apweiler and Hartmut Schl{\"u}ter",
year = "2008",
doi = "10.1186/1752-153X-2-16",
language = "Deutsch",
volume = "2",
pages = "16",

}

RIS

TY - JOUR

T1 - The speciation of the proteome.

AU - Jungblut, Peter R

AU - Holzhütter, Hermann G

AU - Apweiler, Rolf

AU - Schlüter, Hartmut

PY - 2008

Y1 - 2008

N2 - ABSTRACT: INTRODUCTION: In proteomics a paradox situation developed in the last years. At one side it is basic knowledge that proteins are post-translationally modified and occur in different isoforms. At the other side the protein expression concept disclaims post-translational modifications by connecting protein names directly with function. DISCUSSION: Optimal proteome coverage is today reached by bottom-up liquid chromatography/mass spectrometry. But quantification at the peptide level in shotgun or bottom-up approaches by liquid chromatography and mass spectrometry is completely ignoring that a special peptide may exist in an unmodified form and in several-fold modified forms. The acceptance of the protein species concept is a basic prerequisite for meaningful quantitative analyses in functional proteomics. In discovery approaches only top-down analyses, separating the protein species before digestion, identification and quantification by two-dimensional gel electrophoresis or protein liquid chromatography, allow the correlation between changes of a biological situation and function. CONCLUSION: To obtain biological relevant information kinetics and systems biology have to be performed at the protein species level, which is the major challenge in proteomics today.

AB - ABSTRACT: INTRODUCTION: In proteomics a paradox situation developed in the last years. At one side it is basic knowledge that proteins are post-translationally modified and occur in different isoforms. At the other side the protein expression concept disclaims post-translational modifications by connecting protein names directly with function. DISCUSSION: Optimal proteome coverage is today reached by bottom-up liquid chromatography/mass spectrometry. But quantification at the peptide level in shotgun or bottom-up approaches by liquid chromatography and mass spectrometry is completely ignoring that a special peptide may exist in an unmodified form and in several-fold modified forms. The acceptance of the protein species concept is a basic prerequisite for meaningful quantitative analyses in functional proteomics. In discovery approaches only top-down analyses, separating the protein species before digestion, identification and quantification by two-dimensional gel electrophoresis or protein liquid chromatography, allow the correlation between changes of a biological situation and function. CONCLUSION: To obtain biological relevant information kinetics and systems biology have to be performed at the protein species level, which is the major challenge in proteomics today.

U2 - 10.1186/1752-153X-2-16

DO - 10.1186/1752-153X-2-16

M3 - SCORING: Zeitschriftenaufsatz

VL - 2

SP - 16

ER -