Literature DB >> 18780350

Chromatographic benefits of elevated temperature for the proteomic analysis of membrane proteins.

Adele R Blackler1, Anna E Speers, Christine C Wu.   

Abstract

Integral membrane proteins (IMPs) perform crucial cellular functions and are the primary targets for most pharmaceutical agents. However, the hydrophobic nature of their membrane-embedded domains and their intimate association with lipids make them difficult to handle. Numerous proteomic platforms that include LC separations have been reported for the high-throughput profiling of complex protein samples. However, there are still many challenges to overcome for proteomic analyses of IMPs, especially as compared to their soluble counterparts. In particular, considerations for the technical challenges associated with chromatographic separations are just beginning to be investigated. Here, we review the benefits of using elevated temperatures during LC for the proteomic analysis of complex membrane protein samples.

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Year:  2008        PMID: 18780350      PMCID: PMC2765112          DOI: 10.1002/pmic.200800210

Source DB:  PubMed          Journal:  Proteomics        ISSN: 1615-9853            Impact factor:   3.984


  46 in total

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Review 3.  Temperature selectivity in reversed-phase high performance liquid chromatography.

Authors:  John W Dolan
Journal:  J Chromatogr A       Date:  2002-08-02       Impact factor: 4.759

Review 4.  Top-down mass spectrometry of integral membrane proteins.

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Journal:  Expert Rev Proteomics       Date:  2006-12       Impact factor: 3.940

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Authors:  James Martosella; Nina Zolotarjova; Hongbin Liu; Susanne C Moyer; Patrick D Perkins; Barry E Boyes
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Authors:  Y F Maa; C Horváth
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8.  Comprehensive proteomic analysis of Shigella flexneri 2a membrane proteins.

Authors:  Candong Wei; Jian Yang; Junping Zhu; Xiaobing Zhang; Wenchuan Leng; Jing Wang; Ying Xue; Lilian Sun; Weijun Li; Jin Wang; Qi Jin
Journal:  J Proteome Res       Date:  2006-08       Impact factor: 4.466

9.  Proteomic mapping of brain plasma membrane proteins.

Authors:  Peter Aa Nielsen; Jesper V Olsen; Alexandre V Podtelejnikov; Jens R Andersen; Matthias Mann; Jacek R Wisniewski
Journal:  Mol Cell Proteomics       Date:  2005-01-30       Impact factor: 5.911

10.  Direct analysis of protein complexes using mass spectrometry.

Authors:  A J Link; J Eng; D M Schieltz; E Carmack; G J Mize; D R Morris; B M Garvik; J R Yates
Journal:  Nat Biotechnol       Date:  1999-07       Impact factor: 54.908

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  5 in total

Review 1.  Profiling of integral membrane proteins and their post translational modifications using high-resolution mass spectrometry.

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Journal:  Methods       Date:  2011-09-29       Impact factor: 3.608

2.  Quantitative improvements in peptide recovery at elevated chromatographic temperatures from microcapillary liquid chromatography-mass spectrometry analyses of brain using selected reaction monitoring.

Authors:  Santiago E Farias; Kelli G Kline; Jacek Klepacki; Christine C Wu
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3.  Post-translational modifications of integral membrane proteins resolved by top-down Fourier transform mass spectrometry with collisionally activated dissociation.

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Journal:  Mol Cell Proteomics       Date:  2010-01-21       Impact factor: 5.911

4.  Improved precision of proteomic measurements in immunoprecipitation based purifications using relative quantitation.

Authors:  Sarah M Rogstad; Tatiana Sorkina; Alexander Sorkin; Christine C Wu
Journal:  Anal Chem       Date:  2013-04-16       Impact factor: 6.986

5.  Selective capture of glycoproteins using lectin-modified nanoporous gold monolith.

Authors:  Allan J Alla; Felipe B D' Andrea; Jay K Bhattarai; Jared A Cooper; Yih Horng Tan; Alexei V Demchenko; Keith J Stine
Journal:  J Chromatogr A       Date:  2015-10-25       Impact factor: 4.759

  5 in total

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