Literature DB >> 11680867

Phosphoamino acid analysis.

A Sickmann1, H E Meyer.   

Abstract

Phosphorylation of amino acid residues in proteins plays a major role in biological systems. Often, phosphorylation acts as a molecular switch controlling the protein activity in different pathways as in metabolism, signal transduction, cell division etc. Therefore, identification of phosphoamino acids in proteins is an important task in protein analysis. Since the introduction of high resolution two-dimensional polyacrylamide gel electrophoresis (2-D PAGE) a separation of phosphorylated and dephosphorylated protein species is possible. The identification of phosphorylation sites from preparative 2-D gels need very sensitive mass spectrometry methods and a specific enrichment of the phosphoprotein or -peptide.

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Year:  2001        PMID: 11680867     DOI: 10.1002/1615-9861(200102)1:2<200::AID-PROT200>3.0.CO;2-V

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


  33 in total

1.  Profiling of tyrosine phosphorylation pathways in human cells using mass spectrometry.

Authors:  Arthur R Salomon; Scott B Ficarro; Laurence M Brill; Achim Brinker; Qui T Phung; Christer Ericson; Karsten Sauer; Ansgar Brock; David M Horn; Peter G Schultz; Eric C Peters
Journal:  Proc Natl Acad Sci U S A       Date:  2003-01-09       Impact factor: 11.205

2.  Multidimensional nano-HPLC for analysis of protein complexes.

Authors:  Yvonne Wagner; Albert Sickmann; Helmut E Meyer; Günther Daum
Journal:  J Am Soc Mass Spectrom       Date:  2003-09       Impact factor: 3.109

3.  Biosilica formation in diatoms: characterization of native silaffin-2 and its role in silica morphogenesis.

Authors:  Nicole Poulsen; Manfred Sumper; Nils Kröger
Journal:  Proc Natl Acad Sci U S A       Date:  2003-09-24       Impact factor: 11.205

4.  Biochemical activities of the absA two-component system of Streptomyces coelicolor.

Authors:  Nancy L Sheeler; Susan V MacMillan; Justin R Nodwell
Journal:  J Bacteriol       Date:  2005-01       Impact factor: 3.490

5.  Screening for transglutaminase-catalyzed modifications by peptide mass finger printing using multipoint recalibration on recognized peaks for high mass accuracy.

Authors:  Cecilia Sundby Emanuelsson; Sandor Boros; Karin Hjernoe; Wilbert C Boelens; Peter Hojrup
Journal:  J Biomol Tech       Date:  2005-09

6.  Modeling multi-typed structurally viewed chemicals with the UMLS Refined Semantic Network.

Authors:  Ling Chen; C Paul Morrey; Huanying Gu; Michael Halper; Yehoshua Perl
Journal:  J Am Med Inform Assoc       Date:  2008-10-24       Impact factor: 4.497

7.  Enhanced detection of multiply phosphorylated peptides and identification of their sites of modification.

Authors:  Antoine Fleitz; Edward Nieves; Carlos Madrid-Aliste; Sarah J Fentress; L David Sibley; Louis M Weiss; Ruth Hogue Angeletti; Fa-Yun Che
Journal:  Anal Chem       Date:  2013-08-29       Impact factor: 6.986

8.  Spectral Library Based Analysis of Arginine Phosphorylations in Staphylococcus aureus.

Authors:  Sabryna Junker; Sandra Maaβ; Andreas Otto; Stephan Michalik; Friedrich Morgenroth; Ulf Gerth; Michael Hecker; Dörte Becher
Journal:  Mol Cell Proteomics       Date:  2017-11-28       Impact factor: 5.911

Review 9.  Eukaryote-like serine/threonine kinases and phosphatases in bacteria.

Authors:  Sandro F F Pereira; Lindsie Goss; Jonathan Dworkin
Journal:  Microbiol Mol Biol Rev       Date:  2011-03       Impact factor: 11.056

10.  Changes in reflectin protein phosphorylation are associated with dynamic iridescence in squid.

Authors:  Michi Izumi; Alison M Sweeney; Daniel Demartini; James C Weaver; Meghan L Powers; Andrea Tao; Tania V Silvas; Ryan M Kramer; Wendy J Crookes-Goodson; Lydia M Mäthger; Rajesh R Naik; Roger T Hanlon; Daniel E Morse
Journal:  J R Soc Interface       Date:  2009-09-23       Impact factor: 4.118

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