69 results match your criteria bacterial phosphoproteomics


Proteome and phosphoproteome analysis of commensally induced dendritic cell maturation states.

J Proteomics 2018 05 15;180:11-24. Epub 2017 Nov 15.

Institute of Medical Microbiology and Hygiene, University of Tübingen, Germany.

Dendritic cells (DCs) can shape the immune system towards an inflammatory or tolerant state depending on the bacterial antigens and the environment they encounter. In this study we provide a proteomic catalogue of differentially expressed proteins between distinct DC maturation states, brought about by bacteria that differ in their endotoxicity. To achieve this, we have performed proteomics and phosphoproteomics on murine DC cultures. Read More

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Threonine eliminylation by bacterial phosphothreonine lyases rapidly causes cross-linking of mitogen-activated protein kinase (MAPK) in live cells.

J Biol Chem 2017 05 21;292(19):7784-7794. Epub 2017 Mar 21.

From the Team genomic plasticity and infection, Department of Immunology, Infectiology and Hematology, Institut Necker Enfants Malades, INSERM U1151, CNRS UMR 8253, 75993 Paris CEDEX 14, France,

Old long-lived proteins contain dehydroalanine (Dha) and dehydrobutyrine (Dhb), two amino acids engendered by dehydration of serines and threonines, respectively. Although these residues have a suspected role in protein cross-linking and aggregation, their direct implication has yet to be determined. Here, we have taken advantage of the ability of the enteropathogen to convert the phosphothreonine residue of the pT--pY consensus sequence of ERK and p38 into Dhb and followed the impact of dehydration on the fate of the two MAPKs. Read More

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Human NACHT, LRR, and PYD domain-containing protein 3 (NLRP3) inflammasome activity is regulated by and potentially targetable through Bruton tyrosine kinase.

J Allergy Clin Immunol 2017 Oct 16;140(4):1054-1067.e10. Epub 2017 Feb 16.

Interfaculty Institute for Cell Biology, Department of Immunology, University of Tübingen, Tübingen, Germany. Electronic address:

Background: The Nod-like receptor NACHT, LRR, and PYD domain-containing protein 3 (NLRP3) and Bruton tyrosine kinase (BTK) are protagonists in innate and adaptive immunity, respectively. NLRP3 senses exogenous and endogenous insults, leading to inflammasome activation, which occurs spontaneously in patients with Muckle-Wells syndrome; BTK mutations cause the genetic immunodeficiency X-linked agammaglobulinemia (XLA). However, to date, few proteins that regulate NLRP3 inflammasome activity in human primary immune cells have been identified, and clinically promising pharmacologic targeting strategies remain elusive. Read More

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October 2017

Study of O-Phosphorylation Sites in Proteins Involved in Photosynthesis-Related Processes in Synechocystis sp. Strain PCC 6803: Application of the SRM Approach.

J Proteome Res 2016 12 16;15(12):4638-4652. Epub 2016 Nov 16.

Molecular Plant Biology, Department of Biochemistry, University of Turku , FI-20014 Turku, Finland.

O-Phosphorylation has been shown in photosynthesis-related proteins in a cyanobacterium Synechocystis sp. strain PCC 6803 (thereafter Synechocystis 6803), suggesting that phosphorylation of S, T, and Y residues might be important in photosynthesis-related processes. Investigation of biological roles of these phosphorylation events requires confident knowledge of the phosphorylated sites and prospects for their individual assessment. Read More

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December 2016

Quantitative Proteomics Reveals the Dynamics of Protein Phosphorylation in Human Bronchial Epithelial Cells during Internalization, Phagosomal Escape, and Intracellular Replication of Staphylococcus aureus.

J Proteome Res 2016 12 4;15(12):4369-4386. Epub 2016 Nov 4.

Competence Center Functional Genomics, Junior Research Group Pathoproteomics, University of Greifswald , 17489 Greifswald, Germany.

Internalization of Staphylococcus aureus by nonprofessional phagocytic cells is a major suspected cause of persistent and difficult-to-treat infections, including pneumonia. In this study, we established an infection model with 16HBE14o- human bronchial epithelial cells and demonstrated internalization, escape from phagosomal clearance, and intracellular replication of S. aureus HG001 within the first 4 h postinfection. Read More

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December 2016

Proteomic discovery of host kinase signaling in bacterial infections.

Proteomics Clin Appl 2016 10 9;10(9-10):994-1010. Epub 2016 Sep 9.

Competence Center Functional Genomics, Junior Research Group Pathoproteomics, University of Greifswald, Greifswald, Germany.

Protein phosphorylation catalyzed by protein kinases acts as a reversible molecular switch in signal transduction, providing a mechanism for the control of protein function in cellular processes. During microbial infection, cellular signaling essentially contributes to immune control to restrict the dissemination of invading pathogens within the host organism. However, pathogenic microbes compete for the control of host signaling to create a beneficial environment for successful invasion and infection. Read More

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October 2016

Tyrosine 601 of Bacillus subtilis DnaK Undergoes Phosphorylation and Is Crucial for Chaperone Activity and Heat Shock Survival.

Front Microbiol 2016 19;7:533. Epub 2016 Apr 19.

Division of Systems and Synthetic Biology, Department of Biology and Biological Engineering, Chalmers University of Technology Gothenburg, Sweden.

In order to screen for cellular substrates of the Bacillus subtilis BY-kinase PtkA, and its cognate phosphotyrosine-protein phosphatase PtpZ, we performed a triple Stable Isotope Labeling by Amino acids in Cell culture-based quantitative phosphoproteome analysis. Detected tyrosine phosphorylation sites for which the phosphorylation level decreased in the ΔptkA strain and increased in the ΔptpZ strain, compared to the wild type (WT), were considered as potential substrates of PtkA/PtpZ. One of those sites was the residue tyrosine 601 of the molecular chaperone DnaK. Read More

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Induction of Macrophage Function in Human THP-1 Cells Is Associated with Rewiring of MAPK Signaling and Activation of MAP3K7 (TAK1) Protein Kinase.

Front Cell Dev Biol 2016 30;4:21. Epub 2016 Mar 30.

Junior Research Group Pathoproteomics, Competence Center Functional Genomics, University of Greifswald Greifswald, Germany.

Macrophages represent the primary human host response to pathogen infection and link the immediate defense to the adaptive immune system. Mature tissue macrophages convert from circulating monocyte precursor cells by terminal differentiation in a process that is not fully understood. Here, we analyzed the protein kinases of the human monocytic cell line THP-1 before and after induction of macrophage differentiation by using kinomics and phosphoproteomics. Read More

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Mechanisms of Phenotypic Rifampicin Tolerance in Mycobacterium tuberculosis Beijing Genotype Strain B0/W148 Revealed by Proteomics.

J Proteome Res 2016 Apr 24;15(4):1194-204. Epub 2016 Mar 24.

Tuberculosis Reference Laboratory, National Institute for Public Health and the Environment (RIVM) , Bilthoven 3720 BA, The Netherlands.

The "successful" Russian clone B0/W148 of Mycobacterium tuberculosis Beijing is well-known for its capacity to develop antibiotic resistance. During treatment, resistant mutants can occur that have inheritable resistance to specific antibiotics. Next to mutations, M. Read More

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Role of Protein Phosphorylation in the Regulation of Cell Cycle and DNA-Related Processes in Bacteria.

Front Microbiol 2016 16;7:184. Epub 2016 Feb 16.

Micalis Institute, INRA, AgroParisTech, Université Paris-Saclay Jouy-en-Josas, France.

In all living organisms, the phosphorylation of proteins modulates various aspects of their functionalities. In eukaryotes, protein phosphorylation plays a key role in cell signaling, gene expression, and differentiation. Protein phosphorylation is also involved in the global control of DNA replication during the cell cycle, as well as in the mechanisms that cope with stress-induced replication blocks. Read More

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February 2016

Mass Spectrometry Offers Insight into the Role of Ser/Thr/Tyr Phosphorylation in the Mycobacteria.

Front Microbiol 2016 12;7:141. Epub 2016 Feb 12.

Applied and Chemical Proteomics Group, Medical Biochemistry Division, Faculty of Health Sciences, Institute of Infectious Diseases and Molecular Medicine, University of Cape Town Cape Town, South Africa.

Phosphorylation is a post translational modification which can rapidly regulate biochemical pathways by altering protein function, and has been associated with pathogenicity in bacteria. Once engulfed by host macrophages, pathogenic bacteria are exposed to harsh conditions and must respond rapidly in order to survive. The causative agent of TB, Mycobacterium tuberculosis, is unusual amongst the bacteria because it can survive within the host macrophage for decades in a latent state, demonstrating a remarkable capacity to successfully evade the host immune response. Read More

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February 2016

A bacterial type III secretion-based protein delivery tool for broad applications in cell biology.

J Cell Biol 2015 Nov;211(4):913-31

Biozentrum, University of Basel, 4056 Basel, Switzerland Institut National de la Santé et de la Recherche Médicale, U1016, Institut Cochin, 75014 Paris, France Centre National de la Recherche Scientifique, UMR8104, 75014 Paris, France Université Paris Descartes, Sorbonne Paris Cité, 75006 Paris, France

Methods enabling the delivery of proteins into eukaryotic cells are essential to address protein functions. Here we propose broad applications to cell biology for a protein delivery tool based on bacterial type III secretion (T3S). We show that bacterial, viral, and human proteins, fused to the N-terminal fragment of the Yersinia enterocolitica T3S substrate YopE, are effectively delivered into target cells in a fast and controllable manner via the injectisome of extracellular bacteria. Read More

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November 2015

Comparative Phosphoproteomics Reveals the Role of AmpC β-lactamase Phosphorylation in the Clinical Imipenem-resistant Strain Acinetobacter baumannii SK17.

Mol Cell Proteomics 2016 Jan 23;15(1):12-25. Epub 2015 Oct 23.

From the ‡Institute of Biochemical Sciences, College of Life Sciences, National Taiwan University, Taipei 10617, Taiwan; §Institute of Biological Chemistry, Academia Sinica. Taipei 11529, Taiwan; ‖Chemical Biology and Molecular Biophysics Program, Taiwan International Graduate Program, Academia Sinica, Taipei 11529, Taiwan; **Department of Chemistry, National Taiwan University, Taipei 10617, Taiwan;

Nosocomial infectious outbreaks caused by multidrug-resistant Acinetobacter baumannii have emerged as a serious threat to human health. Phosphoproteomics of pathogenic bacteria has been used to identify the mechanisms of bacterial virulence and antimicrobial resistance. In this study, we used a shotgun strategy combined with high-accuracy mass spectrometry to analyze the phosphoproteomics of the imipenem-susceptible strain SK17-S and -resistant strain SK17-R. Read More

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January 2016

Global dynamics of Escherichia coli phosphoproteome in central carbon metabolism under changing culture conditions.

J Proteomics 2015 Aug 23;126:24-33. Epub 2015 May 23.

Australian Institute for Bioengineering and Nanotechnology (AIBN), Corner College and Coopers Rd, The University of Queensland, St Lucia, QLD 4072, Australia.

Little is known about the role of global phosphorylation events in the control of prokaryote metabolism. By performing a detailed analysis of all protein phosphorylation events previously reported in Escherichia coli, dynamic changes in protein phosphorylation were elucidated under three different culture conditions. Using scheduled reaction monitoring, the phosphorylation ratios of 82 peptides corresponding to 71 proteins were quantified to establish whether serine (S), threonine (T) and tyrosine (Y) phosphorylation events displayed a dynamic profile under changing culture conditions. Read More

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Directed analysis of cyanobacterial membrane phosphoproteome using stained phosphoproteins and titanium-enriched phosphopeptides.

J Microbiol 2015 Apr 8;53(4):279-87. Epub 2015 Apr 8.

Biological Disaster Analysis Group, Korea Basic Science Institute, Daejeon, 305-806, Republic of Korea.

Gel-free shotgun phosphoproteomics of unicellular cyanobacterium Synechocystis sp. PCC 6803 has not been reported up to now. The purpose of this study is to develop directed membrane phosphoproteomic method in Synechocystis sp. Read More

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A multi-omics approach identifies key hubs associated with cell type-specific responses of airway epithelial cells to staphylococcal alpha-toxin.

PLoS One 2015 27;10(3):e0122089. Epub 2015 Mar 27.

Competence Center Functional Genomics, Junior Research Group Pathoproteomics, University of Greifswald, 17489, Greifswald, Germany.

Responsiveness of cells to alpha-toxin (Hla) from Staphylococcus aureus appears to occur in a cell-type dependent manner. Here, we compare two human bronchial epithelial cell lines, i.e. Read More

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February 2016

Phosphoproteomics as an emerging weapon to develop new antibiotics against carbapenem resistant strain of Acinetobacter baumannii.

J Proteomics 2015 Jan 20;112:336-8. Epub 2014 Sep 20.

Department of Biochemistry, Central University of Rajasthan, Ajmer 305817, Rajasthan, India.

Acinetobacter baumannii causes pneumonia, bloodstream infections, urinary tract infections, respiratory infections and meningitis. A. baumannii has developed resistance against most of the antibiotics including carbapenem. Read More

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January 2015

Analysis of T4SS-induced signaling by H. pylori using quantitative phosphoproteomics.

Front Microbiol 2014 18;5:356. Epub 2014 Jul 18.

Department of Molecular Biology, Max Planck Institute for Infection Biology Berlin, Germany.

Helicobacter pylori is a Gram-negative bacterial pathogen colonizing the human stomach. Infection with H. pylori causes chronic inflammation of the gastric mucosa and may lead to peptic ulceration and/or gastric cancer. Read More

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Ser/Thr/Tyr phosphoproteome characterization of Acinetobacter baumannii: comparison between a reference strain and a highly invasive multidrug-resistant clinical isolate.

J Proteomics 2014 May 21;102:113-24. Epub 2014 Mar 21.

Laboratorio de Microbiología, Instituto de Investigación Biomedica de A Coruña (INIBIC), Servicio de Microbiología, Complejo Hospitalario Universitario A Coruña (CHUAC), Spain. Electronic address:

Unlabelled: In the current study, the Ser/Thr/Tyr phosphoproteomes of two Acinetobacter baumannii strains, reference (ATCC17978) and highly invasive multidrug-resistant clinical isolate (Abh12O-A2) were analyzed using SCX and TiO2 chromatography followed by high resolution mass spectrometry. We detected a total of 201 unique phosphorylation sites (p-sites), and, after manual validation of peptide spectra, 91 high-confidence phosphorylation events (p-events) could be localized to a specific amino acid residue. The percentage distribution of Ser/Thr/Tyr phosphorylation was 68. Read More

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Quantitative Phosphoproteomics Reveals the Role of Protein Arginine Phosphorylation in the Bacterial Stress Response.

Mol Cell Proteomics 2014 Feb 1;13(2):537-550. Epub 2020 Oct 1.

Research Institute of Molecular Pathology - IMP, Dr. Bohr-Gasse 7, A-1030 Vienna, Austria;. Electronic address:

Arginine phosphorylation is an emerging protein modification implicated in the general stress response of Gram-positive bacteria. The modification is mediated by the arginine kinase McsB, which phosphorylates and inactivates the heat shock repressor CtsR. In this study, we developed a mass spectrometric approach accounting for the peculiar chemical properties of phosphoarginine. Read More

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February 2014

Quantitative phosphoproteome analysis of Bacillus subtilis reveals novel substrates of the kinase PrkC and phosphatase PrpC.

Mol Cell Proteomics 2014 Aug 5;13(8):1965-78. Epub 2014 Jan 5.

From the ‡Proteome Center Tuebingen, Interfaculty Institute for Cell Biology, University of Tuebingen, Germany;

Reversible protein phosphorylation on serine, threonine, and tyrosine (Ser/Thr/Tyr) residues plays a critical role in regulation of vital processes in the cell. Despite of considerable progress in our understanding of the role of this modification in bacterial physiology, the dynamics of protein phosphorylation during bacterial growth has rarely been systematically addressed. In addition, little is known about in vivo substrates of bacterial Ser/Thr/Tyr kinases and phosphatases. Read More

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Quantitative phosphoproteomics reveals the role of protein arginine phosphorylation in the bacterial stress response.

Mol Cell Proteomics 2014 Feb 20;13(2):537-50. Epub 2013 Nov 20.

Research Institute of Molecular Pathology - IMP, Dr. Bohr-Gasse 7, A-1030 Vienna, Austria;

Arginine phosphorylation is an emerging protein modification implicated in the general stress response of Gram-positive bacteria. The modification is mediated by the arginine kinase McsB, which phosphorylates and inactivates the heat shock repressor CtsR. In this study, we developed a mass spectrometric approach accounting for the peculiar chemical properties of phosphoarginine. Read More

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February 2014

Comparative phosphoproteomics reveals components of host cell invasion and post-transcriptional regulation during Francisella infection.

Mol Cell Proteomics 2013 Nov 22;12(11):3297-309. Epub 2013 Aug 22.

Biological Science Division, Pacific Northwest National Laboratory, Richland, Washington;

Francisella tularensis is a facultative intracellular bacterium that causes the deadly disease tularemia. Most evidence suggests that Francisella is not well recognized by the innate immune system that normally leads to cytokine expression and cell death. In previous work, we identified new bacterial factors that were hyper-cytotoxic to macrophages. Read More

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November 2013

Systems-level overview of host protein phosphorylation during Shigella flexneri infection revealed by phosphoproteomics.

Mol Cell Proteomics 2013 Oct 4;12(10):2952-68. Epub 2013 Jul 4.

Biozentrum, University of Basel, Klingelbergstrasse 50/70, 4056 Basel, Switzerland.

The enteroinvasive bacterium Shigella flexneri invades the intestinal epithelium of humans. During infection, several injected effector proteins promote bacterial internalization, and interfere with multiple host cell responses. To obtain a systems-level overview of host signaling during infection, we analyzed the global dynamics of protein phosphorylation by liquid chromatography-tandem MS and identified several hundred of proteins undergoing a phosphorylation change during the first hours of infection. Read More

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October 2013

Protein-serine/threonine/tyrosine kinases in bacterial signaling and regulation.

FEMS Microbiol Lett 2013 Sep 19;346(1):11-9. Epub 2013 Jun 19.

Institute Micalis UMR1319, INRA, F-78350 Jouy-en-Josas, France.

In this review, we address some recent developments in the field of bacterial protein phosphorylation, focusing specifically on serine/threonine and tyrosine kinases. We present an overview of recent studies outlining the scope of physiological processes that are regulated by phosphorylation, ranging from cell cycle, growth, cell morphology, to metabolism, developmental phenomena, and virulence. Specific emphasis is placed on Mycobacterium tuberculosis as a showcase organism for serine/threonine kinases, and Bacillus subtilis to illustrate the importance of protein phosphorylation in developmental processes. Read More

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September 2013

Global dynamics of the Escherichia coli proteome and phosphoproteome during growth in minimal medium.

J Proteome Res 2013 Jun 2;12(6):2611-21. Epub 2013 May 2.

Proteome Center Tuebingen, University of Tuebingen, Germany.

Recent phosphoproteomics studies have generated relatively large data sets of bacterial proteins phosphorylated on serine, threonine, and tyrosine, implicating this type of phosphorylation in the regulation of vital processes of a bacterial cell; however, most phosphoproteomics studies in bacteria were so far qualitative. Here we applied stable isotope labeling by amino acids in cell culture (SILAC) to perform a quantitative analysis of proteome and phosphoproteome dynamics of Escherichia coli during five distinct phases of growth in the minimal medium. Combining two triple-SILAC experiments, we detected a total of 2118 proteins and quantified relative dynamics of 1984 proteins in all measured phases of growth, including 570 proteins associated with cell wall and membrane. Read More

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Comparative phosphoproteomics studies of macrophage response to bacterial virulence effectors.

J Proteomics 2012 Dec 11;77:251-61. Epub 2012 Sep 11.

State Key Laboratory of Virology,College of Life Sciences, Wuhan University, Wuhan, PR China.

Lipopolysaccharide (LPS) from Gram-negative bacteria and cell wall components from Gram-positive bacteria are pathogenic inducers of host cell innate immune systems. In this study, we adapted stable isotope labeling with amino acid in cell culture (SILAC) and Fe(3+)-IMAC phosphopeptide enrichment method to study phosphoproteomic changes in bacterial virulence factors induced macrophage RAW 264.7 cells. Read More

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December 2012

Bacterial phosphoproteomic analysis reveals the correlation between protein phosphorylation and bacterial pathogenicity.

Genomics Proteomics Bioinformatics 2011 Oct;9(4-5):119-27

Laboratory of Integrative Biosciences, College of Life Sciences, Sun Yat-Sen University, Guangzhou 510275, China.

Increasing evidence shows that protein phosphorylation on serine, threonine and tyrosine residues is a major regulatory post-translational modification in the bacteria. This review focuses on the implications of bacterial phosphoproteome in bacterial pathogenicity and highlights recent development of methods in phosphoproteomics and the connectivity of the phosphorylation networks. Recent technical developments in the high accuracy mass spectrometry have dramatically transformed proteomics and made it possible the characterization of a few exhaustive site-specific bacterial phosphoproteomes. Read More

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October 2011

Impact of phosphoproteomics on studies of bacterial physiology.

FEMS Microbiol Rev 2012 Jul 28;36(4):877-92. Epub 2011 Nov 28.

INRA, UMR1319, Jouy-en-Josas, France.

Protein phosphorylation on serine, threonine and tyrosine is recognized as a major tool of signal transduction in bacteria. However, progress in the field has been hampered by the lack of global and site-specific data on bacterial phosphoproteomes. Recent advances in mass spectrometry-based proteomics have encouraged bacteriologists to start using powerful gel-free approaches for global detection of phosphorylated proteins. Read More

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Online nanoflow multidimensional fractionation for high efficiency phosphopeptide analysis.

Mol Cell Proteomics 2011 Nov 25;10(11):O111.011064. Epub 2011 Jul 25.

Department of Cancer Biology and Blais Proteomics Center, Dana-Farber Cancer Institute, Boston, MA 02115, USA.

Despite intense, continued interest in global analyses of signaling cascades through mass spectrometry-based studies, the large-scale, systematic production of phosphoproteomics data has been hampered in-part by inefficient fractionation strategies subsequent to phosphopeptide enrichment. Here we explore two novel multidimensional fractionation strategies for analysis of phosphopeptides. In the first technique we utilize aliphatic ion pairing agents to improve retention of phosphopeptides at high pH in the first dimension of a two-dimensional RP-RP. Read More

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November 2011