Mass spectrometric analysis of post-translational modifications (PTMs) and protein-protein interactions (PPIs). (Q38222148)

31 August 2017

title

Mass spectrometric analysis of post-translational modifications (PTMs) and protein-protein interactions (PPIs). (English)

1 reference

protein-protein interaction

31 August 2017

main subject

1 reference

based on heuristic

inferred from title

author name string

Armand G Ngounou Wetie

series ordinal

1

1 reference

31 August 2017

Alisa G Woods

series ordinal

2

1 reference

31 August 2017

Costel C Darie

series ordinal

3

1 reference

31 August 2017

language of work or name

English

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publication date

1 January 2014

1 reference

Advances in Experimental Medicine and Biology

31 August 2017

published in

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31 August 2017

volume

806

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31 August 2017

page(s)

205-235

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Quality assessment of the human genome sequence

31 August 2017

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Quantitative phosphotyrosine proteomics of EphB2 signaling by stable isotope labeling with amino acids in cell culture (SILAC)

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Quantitative phosphoproteomic analysis reveals vasopressin V2-receptor-dependent signaling pathways in renal collecting duct cells.

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Quantitative phosphoproteomic analysis of the tumor necrosis factor pathway

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The Hallmarks of Cancer

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Comparative proteomic phenotyping of cell lines and primary cells to assess preservation of cell type-specific functions

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Tumor stem cells derived from glioblastomas cultured in bFGF and EGF more closely mirror the phenotype and genotype of primary tumors than do serum-cultured cell lines

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Advanced Maillard Reaction End Products, Free Radicals, and Protein Oxidation in Alzheimer's Diseasea

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Global impact of protein arginine phosphorylation on the physiology of Bacillus subtilis

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The effects of phosphorylation on the structure and function of proteins

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The age of crosstalk: phosphorylation, ubiquitination, and beyond

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Isolation and structural characterization of the Ndh complex from mesophyll and bundle sheath chloroplasts of Zea mays

31 March 2020

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Native electrophoresis for isolation of mitochondrial oxidative phosphorylation protein complexes

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Micelles protect membrane complexes from solution to vacuum.

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Liquid chromatography-mass spectrometry-based quantitative proteomics.

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Functional and quantitative proteomics using SILAC

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Quantitative analysis of complex protein mixtures using isotope-coded affinity tags

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Multiplexed protein quantitation in Saccharomyces cerevisiae using amine-reactive isobaric tagging reagents

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New dimensions in the study of protein complexes using quantitative mass spectrometry

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Mapping the integrin-linked kinase interactome using SILAC.

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Repo-Man recruits PP1 gamma to chromatin and is essential for cell viability

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A proteomics strategy to elucidate functional protein-protein interactions applied to EGF signaling

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Quantitative proteomic analysis of protein complexes: concurrent identification of interactors and their state of phosphorylation

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Phosphospecific proteolysis for mapping sites of protein phosphorylation

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Enrichment analysis of phosphorylated proteins as a tool for probing the phosphoproteome

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Mapping sites of O-GlcNAc modification using affinity tags for serine and threonine post-translational modifications

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A quantitative atlas of mitotic phosphorylation

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Differentiation between peptides containing acetylated or tri-methylated lysines by mass spectrometry: an application for determining lysine 9 acetylation and methylation of histone H3.

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Proteomic approaches to oxidative protein modifications implicated in the mechanism of aging

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Identification of an artifact in the mass spectrometry of proteins derivatized with iodoacetamide

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LC/MS characterization of undesired products formed during iodoacetamide derivatization of sulfhydryl groups of peptides

31 March 2020

1 reference

https://api.crossref.org/works/10.1007%2F978-3-319-06068-2_9

More than 100,000 Detectable Peptide Species Elute in Single Shotgun Proteomics Runs but the Majority is Inaccessible to Data-Dependent LC−MS/MS

31 March 2020

1 reference

https://api.crossref.org/works/10.1007%2F978-3-319-06068-2_9

MaxQuant enables high peptide identification rates, individualized p.p.b.-range mass accuracies and proteome-wide protein quantification

31 March 2020

1 reference

https://api.crossref.org/works/10.1007%2F978-3-319-06068-2_9

A large-scale method to measure absolute protein phosphorylation stoichiometries

31 March 2020

1 reference

https://api.crossref.org/works/10.1007%2F978-3-319-06068-2_9

Studying protein-protein affinity and immobilized ligand-protein affinity interactions using MS-based methods

31 March 2020

1 reference

https://api.crossref.org/works/10.1007%2F978-3-319-06068-2_9

OTX2 directly activates cell cycle genes and inhibits differentiation in medulloblastoma cells

31 March 2020

1 reference

https://api.crossref.org/works/10.1007%2F978-3-319-06068-2_9

Proteomics technologies for the global identification and quantification of proteins

31 March 2020

1 reference

https://api.crossref.org/works/10.1007%2F978-3-319-06068-2_9

Structural analyses of proteins electroblotted from native polyacrylamide gels onto polyvinyldiene difluoride membranes. A method for determining the stoichiometry of protein-protein interaction in solution

31 March 2020

1 reference

https://api.crossref.org/works/10.1007%2F978-3-319-06068-2_9

Electroblotting proteolytic products from native gel for direct N-terminal sequence analysis: an approach for studying protein-protein interaction

31 March 2020

1 reference

https://api.crossref.org/works/10.1007%2F978-3-319-06068-2_9

Capillary Electrophoresis of Proteins and Nucleic Acids

31 March 2020

1 reference

https://api.crossref.org/works/10.1007%2F978-3-319-06068-2_9

Electrophoretic methods for studying protein-protein interactions

31 March 2020

1 reference

https://api.crossref.org/works/10.1007%2F978-3-319-06068-2_9

10.1007/978-3-319-06068-2_9

31 March 2020

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DOI

1 reference

31 August 2017

1 reference