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Towards a systematic map of the functional role of protein phosphorylation

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What this work says

Outgoing claims: the papers this work cites, builds on, or argues with.

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A two‐step method for the introduction of single or multiple defined point mutations into the genome of Saccharomyces cerevisiae

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[10] 5-Fluoroorotic acid as a selective agent in yeast molecular genetics

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[57] Genetic and physical maps of Saccharomyces cerevisiae

inferredcites →https://doi.org/10.1016/j.bbabio.2018.04.011openalex-snapshot

Sit4p-mediated dephosphorylation of Atp2p regulates ATP synthase activity and mitochondrial function

inferredcites →https://doi.org/10.1016/j.cell.2006.09.026openalex-snapshot

Global, In Vivo, and Site-Specific Phosphorylation Dynamics in Signaling Networks

inferredcites →https://doi.org/10.1016/j.cell.2010.05.019openalex-snapshot

Quantitative Genetic Interactions Reveal Biological Modularity

inferredcites →https://doi.org/10.1016/j.cell.2010.11.052openalex-snapshot

Phenotypic Landscape of a Bacterial Cell

inferredcites →https://doi.org/10.1016/j.cell.2012.05.036openalex-snapshot

Systematic Functional Prioritization of Protein Posttranslational Modifications

inferredcites →https://doi.org/10.1016/j.cell.2013.07.033openalex-snapshot

From Structure to Systems: High-Resolution, Quantitative Genetic Analysis of RNA Polymerase II

inferredcites →https://doi.org/10.1016/j.cell.2018.02.030openalex-snapshot

Multiplexed Proteome Dynamics Profiling Reveals Mechanisms Controlling Protein Homeostasis

inferredcites →https://doi.org/10.1016/j.celrep.2013.10.024openalex-snapshot

TORC1 Inhibits GSK3-Mediated Elo2 Phosphorylation to Regulate Very Long Chain Fatty Acid Synthesis and Autophagy

inferredcites →https://doi.org/10.1016/j.celrep.2015.01.052openalex-snapshot

A Cell-Signaling Network Temporally Resolves Specific versus Promiscuous Phosphorylation

inferredcites →https://doi.org/10.1016/j.cels.2016.04.014openalex-snapshot

Systematic Functional Annotation and Visualization of Biological Networks

inferredcites →https://doi.org/10.1016/j.cels.2017.09.002openalex-snapshot

Yeast Creates a Niche for Symbiotic Lactic Acid Bacteria through Nitrogen Overflow

inferredcites →https://doi.org/10.1016/j.str.2011.09.021openalex-snapshot

Phosphorylation in Protein-Protein Binding: Effect on Stability and Function

inferredcites →https://doi.org/10.1016/j.tibs.2008.05.004openalex-snapshot

Non-functional phosphorylations?

inferredcites →https://doi.org/10.1016/j.tig.2009.03.003openalex-snapshot

Weak functional constraints on phosphoproteomes

inferredcites →https://doi.org/10.1038/387067a0openalex-snapshot

Structural features in a brittle–ductile wax model of continental extension

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Optimized base editors enable efficient editing in cells, organoids and mice

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Thermal profiling reveals phenylalanine hydroxylase as an off-target of panobinostat

inferredcites →https://doi.org/10.1038/nprot.2007.13openalex-snapshot

High-efficiency yeast transformation using the LiAc/SS carrier DNA/PEG method

inferredcites →https://doi.org/10.1038/s41467-019-09952-xopenalex-snapshot

Conserved phosphorylation hotspots in eukaryotic protein domain families

inferredcites →https://doi.org/10.1038/s41587-019-0344-3openalex-snapshot

The functional landscape of the human phosphoproteome

inferredcites →https://doi.org/10.1073/pnas.1608396113openalex-snapshot

Cardiolipin binds selectively but transiently to conserved lysine residues in the rotor of metazoan ATP synthases

inferredcites →https://doi.org/10.1073/pnas.1814818116openalex-snapshot

Structural comparison of the vacuolar and Golgi V-ATPases from Saccharomyces cerevisiae

inferredcites →https://doi.org/10.1074/jbc.275.2.1511openalex-snapshot

Regulatory Mechanisms for Modulation of Signaling through the Cell Integrity Slt2-mediated Pathway in Saccharomyces cerevisiae

inferredcites →https://doi.org/10.1074/jbc.m112349200openalex-snapshot

Direct and Novel Regulation of cAMP-dependent Protein Kinase by Mck1p, a Yeast Glycogen Synthase Kinase-3

inferredcites →https://doi.org/10.1074/mcp.m115.051177openalex-snapshot

Structural Analysis of PTM Hotspots (SAPH-ire) – A Quantitative Informatics Method Enabling the Discovery of Novel Regulatory Elements in Protein Families

inferredcites →https://doi.org/10.1074/mcp.ra118.000892openalex-snapshot

Effects of Acetylation and Phosphorylation on Subunit Interactions in Three Large Eukaryotic Complexes

inferredcites →https://doi.org/10.1093/database/bat026openalex-snapshot

The PhosphoGRID Saccharomyces cerevisiae protein phosphorylation site database: version 2.0 update

inferredcites →https://doi.org/10.1093/molbev/msr013openalex-snapshot

Rampant Purifying Selection Conserves Positions with Posttranslational Modifications in Human Proteins

inferredcites →https://doi.org/10.1093/nar/gkg509openalex-snapshot

SIFT: predicting amino acid changes that affect protein function

inferredcites →https://doi.org/10.1093/nar/gku1267openalex-snapshot

PhosphoSitePlus, 2014: mutations, PTMs and recalibrations

inferredcites →https://doi.org/10.1093/nar/gkv007openalex-snapshot

limma powers differential expression analyses for RNA-sequencing and microarray studies

inferredcites →https://doi.org/10.1126/science.1065810openalex-snapshot

Systematic Genetic Analysis with Ordered Arrays of Yeast Deletion Mutants

inferredcites →https://doi.org/10.1126/science.1176495openalex-snapshot

A Global Protein Kinase and Phosphatase Interaction Network in Yeast

inferredcites →https://doi.org/10.1126/science.1180823openalex-snapshot

The Genetic Landscape of a Cell

inferredcites →https://doi.org/10.1126/science.1210148openalex-snapshot

Mass Spectrometry of Intact V-Type ATPases Reveals Bound Lipids and the Effects of Nucleotide Binding

inferredcites →https://doi.org/10.1126/science.1255784openalex-snapshot

Tracking cancer drugs in living cells by thermal profiling of the proteome

inferredcites →https://doi.org/10.1126/science.285.5429.901openalex-snapshot

Functional Characterization of the S. cerevisiae Genome by Gene Deletion and Parallel Analysis

inferredcites →https://doi.org/10.1126/science.aaf2144openalex-snapshot

Evolution of protein phosphorylation across 18 fungal species

inferredcites →https://doi.org/10.1126/scisignal.2005768openalex-snapshot

Dynamic phosphoproteomics reveals TORC1-dependent regulation of yeast nucleotide and amino acid biosynthesis

inferredcites →https://doi.org/10.1128/mmbr.70.1.177-191.2006openalex-snapshot

The Where, When, and How of Organelle Acidification by the Yeast Vacuolar H + -ATPase

inferredcites →https://doi.org/10.1186/gb-2006-7-7-r63openalex-snapshot

A strategy for extracting and analyzing large-scale quantitative epistatic interaction data

inferredcites →https://doi.org/10.1186/s12918-016-0350-8openalex-snapshot

Untargeted metabolomics unravels functionalities of phosphorylation sites in Saccharomyces cerevisiae

inferredcites →https://doi.org/10.1371/journal.pbio.1000134openalex-snapshot

Evolution of Phosphoregulation: Comparison of Phosphorylation Patterns across Yeast Species

inferredcites →https://doi.org/10.1371/journal.pgen.1004062openalex-snapshot

Functional Divergence and Evolutionary Turnover in Mammalian Phosphoproteomes

inferredcites →https://doi.org/10.1371/journal.pone.0023794openalex-snapshot

Seamless Gene Tagging by Endonuclease-Driven Homologous Recombination

inferredcites →https://doi.org/10.1371/journal.ppat.1000939openalex-snapshot

Requirement for Ergosterol in V-ATPase Function Underlies Antifungal Activity of Azole Drugs

inferredcites →https://doi.org/10.15252/msb.20167295openalex-snapshot

An atlas of human kinase regulation

inferredcites →https://doi.org/10.15252/msb.20188242openalex-snapshot

Thermal proteome profiling in bacteria: probing protein state in vivo

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gitter: A Robust and Accurate Method for Quantification of Colony Sizes From Plate Images

inferredcites →https://doi.org/10.15698/mic2019.05.677openalex-snapshot

Ser/Thr protein phosphatases in fungi: structure, regulation and function

inferredcites →https://doi.org/10.3389/fpls.2017.01456openalex-snapshot

Predicted Functional Implications of Phosphorylation of Regulator of G Protein Signaling Protein in Plants

What points at this work

Incoming claims: where this work appears in other papers’ reference lists and arguments.

inferred← citeshttps://doi.org/10.1002/pmic.202100256openalex-snapshot

Recent advances in isobaric labeling and applications in quantitative proteomics

inferred← citeshttps://doi.org/10.1016/j.mito.2020.12.016openalex-snapshot

Mitochondrial protein phosphorylation in yeast revisited

inferred← citeshttps://doi.org/10.1038/s41467-021-25988-4openalex-snapshot

Extensive regulation of enzyme activity by phosphorylation in Escherichia coli

inferred← citeshttps://doi.org/10.1038/s41467-023-35795-8openalex-snapshot

Control of protein stability by post-translational modifications

inferred← citeshttps://doi.org/10.1038/s41592-021-01178-4openalex-snapshot

Identification of phosphosites that alter protein thermal stability

inferred← citeshttps://doi.org/10.1074/jbc.ra120.014576openalex-snapshot

Mutant thermal proteome profiling for characterization of missense protein variants and their associated phenotypes within the proteome

inferred← citeshttps://doi.org/10.1146/annurev-pharmtox-052120-013205openalex-snapshot

Drug Target Identification in Tissues by Thermal Proteome Profiling

inferred← citeshttps://doi.org/10.15252/msb.20199232openalex-snapshot

Thermal proteome profiling for interrogating protein interactions

inferred← citeshttps://doi.org/10.3389/frans.2023.1186623openalex-snapshot

Toward the analysis of functional proteoforms using mass spectrometry-based stability proteomics

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