Brief Communication |
Featured
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Methods in Brief |
Comprehensive glycoprotein characterization
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Correspondence |
Avoiding abundance bias in the functional annotation of posttranslationally modified proteins
- Christian Schölz
- , David Lyon
- & Brian T Weinert
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Methods in Brief |
Ultra-mass-tolerant database searching
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Research Highlights |
Efficient generation of proteins with site-specific phosphoserines
An optimized strategy allows genetic encoding of phosphoserine and its nonhydrolyzable analog.
- Rita Strack
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Method to Watch |
Nanopores for proteins
Nanopores hold promise for single-protein characterization.
- Tal Nawy
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Methods in Brief |
Profiling the N-myristoylated proteome
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Methods in Brief |
Phosphohistidine proteomics
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Research Highlights |
Nanopores sense protein modifications
Protein nanopores can detect post-translational modifications in proteins.
- Tal Nawy
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This Month |
Benjamin F. Cravatt
Building an approach to quantify chinks in a protein's armor.
- Vivien Marx
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Article |
A chemoproteomic platform to quantitatively map targets of lipid-derived electrophiles
A competitive activity–based protein profiling method is reported for quantifying the reactivity of lipid-derived electrophilic compounds with cysteine residues in the human proteome.
- Chu Wang
- , Eranthie Weerapana
- & Benjamin F Cravatt
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Research Highlights |
Constructing complicated carbohydrates
A stepwise strategy of targeted synthesis enables researchers to reconstruct cellular glycomes in vitro.
- Michael Eisenstein
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Research Highlights |
Self-destruct sequences
High-throughput sequencing of massive mutant libraries helps researchers catalog determinants of protein stability.
- Michael Eisenstein
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Research Highlights |
Antibodies, made to order
Informed by existing molecular recognition motifs, researchers design effective scaffolds for directed evolution of post-translational modification–specific antibodies.
- Michael Eisenstein
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Brief Communication |
Site-specific characterization of the Asp- and Glu-ADP-ribosylated proteome
A proteomic method to identify human proteins post-translationally modified by poly(ADP-ribosyl)ation is reported, which will help yield further insights into the biological role of this modification.
- Yajie Zhang
- , Jianqi Wang
- & Yonghao Yu
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Research Highlights |
Matching marks with mechanisms
Reagents that recognize specific chemical modifications while ignoring the surrounding protein offer valuable proteomic insights.
- Michael Eisenstein
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News & Views |
Eavesdropping on PTM cross-talk through serial enrichment
Two approaches to serially enrich protein post-translational modifications allow the detection of multiple modifications in a single biological sample using mass spectrometry.
- Kristofor Webb
- & Eric J Bennett
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Article |
Global analysis of phosphorylation and ubiquitylation cross-talk in protein degradation
Two methods for identifying protein isoforms that are concurrently phosphorylated and ubiquitylated are applied in yeast to identify phosphorylation sites that regulate ubiquitin proteasome–mediated proteome degradation.
- Danielle L Swaney
- , Pedro Beltrao
- & Judit Villén
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Brief Communication |
Integrated proteomic analysis of post-translational modifications by serial enrichment
A mass spectrometry–based method using serial enrichments of different post-translational modifications (SEPTM) enables high-coverage proteomic analysis of multiple PTMs from a single biological sample.
- Philipp Mertins
- , Jana W Qiao
- & Steven A Carr
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Tools in Brief |
Profiling ubiquitin-like modifications
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Brief Communication |
A Y2H-seq approach defines the human protein methyltransferase interactome
A high-sensitivity, high-quality yeast two-hybrid screen using short-read sequencing as its readout is used to map the interactome of human methyltransferases.
- Mareike Weimann
- , Arndt Grossmann
- & Ulrich Stelzl
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Technology Feature |
Making sure PTMs are not lost after translation
Mass spectrometrists travel top down, middle down and bottom up to study post-translational modifications on proteins and their biological functions.
- Vivien Marx
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Tools in Brief |
A mouse model to study SUMOylation
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Tools in Brief |
Measuring phosphorylation-site stoichiometry
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Research Highlights |
Making PTMs a priority
Researchers describe an approach to zero in on post-translational modifications likely to have important regulatory functions.
- Allison Doerr
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Methods in Brief |
Binders of O-glycosylated proteins
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Article |
Polyubiquitin-sensor proteins reveal localization and linkage-type dependence of cellular ubiquitin signaling
Sensor proteins that exploit principles of linkage-specific avidity reveal topology-related functions of polyubiquitin in diverse cell types and pathways.
- Joshua J Sims
- , Francesco Scavone
- & Robert E Cohen
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Research Highlights |
Hidden code in the protein code
Apparently redundant codons may not be redundant after all.
- Monya Baker
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Article |
In situ analysis of tyrosine phosphorylation networks by FLIM on cell arrays
Combining reverse transfection of protein tyrosine kinase substrates on cell arrays with fluorescence resonance energy transfer (FRET) measurements by fluorescence lifetime imaging microscopy (FLIM) allows quantitative assessment of phosphorylation patterns and identification of feedback loops at single-cell resolution.
- Hernán E Grecco
- , Pedro Roda-Navarro
- & Philippe I H Bastiaens