Featured
-
-
Article |
BUDDY: molecular formula discovery via bottom-up MS/MS interrogation
BUDDY is a bottom-up tandem MS (MS/MS) interrogation method for de novo molecular formula annotation with significance estimation.
- Shipei Xing
- , Sam Shen
- & Tao Huan
-
Comment |
Subcellular omics: a new frontier pushing the limits of resolution, complexity and throughput
We argue that the study of single-cell subcellular organelle omics is needed to understand and regulate cell function. This requires and is being enabled by new technology development.
- James Eberwine
- , Junhyong Kim
- & James Zou
-
Article |
Monitoring protein conformational changes using fluorescent nanoantennas
Fluorescent nanoantennas represent a versatile detection strategy for monitoring fast, large- and small-scale protein dynamics.
- Scott G. Harroun
- , Dominic Lauzon
- & Alexis Vallée-Bélisle
-
Article |
Metabolomic profiling of single enlarged lysosomes
Single-lysosome mass spectrometry (SLMS) integrates lysosomal patch-clamp recording and induced nanoESI/MS for concurrent metabolic and electrophysiological profiling of individual enlarged lysosomes.
- Hongying Zhu
- , Qianqian Li
- & Wei Xiong
-
Article |
Plasmonic scattering imaging of single proteins and binding kinetics
Plasmonic scattering microscopy (PSM) enables the imaging of single proteins on SPR instruments. The method enables measurement of protein size and binding kinetics and is fully compatible with simultaneous traditional SPR measurements.
- Pengfei Zhang
- , Guangzhong Ma
- & Nongjian Tao
-
Correspondence |
A five-level classification system for proteoform identifications
- Lloyd M. Smith
- , Paul M. Thomas
- & Neil L. Kelleher
-
Article |
Transmission-mode MALDI-2 mass spectrometry imaging of cells and tissues at subcellular resolution
Adapting a t-MALDI-2 ion source to an Orbitrap mass analyzer enables mass spectrometry imaging of cells and tissues with (sub)cellular resolution.
- M. Niehaus
- , J. Soltwisch
- & K. Dreisewerd
-
Article |
Systems NMR: single-sample quantification of RNA, proteins and metabolites for biomolecular network analysis
A nuclear magnetic resonance spectroscopy-based approach to monitor multiple molecule and reaction types at once, Systems NMR, provides in vitro insights into complex biomolecular network dynamics.
- Yaroslav Nikolaev
- , Nina Ripin
- & Frédéric H.-T. Allain
-
Advertising Feature: Application Note |
Improving biosensor assay development by determining sample quality with Tycho NT.6
- Dennis Breitsprecher
- , Peter A Fung
- & Nuska Tschammer
-
Technology Feature |
Chemical biology: fats as research subjects
Fats add structure, they signal, they interact. In the lab, lipids are tough to work with but worth the challenge.
- Vivien Marx
-
News & Views |
Mass spectrometry imaging goes three dimensional
Two complementary approaches improve 3D mass spectrometry imaging of biomolecules on 3D surfaces and within tissue sections and single cells.
- Klaus Dreisewerd
- & Joanne Y Yew
-
Brief Communication |
Deciphering lipid structures based on platform-independent decision rules
The Lipid Data Analyzer uses sets of decision rules to identify lipid subclasses in high-throughput LC-MS/MS data.
- Jürgen Hartler
- , Alexander Triebl
- & Gerhard G Thallinger
-
Brief Communication |
Autofocusing MALDI mass spectrometry imaging of tissue sections and 3D chemical topography of nonflat surfaces
A mass spectrometry imaging system combined with a laser triangulation system provides simultaneous topographic and molecular information for 3D biological samples and eliminates height-related artifacts in imperfect tissue sections.
- Mario Kompauer
- , Sven Heiles
- & Bernhard Spengler
-
Tools in Brief |
Nanopore-based protein fingerprinting
-
Brief Communication |
High-fidelity mass analysis unveils heterogeneity in intact ribosomal particles
Instrumental modifications enable native mass spectrometry analysis with unprecedented mass resolution, especially at high mass-to-charge ratios, as illustrated through the analysis of intact ribosome particles.
- Michiel van de Waterbeemd
- , Kyle L Fort
- & Albert J R Heck
-
Tools in Brief |
Nanokits for single cells
-
Advertising Feature: Application Note |
DNA fragmentation and quality control analysis using Diagenode shearing systems and Fragment Analyzer
- Wassim Lakha
- , Irina Panteleeva
- & Jonathan Hagopian
-
Brief Communication |
High-resolution mass spectrometry of small molecules bound to membrane proteins
A high-resolution, Orbitrap-based, native mass spectrometry approach allows the direct characterization of lipid, peptide and drug binding to intact membrane proteins.
- Joseph Gault
- , Joseph A C Donlan
- & Carol V Robinson
-
Method to Watch |
Subcellular maps
Methods to systematically map the distribution of proteins in cells are evolving.
- Natalie de Souza
-
Methods in Brief |
Fast reaction kinetics with time-resolved mass spectrometry
-
Methods in Brief |
Rapid reaction inspection
-
Research Highlights |
Magnetic field imaging and more
Two reports demonstrate further advances in the use of nitrogen vacancies for very different imaging applications.
- Daniel Evanko
-
Advertising Feature: Application Note |
Isolate and sequence ribosome-protected mRNA fragments using size-exclusion chromatography
- Lindsay Freeberg
- , Scott Kuersten
- & Fraz Syed
-
Correspondence |
Protein instability following transport or storage on dry ice
- Brian M Murphy
- , Spencer Swarts
- & Mark I Fitchmun
-
News & Views |
Shedding light on G protein–coupled receptor signaling
A new high-throughput method for monitoring G protein–coupled receptor activation is highly suited to assaying Gα12/13-coupled receptors and is used to deorphanize a group of receptors activated by lysophosphatidylserine.
- Marc Parmentier
-
Article |
TGFα shedding assay: an accurate and versatile method for detecting GPCR activation
A G protein–coupled receptor (GPCR) signaling assay based on ectodomain shedding of a membrane-bound proform of alkaline phosphatase-tagged TGFα provides a platform for studying poorly characterized Gα12/13-coupled GPCRs. The assay allowed identification of three orphan GPCRs as Gα12/13-coupled lysophosphatidylserine receptors.
- Asuka Inoue
- , Jun Ishiguro
- & Junken Aoki
-
Brief Communication |
A high-throughput approach for measuring temporal changes in the interactome
A combination of protein correlation profiling–stable isotope labeling by amino acids in cell culture and size-exclusion chromatography allows stoichiometric analysis of changes in the human interactome in response to a growth factor.
- Anders R Kristensen
- , Joerg Gsponer
- & Leonard J Foster
-
Research Highlights |
Secrets of RNA granules
A surprising hydrogel formation promises insight on prions and RNA transport.
- Monya Baker
-
Brief Communication |
M-Track: detecting short-lived protein-protein interactions in vivo
A proximity assay based on methylation of interacting 'prey' proteins by a 'bait' fused to the histone lysine methyltransferase permits the detection of enzyme-substrate protein-protein interactions in yeast.
- Aurora Zuzuarregui
- , Thomas Kupka
- & Egon Ogris
-
News & Views |
Taming the isobaric tagging elephant in the room in quantitative proteomics
Isobaric tagging methods allow multiplexed quantitative analysis of a wide variety of proteome samples but have been severely limited by problems of accuracy. Two groups now explore this issue and provide complementary solutions to address the problem.
- Andy Christoforou
- & Kathryn S Lilley
-
Brief Communication |
Gas-phase purification enables accurate, multiplexed proteome quantification with isobaric tagging
A mass spectrometry instrument control method—QuantMode—allows accurate, large-scale, multiplexed quantitative proteomics measurements using isobaric tagging by removing the problem of precursor interference. Also in this issue, Ting et al. provide a different solution to the same problem.
- Craig D Wenger
- , M Violet Lee
- & Joshua J Coon
-
Article |
A large-scale method to measure absolute protein phosphorylation stoichiometries
The functional role of protein phosphorylation is determined not just by whether a particular site is phosphorylated or not but also by the site's stoichiometry. A method to determine the absolute stoichiometries of protein phosphorylation on a proteomic scale is described.
- Ronghu Wu
- , Wilhelm Haas
- & Steven P Gygi
-
Review Article |
Profiling metabolites and peptides in single cells
- Stanislav S Rubakhin
- , Elena V Romanova
- & Jonathan V Sweedler
-
Advertising Feature: Application Note |
SpikeTides™—proteotypic peptides for large-scale MS-based proteomics
- Karsten Schnatbaum
- , Johannes Zerweck
- & Ulf Reimer
-
Brief Communication |
Organelle-specific, rapid induction of molecular activities and membrane tethering
Chemically inducible dimerization probes selectively target proteins to the surface of specific organelles or tether organelles to each other, thus allowing precise spatiotemporal analysis of signaling events.
- Toru Komatsu
- , Igor Kukelyansky
- & Takanari Inoue
RepoRT: a comprehensive repository for small molecule retention times