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Isotope Signatures Allow Identification of Chemically Cross-Linked Peptides by Mass Spectrometry: A Novel Method to Determine Interresidue Distances in Protein Structures through Cross-Linking
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What this work says
Outgoing claims: the papers this work cites, builds on, or argues with.
inferredcites →https://doi.org/10.1002/jms.559openalex-snapshot
Chemical cross‐linking and mass spectrometry for mapping three‐dimensional structures of proteins and protein complexes
inferredcites →https://doi.org/10.1002/rcm.554openalex-snapshot
Intramolecular cross‐linking experiments on cytochrome c and ribonuclease A using an isotope multiplet method
inferredcites →https://doi.org/10.1016/1044-0305(94)80016-2openalex-snapshot
An approach to correlate tandem mass spectral data of peptides with amino acid sequences in a protein database
inferredcites →https://doi.org/10.1016/j.jasms.2004.05.004openalex-snapshot
Probing three-dimensional structure of bovine serum albumin by chemical cross-linking and mass spectrometry
inferredcites →https://doi.org/10.1016/j.jasms.2006.04.020openalex-snapshot
Isotope-labeled cross-linkers and fourier transform ion cyclotron resonance mass spectrometry for structural analysis of a protein/peptide complex
inferredcites →https://doi.org/10.1016/s1044-0305(03)00327-1openalex-snapshot
MS2Assign, automated assignment and nomenclature of tandem mass spectra of chemically crosslinked peptides
inferredcites →https://doi.org/10.1021/ac001379aopenalex-snapshot
Isotope-Tagged Cross-Linking Reagents. A New Tool in Mass Spectrometric Protein Interaction Analysis
inferredcites →https://doi.org/10.1021/ac0700833openalex-snapshot
High-Speed Data Reduction, Feature Detection, and MS/MS Spectrum Quality Assessment of Shotgun Proteomics Data Sets Using High-Resolution Mass Spectrometry
inferredcites →https://doi.org/10.1021/ac801646fopenalex-snapshot
Characterization of Protein Cross-Links via Mass Spectrometry and an Open-Modification Search Strategy
inferredcites →https://doi.org/10.1021/pr025572sopenalex-snapshot
Dissection of Proteolytic 18O Labeling: Endoprotease-Catalyzed 16O-to-18O Exchange of Truncated Peptide Substrates
inferredcites →https://doi.org/10.1021/pr060154zopenalex-snapshot
Protein Cross-Linking Analysis Using Mass Spectrometry, Isotope-Coded Cross-Linkers, and Integrated Computational Data Processing
inferredcites →https://doi.org/10.1021/pr070234iopenalex-snapshot
Shotgun Cross-Linking Analysis for Studying Quaternary and Tertiary Protein Structures
inferredcites →https://doi.org/10.1038/35001009openalex-snapshot
A comprehensive analysis of protein–protein interactions in Saccharomyces cerevisiae
inferredcites →https://doi.org/10.1038/415141aopenalex-snapshot
Functional organization of the yeast proteome by systematic analysis of protein complexes
inferredcites →https://doi.org/10.1038/415180aopenalex-snapshot
Systematic identification of protein complexes in Saccharomyces cerevisiae by mass spectrometry
inferredcites →https://doi.org/10.1038/nature04209openalex-snapshot
Towards a proteome-scale map of the human protein–protein interaction network
inferredcites →https://doi.org/10.1038/nmeth.1192openalex-snapshot
Identification of cross-linked peptides from large sequence databases
inferredcites →https://doi.org/10.1038/nmeth1113openalex-snapshot
Semi-supervised learning for peptide identification from shotgun proteomics datasets
inferredcites →https://doi.org/10.1038/nsb1001-833openalex-snapshot
Structure of a BRCA1-BARD1 heterodimeric RING-RING complex.
inferredcites →https://doi.org/10.1073/pnas.0509355103openalex-snapshot
Physically realistic homology models built with rosetta can be more accurate than their templates
inferredcites →https://doi.org/10.1073/pnas.061034498openalex-snapshot
A comprehensive two-hybrid analysis to explore the yeast protein interactome
inferredcites →https://doi.org/10.1074/jbc.m601785200openalex-snapshot
Identification of the Interactions between Cytochrome P450 2E1 and Cytochrome b5 by Mass Spectrometry and Site-directed Mutagenesis
inferredcites →https://doi.org/10.1110/ps.051685706openalex-snapshot
“Zero‐length” cross‐linking in solid state as an approach for analysis of protein–protein interactions
inferredcites →https://doi.org/10.1110/ps.51201openalex-snapshot
Quantitative evaluation of the lengths of homobifunctional protein cross‐linking reagents used as molecular rulers
What points at this work
Incoming claims: where this work appears in other papers’ reference lists and arguments.
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Identification of Peptide Features in Precursor Spectra Using Hardklör and Krönik
inferred← citeshttps://doi.org/10.1002/9781118232125.ch4openalex-snapshot
Mass Spectrometry Based Approaches to Study Biomolecular Higher Order Structure
inferred← citeshttps://doi.org/10.1002/jcc.26736openalex-snapshot
Pseudopotentials for coarse‐grained cross‐link‐assisted modeling of protein structures
inferred← citeshttps://doi.org/10.1002/jms.1665openalex-snapshot
Current literature in mass spectrometry
inferred← citeshttps://doi.org/10.1002/pmic.201200305openalex-snapshot
Chemical cross‐linkers for protein structure studies by mass spectrometry
inferred← citeshttps://doi.org/10.1002/pro.2458openalex-snapshot
Distance restraints from crosslinking mass spectrometry: Mining a molecular dynamics simulation database to evaluate lysine–lysine distances
inferred← citeshttps://doi.org/10.1002/rcm.9859openalex-snapshot
A hydrolyzed N ‐propionylthiosuccinimide linker is cleaved by metastable fragmentation, increasing reliability of conjugation site identification in conjugate vaccines
inferred← citeshttps://doi.org/10.1007/978-3-319-06068-2_11openalex-snapshot
A Mass Spectrometry View of Stable and Transient Protein Interactions
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Molecular networking and collision cross section prediction for structural isomer and unknown compound identification in plant metabolomics: a case study applied to Zhanthoxylum heitzii extracts
inferred← citeshttps://doi.org/10.1016/bs.aivir.2019.07.003openalex-snapshot
Structural mass spectrometry goes viral
inferred← citeshttps://doi.org/10.1016/j.jsb.2010.10.014openalex-snapshot
The beginning of a beautiful friendship: Cross-linking/mass spectrometry and modelling of proteins and multi-protein complexes
inferred← citeshttps://doi.org/10.1016/j.jsb.2016.03.006openalex-snapshot
Structure of γ-tubulin small complex based on a cryo-EM map, chemical cross-links, and a remotely related structure
inferred← citeshttps://doi.org/10.1016/j.microc.2024.111025openalex-snapshot
On the utility of the extracted ion chromatograms for assigning the conjugation sites and side reactions in bioconjugates synthesized by the maleimide-thiol chemistry
inferred← citeshttps://doi.org/10.1016/j.str.2020.05.012openalex-snapshot
Combining Information from Crosslinks and Monolinks in the Modeling of Protein Structures
inferred← citeshttps://doi.org/10.1021/ac3033257openalex-snapshot
Proteomics-Based Methods for Discovery, Quantification, and Validation of Protein–Protein Interactions
inferred← citeshttps://doi.org/10.1021/ac400666popenalex-snapshot
Discovery of Undefined Protein Cross-Linking Chemistry: A Comprehensive Methodology Utilizing 18O-Labeling and Mass Spectrometry
inferred← citeshttps://doi.org/10.1021/acs.analchem.6b01585openalex-snapshot
Xilmass: A New Approach toward the Identification of Cross-Linked Peptides
inferred← citeshttps://doi.org/10.1021/acs.analchem.9b02491openalex-snapshot
Covalent Cross-Linking as an Enabler for Structural Mass Spectrometry
inferred← citeshttps://doi.org/10.1021/acs.jproteome.7b00881openalex-snapshot
Mass-Spectrometry-Based Identification of Cross-Links in Proteins Exposed to Photo-Oxidation and Peroxyl Radicals Using 18O Labeling and Optimized Tandem Mass Spectrometry Fragmentation
inferred← citeshttps://doi.org/10.1021/cb100338xopenalex-snapshot
Isotopic Signature Transfer and Mass Pattern Prediction (IsoStamp): An Enabling Technique for Chemically-Directed Proteomics
inferred← citeshttps://doi.org/10.1021/pr501321hopenalex-snapshot
Kojak: Efficient Analysis of Chemically Cross-Linked Protein Complexes
inferred← citeshttps://doi.org/10.1038/ncomms9673openalex-snapshot
The molecular architecture of the Dam1 kinetochore complex is defined by cross-linking based structural modelling
inferred← citeshttps://doi.org/10.1038/s41594-018-0147-0openalex-snapshot
Cross-linking mass spectrometry: methods and applications in structural, molecular and systems biology
inferred← citeshttps://doi.org/10.1039/9781788010016-00087openalex-snapshot
Mass Spectrometry in Biophysics: from High Throughput Screening to Structural Biology
inferred← citeshttps://doi.org/10.1039/9781849737081-00151openalex-snapshot
Integrating chemical cross-linking with mass spectrometric analysis of peptides and proteins
inferred← citeshttps://doi.org/10.1071/ch13164openalex-snapshot
Chemical Cross-linking and Mass Spectrometry for the Structural Analysis of Protein Assemblies
inferred← citeshttps://doi.org/10.1074/mcp.m111.008318openalex-snapshot
An Integrated Chemical Cross-linking and Mass Spectrometry Approach to Study Protein Complex Architecture and Function
inferred← citeshttps://doi.org/10.1093/bioinformatics/btr348openalex-snapshot
Xwalk: computing and visualizing distances in cross-linking experiments
inferred← citeshttps://doi.org/10.1093/braincomms/fcaf019openalex-snapshot
Dehydroamino acids and their crosslinks in Alzheimer’s disease aggregates
inferred← citeshttps://doi.org/10.1101/2024.09.23.614558openalex-snapshot
Discovery of dehydroamino acids and their crosslinks in Tau and other aggregating proteins of Alzheimer’s disease
inferred← citeshttps://doi.org/10.1126/science.1221483openalex-snapshot
Structural Probing of a Protein Phosphatase 2A Network by Chemical Cross-Linking and Mass Spectrometry
inferred← citeshttps://doi.org/10.1371/journal.pone.0073411openalex-snapshot
Cross-Link Guided Molecular Modeling with ROSETTA
inferred← citeshttps://doi.org/10.17760/d20128343openalex-snapshot
Development of methods for the analysis of protein post-translational modifications
inferred← citeshttps://doi.org/10.26434/chemrxiv-2023-3g9g6openalex-snapshot
On the utility of the extracted ion chromatograms for assigning the conjugation sites in bioconjugates synthesized by the maleimide-thiol chemistry
inferred← citeshttps://doi.org/10.26434/chemrxiv-2023-3g9g6-v2openalex-snapshot
On the utility of the extracted ion chromatograms for assigning the conjugation sites in bioconjugates synthesized by the maleimide-thiol chemistry
inferred← citeshttps://doi.org/10.26434/chemrxiv-2024-80jqwopenalex-snapshot
N-propionyl thiosuccinimide linker upon hydrolysis becomes into a cleavable crosslinker by a gas phase metastable fragmentation and makes more reliable the conjugation sites identification.
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