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A Set of Organelle-Localizable Reactive Molecules for Mitochondrial Chemical Proteomics in Living Cells and Brain Tissues
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The 65 checked references that resolve
resolves10.1021/ja3094313
The Revolution and Evolution of Shotgun Proteomics for Large-Scale Proteome Analysis
resolves10.1038/nature09472
Quantitative reactivity profiling predicts functional cysteines in proteomes
resolves10.1038/nmeth.3366
Isotope-targeted glycoproteomics (IsoTaG): a mass-independent platform for intact N- and O-glycopeptide discovery and analysis
resolves10.1021/ja4043214
Semisynthetic Lectin–4-Dimethylaminopyridine Conjugates for Labeling and Profiling Glycoproteins on Live Cell Surfaces
resolves10.1021/ja210528v
Quantitative Chemical Proteomics Approach To Identify Post-translational Modification-Mediated Protein–Protein Interactions
resolves10.1021/ja209008w
Site-Specific Incorporation of Photo-Cross-Linker and Bioorthogonal Amino Acids into Enteric Bacterial Pathogens
resolves10.1146/annurev.biochem.75.101304.124125
Activity-Based Protein Profiling: From Enzyme Chemistry to Proteomic Chemistry
resolves10.1126/science.1230593
Proteomic Mapping of Mitochondria in Living Cells via Spatially Restricted Enzymatic Tagging
resolves10.1016/j.molcel.2014.06.003
Proteomic Mapping of the Human Mitochondrial Intermembrane Space in Live Cells via Ratiometric APEX Tagging
resolves10.1073/pnas.1515623112
Proteomic mapping in live
<i>Drosophila</i>
tissues using an engineered ascorbate peroxidase
resolves10.1002/asia.201100306
Chemical Modification and Organelle‐Specific Localization of Orlistat‐Like Natural‐Product‐Based Probes
resolves10.1246/cl.151083
Nucleus-selective Chemical Proteomics Using Hoechst-tagged Reactive Molecules
resolves10.1002/anie.200900942
Bioorthogonal Chemistry: Fishing for Selectivity in a Sea of Functionality
resolves10.1002/anie.201207089
Protein Organic Chemistry and Applications for Labeling and Engineering in Live‐Cell Systems
resolves10.1039/c2ay25106j
Covalent labeling of mitochondria with a photostable fluorescent thiol-reactive rhodamine-based probe
resolves10.1021/cb100007s
Isozyme-Specific Fluorescent Inhibitor of Glutathione <i>S</i>-Transferase Omega 1
resolves10.1021/cb400769v
Live Cell Chemical Profiling of Temporal Redox Dynamics in a Photoautotrophic Cyanobacterium
resolves10.1021/ja204422r
Chemical Cell-Surface Receptor Engineering Using Affinity-Guided, Multivalent Organocatalysts
resolves10.1021/bc960059o
PEG Thiazolidine-2-thione, a Novel Reagent for Facile Protein Modification: Conjugation of Bovine Hemoglobin
resolves10.1016/j.cbpa.2014.10.021
Covalent protein modification: the current landscape of residue-specific electrophiles
resolves10.1016/j.chembiol.2013.01.016
Chemical Proteomics with Sulfonyl Fluoride Probes Reveals Selective Labeling of Functional Tyrosines in Glutathione Transferases
resolves10.1002/cbic.201402051
Comparison of the Reactivity of Carbohydrate Photoaffinity Probes with Different Photoreactive Groups
resolves10.1016/0005-2728(86)90112-X
Rhodamine 123 as a probe of transmembrane potential in isolated rat-liver mitochondria: spectral and metabolic properties
resolves10.1242/jcs.114.15.2855
Temporal relationship between cytochrome c release and mitochondrial swelling during UV-induced apoptosis in living HeLa cells
resolves10.1016/j.bbabio.2009.02.023
IF1, the endogenous regulator of the F1Fo-ATPsynthase, defines mitochondrial volume fraction in HeLa cells by regulating autophagy
resolves10.1021/pr700658q
Phase Transfer Surfactant-Aided Trypsin Digestion for Membrane Proteome Analysis
resolves10.1038/cdd.2014.197
The endogenous caspase-8 inhibitor c-FLIPL regulates ER morphology and crosstalk with mitochondria
resolves10.1021/pr200553c
Proteome of Skeletal Muscle Lipid Droplet Reveals Association with Mitochondria and Apolipoprotein A-I
resolves10.1016/j.cell.2008.06.016
A Mitochondrial Protein Compendium Elucidates Complex I Disease Biology
resolves10.1038/nprot.2008.211
Systematic and integrative analysis of large gene lists using DAVID bioinformatics resources
resolves10.1038/nprot.2006.427
A practical recipe for stable isotope labeling by amino acids in cell culture (SILAC)
resolves10.1080/10915810490265432
The Involvement of p53 in Paraquat-Induced Apoptosis in Human Lung Epithelial-Like Cells
resolves10.4070/kcj.2012.42.1.23
Protective Effects of Peroxiredoxin on Hydrogen Peroxide Induced Oxidative Stress and Apoptosis in Cardiomyocytes
resolves10.1007/s11010-013-1891-4
Peroxiredoxin 2 is upregulated in colorectal cancer and contributes to colorectal cancer cells’ survival by protecting cells from oxidative stress
resolves10.1074/jbc.273.35.22528
Mice with a Homozygous Null Mutation for the Most Abundant Glutathione Peroxidase, Gpx1, Show Increased Susceptibility to the Oxidative Stress-inducing Agents Paraquat and Hydrogen Peroxide
resolves10.1039/c4mb00026a
Quantitative proteomic analysis reveals mitochondrial protein changes in MPP+-induced neuronal cells
resolves10.1016/j.cell.2004.05.008
Disruption of Mitochondrial Function during Apoptosis Is Mediated by Caspase Cleavage of the p75 Subunit of Complex I of the Electron Transport Chain
resolves10.1371/journal.pone.0107842
The Selective Target of Capsaicin on FASN Expression and De Novo Fatty Acid Synthesis Mediated through ROS Generation Triggers Apoptosis in HepG2 Cells
resolves10.1038/sj.onc.1209980
HRPAP20: a novel calmodulin-binding protein that increases breast cancer cell invasion
resolves10.1523/JNEUROSCI.0984-06.2006
Parkinson's Disease Brain Mitochondrial Complex I Has Oxidatively Damaged Subunits and Is Functionally Impaired and Misassembled
resolves10.1002/iub.335
Assembly factors of human mitochondrial complex I and their defects in disease
resolves10.1016/j.bbabio.2011.08.010
Understanding mitochondrial complex I assembly in health and disease
resolves10.1038/ncb836
Lon protease preferentially degrades oxidized mitochondrial aconitase by an ATP-stimulated mechanism
resolves10.1038/onc.2013.228
Mitochondrial matrix proteases as novel therapeutic targets in malignancy
resolves10.1002/anie.201100935
A Mitochondrial Surface‐Specific Fluorescent Probe Activated by Bioconversion
The 1 reference without a DOI — listed, not checked
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