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1. Full Text ECM Remodeling in Breast Cancer with Different Grade: Contribution of 2D‐DIGE Proteomics
by Moriggi, Manuela and Giussani, Marta and Torretta, Enrica and Capitanio, Daniele and Sandri, Marco and Leone, Roberta and Palma, Sara and Vasso, Michele and Vozzi, Giovanni and Tagliabue, Elda and Gelfi, Cecilia
Proteomics (Weinheim), ISSN 1615-9853, 12/2018, Volume 18, Issue 24, pp. e1800278 - n/a
breast cancer | mass spectrometry | 2D‐DIGE | ECM | TN tumors | 2D-DIGE | Biochemistry & Molecular Biology | Life Sciences & Biomedicine | Biochemical Research Methods | Science & Technology | Index Medicus
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2. Full Text Effects of intrauterine devices on proteins in the uterine lavage fluid of mares
by Rivera del Alamo, M.M and Katila, T and Palviainen, M and Reilas, T
Theriogenology, ISSN 0093-691X, 04/2021, Volume 165, pp. 1 - 9
Pregnancy | Mare | 2D-DIGE | Endometrial proteins | Intrauterine device
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3. Full Text Identification of S-nitrosated mitochondrial proteins by S-nitrosothiol difference in gel electrophoresis (SNO-DIGE): Implications for the regulation of mitochondrial function by reversible S-nitrosation
by Chouchani, Edward T and Hurd, Thomas R and Nadtochiy, Sergiy M and Brookes, Paul S and Fearnley, Ian M and Lilley, Kathryn S and Smith, Robin A. J and Murphy, Michael P
Biochemical journal, ISSN 0264-6021, 08/2010, Volume 430, Issue 1, pp. 49 - 59
S-nitrosation | Mitochondria | Redox signalling | Difference in gel electrophoresis (DIGE) | Nitric oxide (NO) | S-nitrosylation | Life Sciences & Biomedicine | Biochemistry & Molecular Biology | Science & Technology | Oxidation-Reduction | Mice, Inbred C57BL | Rats | Electrophoresis, Gel, Two-Dimensional | Male | Myocardium - pathology | S-Nitrosothiols - metabolism | Myocardial Reperfusion Injury - metabolism | Mitochondrial Proteins - pharmacology | Myocardial Reperfusion Injury - pathology | Animals | Mitochondrial Proteins - metabolism | Myocardium - metabolism | Membrane Potential, Mitochondrial | Proteomics | Superoxides - metabolism | Mice | In Vitro Techniques | Mitochondria - physiology | Index Medicus | BVA, biological variance analysis | nitric oxide (NO) | AR, area at risk | RHM, rat heart mitochondria | SA, standardized abundance | DIGE, difference in gel electrophoresis | GSNO, S-nitrosoglutathione | SNO-DIGE, S-nitrosothiol difference in gel electrophoresis | DTT, dithiothreitol | R, ischaemia | redox signalling | RLM, rat liver mitochondria | 2D, two-dimensional | difference in gel electrophoresis (DIGE) | Cy3, indocarbocyanine | ROS, reactive oxygen species | reperfusion | PrSNO, protein S-nitrosothiol | MitoNAP, mito-N-acetylpenicillamine | Cy5, indodicarbocyanine | LAD, left anterior descending coronary artery | NEM, N-ethylmaleimide | LV, left ventricle | SNAP, S-nitroso-N-acetylpenicillamine | mitochondria | MitoSNO, mitochondria-targeted S-nitrosothiol | α-KGDH, α-ketoglutarate dehydrogenase | TPP, triphenylphosphonium | NIH, National Institutes for Health | ALDH2, aldehyde dehydrogenase | MALDI–TOF-TOF, matrix-assisted laser-desorption ionization–time-of-flight time-of-flight
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4. Full Text Long-term cadmium exposure influences the abundance of proteins that impact the cell wall structure in Medicago sativa stems
by Gutsch, A and Keunen, E and Guerriero, G and Renaut, J and Cuypers, A and Hausman, J.-F and Sergeant, K
Plant biology (Stuttgart, Germany), ISSN 1435-8603, 11/2018, Volume 20, Issue 6, pp. 1023 - 1035
cadmium | 2-D DIGE | cell wall proteins | soluble proteins | gene expression | Medicago sativa | Life Sciences & Biomedicine | Plant Sciences | Science & Technology | Plant Roots - metabolism | Cadmium - toxicity | Electrophoresis, Gel, Two-Dimensional | Medicago sativa - genetics | Cadmium - metabolism | Medicago sativa - metabolism | Medicago sativa - drug effects | Plant Proteins - genetics | Cell Wall - drug effects | Plant Leaves - metabolism | Plant Stems - metabolism | Proteomics | Plant Proteins - metabolism | Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization | Real-Time Polymerase Chain Reaction | Proteins | Physiological aspects | Cadmium | Carbohydrate metabolism | Gene expression | Analysis | Carbohydrates | Gel electrophoresis | Toxicity | Cell walls | Ecosystems | Health risks | Environmental changes | Alfalfa | Exposure | Metabolism | Stems | Heavy metals | Leaves | Molecular modelling | Dimensional changes | Electrophoresis | Growth stage | Index Medicus | Research Papers | Research Paper | 2‐D DIGE
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5. Full Text The development of the DIGE system: 2D fluorescence difference gel analysis technology
by Marouga, Rita and David, Stephen and Hawkins, Edward
Analytical and bioanalytical chemistry, ISSN 1618-2642, 6/2005, Volume 382, Issue 3, pp. 669 - 678
Chemistry | DeCyder differential analysis software | CyDye DIGE fluors | 2D DIGE | Fluorescent labeling | Proteomics | Biochemistry & Molecular Biology | Physical Sciences | Life Sciences & Biomedicine | Biochemical Research Methods | Chemistry, Analytical | Science & Technology | Sensitivity and Specificity | Electrophoresis, Gel, Two-Dimensional - methods | Fluorescent Dyes - analysis | Index Medicus
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6. Full Text Specific protein changes contribute to the differential muscle mass loss during ageing
by Capitanio, Daniele and Vasso, Michele and Palma, Sara and Fania, Chiara and Torretta, Enrica and Cammarata, Francesco P and Magnaghi, Valerio and Procacci, Patrizia and Gelfi, Cecilia
Proteomics (Weinheim), ISSN 1615-9853, 02/2016, Volume 16, Issue 4, pp. 645 - 656
Muscle ageing | Animal proteomics | 2D‐DIGE | Muscle proteome | Mass spectrometry | Intermediate metabolism | 2D-DIGE | Biochemistry & Molecular Biology | Life Sciences & Biomedicine | Biochemical Research Methods | Science & Technology | Muscular Diseases - metabolism | Two-Dimensional Difference Gel Electrophoresis | Male | Mitochondria - metabolism | Muscular Diseases - pathology | Mitochondria - pathology | Muscle, Skeletal - physiology | Autophagy | Myosin Heavy Chains - metabolism | Rats, Sprague-Dawley | Animals | Muscle Proteins - analysis | Muscle Proteins - metabolism | Proteomics | Aging | Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization | Muscle, Skeletal - pathology | Myosin Heavy Chains - analysis | Myoglobin | Analysis | Myosin | Physiological aspects | Muscles | Muscle proteins | Oxidative metabolism | Homeostasis | Chains | Immunoblotting | Satellite cells | Nuclei | Proteins | ATP synthase | Mitochondria | Rodents | Acetyltransferase | Acetylation | Gastrocnemius muscle | Two dimensional analysis | Localization | Rats | Metabolism | Electron microscopy | Molecular chains | Skeletal muscle | Cells (biology) | Electron transport | Phagocytosis | Index Medicus
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7. Full Text Current trends in quantitative proteomics
by Elliott, Monica H and Smith, Derek S and Parker, Carol E and Borchers, Christoph
Journal of mass spectrometry., ISSN 1076-5174, 12/2009, Volume 44, Issue 12, pp. 1637 - 1660
proteomics | SISCAPA | DIGE, 15N | quantitation | iTRAQ | 18O | MRM | Label‐free | SILAC | plasma | iMALDI | ICAT | Plasma | DIGE | Proteomics | Quantitation | Label-free | Spectroscopy | Biochemistry & Molecular Biology | Physical Sciences | Chemistry | Life Sciences & Biomedicine | Technology | Biochemical Research Methods | Chemistry, Analytical | Science & Technology | Fundamental and applied biological sciences. Psychology | Proteins | Biological and medical sciences | General aspects, investigation methods | Analytical, structural and metabolic biochemistry | Peptide Fragments - metabolism | Humans | Nitrogen Isotopes | Oxygen Isotopes | Peptide Fragments - analysis | Tandem Mass Spectrometry | Spectrometry, Mass, Electrospray Ionization | Proteomics - trends | Sensitivity and Specificity | Isotope Labeling | Software | Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization | Proteomics - methods | Mass Spectrometry - methods | Fluorescent Dyes | Peptide Hydrolases - metabolism | Pathways | Trends | Mass spectrometry | Biologists | Guidelines | Index Medicus
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