Quantitative profiling of differentiation-induced microsomal proteins using isotope-coded affinity tags and mass spectrometry
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Summary
The method and the new software tools to support it are well suited to the large-scale, quantitative analysis of membrane proteins and other classes of proteins that have been refractory to standard proteomics technology.
- Type
- article
- Published
- 2001-10-01
- Cited by
- 830
- References
- 41
- Access
- Open access
- OpenAlex
- https://openalex.org/W1797925867
- Semantic Scholar
- https://api.semanticscholar.org/CorpusID:205271318
Keywords
Microsome, Chemistry, Mass spectrometry, Proteomics, Tandem mass spectrometry
References
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- The cell surface membrane: biochemical aspects and biophysical probes.
- Temporal changes in intracellular distribution of protein kinase C during differentiation of human leukemia HL60 cells induced by phorbol ester
- Extraction of membrane proteins by differential solubilization for separation using two‐dimensional gel electrophoresis
- Activation of membrane-bound phospholipase D by protein kinase C in HL60 cells: synergistic action of a small GTP-binding protein RhoA.
- Proteomic analysis of the human colon carcinoma cell line (LIM 1215): Development of a membrane protein database
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- The molecular make-up of a tumour: proteomics in cancer research.
- Microseparation of membrane proteins.
- A review of current applications of mass spectrometry for neuroproteomics in epilepsy.
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- Androgen-sensitive microsomal signaling networks coupled to the proliferation and differentiation of human prostate cancer cells.
- Mass Spectrometry of Membrane Proteins: A Focus on Aquaporins
- The introduction of toxicogenomics; potential new markers of hepatotoxicity
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- Use of Proteomics Analysis for Molecular Precision Approaches in Cancer Therapy
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- Identification and relative quantification of native and proteolytically generated protein C-termini from complex proteomes: C-terminome analysis.
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