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PLoS ONE, ISSN 1932-6203, 03/2012, Volume 7, Issue 3, p. e33377
Store-operated Ca2+ channels are a major Ca2+ entry pathway in nonexcitable cells, which drive various essential cellular functions. Recently, STIM1 and Orai... 
PROTEIN INTERACTIONS | CALCIUM-CHANNELS | MULTIDISCIPLINARY SCIENCES | CA2+ SENSOR | STORE | PORE SUBUNIT | INTERACTION MOLECULE-1 STIM1 | ACTIVATES CRAC CHANNELS | FLUORESCENCE COMPLEMENTATION | PLASMA-MEMBRANE | LIVING CELLS | Calcium Channels - metabolism | Humans | Protein Multimerization | Bacterial Proteins - chemistry | Endoplasmic Reticulum - metabolism | Resting Phase, Cell Cycle | Neoplasm Proteins - metabolism | Recombinant Fusion Proteins - metabolism | HEK293 Cells | Protein Structure, Quaternary | Fluorescence Resonance Energy Transfer | Luminescent Proteins - chemistry | Cell Membrane - metabolism | Membrane Proteins - metabolism | Protein Interaction Domains and Motifs | Neoplasm Proteins - genetics | Calcium Channels - genetics | Photobleaching | Stromal Interaction Molecule 1 | Boron Compounds - pharmacology | Membrane Proteins - genetics | Bacterial Proteins - genetics | Neoplasm Proteins - chemistry | Recombinant Fusion Proteins - chemistry | ORAI1 Protein | Membrane Proteins - chemistry | Calcium Channels - chemistry | Recombinant Fusion Proteins - genetics | Bacterial Proteins - metabolism | Luminescent Proteins - genetics | Microscopy, Fluorescence | Luminescent Proteins - metabolism | Oligomers | Proteins | Fluorescence | Information management | Protein-protein interactions | Calcium channels | Laboratories | STIM1 protein | Histology | Identification | C-Terminus | Gene expression | Orai1 protein | Experiments | Calcium influx | Recruitment | Embryology | Depletion | Plasmids | Cells (biology) | Fluorescence resonance energy transfer | Sensors | Localization | Protein interaction | Energy transfer
Journal Article
PLoS ONE, ISSN 1932-6203, 04/2012, Volume 7, Issue 4, p. e33231
Journal Article
PLoS ONE, ISSN 1932-6203, 02/2014, Volume 9, Issue 2, p. e88893
Use of fusion protein tags to investigate lysosomal proteins can be complicated by the acidic, protease-rich environment of the lysosome. Potential artifacts... 
SYSTEM | FORMS | GENE | NPC2 | MULTIDISCIPLINARY SCIENCES | DEFICIENT | DEGRADATION | TRIPEPTIDYL PEPTIDASE-I | IDENTIFICATION | BINDING | EXPRESSION | Recombinant Fusion Proteins - adverse effects | Vesicular Transport Proteins - metabolism | Fluorescent Dyes - adverse effects | Immunoblotting | DNA Primers - genetics | Protein Transport - drug effects | Glycosylation - drug effects | Dipeptidyl-Peptidases and Tripeptidyl-Peptidases - metabolism | Lysosomes - metabolism | Protein Folding - drug effects | Aminopeptidases - chemistry | Cloning, Molecular | Luminescent Proteins - chemistry | Serine Proteases - chemistry | Aminopeptidases - metabolism | Serine Proteases - metabolism | Tissue Culture Techniques | Models, Molecular | Vesicular Transport Proteins - chemistry | Dipeptidyl-Peptidases and Tripeptidyl-Peptidases - chemistry | Lysosomes - ultrastructure | Microscopy, Confocal | Animals | Chromatography, Affinity | Protein Conformation | Mice | Luminescent Proteins - metabolism | Proteins | Proline | Fluorescence | Hostages | Glycine | Proteases | Niemann-Pick disease | Biotechnology | Phosphorylation | C protein | Proteinase | Trafficking | Insertion | Mannose | Insulin-like growth factors | Biochemistry | Medical schools | Quenching (cooling) | Defects | Clonal deletion | Protease | Protein folding | Deletion | Cleavage | Localization | Fusion protein | Tags | Biodegradation | Enzymes | Peptidase | Cloning | Glycosylation | Organelles | Medicine | Studies | Artifacts | Molecular modelling | Environmental degradation | Stem cells | Tagging | Molecular biology | Position (location) | Lysosomal protein
Journal Article
Journal Article
BMC Biology, ISSN 1741-7007, 12/2012, Volume 10, Issue 1, pp. 107 - 107
Journal Article
Journal Article
PLoS ONE, ISSN 1932-6203, 06/2014, Volume 9, Issue 6, p. e100637
Journal Article