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animals (30) 30
exocytosis (20) 20
cell biology (13) 13
secretion (12) 12
cells (11) 11
phosphorylation (10) 10
signal transduction (10) 10
cell membranes (9) 9
parafusin (9) 9
paramecium - ultrastructure (8) 8
phosphoglucomutase (8) 8
phosphoproteins - metabolism (8) 8
cell membrane - ultrastructure (7) 7
paramecium (7) 7
calcium (6) 6
calcium - metabolism (6) 6
freeze fracturing (6) 6
humans (6) 6
microscopy, electron (6) 6
paramecium - metabolism (6) 6
phosphoproteins - genetics (6) 6
protein (6) 6
protozoan proteins - genetics (6) 6
sensitive phosphoprotein (6) 6
amino acid sequence (5) 5
index medicus (5) 5
membrane fusion (5) 5
molecular sequence data (5) 5
paramecium tetraurelia - genetics (5) 5
paramecium tetraurelia - metabolism (5) 5
proteins (5) 5
protozoan proteins - metabolism (5) 5
research (5) 5
wild-type (5) 5
biochemistry & molecular biology (4) 4
calcimycin - pharmacology (4) 4
cilia - physiology (4) 4
membrane-fusion (4) 4
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paramecium - physiology (4) 4
phosphoglucomutase - genetics (4) 4
physiological regulation (4) 4
saccharomyces-cerevisiae (4) 4
sequence homology, amino acid (4) 4
temperature (4) 4
tetrahymena - metabolism (4) 4
antibodies (3) 3
base sequence (3) 3
calcium - pharmacology (3) 3
cells, cultured (3) 3
cellular signal transduction (3) 3
cilia (3) 3
cytoplasmic granules - ultrastructure (3) 3
dna (3) 3
enzymes (3) 3
fluorescent antibody technique (3) 3
glyceraldehyde-3-phosphate dehydrogenase (3) 3
multidisciplinary sciences (3) 3
mutation (3) 3
paramecium - drug effects (3) 3
paramecium - genetics (3) 3
paramecium-tetraurelia (3) 3
phosphoglucomutase - metabolism (3) 3
phosphoproteins (3) 3
phylogeny (3) 3
picrates - pharmacology (3) 3
primary cilium (3) 3
rats (3) 3
sequence alignment (3) 3
tetrahymena (3) 3
toxoplasma gondii (3) 3
trifluoperazine - pharmacology (3) 3
3-d deconvolution (2) 2
analysis (2) 2
biochemical research methods (2) 2
blotting, southern (2) 2
calcium-binding proteins - analysis (2) 2
calmodulin - analysis (2) 2
calmodulin - metabolism (2) 2
cell line (2) 2
cell membrane (2) 2
cell membrane - metabolism (2) 2
cell membrane - physiology (2) 2
cell physiology (2) 2
cellular biology (2) 2
cilia - metabolism (2) 2
cilia - ultrastructure (2) 2
ciliates (2) 2
cloning, molecular (2) 2
cytology (2) 2
cytoplasmic granules - metabolism (2) 2
disease (2) 2
dynein (2) 2
enzyme activation (2) 2
epithelial cells (2) 2
exocytosis - drug effects (2) 2
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Modern cell biology, ISSN 0745-3000, 1983
Journal
JOURNAL OF CELL SCIENCE, ISSN 0021-9533, 08/2019, Volume 132, Issue 15, p. jcs230441
Many signaling molecules are localized to both the primary cilium and nucleus. Localization of specific transmembrane receptors and their signaling scaffold... 
CELLS | LOCALIZATION | PROTEIN | Huntingtin | Transmembrane receptor | TRANSCRIPTION | Primary cilium | TRAFFICKING | OUTER SEGMENT | CELL BIOLOGY | Nuclear pore | PDGFR-ALPHA | DISEASE | Signaling scaffold molecule | INTRAFLAGELLAR TRANSPORT
Journal Article
Journal Article
European Journal of Cell Biology, ISSN 0171-9335, 05/2009, Volume 88, Issue 5, pp. 301 - 313
The Paramecium tetraurelia protein parafusin (PFUS) and the Toxoplasma gondii protein parafusin- related protein 1 (PRP1) both have two covalent modifications... 
Journal Article
European Journal of Cell Biology, ISSN 0171-9335, 05/2009, Volume 88, Issue 5, p. 301
The Paramecium tetraurelia protein parafusin (PFUS) and the Toxoplasma gondii protein parafusin-related protein 1 (PRP1) both have two covalent modifications... 
Post-translational modification | Fluorescence | Muscle proteins
Journal Article
European Journal of Cell Biology, ISSN 0171-9335, 2009, Volume 88, Issue 5, pp. 301 - 313
The Paramecium tetraurelia protein parafusin (PFUS) and the Toxoplasma gondii protein parafusin-related protein 1 (PRP1) both have two covalent modifications... 
Ortholog assay | Membrane fusion | Site-specific mutagenesis | PFUS/PRP1 | Parafusin | Ca 2+-regulated exocytosis
Journal Article
European Journal of Cell Biology, ISSN 0171-9335, 05/2009, Volume 88, Issue 5, pp. 301 - 313
The Paramecium tetraurelia protein parafusin (PFUS) and the Toxoplasma gondii protein parafusin-related protein 1 (PRP1) both have two covalent modifications... 
Membrane fusion | Ortholog assay | regulated exocytosis | PFUS/PRP1 | Site-specific mutagenesis | Parafusin | WILD-TYPE | PROTEIN | PHOSPHORYLATION | PHOSPHOGLYCOPROTEIN | PARAMECIUM-TETRAURELIA | Ca2+-regulated exocytosis | SENSITIVE PHOSPHOPROTEIN | CELL BIOLOGY | SIGNAL-TRANSDUCTION | MEMBRANE-FUSION | PP63/PARAFUSIN | SECRETION
Journal Article
Trends in Genetics, ISSN 0168-9525, 2001, Volume 17, Issue 6, pp. 306 - 308
A consortium of laboratories undertook a pilot sequencing project to gain insight into the genome of Paramecium. Plasmid-end sequencing of DNA fragments from... 
genomics | paramecium | ciliate | sequencing | FUNCTIONAL COMPLEMENTATION | MOLECULAR-GENETICS | CLONING | GENES | GENETICS & HEREDITY | TETRAHYMENA | REARRANGEMENTS | Paramecium - classification | Pilot Projects | Animals | Genome, Protozoan | Paramecium - genetics | Humans | Phylogeny | Protozoan Proteins - genetics
Journal Article
European Journal of Protistology, ISSN 0932-4739, 2003, Volume 39, Issue 4, pp. 394 - 398
Trichocyst discharge in Paramecium is associated with a calcium-dependent dephosphoglucosylation of the protein parafusin (PFUS), which is believed to be a... 
Alveolata | Toxoplasma gondii | Cell invasion | Exocytosis | Parafusin | Paramecium | MICRONEME DISCHARGE | WILD-TYPE | alveolata | PROTEIN | ORGANELLES | MICROBIOLOGY | parafusin | FREEZE-FRACTURE | HOST-CELL | CALCIUM | exocytosis | cell invasion | GONDII | SECRETION
Journal Article
Biochemistry and Cell Biology, ISSN 0829-8211, 12/2000, Volume 78, Issue 6, pp. 683 - 690
Molecular probes designed for the parafusin (PFUS), the Paramecium exocytic-sensitive phospho glyco protein, gave distinct hybridization patterns in... 
Journal Article
Cellular Microbiology, ISSN 1462-5814, 09/2003, Volume 5, Issue 9, pp. 613 - 624
Journal Article
Journal Article
Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 12/1992, Volume 89, Issue 23, pp. 11297 - 11301
Parafusin, a cytosolic phosphoglycoprotein of M 63,000, is dephosphorylated and rephosphorylated rapidly in a Ca -dependent manner upon stimulation of... 
Enzymes | Molecules | Phosphorylation | Phosphatases | Homogenization | Glycoproteins | Cell membranes | Exocytosis | Product labeling | Room temperature | Membrane fusion | Secretion | Ciliates | RAT-LIVER | PROTEIN | PHOSPHORYLATION | MULTIDISCIPLINARY SCIENCES | DEPHOSPHORYLATION | SECRETION | MEMBRANE FUSION | CILIATES | SENSITIVE PHOSPHOPROTEIN | Physiological aspects | Cellular signal transduction | Research
Journal Article
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