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animals (35) 35
biochemistry & molecular biology (28) 28
calcium-dependent oligomerization (23) 23
rats (19) 19
humans (18) 18
index medicus (17) 17
calcium - metabolism (16) 16
molecular sequence data (16) 16
cell biology (15) 15
amino acid sequence (14) 14
exocytosis (13) 13
nerve tissue proteins - metabolism (13) 13
pc12 cells (13) 13
calcium (12) 12
mice (12) 12
neurotransmitter release (12) 12
proteins (12) 12
synaptotagmins (12) 12
protein structure, tertiary (10) 10
synaptic vesicle (9) 9
cell membrane - metabolism (8) 8
membrane glycoproteins - metabolism (8) 8
tandem c2 domains (8) 8
transmitter release (8) 8
calcium-binding proteins (7) 7
nerve tissue proteins - genetics (7) 7
phospholipid-binding (7) 7
phosphorylation (7) 7
c2 domain (6) 6
calmodulin (6) 6
dense-core vesicles (6) 6
membrane glycoproteins - genetics (6) 6
nerve tissue proteins - chemistry (6) 6
protein-kinase-c (6) 6
recombinant proteins - metabolism (6) 6
transfection (6) 6
antibody injection (5) 5
beta-cells (5) 5
biology (5) 5
ca2+ sensor (5) 5
ca2+-dependent exocytosis (5) 5
calcium-binding proteins - metabolism (5) 5
calcium-dependent inactivation (5) 5
cloning, molecular (5) 5
family (5) 5
life sciences (5) 5
membrane glycoproteins - chemistry (5) 5
molecular-cloning (5) 5
neurons - metabolism (5) 5
neurosciences (5) 5
phospholipids - metabolism (5) 5
squid giant synapse (5) 5
synaptotagmin (5) 5
synaptotagmin i (5) 5
synaptotagmins - metabolism (5) 5
base sequence (4) 4
binding (4) 4
binding sites (4) 4
biochemistry, general (4) 4
c2 domains (4) 4
c2b domain (4) 4
calcium-dependent protein kinase (4) 4
crystal-structure (4) 4
dimerization (4) 4
fluorescence (4) 4
gene expression (4) 4
models, biological (4) 4
oligomerization (4) 4
pancreatic beta-cells (4) 4
phylogeny (4) 4
physiological aspects (4) 4
plant sciences (4) 4
protein (4) 4
protein conformation (4) 4
protein isoforms (4) 4
review (4) 4
sequence homology, amino acid (4) 4
signal transduction (4) 4
slp homology domain (4) 4
analysis (3) 3
arabidopsis - genetics (3) 3
article (3) 3
bacteria (3) 3
biophysics (3) 3
ca2 (3) 3
ca2+ binding (3) 3
calcium-dependent exocytosis (3) 3
carrier proteins - metabolism (3) 3
cattle (3) 3
cell line (3) 3
cells, cultured (3) 3
cos cells (3) 3
drosophila (3) 3
endocytosis (3) 3
exocytosis - physiology (3) 3
expression (3) 3
high-polyphosphate binding (3) 3
immunoblotting (3) 3
insulin exocytosis (3) 3
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1. Full Text Sucrose Synthase Oligomerization and F-actin Association are Regulated by Sucrose Concentration and Phosphorylation
by Duncan, Kateri A and Huber, Steven C
Plant and Cell Physiology, ISSN 0032-0781, 11/2007, Volume 48, Issue 11, pp. 1612 - 1623
Sucrose synthase (SUS) is a key enzyme in plant metabolism, as it serves to cleave the photosynthetic end-product sucrose into UDP-glucose and fructose. SUS is... 
Calcium dependent protein kinase | F-actin binding | Sucrose synthase | Protein phosphorylation | Sugar sensing | Protein oligomerization | calcium dependent protein kinase | MAIZE ENDOSPERM | ISOFORMS | TISSUE | protein phosphorylation | sugar sensing | COILED-COILS | PLANT SCIENCES | CELL BIOLOGY | HIGHER-PLANTS | BINDING PROTEINS | protein oligomerization | SYNTHETASE | METABOLIZING ENZYMES | EXPRESSION | MEMBRANE ASSOCIATION | sucrose synthase | Recombinant Proteins - metabolism | Zea mays - genetics | Phosphorylation | Zea mays - drug effects | Actins - metabolism | Recombinant Proteins - chemistry | Seedlings - genetics | Sucrose - pharmacology | Immunoblotting | Seedlings - drug effects | Glucosyltransferases - metabolism | Plant Proteins - genetics | Focal Adhesion Kinase 2 - metabolism | Plant Proteins - chemistry | Light | Protein Binding - drug effects | Glucosyltransferases - chemistry | Plant Proteins - metabolism | Zea mays - metabolism | Chromatography, Gel | Dimerization | Glucosyltransferases - genetics | Seedlings - metabolism
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2. Full Text Calmodulin overexpression does not alter Ca(v)1.2 function or oligomerization state
by Findeisen, F and Tolia, A and Arant, R and Kim, EY and Isacoff, EY and Minor, DL
CHANNELS, ISSN 1933-6950, 07/2011, Volume 5, Issue 4, pp. 320 - 324
Interactions between calmodulin (CaM) and voltage-gated calcium channels (Ca(v)s) are crucial for Ca-v activity-dependent feedback modulation. We recently... 
stoichiometry | calcium-dependent inactivation (CDI) | DOMAIN | PROTEIN | RECOGNITION | CRYSTAL-STRUCTURE | CA2+/CALMODULIN | BIOCHEMISTRY & MOLECULAR BIOLOGY | Ca(v)1.2 | CA2+ CHANNELS | calmodulin | GATED CALCIUM-CHANNEL | INACTIVATION | voltage-gated calcium channel | REVEALS
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3. Full Text Calmodulin overexpression does not alter Cav1.2 function or oligomerization state
by Findeisen, Felix and Tolia, Alexandra and Arant, Ryan and Young Kim, Eun and Isacoff, Ehud and Minor, Jr, Daniel L
Channels, ISSN 1933-6950, 07/2011, Volume 5, Issue 4, pp. 320 - 324
Interactions between calmodulin (CaM) and voltage-gated calcium channels (Ca v s) are crucial for Ca v activity-dependent feedback modulation. We recently... 
Binding | Proteins | Landes | Calcium | Bioscience | Biology | Cell | Cycle | Cancer | Organogenesis | Stoichiometry | Calcium-dependent inactivation (CDI) | Voltage-gated calcium channel | Calmodulin | Protein Structure, Tertiary | Calmodulin - genetics | Gene Expression | Calmodulin - biosynthesis | Calcium - metabolism | Humans | Protein Multimerization | Xenopus laevis | Cell Membrane - genetics | Animals | Calcium Channels, L-Type - genetics | Cell Membrane - metabolism | Calcium Channels, L-Type - metabolism | Addendum | voltage-gated calcium channel | stoichiometry | calcium-dependent inactivation (CDI) | Cav1.2 | calmodulin
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4. Full Text How does synaptotagmin trigger neurotransmitter release?
by Chapman, Edwin R
Annual Review of Biochemistry, ISSN 0066-4154, 2008, Volume 77, Issue 1, pp. 615 - 641
Neurotransmitter release at synapses involves a highly specialized form of membrane fusion that is triggered by Ca2+ ions and is optimized for speed. These... 
Membrane fusion | Synapse | Fusion pore | SNARE | MEMBRANE-PENETRATION ACTIVITY | BIOCHEMISTRY & MOLECULAR BIOLOGY | fusion pore | ADRENAL CHROMAFFIN CELLS | DROSOPHILA NEUROMUSCULAR-JUNCTIONS | synapse | membrane fusion | PRESYNAPTIC ACTIVE ZONES | CALCIUM-DEPENDENT OLIGOMERIZATION | SYNAPTIC VESICLE DOCKING | PROTEIN-PROTEIN INTERACTIONS | TANDEM C2 DOMAINS | DENSE-CORE VESICLES | KISS-AND-RUN | Synaptotagmins - physiology | Calcium - metabolism | Humans | Neurotransmitter Agents - metabolism | Ions | Synaptotagmin I - chemistry | Exocytosis | Synaptotagmins - metabolism | Phenotype | Animals | Synapses - metabolism | Models, Biological | Cell Membrane - metabolism | Neurons - metabolism | Kinetics | SNARE Proteins - metabolism | Evaluation | Neurotransmitters | Neuroendocrinology | Analysis | Synaptic vesicles | Research | Calcium ions
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5. Full Text Synaptotagmin: A Ca2+ sensor that triggers exocytosis?
by Chapman, Edwin R
Nature Reviews Molecular Cell Biology, ISSN 1471-0072, 2002, Volume 3, Issue 7, pp. 498 - 508
It has been fifty years since the discovery that Ca2+ triggers the rapid exocytosis of neurotransmitters from neurons. One of the proteins that has a crucial... 
TRANSMITTER RELEASE | READILY RELEASABLE POOL | DRIVES MEMBRANE-FUSION | PROTEIN-KINASE-C | C2B DOMAIN | SNARE COMPLEX | NEUROTRANSMITTER RELEASE | CALCIUM-DEPENDENT OLIGOMERIZATION | DENSE-CORE VESICLES | SQUID GIANT SYNAPSE | CELL BIOLOGY
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6. Full Text Visualization of Synaptotagmin I Oligomers Assembled onto Lipid Monolayers
by Yi Wu and Yuhong He and Jihong Bai and Shang-Rong Ji and Ward C. Tucker and Edwin R. Chapman and Sen-Fang Sui
Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 2/2003, Volume 100, Issue 4, pp. 2082 - 2087
Neuronal exocytosis is mediated by Ca -triggered rearrangements between proteins and lipids that result in the opening and dilation of fusion pores.... 
Oligomers | Biological Sciences | Contaminants | Neurons | Quantum statistics | Synaptotagmins | Fluorescence | Lipids | Cell membranes | Liposomes | Exocytosis | Membrane | C2 domain | Oligomerization | Calcium | C-REACTIVE PROTEIN | calcium | membrane | C2B DOMAIN | 2-DIMENSIONAL CRYSTALLIZATION | NEUROTRANSMITTER RELEASE | CA DOMAIN | MULTIDISCIPLINARY SCIENCES | SYNAPTIC VESICLE | oligomerization | SNARE COMPLEX | CALCIUM-DEPENDENT OLIGOMERIZATION | CA2+ BINDING | BINDING-SITES | Nerve Tissue Proteins - metabolism | Recombinant Proteins - metabolism | Animals | Calcium-Binding Proteins | Membrane Glycoproteins - metabolism | Calcium - metabolism | Rats | Lipid Metabolism | Synaptotagmin I | Biopolymers - metabolism | Physiological aspects | Endocytosis | Calcium-binding proteins | C2 domain‖oligomerization‖calcium‖membrane
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7. Full Text Mechanistic studies on the effect of membrane lipid acyl chain composition on daptomycin pore formation
by Beriashvili, David and Taylor, Robert and Taylor, Scott D and Kralt, Braden and Abu Mazen, Nooran and Palmer, Michael
Chemistry and Physics of Lipids, ISSN 0009-3084, 11/2018, Volume 216, pp. 73 - 79
Daptomycin is a lipopeptide antibiotic that binds and permeabilizes the cell membranes of Gram-positive bacteria. Membrane permeabilization requires both... 
Phosphatidylglycerol | Membrane permeabilization | Membrane fluidity | Cardiolipin | Calcium-dependent lipopeptide antibiotics | CELL-MEMBRANE | BIOCHEMISTRY & MOLECULAR BIOLOGY | RESISTANT STAPHYLOCOCCUS-AUREUS | MODEL MEMBRANES | DEPOLARIZATION | INHIBITION | BIOPHYSICS | BACTERICIDAL ACTIVITY | FLUORESCENCE | DEPENDENT ANTIBIOTIC DAPTOMYCIN | OLIGOMERIZATION | BINDING | Gram-Positive Bacteria - metabolism | Liposomes - chemistry | Daptomycin - chemistry | Daptomycin - biosynthesis | Anti-Bacterial Agents - chemistry | Gram-Positive Bacteria - chemistry | Phospholipids - chemistry | Liposomes - metabolism | Anti-Bacterial Agents - biosynthesis | Phospholipids - metabolism | Lipids | Monounsaturated fatty acids | Analysis
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8. Full Text Synaptotagmins I and II Mediate Entry of Botulinum Neurotoxin B into Cells
by Min Dong and David A. Richards and Michael C. Goodnough and William H. Tepp and Eric A. Johnson and Edwin R. Chapman
The Journal of Cell Biology, ISSN 0021-9525, 9/2003, Volume 162, Issue 7, pp. 1293 - 1303
Botulinum neurotoxins (BoNTs) cause botulism by entering neurons and cleaving proteins that mediate neurotransmitter release; disruption of exocytosis results... 
Receptors | Neurotoxins | Neurons | Cell lines | Antibodies | Synaptotagmins | Toxins | Gangliosides | PC12 cells | Cells | Synaptobrevin | Neurotoxin receptor | Clostridial neurotoxin | Synaptotagmin | NEUROTRANSMITTER RELEASE | gangliosides | SYNAPTIC VESICLE | CELL BIOLOGY | TETANUS TOXIN BINDING | synaptobrevin | INTERNALIZATION | CLOSTRIDIUM-BOTULINUM | PURIFICATION | clostridial neurotoxin | CALCIUM-DEPENDENT OLIGOMERIZATION | neurotoxin receptor | synaptotagmin | PC12 CELLS | BRAIN | Protein Structure, Tertiary | Amino Acid Sequence | Synaptotagmin II | Calcium-Binding Proteins | Membrane Glycoproteins - metabolism | Membrane Glycoproteins - chemistry | Molecular Sequence Data | Rats | Botulism - metabolism | Nerve Tissue Proteins - genetics | PC12 Cells | Membrane Glycoproteins - genetics | Motor Neurons - metabolism | Nerve Tissue Proteins - metabolism | Nerve Tissue Proteins - chemistry | Animals | Botulinum Toxins, Type A | Gangliosides - metabolism | Cytoplasmic Vesicles - metabolism | Female | Mice | Botulinum Toxins - pharmacokinetics | Neurotransmitters | Botulism | Cytology | Physiological aspects | Causes of | Genetic aspects | Research | Binding proteins | Neurotoxic agents | synaptotagmin; synaptobrevin; clostridial neurotoxin; neurotoxin receptor; gangliosides
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9. Full Text There's more to life than neurotransmission: the regulation of exocytosis by synaptotagmin VII
by Andrews, Norma W and Chakrabarti, Sabyasachi
Trends in Cell Biology, ISSN 0962-8924, 2005, Volume 15, Issue 11, pp. 626 - 631
Among the 16 known vertebrate synaptotagmins, only Syt I, IV and VII are also present in and , suggesting that these isoforms play especially important roles .... 
PROTEIN-KINASE-C | CALCIUM-DEPENDENT OLIGOMERIZATION | CA2+ SENSOR | CA2+-DEPENDENT EXOCYTOSIS | PC12 CELLS | PLASMA-MEMBRANE REPAIR | SYNAPTIC VESICLE | SECRETORY GRANULES | PHOSPHOLIPID-BINDING | LYSOSOMAL EXOCYTOSIS | CELL BIOLOGY | Receptors, Calcium-Sensing - physiology | Animals | Lysosomes - metabolism | Synaptic Transmission - physiology | Synaptotagmins - physiology | Models, Biological | Humans | Secretory Vesicles - metabolism | Cell Membrane - metabolism | Membrane Fusion - physiology | Exocytosis - physiology | Synaptotagmin I - physiology
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10. Full Text Dual Roles of the C2B Domain of Synaptotagmin I in Synchronizing Ca2+-Dependent Neurotransmitter Release
by Nishiki, Tei-ichi and Augustine, George J
Journal of Neuroscience, ISSN 0270-6474, 09/2004, Volume 24, Issue 39, pp. 8542 - 8550
Although the vesicular protein synaptotagmin I contains two Ca2+-binding domains (C(2)A and C2B), Ca2+ binding to the C2B domain is more important for... 
Synaptic vesicle | Hippocampal neurons | Calcium | Exocytosis | Synaptic transmission | SNARE | PROTEIN-KINASE-C | calcium | CA DOMAIN | T-SNARE | HIPPOCAMPAL-NEURONS | PLASMA-MEMBRANE | NEUROSCIENCES | hippocampal neurons | synaptic vesicle | MEMBRANE-FUSION | TRANSMITTER RELEASE | CALCIUM-DEPENDENT OLIGOMERIZATION | CA2+ BINDING | SYNAPTIC VESICLE DOCKING | synaptic transmission | exocytosis | Synaptic Vesicles - metabolism | Calcium - metabolism | Aspartic Acid | Excitatory Postsynaptic Potentials - physiology | Membrane Glycoproteins - physiology | Calcium - physiology | Transfection | Time Factors | Neurons - metabolism | Protein Structure, Tertiary | Nerve Tissue Proteins - physiology | Mutagenesis, Site-Directed | Cells, Cultured | Neurotransmitter Agents - metabolism | Binding Sites - genetics | Hippocampus - cytology | Nerve Tissue Proteins - genetics | Membrane Glycoproteins - genetics | Mice, Knockout | Hippocampus - metabolism | Animals | Calcium-Binding Proteins - physiology | Synaptotagmins | Mice | Synaptotagmin I | Calcium-Binding Proteins - genetics | Cellular | Molecular
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11. Full Text Developmental expression and subcellular distribution of synaptotagmin 11 in rat hippocampus
by Yeo, H and Kim, H.-w and Mo, J and Lee, D and Han, S and Hong, S and Koh, M.J and Sun, W and Choi, S and Rhyu, I.J and Kim, H and Lee, H.W
Neuroscience, ISSN 0306-4522, 2012, Volume 225, pp. 35 - 43
Graphical abstract Highlights ► Syt11 is expressed in the central nervous system. ► Syt11 is a pre and postsynaptic molecule in rat hippocampal neurons. ►... 
Neurology | synaptotagmin 11 | presynapse | hippocampus | postsynapse | synaptic vesicle | Postsynapse | Presynapse | Synaptic vesicle | Synaptotagmin 11 | Hippocampus | EXOCYTOSIS | NEUROTRANSMITTER RELEASE | O-GLYCOSYLATION | NEUROSCIENCES | FAMILY | C2 DOMAINS | MEMBRANE-FUSION | CALCIUM-DEPENDENT OLIGOMERIZATION | PC12 CELLS | POLYPHOSPHATE BINDING-PROTEIN | SQUID GIANT SYNAPSE | Disks Large Homolog 4 Protein | Age Factors | Embryo, Mammalian | Coculture Techniques | Humans | Glucose Transporter Type 1 - metabolism | Green Fluorescent Proteins - genetics | Intracellular Signaling Peptides and Proteins - metabolism | Brain - growth & development | RNA, Messenger - metabolism | Brain - metabolism | Neurons - ultrastructure | Synapses - metabolism | Transfection | Brain - ultrastructure | Cell Membrane - metabolism | Membrane Proteins - metabolism | Neurons - metabolism | Gene Expression Regulation, Developmental - physiology | Animals, Newborn | Microscopy, Electron, Transmission | Cells, Cultured | Rats | Synapses - ultrastructure | Hippocampus - cytology | Nerve Tissue Proteins - metabolism | Synaptotagmins - metabolism | Animals | Carrier Proteins - metabolism | Vesicular Inhibitory Amino Acid Transport Proteins - metabolism | Intracellular Space - metabolism | Synaptotagmins - genetics | Brain | Neurosciences
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12. Full Text Role of synaptotagmin in Ca2+-triggered exocytosis
by Tucker, Ward C and Chapman, Edwin R
Biochemical Journal, ISSN 0264-6021, 08/2002, Volume 366, Issue 1, pp. 1 - 13
The Ca2+-binding synaptic-vesicle protein synaptotagrnin I has attracted considerable interest as a potential Ca2+ sensor that regulates exocytosis from... 
Membrane fusion | C2-domain | Synapse | Calcium | Exocytosis | PROTEIN-KINASE-C | CYTOSOLIC PHOSPHOLIPASE A | calcium | NEUROTRANSMITTER RELEASE | BIOCHEMISTRY & MOLECULAR BIOLOGY | synapse | membrane fusion | TRANSMITTER RELEASE | READILY RELEASABLE POOL | PRESYNAPTIC ACTIVE ZONES | CALCIUM-DEPENDENT OLIGOMERIZATION | PANCREATIC BETA-CELLS | exocytosis | DENSE-CORE VESICLES | SQUID GIANT SYNAPSE | Protein Structure, Tertiary | Nerve Tissue Proteins - physiology | Calcium-Binding Proteins | Membrane Fusion | Calcium - metabolism | Humans | Membrane Glycoproteins - chemistry | Nervous System - metabolism | Endocytosis | Membrane Glycoproteins - physiology | Nerve Tissue Proteins - chemistry | Animals | Models, Biological | Protein Isoforms | Synaptotagmins | Cell Membrane - metabolism | Membrane Proteins - metabolism | Kinetics | Synaptotagmin I | SNARE Proteins | Vesicular Transport Proteins
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13. Full Text Synaptotagmin VII Is Targeted to Dense-core Vesicles and Regulates Their Ca2+-dependent Exocytosis in PC12 Cells
by Mitsunori Fukuda and Eiko Kanno and Megumi Satoh and Chika Saegusa and Akitsugu Yamamoto
Journal of Biological Chemistry, ISSN 0021-9258, 12/2004, Volume 279, Issue 50, pp. 52677 - 52684
It has recently been proposed that synaptotagmin (Syt) VII functions as a plasma membrane Ca 2+ sensor for dense-core vesicle exocytosis in PC12 cells based on... 
RNA INTERFERENCE | ANTIBODY INJECTION | CONSERVED WHXL MOTIF | NEUROTRANSMITTER RELEASE | BIOCHEMISTRY & MOLECULAR BIOLOGY | BETA-CELLS | CALCIUM-DEPENDENT OLIGOMERIZATION | INSULIN EXOCYTOSIS | MOLECULAR-CLONING | DISTINCT CA2 | TANDEM C2 DOMAINS | Calcium-Binding Proteins - metabolism | Green Fluorescent Proteins - metabolism | Membrane Glycoproteins - metabolism | Calcium - metabolism | Secretory Vesicles - metabolism | Rats | Green Fluorescent Proteins - genetics | Exocytosis | Nerve Tissue Proteins - genetics | PC12 Cells | Recombinant Fusion Proteins - metabolism | Microscopy, Immunoelectron | Membrane Glycoproteins - genetics | Nerve Tissue Proteins - metabolism | Animals | Transfection | Recombinant Fusion Proteins - genetics | Synaptotagmins | Cell Membrane - metabolism | Mice | Calcium-Binding Proteins - genetics
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14. Full Text RNA interference-mediated silencing of synaptotagmin IX, but not synaptotagmin I, inhibits dense-core vesicle exocytosis but not in PC12 cells
by Fukuda, M
BIOCHEMICAL JOURNAL, ISSN 0264-6021, 06/2004, Volume 380, pp. 875 - 879
Although PC12 cells express three synaptotagmin isoforms (Syts I, IV and IX), all of which have been proposed to regulate dense-core vesicle exocytosis, it... 
ANTIBODY INJECTION | Ca2+ sensor | BIOCHEMISTRY & MOLECULAR BIOLOGY | BETA-CELLS | PC12 cell | RELEASE | FAMILY | endocrine cell exocytosis | CALCIUM-DEPENDENT OLIGOMERIZATION | INSULIN EXOCYTOSIS | MOLECULAR-CLONING | synaptotagmin | TANDEM C2 DOMAINS | BINDING | doublestranded RNA-mediated interference (RNAi)
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15. Full Text Rice small C2-domain proteins are phosphorylated by calcium-dependent protein kinase
by Kang, Chang Ho and Moon, Byeong Cheol and Park, Hyeong Cheol and Koo, Sung Cheol and Chi, Yong Hun and Cheong, Yong Hwa and Yoon, Byung-Dae and Lee, Sang Yeol and Kim, Cha Young
Molecules and Cells, ISSN 1016-8478, 5/2013, Volume 35, Issue 5, pp. 381 - 387
We previously reported that OsERG1 and OsERG3 encode rice small C2-domain proteins with different biochemical properties in Ca2+- and phospholipid-binding... 
Life Sciences | Biochemistry, general | Biotechnology | oligomerization | small C2-domain protein | calcium-dependent protein kinase | phosphorylation | Biomedicine general | Cell Biology | Ca 2+ /phospholipid-binding | phospholipid-binding | PLANT | SYNAPTOTAGMIN | BIOCHEMISTRY & MOLECULAR BIOLOGY | C2 DOMAIN | MULTIPLE | CELL BIOLOGY | MEMBRANE-BINDING | GENE FAMILY | DIVERSITY | Ca2+/phospholipid-binding | ARABIDOPSIS | STRESS | EXPRESSION | Protein Kinases - metabolism | Amino Acid Sequence | Phosphorylation | Calcium - metabolism | Oryza - metabolism | Molecular Sequence Data | Serine - genetics | Oryza - enzymology | Alanine - genetics | Plant Proteins - chemistry | Cytosol - metabolism | Cell Membrane - metabolism | Plant Proteins - metabolism | Mutation | Phospholipids - metabolism | Binding Sites | Proteins | Oligomers | Crosslinked polymers | Rural development | Analysis | Lipids | Protein kinases | Protein binding | Ca2 | 생물학
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16. Full Text Rabphilin and Noc2 Are Recruited to Dense-core Vesicles through Specific Interaction with Rab27A in PC12 Cells
by Mitsunori Fukuda and Eiko Kanno and Akitsugu Yamamoto
Journal of Biological Chemistry, ISSN 0021-9258, 03/2004, Volume 279, Issue 13, pp. 13065 - 13075
Rabphilin and Noc2 were originally described as Rab3A effector proteins involved in the regulation of secretory vesicle exocytosis, however, recently both... 
GRISCELLI-SYNDROME | REGULATED SECRETION | GTP-BINDING PROTEIN | MYOSIN-VA | BIOCHEMISTRY & MOLECULAR BIOLOGY | SYNAPTOTAGMIN FAMILY | CALCIUM-DEPENDENT OLIGOMERIZATION | CA2+-DEPENDENT EXOCYTOSIS | SLP HOMOLOGY DOMAIN | TANDEM C2 DOMAINS | MELANOSOME TRANSPORT | Humans | Caenorhabditis elegans Proteins - metabolism | Molecular Sequence Data | Immunoblotting | rab GTP-Binding Proteins - genetics | Phylogeny | Exocytosis | PC12 Cells | Neuropeptide Y - chemistry | Transfection | Gene Deletion | Cloning, Molecular | Carrier Proteins - chemistry | Neurons - metabolism | Potassium Chloride - chemistry | Vesicular Transport Proteins | Binding, Competitive | Protein Structure, Tertiary | rab GTP-Binding Proteins - metabolism | Amino Acid Sequence | Mutagenesis, Site-Directed | Drosophila | Rats | Plasmids - metabolism | Precipitin Tests | Nerve Tissue Proteins - metabolism | Sequence Homology, Amino Acid | rab3 GTP-Binding Proteins - genetics | Caenorhabditis elegans | Adaptor Proteins, Signal Transducing | Animals | Proteins - metabolism | Protein Isoforms | Protein Binding | rab27 GTP-Binding Proteins | rab GTP-Binding Proteins - chemistry | Mice | Models, Genetic | Mutation | Caenorhabditis elegans Proteins - genetics | DNA, Complementary - metabolism
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