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animals (41) 41
inositol 1,4,5-trisphosphate receptors (33) 33
biochemistry & molecular biology (31) 31
mice (27) 27
calcium (22) 22
calcium - metabolism (22) 22
humans (22) 22
inositol 1,4,5-trisphosphate - metabolism (18) 18
calcium channels - metabolism (17) 17
receptors, cytoplasmic and nuclear - metabolism (16) 16
index medicus (15) 15
ligands (14) 14
receptors, cytoplasmic and nuclear - chemistry (14) 14
calcium channels - chemistry (13) 13
amino acid sequence (12) 12
cell biology (12) 12
molecular sequence data (12) 12
cell line (10) 10
inositol 1,4,5-trisphosphate receptor (10) 10
protein binding (10) 10
signal transduction (10) 10
calcium channels - physiology (9) 9
calcium signaling - physiology (9) 9
inositol (9) 9
receptors, cytoplasmic and nuclear - physiology (9) 9
channel (8) 8
hela cells (8) 8
inositol 1,4,5-trisphosphate (8) 8
inositol 1,4,5-trisphosphate receptors - metabolism (8) 8
insp3 receptor (8) 8
protein structure, tertiary (8) 8
proteins (8) 8
trisphosphate receptor (8) 8
binding sites (7) 7
calcium channels - genetics (7) 7
cells (7) 7
cos cells (7) 7
kinetics (7) 7
neurosciences (7) 7
sequence homology, amino acid (7) 7
trisphosphate (7) 7
biophysics (6) 6
calcium-release (6) 6
endoplasmic-reticulum (6) 6
female (6) 6
fluorescence resonance energy transfer (6) 6
functional-characterization (6) 6
models, molecular (6) 6
mouse cerebellum (6) 6
neurology (6) 6
protein (6) 6
receptors, cytoplasmic and nuclear - genetics (6) 6
recombinant fusion proteins - metabolism (6) 6
research (6) 6
activation (5) 5
alzheimer's disease (5) 5
blotting, western (5) 5
calcium signaling (5) 5
calmodulin (5) 5
cytosol - metabolism (5) 5
green fluorescent proteins (5) 5
inositol 1,4,5-trisphosphate receptors - chemistry (5) 5
inositol 1,4,5-trisphosphate receptors - genetics (5) 5
multidisciplinary sciences (5) 5
protein conformation (5) 5
protein isoforms - genetics (5) 5
protein isoforms - metabolism (5) 5
reconstituted lipid vesicles (5) 5
time factors (5) 5
trisphosphate receptors (5) 5
analysis (4) 4
apoptosis (4) 4
ca2 (4) 4
ca2+ release channels (4) 4
calcium - pharmacology (4) 4
calcium imaging (4) 4
crystallography, x-ray (4) 4
dynamics (4) 4
endoplasmic reticulum - metabolism (4) 4
expression (4) 4
green fluorescent proteins - metabolism (4) 4
in-vivo (4) 4
inositol 1,4,5-trisphosphate - pharmacology (4) 4
inositol phosphates (4) 4
ligand-binding site (4) 4
luminescent proteins - metabolism (4) 4
male (4) 4
mutagenesis, site-directed (4) 4
mutation (4) 4
neurons (4) 4
phosphorylation (4) 4
protein structure, secondary (4) 4
release (4) 4
rna interference (4) 4
smooth-muscle (4) 4
transfection (4) 4
type-1 (4) 4
amino acid substitution (3) 3
binding sites - genetics (3) 3
brain (3) 3
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1. Full Text Spontaneous network activity visualized by ultrasensitive Ca2+ indicators, yellow Cameleon-Nano
by Horikawa, K and Yamada, Y and Matsuda, T and Kobayashi, K and Hashimoto, M and Matsu-ura, T and Miyawaki, A and Michikawa, T and Mikoshiba, K and Nagai, T
NATURE METHODS, ISSN 1548-7091, 09/2010, Volume 7, Issue 9, pp. 729 - U88
We report ultrasensitive Ca2+ indicators, yellow cameleon-Nano (YC-Nano), developed by engineering the Ca2+-sensing domain of a genetically encoded Ca2+... 
VITRO | DICTYOSTELIUM | CELLS | CALMODULIN | IN-VIVO | FLUORESCENT INDICATORS | BIOCHEMICAL RESEARCH METHODS | CALCIUM INDICATORS | NEURAL ACTIVITY | PROTEINS | PEPTIDE HYBRID MOLECULE | Signal transduction | Scientific imaging | Cellular biology | Neurons | Information processing
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2. Full Text Spontaneous network activity visualized by ultrasensitive Ca 2+ indicators, yellow Cameleon-Nano
by Yamada, Yoshiyuki and Miyawaki, Atsushi and Hashimoto, Mitsuhiro and Matsu-ura, Toru and Michikawa, Takayuki and Mikoshiba, Katsuhiko and Kobayashi, Kentarou and Nagai, Takeharu and Horikawa, Kazuki and Matsuda, Tomoki
Nature Methods, ISSN 1548-7091, 09/2010, Volume 7, Issue 9, pp. 729 - 732
We report ultrasensitive Ca2+ indicators, yellow cameleon-Nano (YC-Nano), developed by engineering the Ca2+-sensing domain of a genetically encoded Ca2+... 
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3. Full Text Dual-FRET imaging of IP3 and Ca2+ revealed Ca2+-induced IP3 production maintains long lasting Ca2+ oscillations in fertilized mouse eggs
by Matsu-ura, T and Shirakawa, H and Suzuki, KGN and Miyamoto, A and Sugiura, K and Michikawa, T and Kusumi, A and Mikoshiba, K
SCIENTIFIC REPORTS, ISSN 2045-2322, 03/2019, Volume 9, Issue 1, pp. 1 - 11
In most species, fertilization induces Ca2+ transients in the egg. In mammals, the Ca2+ rises are triggered by phospholipase C zeta (PLC zeta) released from... 
ACTIVATION | WAVES | CALCIUM OSCILLATIONS | PHOSPHOLIPASE-C-ZETA | SPERM | INTRACELLULAR CALCIUM | MULTIDISCIPLINARY SCIENCES | DYNAMICS | RELEASE | IDENTIFICATION | INOSITOL 1,4,5-TRISPHOSPHATE RECEPTOR | Calcium signalling | Proteins | Phospholipase | Calcium (intracellular) | Fertilization | Green fluorescent protein | Calcium imaging | Oscillations | Fluorescence resonance energy transfer | Inositol 1,4,5-trisphosphate | Eggs | Phospholipase C
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4. Full Text Phospholipase C-β1 and β4 contribute to non-genetic cell-to-cell variability in histamine-induced calcium signals in HeLa cells
by Ishida, Sachiko and Matsu-ura, Toru and Fukami, Kiyoko and Michikawa, Takayuki and Mikoshiba, Katsuhiko
PLoS ONE, ISSN 1932-6203, 01/2014, Volume 9, Issue 1, p. e86410
A uniform extracellular stimulus triggers cell-specific patterns of Ca(2+) signals, even in genetically identical cell populations. However, the underlying... 
Phospholipase C beta - metabolism | RNA, Small Interfering - genetics | Histamine - pharmacology | Receptors, G-Protein-Coupled - metabolism | Calcium Signaling - physiology | Humans | DNA Primers - genetics | Reverse Transcriptase Polymerase Chain Reaction | Blotting, Western | Histamine - metabolism | RNA Interference | Calcium Signaling - drug effects | Isoenzymes - metabolism | Cytosol - metabolism | HeLa Cells | Inositol 1,4,5-Trisphosphate - metabolism | Neurosciences | Populations | Calcium | Laboratories | Variability | Neurobiology | Oscillations | Science | Fluorescence | Kinases | Population genetics | Calcium signalling | Proteins | Physiology | Time constant | Inositol 1,4,5-trisphosphate | Inositol 1,4,5-trisphosphate receptors | Isoenzymes | RNA-mediated interference | siRNA | Phospholipase C | Polymerase chain reaction | Phospholipase | Histamine | Ribonucleic acids | Genetic engineering
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5. Full Text Excitatory Neuronal Hubs Configure Multisensory Integration of Slow Waves in Association Cortex
by Kuroki, Satoshi and Yoshida, Takamasa and Tsutsui, Hidekazu and Iwama, Mizuho and Ando, Reiko and Michikawa, Takayuki and Miyawaki, Atsushi and Ohshima, Toshio and Itohara, Shigeyoshi
Cell Reports, ISSN 2211-1247, 03/2018, Volume 22, Issue 11, pp. 2873 - 2885
Multisensory integration (MSI) is a fundamental emergent property of the mammalian brain. During MSI, perceptual information encoded in patterned activity is... 
mouse | excitatory neuron | cortical slow waves | multisensory integration | association cortex | fluorescence resonance energy transfer | spontaneous activity | inhibitory neuron | phase locking | wide-field calcium imaging | AUDITORY-CORTEX | IN-VIVO | MICE | FLUORESCENT PROTEINS | CORTICAL ACTIVITY | OSCILLATIONS | PHASE SYNCHRONIZATION | MOUSE VISUAL-CORTEX | CIRCUIT | RANGE | CELL BIOLOGY
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6. Full Text Molecular Basis of the Isoform-specific Ligand-binding Affinity of Inositol 1,4,5-Trisphosphate Receptors
by Miwako Iwai and Takayuki Michikawa and Ivan Bosanac and Mitsuhiko Ikura and Katsuhiko Mikoshiba
Journal of Biological Chemistry, ISSN 0021-9258, 04/2007, Volume 282, Issue 17, pp. 12755 - 12764
Three isoforms of the inositol 1,4,5-trisphosphate (IP 3 ) receptor (IP 3 R), IP 3 R1, IP 3 R2, and IP 3 R3, have different IP 3 -binding affinities and... 
SUPPRESSOR DOMAIN | SITE | CELLS | COMPLEX | TYPE-3 | BIOCHEMISTRY & MOLECULAR BIOLOGY | CALCIUM | SEQUENCE | XENOPUS OOCYTES | Protein Binding - genetics | Inositol 1,4,5-Trisphosphate Receptors - chemistry | Inositol 1,4,5-Trisphosphate - chemistry | Protein Structure, Tertiary - genetics | Structure-Activity Relationship | Animals | Protein Isoforms - metabolism | Inositol 1,4,5-Trisphosphate Receptors - metabolism | Protein Isoforms - chemistry | Ligands | Mice | Kinetics | Inositol 1,4,5-Trisphosphate - metabolism | Inositol 1,4,5-Trisphosphate Receptors - genetics | Amino Acid Substitution | Protein Isoforms - genetics
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7. Full Text Cytosolic Inositol 1,4,5-Trisphosphate Dynamics during Intracellular Calcium Oscillations in Living Cells
by Toru Matsu-ura and Takayuki Michikawa and Takafumi Inoue and Atsushi Miyawaki and Manabu Yoshida and Katsuhiko Mikoshiba
The Journal of Cell Biology, ISSN 0021-9525, 6/2006, Volume 173, Issue 5, pp. 755 - 765
We developed genetically encoded fluorescent inositol 1,4,5-trisphosphate (IP ) sensors that do not severely interfere with intracellular Ca dynamics and used... 
Inositols | Receptors | Calcium | Hepatocytes | Neurons | HeLa cells | Inositol 1 | Histamines | Sensors | Cytosol | SPIKING | HELA-CELLS | CA2+-INDUCED CA2+ RELEASE | STORES | PHOSPHOLIPASE-C | RECEPTOR | XENOPUS OOCYTES | MODEL | TRISPHOSPHATE | CA-2 | CELL BIOLOGY | Calcium Channels - metabolism | Calcium - metabolism | Calcium Signaling - physiology | Humans | Receptors, Metabotropic Glutamate - metabolism | Inositol 1,4,5-Trisphosphate - biosynthesis | Receptors, Histamine - metabolism | Receptors, Metabotropic Glutamate - genetics | Time Factors | Inositol 1,4,5-Trisphosphate Receptors | Protein Binding | Receptor, Metabotropic Glutamate 5 | Cytosol - metabolism | Cell Membrane - metabolism | HeLa Cells | In Vitro Techniques | Inositol 1,4,5-Trisphosphate - metabolism | Receptors, Cytoplasmic and Nuclear - metabolism | Research | Cells | Oscillation
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8. Full Text Regulation of TRPC6 Channel Activity by Tyrosine Phosphorylation
by Chihiro Hisatsune and Yukiko Kuroda and Kyoko Nakamura and Takafumi Inoue and Takeshi Nakamura and Takayuki Michikawa and Akihiro Mizutani and Katsuhiko Mikoshiba
Journal of Biological Chemistry, ISSN 0021-9258, 04/2004, Volume 279, Issue 18, pp. 18887 - 18894
Various hormonal stimuli and growth factors activate the mammalian canonical transient receptor potential (TRPC) channel through phospholipase C (PLC)... 
CA2+-PERMEABLE CATION CHANNEL | OPERATED HTRP3 CHANNELS | CALCIUM-ENTRY CHANNEL | CA2+ ENTRY | IP3 RECEPTOR | BIOCHEMISTRY & MOLECULAR BIOLOGY | INOSITOL 1,4,5-TRISPHOSPHATE RECEPTORS | STORE DEPLETION | G-PROTEIN | SMOOTH-MUSCLE CELLS | TRANSIENT RECEPTOR | Proto-Oncogene Proteins - metabolism | Brain | Cell Line | Phosphorylation | Calcium Channels - metabolism | TRPC Cation Channels | Calcium - metabolism | Proto-Oncogene Proteins c-fyn | Rats | Microsomes - chemistry | Receptor, Epidermal Growth Factor - metabolism | Tyrosine - metabolism | Animals | Transfection | src-Family Kinases - metabolism | Mice | Calcium Channels - genetics
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9. Full Text Subtype-Specific and ER Lumenal Environment-Dependent Regulation of Inositol 1,4,5-Trisphosphate Receptor Type 1 by ERp44
by Higo, Takayasu and Hattori, Mitsuharu and Nakamura, Takeshi and Natsume, Tohru and Michikawa, Takayuki and Mikoshiba, Katsuhiko
Cell, ISSN 0092-8674, 2005, Volume 120, Issue 1, pp. 85 - 98
Inositol 1,4,5-trisphosphate receptors (IP Rs) are intracellular channel proteins that mediate Ca release from the endoplasmic reticulum (ER) and are involved... 
CA2 | STORES | CALRETICULIN | BIOCHEMISTRY & MOLECULAR BIOLOGY | CALCIUM-RELEASE | CHROMOGRANIN | NEURONS | ENDOPLASMIC-RETICULUM | TYPE-1 | CELL-DEATH | CELL BIOLOGY | Cell Line | Molecular Chaperones - metabolism | Calcium Channels - metabolism | Oxidation-Reduction | Calcium - metabolism | Membrane Proteins - genetics | Humans | Molecular Chaperones - genetics | Endoplasmic Reticulum - metabolism | Molecular Chaperones - antagonists & inhibitors | Protein Subunits - metabolism | Two-Hybrid System Techniques | Animals | Membrane Proteins - antagonists & inhibitors | RNA Interference | Inositol 1,4,5-Trisphosphate Receptors | Protein Binding | Membrane Proteins - metabolism | Mice | HeLa Cells | COS Cells | Protein Structure, Tertiary - physiology | Receptors, Cytoplasmic and Nuclear - metabolism | Research | Thioredoxin | Endoplasmic reticulum | Protein binding
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10. Full Text IRBIT Suppresses IP 3 Receptor Activity by Competing with IP 3 for the Common Binding Site on the IP 3 Receptor
by Ando, Hideaki and Mizutani, Akihiro and Kiefer, Hélène and Tsuzurugi, Dai and Michikawa, Takayuki and Mikoshiba, Katsuhiko
Molecular Cell, ISSN 1097-2765, 2006, Volume 22, Issue 6, pp. 795 - 806
The inositol 1,4,5-trisphosphate (IP ) receptors (IP Rs) are IP -gated intracellular Ca channels. We previously identified an IP R binding protein, IRBIT,... 
MOLNEURO | SIGNALING
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11. Full Text Calreticulin and integrin alpha dissociation induces anti-inflammatory programming in animal models of inflammatory bowel disease
by Ohkuro, Masayoshi and Kim, Jun-Dal and Kuboi, Yoshikazu and Hayashi, Yuki and Mizukami, Hayase and Kobayashi-Kuramochi, Hiroko and Muramoto, Kenzo and Shirato, Manabu and Michikawa-Tanaka, Fumiko and Moriya, Jun and Kozaki, Teruya and Takase, Kazuma and Chiba, Kenichi and Agarwala, Kishan Lal and Kimura, Takayuki and Kotake, Makoto and Kawahara, Tetsuya and Yoneda, Naoki and Hirota, Shinsuke and Azuma, Hiroshi and Ozasa-Komura, Nobuko and Ohashi, Yoshiaki and Muratani, Masafumi and Kimura, Keiji and Hishinuma, Ieharu and Fukamizu, Akiyoshi
Nature Communications, ISSN 2041-1723, 12/2018, Volume 9, Issue 1, pp. 1982 - 10
Inflammatory bowel disease (IBD), including ulcerative colitis and Crohn's disease, is a chronic intestinal inflammatory condition initiated by... 
COLON-CANCER | ANTIBODIES | MIGRATION | CYTOKINES | PROTEIN | MULTIDISCIPLINARY SCIENCES | ULCERATIVE-COLITIS | CELL-ADHESION | LEUKOCYTE ADHESION | EXPRESSION | MOUSE MODELS | Colon - cytology | Cyclohexanes - pharmacology | Humans | Colon - immunology | Male | Healthy Volunteers | Colitis, Ulcerative - immunology | Cyclohexanes - therapeutic use | T-Lymphocytes - drug effects | Integrin alpha Chains - immunology | Anti-Inflammatory Agents - therapeutic use | Female | Colitis, Ulcerative - drug therapy | Neutrophil Infiltration - drug effects | Disease Models, Animal | Neutrophil Infiltration - immunology | Anti-Inflammatory Agents - pharmacology | Colon - pathology | Jurkat Cells | Neutrophils - drug effects | Neutrophils - immunology | Integrin alpha Chains - metabolism | Piperazines - therapeutic use | Mice, SCID | Piperazines - pharmacology | Dextran Sulfate - toxicity | Animals | Colitis, Ulcerative - chemically induced | Calreticulin - antagonists & inhibitors | Protein Binding | T-Lymphocytes - immunology | Mice | Mice, Inbred BALB C | Calreticulin - immunology | Animal models | Inflammatory bowel diseases | Calcium | Pathogenesis | Lymphocytes T | Leukocytes | Sodium sulfates | Calreticulin | Lymphocytes | Intestine | Rodents | Sodium sulfate | Colon | Binding | Leukocytes (neutrophilic) | Gene expression | Molecular chains | Endothelium | Inflammatory bowel disease | White blood cells | Dextran | Sodium | Infiltration | Microvasculature | Sulfate | Ulcerative colitis | Integrins
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12. Full Text Quantitative comparison of genetically encoded Ca2+ indicators in cortical pyramidal cells and cerebellar Purkinje cells
by Yamada, Y and Michikawa, T and Hashimoto, M and Horikawa, K and Nagai, T and Miyawaki, A and Hausser, M and Mikoshiba, K
FRONTIERS IN CELLULAR NEUROSCIENCE, ISSN 1662-5102, 09/2011, Volume 5
Genetically encoded Ca2+ indicators (GECIs) are promising tools for cell type-specific and chronic recording of neuronal activity. In the mammalian central... 
ACTION-POTENTIALS | acute brain slice | NEURONAL-ACTIVITY | CELLULAR RESOLUTION | cortical pyramidal cell | cerebellar Purkinje cell | BIRTH-DATE | patch-clamp recording | FLUORESCENT PROTEINS | NEUROSCIENCES | CALCIUM TRANSIENTS | two-photon imaging | genetically encoded Ca2+ indicators | VISUAL-CORTEX | adenovirus | IN-VIVO | NEURAL ACTIVITY | MICE | Cerebellum | Neuroimaging | Neurosciences | Biomedical research | Calcium | Peptides | Laboratories | Brain slice preparation | Central nervous system | Science | Kinases | Hepatitis | Purkinje cells | Physiology | Expression vectors | Cytomegalovirus | Cloning | Cortex | Injection | Musculoskeletal system | Brain research | Pyramidal cells | Adenoviruses | Growth hormones | Hippocampus
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13. Full Text Structural insights into the regulatory mechanism of IP 3 receptor
by Bosanac, Ivan and Michikawa, Takayuki and Mikoshiba, Katsuhiko and Ikura, Mitsuhiko
BBA - Molecular Cell Research, ISSN 0167-4889, 2004, Volume 1742, Issue 1, pp. 89 - 102
Inositol 1,4,5-trisphosphate receptors (IP R) are intracellular Ca release channels whose opening requires binding of two intracellular messengers IP and Ca .... 
Calcium signaling | IP 3 | IP 3 receptor structure | receptor structure
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14. Full Text Tyr-167/Trp-168 in type 1/3 inositol 1,4,5-trisphosphate receptor mediates functional coupling between ligand binding and channel opening
by Yamazaki, Haruka and Chan, Jenny and Ikura, Mitsuhiko and Michikawa, Takayuki and Mikoshiba, Katsuhiko
Journal of Biological Chemistry, ISSN 0021-9258, 11/2010, Volume 285, Issue 46, pp. 36081 - 36091
The N-terminal similar to 220-amino acid region of the inositol 1,4,5-trisphosphate (IP3) receptor (IP3R)/Ca2+ release channel has been referred to as the... 
CALCIUM RELEASE | SITE | COMPLEX | AFFINITY | BIOCHEMISTRY & MOLECULAR BIOLOGY | XENOPUS EMBRYOS | ENDOPLASMIC-RETICULUM | MOLECULAR-CLONING | MONOCLONAL-ANTIBODIES | DOMAINS | MICE LACKING | Inositol 1,4,5-Trisphosphate Receptors - chemistry | Calcium - metabolism | Inositol 1,4,5-Trisphosphate - chemistry | Molecular Sequence Data | Tryptophan - chemistry | Inositol 1,4,5-Trisphosphate - pharmacology | Tryptophan - metabolism | Ion Channel Gating - physiology | Protein Isoforms - metabolism | Inositol 1,4,5-Trisphosphate Receptors - metabolism | Protein Isoforms - chemistry | Tyrosine - chemistry | Protein Structure, Tertiary | Amino Acid Sequence | Mutagenesis, Site-Directed | Tryptophan - genetics | Models, Molecular | Binding Sites - genetics | Trypsin - metabolism | Blotting, Western | Sequence Homology, Amino Acid | Tyrosine - metabolism | Animals | Ion Channel Gating - genetics | Cell Line, Tumor | Protein Binding | Ligands | Mice | Mutation | Inositol 1,4,5-Trisphosphate - metabolism | Inositol 1,4,5-Trisphosphate Receptors - genetics | Amino Acid Substitution | Ion Channel Gating - drug effects | Protein Isoforms - genetics | Tyrosine - genetics | Index Medicus | Protein Structure and Folding | Calcium | Calcium Channels | Ion Channels | Signal Transduction | Inositol Phosphates | Intracellular Calcium Release
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15. Full Text Dual-FRET imaging of IP 3 and Ca 2+ revealed Ca 2+ -induced IP 3 production maintains long lasting Ca 2+ oscillations in fertilized mouse eggs
by Matsu-ura, Toru and Shirakawa, Hideki and Suzuki, Kenichi G. N and Miyamoto, Akitoshi and Sugiura, Kotomi and Michikawa, Takayuki and Kusumi, Akihiro and Mikoshiba, Katsuhiko
Scientific Reports, 12/2019, Volume 9, Issue 1, p. 4829
In most species, fertilization induces Ca transients in the egg. In mammals, the Ca rises are triggered by phospholipase Cζ (PLCζ) released from the sperm; IP... 
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16. Full Text Critical Regions for Activation Gating of the Inositol 1,4,5-Trisphosphate Receptor
by Keiko Uchida and Hiroshi Miyauchi and Teiichi Furuichi and Takayuki Michikawa and Katsuhiko Mikoshiba
Journal of Biological Chemistry, ISSN 0021-9258, 05/2003, Volume 278, Issue 19, pp. 16551 - 16560
To understand the molecular mechanism of ligand-induced gating of the inositol 1,4,5-trisphosphate (IP 3 ) receptor (IP 3 R)/Ca 2+ release channel, we analyzed... 
TRISPHOSPHATE RECEPTORS | SIGNAL-TRANSDUCTION | COMPLEX-FORMATION | CONFORMATIONAL-CHANGES | INSP3 RECEPTOR | CHANNEL | PURKINJE-CELL | BIOCHEMISTRY & MOLECULAR BIOLOGY | CALCIUM-RELEASE | LIGAND-BINDING SITE | MOUSE CEREBELLUM | Protein Structure, Tertiary | Amino Acid Sequence | Cysteine | Mutagenesis, Site-Directed | Molecular Sequence Data | Receptors, Cytoplasmic and Nuclear - physiology | Receptors, Cytoplasmic and Nuclear - genetics | Binding Sites - genetics | Calcium Channels - physiology | Animals | Ion Channel Gating - genetics | Conserved Sequence | Inositol 1,4,5-Trisphosphate Receptors | Ligands | Mice | Mutation | Calcium Channels - genetics
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17. Full Text Crystal Structure of the Ligand Binding Suppressor Domain of Type 1 Inositol 1,4,5-Trisphosphate Receptor
by Bosanac, Ivan and Yamazaki, Haruka and Matsu-ura, Toru and Michikawa, Takayuki and Mikoshiba, Katsuhiko and Ikura, Mitsuhiko and Argonne National Lab. (ANL), Argonne, IL (United States). Advanced Photon Source (APS)
Molecular Cell, ISSN 1097-2765, 10/2015, Volume 17, Issue (2) ; 01, 2005
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18. Full Text Angiotensin-converting enzyme converts amyloid β-protein 1-42 (Aβ1-42) to Aβ1-40, and its inhibition enhances brain Aβ deposition
by Zou, Kun and Yamaguchi, Haruyasu and Akatsu, Hiroyasu and Sakamoto, Takaaki and Ko, Mihee and Mizoguchi, Kazushige and Gong, Jian-Sheng and Yu, Wenxin and Yamamoto, Takayuki and Kosaka, Kenji and Yanagisawa, Katsuhiko and Michikawa, Makoto
Journal of Neuroscience, ISSN 0270-6474, 08/2007, Volume 27, Issue 32, pp. 8628 - 8635
The abnormal deposition of the amyloid β-protein (Aβ) in the brain appears crucial to the pathogenesis of Alzheimer's disease (AD). Recent studies have... 
ACE | APP transgenic mouse | Aβ degradation | Aβ deposition | Angiotensin-converting enzyme | Amyloid β-protein | Alzheimer's disease | amyloid β-protein | angiotensin-converting enzyme
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