About: Koichiro Ishimori

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researcher

Attributes	Values
rdf:type	Item
description	researcher (en) 연구원 (ko) 研究者 (ja) araştırmacı (tr) wetenschapper (nl) дослідник (uk) эрдэмтэн (mn) изилдөөчү (ky) 研究者 (zh) հետազոտող (hy)
rdfs:label	Koichiro Ishimori (en) Koichiro Ishimori (es) Koichiro Ishimori (nl) Koichiro Ishimori (sl) Koichiro Ishimori (ast) 石森浩一郎 (ja)
skos:prefLabel	Koichiro Ishimori (en) Koichiro Ishimori (es) Koichiro Ishimori (nl) Koichiro Ishimori (sl) Koichiro Ishimori (ast) 石森浩一郎 (ja)
name	Koichiro Ishimori (en) Koichiro Ishimori (es) Koichiro Ishimori (nl) Koichiro Ishimori (sl) Koichiro Ishimori (ast) 石森浩一郎 (ja)
Scopus author ID	wds:Q55664881-FC141445-B903-49E5-8C4E-983223045333
Scopus author ID	7005759631
given name	wds:Q55664881-7C20ADE5-2D2D-48C5-B55F-93E2F4F01D6C
given name	Kōichirō
instance of	wds:Q55664881-2FBE1081-FEF1-497C-B1E7-790D7681C605
instance of	Homo sapiens
Loop ID	wds:Q55664881-EB16CA21-D664-49A0-80ED-C17B7FA31AE7
Loop ID	299370
Researchmap ID	wds:Q55664881-A042DC2C-5529-45B7-8B95-8BDCCDEA6EFC
Researchmap ID	k_ishimori
occupation	wds:Q55664881-E59B4A95-2D10-43C1-825B-F8D441CB74A0
employer	wds:Q55664881-05C9B551-B400-4DF5-BD97-C59AF0C00202 wds:Q55664881-F9D49532-FD16-47B2-84BC-9593091E89A1
CiNii Research ID	wds:Q55664881-205F7CD6-BADB-4A33-8D4A-A4D1B10A03F3
educated at	wds:Q55664881-35133F6A-FF10-45F1-8DF8-DFE1270D01AB
family name	wds:Q55664881-6F2038A7-0E80-4926-8A0B-0B8CC1D1D604
J-GLOBAL ID	wds:Q55664881-5BAF4D51-434D-4A4A-941C-BFEE53D5981A
CiNii Research ID	https://cir.nii.ac.jp/crid/1420845751159222272.rdf
occupation	researcher
employer	Hokkaido University Kyoto University
CiNii Research ID	1420845751159222272
educated at	Kyoto University
family name	Ishimori
J-GLOBAL ID	200901006051594815
ORCID iD	wds:Q55664881-E1B4FA35-2777-4E70-BB84-80523C275DE4
ORCID iD	https://orcid.org/0000-0002-5868-0462
ORCID iD	0000-0002-5868-0462
e-Rad researcher number	wds:Q55664881-7B704743-6B5B-4A4C-BAB4-E47BE53AC3E1
e-Rad researcher number	20192487
ResearcherID	wds:Q55664881-7B412FBC-1660-42B0-A7A8-6FAEB5BDED64
ResearcherID	S-1247-2016
is about of	https://www.wikidata.org/wiki/Special:EntityData/Q55664881 https://ja.wikipedia.org/wiki/%E7%9F%B3%E6%A3%AE%E6%B5%A9%E4%B8%80%E9%83%8E
is author of	Binding of CO at the Pro2 side is crucial for the activation of CO-sensing transcriptional activator CooA. (1)H NMR spectroscopic studies. NO-induced activation mechanism of the heme-regulated eIF2alpha kinase. Two heme binding sites are involved in the regulated degradation of the bacterial iron response regulator (Irr) protein. Identification of the ubiquitin-protein ligase that recognizes oxidized IRP2 Crystal structure of the cytochrome p450cam mutant that exhibits the same spectral perturbations induced by putidaredoxin binding Hydrogen bond network in the distal site of peroxidases: spectroscopic properties of Asn70 --> Asp horseradish peroxidase mutant Luminol activity of horseradish peroxidase mutants mimicking a proposed binding site for luminol in Arthromyces ramosus peroxidase Specifically collapsed intermediate in the early stage of the folding of ribonuclease A. Ligand migration in human myoglobin: steric effects of isoleucine 107(G8) on O(2) and CO binding. Structure and ligand binding properties of leucine 29(B10) mutants of human myoglobin. Unusual pressure effects on ligand rebinding to the human myoglobin Leucine 29 mutants Unusual heme binding in the bacterial iron response regulator protein: spectral characterization of heme binding to the heme regulatory motif Conformational landscape of cytochrome c folding studied by microsecond-resolved small-angle x-ray scattering. Heme-binding characteristics of the isolated PAS-A domain of mouse Per2, a transcriptional regulatory factor associated with circadian rhythms. Cerebral oxygen utilization analyzed by the use of oxygen-17 and its nuclear magnetic resonance Roles of negatively charged surface residues of putidaredoxin in interactions with redox partners in p450cam monooxygenase system. Collapse and search dynamics of apomyoglobin folding revealed by submillisecond observations of alpha-helical content and compactness. 'Module'-substituted globins: artificial exon shuffling among myoglobin, hemoglobin alpha- and beta-subunits. The artificial alpha1beta1-contact mutant hemoglobin, Hb Phe-35beta, shows only small functional abnormalities Molecular basis of guanine nucleotide dissociation inhibitor activity of human neuroglobin by chemical cross-linking and mass spectrometry Haem-dependent dimerization of PGRMC1/Sigma-2 receptor facilitates cancer proliferation and chemoresistance Roles of the axial push effect in cytochrome P450cam studied with the site-directed mutagenesis at the heme proximal site Structural roles of the highly conserved glu residue in the heme distal site of peroxidases. Proximal cysteine residue is essential for the enzymatic activities of cytochrome P450cam. Direct observation of the multistep helix formation of poly-L-glutamic acids NMR basis for interprotein electron transfer gating between cytochrome c and cytochrome c oxidase. Site-directed mutagenesis in hemoglobin: functional and structural role of inter- and intrasubunit hydrogen bonds as studied with 37 beta and 145 beta mutations Site-directed mutagenesis in haemoglobin. Functional role of tyrosine-42(C7) alpha at the alpha 1-beta 2 interface Site-directed mutagenesis in hemoglobin: functional and structural study of the intersubunit hydrogen bond of threonine-38(C3)alpha at the alpha 1-beta 2 interface in human hemoglobin. Unique peroxidase reaction mechanism in prostaglandin endoperoxide H synthase-2: compound I in prostaglandin endoperoxide H synthase-2 can be formed without assistance by distal glutamine residue Hierarchical folding mechanism of apomyoglobin revealed by ultra-fast H/D exchange coupled with 2D NMR. Alteration of human myoglobin proximal histidine to cysteine or tyrosine by site-directed mutagenesis: characterization and their catalytic activities Roles of proximal ligand in heme proteins: replacement of proximal histidine of human myoglobin with cysteine and tyrosine by site-directed mutagenesis as models for P-450, chloroperoxidase, and catalase Identification and functional and spectral characterization of a globin-coupled histidine kinase from Anaeromyxobacter sp. Fw109-5. NMR study on the structural changes of cytochrome P450cam upon the complex formation with putidaredoxin. Functional significance of the putidaredoxin-induced structural changes. Identification of histidine 77 as the axial heme ligand of carbonmonoxy CooA by picosecond time-resolved resonance Raman spectroscopy Effects of the bHLH domain on axial coordination of heme in the PAS-A domain of neuronal PAS domain protein 2 (NPAS2): conversion from His119/Cys170 coordination to His119/His171 coordination

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