About: Resonance Raman spectra of the FMN of the bovine heart NADH: ubiquinone oxidoreductase, the largest membrane protein in the mitochondrial respiratory system

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About: Resonance Raman spectra of the FMN of the bovine heart NADH: ubiquinone oxidoreductase, the largest membrane protein in the mitochondrial respiratory system Goto Sponge NotDistinct Permalink

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scientific article published on 14 April 2007

Attributes	Values
rdf:type	Item
description	wetenschappelijk artikel (nl) наукова стаття, опублікована у квітні 2007 (uk) article scientifique publié en 2007 (fr) im April 2007 veröffentlichter wissenschaftlicher Artikel (de) scientific article published on 14 April 2007 (en) artículu científicu espublizáu n'abril de 2007 (ast)
publication date	wds:Q80162409-715987DB-9697-48DA-A0F0-D9B0EB499407
publication date	2007-04-14 00:00:00Z (xsd:dateTime)
exact match	wds:Q80162409-3E880096-7DA4-46FB-8534-4A785ED64A06
exact match	https://scigraph.springernature.com/pub.10.1007/s10863-007-9072-3
cites work	wds:Q80162409-1ABA53AC-0AEF-439C-B1B9-E33774BE89B6 wds:Q80162409-26E32E69-4B62-458F-80DD-EE71D007B64B wds:Q80162409-2E22DB2D-5FDF-4664-91DC-3BAB99D5B10E wds:Q80162409-33512472-F9CD-484C-A58F-A9BBE1EBA487 wds:Q80162409-6D58E211-D6A1-4242-804C-2B597ADD1578 wds:Q80162409-7F99B01C-7433-44B1-8E14-66D3048F1C29 wds:Q80162409-913AEE79-0B48-4C30-A719-32E80C648A01 wds:Q80162409-E886BCF9-E8DE-4325-97F9-B362C56D9E59 wds:Q80162409-F5D457FD-6F4E-4A20-9F5E-BA70E69697AE wds:Q80162409-F8BEAE1A-6478-4AC7-9DDF-D6DCC5D27F50
cites work	Iron-sulfur clusters/semiquinones in complex I. Structure of the hydrophilic domain of respiratory complex I from Thermus thermophilus The nuclear encoded subunits of complex I from bovine heart mitochondria The NADH:ubiquinone oxidoreductase (complex I) of respiratory chains Comparing protein-ligand interactions in solution and single crystals by Raman spectroscopy EPR studies of iron-sulfur clusters in isolated subunits and subfractions of NADH-ubiquinone oxidoreductase Resolution of complex I and isolation of NADH dehydrogenase and an iron--sulfur protein Steady-state kinetics of NADH:coenzyme Q oxidoreductase isolated from bovine heart mitochondria Studies on the electron transport system. XXX. DPNH-cytochrome c reductase I Resonance Raman spectra of carbon-13- and nitrogen-15-labeled riboflavin bound to egg-white flavoprotein
author name string	wds:Q80162409-0E3054F4-E394-4AE1-BC28-6335F5567FE6 wds:Q80162409-4A5B9455-CE48-4626-8D87-3681C61B06C6 wds:Q80162409-65A4E903-528D-4C21-A29B-CC907EFD1F86 wds:Q80162409-6A5021B0-C611-4D74-B614-442981344D21 wds:Q80162409-79E273CA-B8A0-4585-99C9-602835772EE4 wds:Q80162409-99B15FA8-14B8-4DA4-A6CC-C988680E911C
author name string	Shinya Yoshikawa Satoru Yamaguchi Takashi Ogura Kyoko Shinzawa-Itoh Hidehisa Sugiyama Ryohei Nakatsubo
rdfs:label	Resonance Raman spectra of the FMN of the bovine heart NADH: ubiquinone oxidoreductase, the largest membrane protein in the mitochondrial respiratory system (en) Resonance Raman spectra of the FMN of the bovine heart NADH: ubiquinone oxidoreductase, the largest membrane protein in the mitochondrial respiratory system (nl)
skos:prefLabel	Resonance Raman spectra of the FMN of the bovine heart NADH: ubiquinone oxidoreductase, the largest membrane protein in the mitochondrial respiratory system (en) Resonance Raman spectra of the FMN of the bovine heart NADH: ubiquinone oxidoreductase, the largest membrane protein in the mitochondrial respiratory system (nl)
name	Resonance Raman spectra of the FMN of the bovine heart NADH: ubiquinone oxidoreductase, the largest membrane protein in the mitochondrial respiratory system (en) Resonance Raman spectra of the FMN of the bovine heart NADH: ubiquinone oxidoreductase, the largest membrane protein in the mitochondrial respiratory system (nl)
title	wds:Q80162409-FCB812E7-3FF2-4EAA-99C5-45697DCF0F6F
title	Resonance Raman spectra of the FMN of the bovine heart NADH: ubiquinone oxidoreductase, the largest membrane protein in the mitochondrial respiratory system (en)
page(s)	wds:Q80162409-EF901C31-4EB9-4B2F-A95A-B5F94120E2DF
page(s)	145-148
instance of	wds:Q80162409-C05A663C-CB9C-4CC4-979C-7432A97FAC9B
instance of	scholarly article
main subject	wds:Q80162409-7F647F5D-A747-4FCD-8D4D-17D4D24BAEDF
main subject	membrane proteins
PubMed ID	wds:Q80162409-6F3EB3C1-9BBF-4626-B184-FB8CB4B1A19A
PubMed ID	http://rdf.ncbi.nlm.nih.gov/pubchem/reference/17436066
PubMed ID	17436066
published in	wds:Q80162409-F5DF35FC-5C30-4BF2-A659-759D0BF7FA59
published in	Journal of Bioenergetics and Biomembranes
issue	wds:Q80162409-163F86CD-44EB-4C0E-8414-EDEBF3DFDC16
volume	wds:Q80162409-3B3B2423-F5BF-4F7E-9C55-72D5DFC91BBC
issue	2
volume	39
DOI	wds:Q80162409-E23244B3-F591-43DC-B66B-37771CBF0117
DOI	http://dx.doi.org/10.1007/S10863-007-9072-3
DOI	10.1007/S10863-007-9072-3
Dimensions Publication ID	wds:Q80162409-DE218D97-B108-4337-9D84-C9AD40A8156D
Dimensions Publication ID	1002080225
is about of	https://www.wikidata.org/wiki/Special:EntityData/Q80162409
is cites work of	Were there any "misassignments" among iron-sulfur clusters N4, N5 and N6b in NADH-quinone oxidoreductase (complex I)?
is cites work of	wds:Q37166544-F3B1E475-374A-451D-98C3-6C26909C4535

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