About: Tight binding of NADPH to the 39-kDa subunit of complex I is not required for catalytic activity but stabilizes the multiprotein complex

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About: Tight binding of NADPH to the 39-kDa subunit of complex I is not required for catalytic activity but stabilizes the multiprotein complex Goto Sponge NotDistinct Permalink

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scientific article published on 19 September 2006

Attributes	Values
rdf:type	Item
description	wetenschappelijk artikel (nl) наукова стаття, опублікована в грудні 2006 (uk) scientific article published on 19 September 2006 (en) artículu científicu espublizáu en setiembre de 2006 (ast)
publication date	wds:Q58782362-EBE0F86B-15F3-4369-8A17-ECA46DF2CC8B
publication date	2006-09-19 00:00:00Z (xsd:dateTime)
author name string	wds:Q58782362-388B6E88-6E86-42CA-8B96-A15E020429B0 wds:Q58782362-64EFAEBD-8C95-45FE-9490-CD36B61D659F wds:Q58782362-696D941D-D659-451D-B985-18517C1D0DD6 wds:Q58782362-DEBC35F4-6E75-405C-8B8E-3BF519908FEB
author name string	Klaus Zwicker Stefan Kerscher Volker Zickermann Albina Abdrakhmanova
rdfs:label	Tight binding of NADPH to the 39-kDa subunit of complex I is not required for catalytic activity but stabilizes the multiprotein complex (en) Tight binding of NADPH to the 39-kDa subunit of complex I is not required for catalytic activity but stabilizes the multiprotein complex (nl)
skos:prefLabel	Tight binding of NADPH to the 39-kDa subunit of complex I is not required for catalytic activity but stabilizes the multiprotein complex (en) Tight binding of NADPH to the 39-kDa subunit of complex I is not required for catalytic activity but stabilizes the multiprotein complex (nl)
name	Tight binding of NADPH to the 39-kDa subunit of complex I is not required for catalytic activity but stabilizes the multiprotein complex (en) Tight binding of NADPH to the 39-kDa subunit of complex I is not required for catalytic activity but stabilizes the multiprotein complex (nl)
author	wds:Q58782362-5DD0FDEA-E227-4823-A1D5-93CA0C335ED8
author	Ulrich Brandt
title	wds:Q58782362-EFEA0038-6DC7-4E50-91A9-665981B1190C
title	Tight binding of NADPH to the 39-kDa subunit of complex I is not required for catalytic activity but stabilizes the multiprotein complex (en)
page(s)	wds:Q58782362-975C7438-A751-4019-B857-069BEA1904CD
page(s)	1676-1682
instance of	wds:Q58782362-F884AD8D-E296-43B4-9AEC-F2F0D1FC5E45
instance of	scholarly article
PubMed ID	wds:Q58782362-B86DE1BC-1EC8-411F-8BC7-5CE9DF34C859
PubMed ID	http://rdf.ncbi.nlm.nih.gov/pubchem/reference/17046710
PubMed ID	17046710
published in	wds:Q58782362-4A80776B-DBF9-48CF-9146-7753AC6E261B
published in	Biochimica et Biophysica Acta
issue	wds:Q58782362-FE405A8F-6136-40AC-BFEC-22F660360351
volume	wds:Q58782362-0FE30110-9B1F-4143-9BCE-57475323AF82
issue	12
volume	1757
DOI	wds:Q58782362-6ABE5BD6-C7E1-4AF0-902D-6ABDDAB3864F
DOI	http://dx.doi.org/10.1016/J.BBABIO.2006.09.003
DOI	10.1016/J.BBABIO.2006.09.003
is about of	https://www.wikidata.org/wiki/Special:EntityData/Q58782362
is cites work of	ND3, ND1 and 39kDa subunits are more exposed in the de-active form of bovine mitochondrial complex I. Regulation of Mitochondrial Complex I Biogenesis in Drosophila Flight Muscles Architecture of mammalian respiratory complex I. Structural biology. Mechanistic insight from the crystal structure of mitochondrial complex I Atomic structure of the entire mammalian mitochondrial complex I. Extending the models for iron and sulfur oxidation in the extreme acidophile Acidithiobacillus ferrooxidans Protein kinase C-epsilon activation induces mitochondrial dysfunction and fragmentation in renal proximal tubules Challenges in elucidating structure and mechanism of proton pumping NADH:ubiquinone oxidoreductase (complex I). The reaction of NADPH with bovine mitochondrial NADH:ubiquinone oxidoreductase revisited: I. Proposed consequences for electron transfer in the enzyme Accessory subunits of mitochondrial complex I. Structure of mammalian respiratory complex I Ischemic A/D transition of mitochondrial complex I and its role in ROS generation Molecular mechanism and physiological role of active-deactive transition of mitochondrial complex I. The mitochondrial complex I of trypanosomatids--an overview of current knowledge Cytoplasmic and Mitochondrial NADPH-Coupled Redox Systems in the Regulation of Aging Novel large-range mitochondrial DNA deletions and fatal multisystemic disorder with prominent hepatopathy A three-dimensional topology of complex I inferred from evolutionary correlations.
is cites work of	wds:Q38690884-6FD5063D-6FC2-44FE-BAA6-BEB253C0D9CA wds:Q30832310-5B953757-6B0A-4470-968E-DBD53078C5EB wds:Q37316694-4E1EDB6A-2592-4848-9023-7FFC0C81D8BF wds:Q41875296-94861F25-D498-4AA9-8190-1BC5C1C9C540 wds:Q38222864-731A8669-6600-43AA-B958-18D4DBEF6F9C wds:Q41121933-CF13FA2D-F847-4C8A-BB26-D7BFB65B5DD8 wds:Q35581352-F4AD8997-6BC3-4C78-BD42-7CE96BDCCAB5 wds:Q38809592-D3BA86B0-7355-496C-871D-7E17660B5FED wds:Q64096823-877AFE47-3C01-42B1-89DB-C19DC8CAF28C wds:Q28074253-E1455A79-6AF8-411D-A835-28E9428CF3AC wds:Q34362913-258C7518-A58F-495A-97C0-BAB7FEAD0F1B wds:Q41607512-7482172D-723F-482A-8F6B-5D095042701F wds:Q27697274-F56CADA7-E422-429B-8A0B-BCC34623FCAB wds:Q38141073-B635F6EA-9C6D-4410-8544-ECE5065E65A7 wds:Q42971064-C1E4763B-68A5-482F-A43D-832D59996667 wds:Q21283753-74F213B5-0229-4F41-B23E-47AEED4D1F22 wds:Q35086987-895314BC-EDF4-4733-8B98-5139050F2E58

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