Post-translational modifications near the quinone binding site of mammalian complex I.
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Human METTL20 methylates lysine residues adjacent to the recognition loop of the electron transfer flavoprotein in mitochondriaHyperglycemic Stress and Carbon Stress in Diabetic GlucotoxicityRoles of Pyruvate, NADH, and Mitochondrial Complex I in Redox Balance and Imbalance in β Cell Function and DysfunctionEnergy conversion, redox catalysis and generation of reactive oxygen species by respiratory complex INDUFAF7 methylates arginine 85 in the NDUFS2 subunit of human complex INDUFAF5 Hydroxylates NDUFS7 at an Early Stage in the Assembly of Human Complex IAtomic structure of the entire mammalian mitochondrial complex I.An update on complex I assembly: the assembly of players.Structure of mammalian respiratory complex IHuman METTL12 is a mitochondrial methyltransferase that modifies citrate synthase.Cryo-EM structures of complex I from mouse heart mitochondria in two biochemically defined states
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P2860
Post-translational modifications near the quinone binding site of mammalian complex I.
description
article científic
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article scientifique
@fr
articolo scientifico
@it
artigo científico
@pt
bilimsel makale
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scientific article published on 08 July 2013
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vedecký článok
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vetenskaplig artikel
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videnskabelig artikel
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vědecký článek
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name
Post-translational modifications near the quinone binding site of mammalian complex I.
@en
Post-translational modifications near the quinone binding site of mammalian complex I.
@nl
type
label
Post-translational modifications near the quinone binding site of mammalian complex I.
@en
Post-translational modifications near the quinone binding site of mammalian complex I.
@nl
prefLabel
Post-translational modifications near the quinone binding site of mammalian complex I.
@en
Post-translational modifications near the quinone binding site of mammalian complex I.
@nl
P2093
P2860
P356
P1476
Post-translational modifications near the quinone binding site of mammalian complex I
@en
P2093
Ian M Fearnley
Joe Carroll
Shujing Ding
P2860
P304
24799-24808
P356
10.1074/JBC.M113.488106
P407
P577
2013-07-08T00:00:00Z