The post-translational modifications of the nuclear encoded subunits of complex I from bovine heart mitochondria. (Q33212241)

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8 January 2020

title

The post-translational modifications of the nuclear encoded subunits of complex I from bovine heart mitochondria (English)

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8 January 2020

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6

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8 January 2020

John E. Walker

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8 January 2020

author name string

Joe Carroll

1

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8 January 2020

Ian M Fearnley

2

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J Mark Skehel

3

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Michael J Runswick

4

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Richard J Shannon

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publication date

22 February 2005

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Molecular & Cellular Proteomics

8 January 2020

published in

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volume

4

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issue

5

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page(s)

693-699

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The NADH:ubiquinone oxidoreductase (complex I) of respiratory chains

8 January 2020

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Three-dimensional structure of bovine NADH:ubiquinone oxidoreductase (complex I) at 22 A in ice.

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Sequences of 20 subunits of NADH: Ubiquinone oxidoreductase from bovine heart mitochondria

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GRIM-19, a cell death regulatory gene product, is a subunit of bovine mitochondrial NADH:ubiquinone oxidoreductase (complex I)

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Definition of the nuclear encoded protein composition of bovine heart mitochondrial complex I. Identification of two new subunits.

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Analysis of the subunit composition of complex I from bovine heart mitochondria

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Complete sequence of bovine mitochondrial DNA. Conserved features of the mammalian mitochondrial genome

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Six unidentified reading frames of human mitochondrial DNA encode components of the respiratory-chain NADH dehydrogenase

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URF6, last unidentified reading frame of human mtDNA, codes for an NADH dehydrogenase subunit

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The nuclear encoded subunits of complex I from bovine heart mitochondria

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NADH:ubiquinone oxidoreductase from bovine heart mitochondria: sequence of a novel 17.2-kDa subunit.

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Complementary DNA sequences of two 14.5 kDa subunits of NADH:ubiquinone oxidoreductase from bovine heart mitochondria. Completion of the primary structure of the complex?

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Specific protein methylation defects and gene expression perturbations in coactivator-associated arginine methyltransferase 1-deficient mice

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A highly conserved 3-methylhistidine modification is absent in yeast actin

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Methylated lysines and 3-methylhistidine in myosin: tissue and developmental differences.

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Comparison of three methyl-coenzyme M reductases from phylogenetically distant organisms: unusual amino acid modification, conservation and adaptation

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Presence of an acyl carrier protein in NADH:ubiquinone oxidoreductase from bovine heart mitochondria

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Electrospray ionization mass spectrometric analysis of subunits of NADH:ubiquinone oxidoreductase (complex I) from bovine heart mitochondria

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His(73), often methylated, is an important structural determinant for actin. A mutagenic analysis of HIS(73) of yeast actin

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Sequences of 20 subunits of NADH:ubiquinone oxidoreductase from bovine heart mitochondria. Application of a novel strategy for sequencing proteins using the polymerase chain reaction

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Isoenergetic dietary protein restriction decreases myosin heavy chain IIx fraction and myosin heavy chain production in humans

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Structural analysis of NADH: ubiquinone oxidoreductase from bovine heart mitochondria.

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Resolution of the Membrane Domain of Bovine Complex I into Subcomplexes: Implications for the Structural Organization of the Enzyme

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Protein methylation: a signal event in post-translational modification

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Actin amino-terminal acetylation and processing in a rabbit reticulocyte lysate

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Two protons are pumped from the mitochondrial matrix per electron transferred between NADH and ubiquinone

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Amino-terminal acetylation of proteins: an overview

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Identifiers

DOI

10.1074/MCP.M500014-MCP200

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:15728260 AND SRC:MED&resulttype=core&format=json

8 January 2020

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