Dihydrolipoamide

Dihydrolipoamide is a lipid of Fatty Acyls (FA) class. Dihydrolipoamide is associated with abnormalities such as Wiskott-Aldrich Syndrome. The involved functions are known as Citric Acid Cycle, Electron Transport, NADH oxidation, Oxidation and Oxidants. Dihydrolipoamide often locates in Mitochondria, Mitochondrial matrix and Chloroplasts. The associated genes with Dihydrolipoamide are Mutant Proteins, Recombinant Proteins, mycothione reductase, Genes, Mitochondrial and alanylproline.

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Introduction

To understand associated biological information of Dihydrolipoamide, we collected biological information of abnormalities, associated pathways, cellular/molecular locations, biological functions, related genes/proteins, lipids and common seen animal/experimental models with organized paragraphs from literatures.

What diseases are associated with Dihydrolipoamide?

Dihydrolipoamide is suspected in and other diseases in descending order of the highest number of associated sentences.

Related references are mostly published in these journals:

Disease Cross reference Weighted score Related literature
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Possible diseases from mapped MeSH terms on references

We collected disease MeSH terms mapped to the references associated with Dihydrolipoamide

MeSH term MeSH ID Detail
Parkinsonian Disorders D020734 20 associated lipids
Total 1

PubChem Associated disorders and diseases

What pathways are associated with Dihydrolipoamide

There are no associated biomedical information in the current reference collection.

PubChem Biomolecular Interactions and Pathways

Link to PubChem Biomolecular Interactions and Pathways

What cellular locations are associated with Dihydrolipoamide?

Related references are published most in these journals:

Location Cross reference Weighted score Related literatures
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What functions are associated with Dihydrolipoamide?


Related references are published most in these journals:

Function Cross reference Weighted score Related literatures

What lipids are associated with Dihydrolipoamide?

There are no associated biomedical information in the current reference collection.

What genes are associated with Dihydrolipoamide?

Related references are published most in these journals:


Gene Cross reference Weighted score Related literatures

What common seen animal models are associated with Dihydrolipoamide?

There are no associated biomedical information in the current reference collection.

NCBI Entrez Crosslinks

All references with Dihydrolipoamide

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Authors Title Published Journal PubMed Link
Song J and Jordan F Interchain acetyl transfer in the E2 component of bacterial pyruvate dehydrogenase suggests a model with different roles for each chain in a trimer of the homooligomeric component. 2012 Biochemistry pmid:22413895
Jiang Y and Wang X Comparative mitochondrial proteomics: perspective in human diseases. 2012 J Hematol Oncol pmid:22424240
Peano C et al. Comparative genomics and transcriptional profiles of Saccharopolyspora erythraea NRRL 2338 and a classically improved erythromycin over-producing strain. 2012 Microb. Cell Fact. pmid:22401291
Redanz S et al. A five-species transcriptome array for oral mixed-biofilm studies. 2011 PLoS ONE pmid:22194794
Kehr S et al. Protein S-glutathionylation in malaria parasites. 2011 Antioxid. Redox Signal. pmid:21595565
Harvey RM et al. A variable region within the genome of Streptococcus pneumoniae contributes to strain-strain variation in virulence. 2011 PLoS ONE pmid:21573186
Brautigam CA et al. Structural and thermodynamic basis for weak interactions between dihydrolipoamide dehydrogenase and subunit-binding domain of the branched-chain alpha-ketoacid dehydrogenase complex. 2011 J. Biol. Chem. pmid:21543315
Feeney MA et al. Repurposing lipoic acid changes electron flow in two important metabolic pathways of Escherichia coli. 2011 Proc. Natl. Acad. Sci. U.S.A. pmid:21521794
Kumar A et al. Redox homeostasis in mycobacteria: the key to tuberculosis control? 2011 Expert Rev Mol Med pmid:22172201
Miller JA et al. 1,3-Dinitrobenzene-induced metabolic impairment through selective inactivation of the pyruvate dehydrogenase complex. 2011 Toxicol. Sci. pmid:21551353