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
Ortega-Galisteo AP et al. S-Nitrosylated proteins in pea (Pisum sativum L.) leaf peroxisomes: changes under abiotic stress. 2012 J. Exp. Bot. pmid:22213812
Schriek S et al. Detection of an L-amino acid dehydrogenase activity in Synechocystis sp. PCC 6803. 2009 J. Exp. Bot. pmid:19213808
Aranjuelo I et al. Plant physiology and proteomics reveals the leaf response to drought in alfalfa (Medicago sativa L.). 2011 J. Exp. Bot. pmid:20797998
Vasquez-Robinet C et al. Physiological and molecular adaptations to drought in Andean potato genotypes. 2008 J. Exp. Bot. pmid:18535297
Norton GJ et al. Rice-arsenate interactions in hydroponics: whole genome transcriptional analysis. 2008 J. Exp. Bot. pmid:18453530
Katz E et al. Label-free shotgun proteomics and metabolite analysis reveal a significant metabolic shift during citrus fruit development. 2011 J. Exp. Bot. pmid:21841177
Hallström T et al. Dihydrolipoamide dehydrogenase of Pseudomonas aeruginosa is a surface-exposed immune evasion protein that binds three members of the factor H family and plasminogen. 2012 J. Immunol. pmid:23071278
Quintana E et al. Dihydrolipoamide dehydrogenase (DLD) deficiency in a Spanish patient with myopathic presentation due to a new mutation in the interface domain. 2010 J. Inherit. Metab. Dis. pmid:20652410
Lee EH et al. A Korean female patient with thiamine-responsive pyruvate dehydrogenase complex deficiency due to a novel point mutation (Y161C)in the PDHA1 gene. 2006 J. Korean Med. Sci. pmid:17043409
Gerards M et al. Defective complex I assembly due to C20orf7 mutations as a new cause of Leigh syndrome. 2010 J. Med. Genet. pmid:19542079
Brautigam CA et al. Crystal structure of human dihydrolipoamide dehydrogenase: NAD+/NADH binding and the structural basis of disease-causing mutations. 2005 J. Mol. Biol. pmid:15946682
Vijayakrishnan S et al. Solution structure and characterisation of the human pyruvate dehydrogenase complex core assembly. 2010 J. Mol. Biol. pmid:20361979
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Katsuki H et al. Superoxide dismutase activity in organotypic midbrain-striatum co-cultures is associated with resistance of dopaminergic neurons to excitotoxicity. 2001 J. Neurochem. pmid:11238718
Klivenyi P et al. Mice deficient in dihydrolipoamide dehydrogenase show increased vulnerability to MPTP, malonate and 3-nitropropionic acid neurotoxicity. 2004 J. Neurochem. pmid:15009635
Starkov AA et al. Mitochondrial alpha-ketoglutarate dehydrogenase complex generates reactive oxygen species. 2004 J. Neurosci. pmid:15356189
Ramos EI et al. 2,3-diphenyl-1,4-naphthoquinone: a potential chemotherapeutic agent against Trypanosoma cruzi. 2009 J. Parasitol. pmid:18788881
Campanucci VA et al. A novel O2-sensing mechanism in rat glossopharyngeal neurones mediated by a halothane-inhibitable background K+ conductance. 2003 J. Physiol. (Lond.) pmid:12640017
Holbrook ED et al. Definition of the extracellular proteome of pathogenic-phase Histoplasma capsulatum. 2011 J. Proteome Res. pmid:21291285