lipoamide

Lipoamide is a lipid of Fatty Acyls (FA) class. Lipoamide is associated with abnormalities such as Wiskott-Aldrich Syndrome. The involved functions are known as Phosphorylation, Protonation, Mutagenesis, Site-Directed, Oxidants and Acetylation. Lipoamide often locates in Mitochondria, Mitochondrial matrix, nucleocapsid location and Chloroplasts. The associated genes with lipoamide are Mutant Proteins, Recombinant Proteins, mycothione reductase, alanylproline and Genes, Mitochondrial.

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Introduction

To understand associated biological information of lipoamide, 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 lipoamide?

lipoamide 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 lipoamide

MeSH term MeSH ID Detail
Body Weight D001835 333 associated lipids
Liver Cirrhosis, Biliary D008105 12 associated lipids
Nerve Degeneration D009410 53 associated lipids
Prostatic Neoplasms D011471 126 associated lipids
Hyperglycinemia, Nonketotic D020158 2 associated lipids
Total 5

PubChem Associated disorders and diseases

What pathways are associated with lipoamide

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 lipoamide?

Related references are published most in these journals:

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


Related references are published most in these journals:

Function Cross reference Weighted score Related literatures

What lipids are associated with lipoamide?

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

What genes are associated with lipoamide?

Related references are published most in these journals:


Gene Cross reference Weighted score Related literatures

What common seen animal models are associated with lipoamide?

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

NCBI Entrez Crosslinks

All references with lipoamide

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Authors Title Published Journal PubMed Link
Song JL et al. Encapsulation of an 86-kDa assembly intermediate inside the cavities of GroEL and its single-ring variant SR1 by GroES. 2003 J. Biol. Chem. pmid:12431983
Wynn RM et al. Roles of active site and novel K+ ion-binding site residues in human mitochondrial branched-chain alpha-ketoacid decarboxylase/dehydrogenase. 2001 J. Biol. Chem. pmid:11069910
Nemeria N et al. Glutamate 636 of the Escherichia coli pyruvate dehydrogenase-E1 participates in active center communication and behaves as an engineered acetolactate synthase with unusual stereoselectivity. 2005 J. Biol. Chem. pmid:15802265
Cabiscol E et al. Oxidative stress promotes specific protein damage in Saccharomyces cerevisiae. 2000 J. Biol. Chem. pmid:10852912
Wynn RM et al. Roles of His291-alpha and His146-beta' in the reductive acylation reaction catalyzed by human branched-chain alpha-ketoacid dehydrogenase: refined phosphorylation loop structure in the active site. 2003 J. Biol. Chem. pmid:12902323
Kale S et al. A dynamic loop at the active center of the Escherichia coli pyruvate dehydrogenase complex E1 component modulates substrate utilization and chemical communication with the E2 component. 2007 J. Biol. Chem. pmid:17635929
Gazaryan IG et al. Zinc irreversibly damages major enzymes of energy production and antioxidant defense prior to mitochondrial permeability transition. 2007 J. Biol. Chem. pmid:17565998
Klyachko NL et al. pH-dependent substrate preference of pig heart lipoamide dehydrogenase varies with oligomeric state: response to mitochondrial matrix acidification. 2005 J. Biol. Chem. pmid:15710613
Argyrou A et al. Characterization of a new member of the flavoprotein disulfide reductase family of enzymes from Mycobacterium tuberculosis. 2004 J. Biol. Chem. pmid:15456792
Li J et al. The two active sites in human branched-chain alpha-keto acid dehydrogenase operate independently without an obligatory alternating-site mechanism. 2007 J. Biol. Chem. pmid:17329260