2-bromoacetic acid

2-bromoacetic acid is a lipid of Fatty Acyls (FA) class.

Cross Reference

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

Current reference collection contains 872 references associated with 2-bromoacetic acid in LipidPedia. Due to lack of full text of references or no associated biomedical terms are recognized in our current text-mining method, we cannot extract any biomedical terms related to diseases, pathways, locations, functions, genes, lipids, and animal models from the associated reference collection.

Users can download the reference list at the bottom of this page and read the reference manually to find out biomedical information.


Here are additional resources we collected from PubChem and MeSH for 2-bromoacetic acid

Possible diseases from mapped MeSH terms on references

We collected disease MeSH terms mapped to the references associated with 2-bromoacetic acid

MeSH term MeSH ID Detail
Body Weight D001835 333 associated lipids
Liver Neoplasms, Experimental D008114 46 associated lipids
Neuroblastoma D009447 66 associated lipids
Total 3

PubChem Biomolecular Interactions and Pathways

NCBI Entrez Crosslinks

All references with 2-bromoacetic acid

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Authors Title Published Journal PubMed Link
Tubić A et al. Insight into changes during coagulation in NOM reactivity for trihalomethanes and haloacetic acids formation. 2013 J. Environ. Manage. pmid:23428464
German DP and Bittong RA Digestive enzyme activities and gastrointestinal fermentation in wood-eating catfishes. 2009 J. Comp. Physiol. B, Biochem. Syst. Environ. Physiol. pmid:19568757
Ito Y et al. Studies on an abnormally sharpened elution peak observed in counter-current chromatography. 1992 J. Chromatogr. pmid:1474121
Baran DT et al. Binding of 1alpha,25-dihydroxyvitamin D(3) to annexin II: effect of vitamin D metabolites and calcium. 2000 J. Cell. Biochem. pmid:11074597
Baran DT et al. Annexin II is the membrane receptor that mediates the rapid actions of 1alpha,25-dihydroxyvitamin D(3). 2000 J. Cell. Biochem. pmid:10797564
Guo L et al. The effect of histidine residue modification on tyrosinase activity and conformation: inhibition kinetics and computational prediction. 2008 J. Biomol. Struct. Dyn. pmid:18808205
Chambers JE et al. The reduction potential of the active site disulfides of human protein disulfide isomerase limits oxidation of the enzyme by Ero1α. 2010 J. Biol. Chem. pmid:20657012
Ghisla S et al. Covalent adducts of lactate oxidase. Photochemical formation and structure identification. 1979 J. Biol. Chem. pmid:500603
Chin CC and Warren JC Synthesis of 16alpha-bromoacetoxyestradiol 3-methyl ether and study of the steroid binding site of human placental estradiol 17beta-dehydrogenase. 1975 J. Biol. Chem. pmid:1176443
Goux WJ and Allerhand A Studies of chemically modified histidine residues of proteins by carbon 13 nuclear magnetic resonance spectroscopy. Reaction of hen egg white lysozyme with iodoacetate. 1979 J. Biol. Chem. pmid:34602