Dl-leucine

Dl-leucine 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 544 references associated with Dl-leucine 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 Dl-leucine

Possible diseases from mapped MeSH terms on references

We collected disease MeSH terms mapped to the references associated with Dl-leucine

MeSH term MeSH ID Detail
Nerve Degeneration D009410 53 associated lipids
Myoclonic Epilepsies, Progressive D020191 3 associated lipids
Communicable Diseases, Emerging D021821 3 associated lipids
Influenza in Birds D005585 1 associated lipids
Total 4

NCBI Entrez Crosslinks

All references with Dl-leucine

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Authors Title Published Journal PubMed Link
Porter MJ et al. Polyamino acids as catalysts in asymmetric synthesis. 1999 Bioorg. Med. Chem. pmid:10579519
Efremov RG et al. A solvent model for simulations of peptides in bilayers. I. Membrane-promoting alpha-helix formation. 1999 Biophys. J. pmid:10233062
Monné M et al. Positively and negatively charged residues have different effects on the position in the membrane of a model transmembrane helix. 1998 J. Mol. Biol. pmid:9837735
Chipot C and Pohorille A Folding and translocation of the undecamer of poly-L-leucine across the water-hexane interface. A molecular dynamics study. 1998 J. Am. Chem. Soc. pmid:11542762
Lew S and London E Simple procedure for reversed-phase high-performance liquid chromatographic purification of long hydrophobic peptides that form transmembrane helices. 1997 Anal. Biochem. pmid:9300091
Hatsuzawa K et al. The hydrophobic region of signal peptides is a determinant for SRP recognition and protein translocation across the ER membrane. 1997 J. Biochem. pmid:9089400
Takei T et al. Characterization of poly-leucine substituted analogues of the human surfactant protein SP-C. 1996 Biol. Pharm. Bull. pmid:8996637
Whitley P et al. A 12-residue-long polyleucine tail is sufficient to anchor synaptobrevin to the endoplasmic reticulum membrane. 1996 J. Biol. Chem. pmid:8631791
Oliver AE and Deamer DW Alpha-helical hydrophobic polypeptides form proton-selective channels in lipid bilayers. 1994 Biophys. J. pmid:7520289
Lemmon MA et al. A dimerization motif for transmembrane alpha-helices. 1994 Nat. Struct. Biol. pmid:7656033