Neryl diphosphate

Neryl diphosphate is a lipid of Prenol Lipids (PR) class. The involved functions are known as Phenomenon. Neryl diphosphate often locates in Chloroplasts and Head. The associated genes with Neryl diphosphate are IPP gene.

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Introduction

To understand associated biological information of Neryl diphosphate, 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 Neryl diphosphate?

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

No disease MeSH terms mapped to the current reference collection.

PubChem Associated disorders and diseases

What pathways are associated with Neryl diphosphate

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

PubChem Biomolecular Interactions and Pathways

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What cellular locations are associated with Neryl diphosphate?

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What functions are associated with Neryl diphosphate?


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What lipids are associated with Neryl diphosphate?

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

What genes are associated with Neryl diphosphate?

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Gene Cross reference Weighted score Related literatures

What common seen animal models are associated with Neryl diphosphate?

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

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All references with Neryl diphosphate

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Authors Title Published Journal PubMed Link
Hallahan TW and Croteau R Monoterpene biosynthesis: mechanism and stereochemistry of the enzymatic cyclization of geranyl pyrophosphate to (+)-cis- and (+)-trans-sabinene hydrate. 1989 Arch. Biochem. Biophys. pmid:2916845
Light DR and Dennis MS Purification of a prenyltransferase that elongates cis-polyisoprene rubber from the latex of Hevea brasiliensis. 1989 J. Biol. Chem. pmid:2808388
Light DR et al. Rubber elongation by farnesyl pyrophosphate synthases involves a novel switch in enzyme stereospecificity. 1989 J. Biol. Chem. pmid:2808389
Wheeler CJ et al. Uncompetitive inhibition of monoterpene cyclases by an analog of the substrate geranyl pyrophosphate and inhibition of monoterpene biosynthesis in vivo by an analog of geraniol. 1990 Arch. Biochem. Biophys. pmid:2350172
Croteau R et al. Biosynthesis of monoterpenes: stereochemistry of the coupled isomerization and cyclization of geranyl pyrophosphate to camphane and isocamphane monoterpenes. 1990 Arch. Biochem. Biophys. pmid:2178556
Oulmouden A and Karst F Nucleotide sequence of the ERG12 gene of Saccharomyces cerevisiae encoding mevalonate kinase. 1991 Curr. Genet. pmid:1645230
Lewinsohn E et al. Wound-inducible pinene cyclase from grand fir: purification, characterization, and renaturation after SDS-PAGE. 1992 Arch. Biochem. Biophys. pmid:1731633
Ericsson J et al. Substrate specificity of cis-prenyltransferase in rat liver microsomes. 1992 J. Biol. Chem. pmid:1527094
Alonso WR et al. Purification of 4S-limonene synthase, a monoterpene cyclase from the glandular trichomes of peppermint (Mentha x piperita) and spearmint (Mentha spicata). 1992 J. Biol. Chem. pmid:1559995
McGeady P et al. Biosynthesis of monoterpenes: inhibition of (+)-pinene and (-)-pinene cyclases by thia and aza analogs of the 4R- and 4S-alpha-terpinyl carbocation. 1992 Arch. Biochem. Biophys. pmid:1444453