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?

Related references are published most in these journals:


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.

NCBI Entrez Crosslinks

All references with Neryl diphosphate

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Authors Title Published Journal PubMed Link
Ericsson J et al. Substrate specificity of cis-prenyltransferase in rat liver microsomes. 1992 J. Biol. Chem. pmid:1527094
Croteau R et al. Biosynthesis of monoterpenes. Stereochemistry of the enzymatic cyclization of geranyl pyrophosphate to (-)-endo-fenchol. 1988 J. Biol. Chem. pmid:3170591
Croteau R et al. Stereochemistry at C-1 of geranyl pyrophosphate and neryl pyrophosphate in the cyclization to (+)- and (-)-bornyl pyrophosphate. 1985 J. Biol. Chem. pmid:3997807
Gambliel H and Croteau R Pinene cyclases I and II. Two enzymes from sage (Salvia officinalis) which catalyze stereospecific cyclizations of geranyl pyrophosphate to monoterpene olefins of opposite configuration. 1984 J. Biol. Chem. pmid:6693393
Gambliel H and Croteau R Biosynthesis of (+/-)-alpha-pinene and (-)-beta-pinene from geranyl pyrophosphate by a soluble enzyme system from sage (Salvia officinalis). 1982 J. Biol. Chem. pmid:7037765
Wise ML et al. Monoterpene synthases from common sage (Salvia officinalis). cDNA isolation, characterization, and functional expression of (+)-sabinene synthase, 1,8-cineole synthase, and (+)-bornyl diphosphate synthase. 1998 J. Biol. Chem. pmid:9614092
Burke C and Croteau R Interaction with the small subunit of geranyl diphosphate synthase modifies the chain length specificity of geranylgeranyl diphosphate synthase to produce geranyl diphosphate. 2002 J. Biol. Chem. pmid:11733504
Montalvetti A et al. Bisphosphonates are potent inhibitors of Trypanosoma cruzi farnesyl pyrophosphate synthase. 2001 J. Biol. Chem. pmid:11435429
Wagner PD and Vu ND Phosphorylation of geranyl and farnesyl pyrophosphates by Nm23 proteins/nucleoside diphosphate kinases. 2000 J. Biol. Chem. pmid:10952986
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