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.

Cross Reference

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

Link to PubChem Biomolecular Interactions and Pathways

What cellular locations are associated with Neryl diphosphate?

Related references are published most in these journals:

Location Cross reference Weighted score Related literatures
Loading... please refresh the page if content is not showing up.

What functions are associated with Neryl diphosphate?


Related references are published most in these journals:

Function Cross reference Weighted score Related literatures

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

Download all related citations
Per page 10 20 50 100 | Total 76
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
Satterwhite DM et al. Biosynthesis of monoterpenes. Enantioselectivity in the enzymatic cyclization of linalyl pyrophosphate to (-)-endo-fenchol. 1985 J. Biol. Chem. pmid:4055764
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
Croteau R et al. Biosynthesis of monoterpenes. Stereochemistry of the enzymatic cyclizations of geranyl pyrophosphate to (+)-alpha-pinene and (-)-beta-pinene. 1989 J. Biol. Chem. pmid:2644252
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
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
Light DR et al. Rubber elongation by farnesyl pyrophosphate synthases involves a novel switch in enzyme stereospecificity. 1989 J. Biol. Chem. pmid:2808389
Fujisaki S et al. Biosynthesis of isoprenoids in intact cells of Escherichia coli. 1986 J. Biochem. pmid:3519600
Takahashi I and Ogura K Farnesyl pyrophosphate synthetase from Bacillus subtilis. 1981 J. Biochem. pmid:6792191
Du CQ et al. Inhibition of farnesyl pyrophosphate synthase prevents norepinephrine-induced fibrotic responses in vascular smooth muscle cells from spontaneously hypertensive rats. 2014 Hypertens. Res. pmid:23985701
Oulmouden A and Karst F Nucleotide sequence of the ERG12 gene of Saccharomyces cerevisiae encoding mevalonate kinase. 1991 Curr. Genet. pmid:1645230
Bhardwaj S et al. Muscular effects of statins in the elderly female: a review. 2013 Clin Interv Aging pmid:23355775
Singh RS et al. Expression of 3-hydroxy-3-methylglutaryl-CoA reductase, p-hydroxybenzoate-m-geranyltransferase and genes of phenylpropanoid pathway exhibits positive correlation with shikonins content in arnebia [Arnebia euchroma (Royle) Johnston]. 2010 BMC Mol. Biol. pmid:21092138
De Schutter JW et al. Novel bisphosphonate inhibitors of the human farnesyl pyrophosphate synthase. 2010 Bioorg. Med. Chem. Lett. pmid:20801032
Hagiwara K et al. Analysis of the molecular interaction of the farnesyl moiety of transducin through the use of a photoreactive farnesyl analogue. 2004 Biochemistry pmid:14717583