The world's first wiki where authorship really matters (Nature Genetics, 2008). Due credit and reputation for authors. Imagine a global collaborative knowledge base for original thoughts. Search thousands of articles and collaborate with scientists around the globe.

wikigene or wiki gene protein drug chemical gene disease author authorship tracking collaborative publishing evolutionary knowledge reputation system wiki2.0 global collaboration genes proteins drugs chemicals diseases compound
Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
Gene Review

OR10B1P  -  olfactory receptor, family 10, subfamily B...

Homo sapiens

Welcome! If you are familiar with the subject of this article, you can contribute to this open access knowledge base by deleting incorrect information, restructuring or completely rewriting any text. Read more.

Disease relevance of OR10B1P


High impact information on OR10B1P

  • Acetohydroxyacid synthase (AHAS) (acetolactate synthase, EC ) catalyzes the first step in branched-chain amino acid biosynthesis and is the target for sulfonylurea and imidazolinone herbicides [4].
  • A naturally occurring point mutation confers broad range tolerance to herbicides that target acetolactate synthase [5].
  • We have investigated the molecular basis of imidazolinone tolerance of two field isolates of cocklebur (Xanthium sp.) from Mississippi and Missouri. In both cases, tolerance was conferred by a form of ALS that was less sensitive to inhibitors than the wild type [6].
  • ALS inhibition caused an increase of the alternative oxidase (AOX) protein and an accumulation of pyruvate [7].
  • The adaptation of the respiratory metabolism in roots of soybean (Glycine max L. Merr. cv Ransom) treated with herbicides that inhibit the enzyme acetolactate synthase (ALS) was analyzed [7].

Biological context of OR10B1P


Anatomical context of OR10B1P

  • Results showed that mixtures of herbicides with similar molecular targets, i.e. chlorsulfuron and metsulfuron (acetolactate synthase (ALS) inhibitors), and with different molecular targets, i.e. pendimethalin (microtubule assembly inhibitor) and pretilachlor (very long chain fatty acids (VLCFAs) inhibitor), followed the ADM [12].

Associations of OR10B1P with chemical compounds


Other interactions of OR10B1P


  1. Oxygen toxicity from plants to people. Schloss, J.V. Planta (2002) [Pubmed]
  2. Attenuation regulation of amino acid biosynthetic operons in proteobacteria: comparative genomics analysis. Vitreschak, A.G., Lyubetskaya, E.V., Shirshin, M.A., Gelfand, M.S., Lyubetsky, V.A. FEMS Microbiol. Lett. (2004) [Pubmed]
  3. Response of the bacteria and fungi of two soils to the sulfonylurea herbicide cinosulfuron. Allievi, L., Gigliotti, C. Journal of environmental science and health. Part. B, Pesticides, food contaminants, and agricultural wastes. (2001) [Pubmed]
  4. Molecular basis of sulfonylurea herbicide inhibition of acetohydroxyacid synthase. Pang, S.S., Guddat, L.W., Duggleby, R.G. J. Biol. Chem. (2003) [Pubmed]
  5. A naturally occurring point mutation confers broad range tolerance to herbicides that target acetolactate synthase. Bernasconi, P., Woodworth, A.R., Rosen, B.A., Subramanian, M.V., Siehl, D.L. J. Biol. Chem. (1996) [Pubmed]
  6. A naturally occurring point mutation confers broad range tolerance to herbicides that target acetolactate synthase. Bernasconi, P., Woodworth, A.R., Rosen, B.A., Subramanian, M.V., Siehl, D.L. J. Biol. Chem. (1995) [Pubmed]
  7. Changes in mitochondrial electron partitioning in response to herbicides inhibiting branched-chain amino acid biosynthesis in soybean. Gaston, S., Ribas-Carbo, M., Busquets, S., Berry, J.A., Zabalza, A., Royuela, M. Plant Physiol. (2003) [Pubmed]
  8. Three-dimensional quantitative structure-activity relationship analysis of the new potent sulfonylureas using comparative molecular similarity indices analysis. Hou, T.J., Li, Z.M., Li, Z., Liu, J., Xu, X.J. Journal of chemical information and computer sciences. (2000) [Pubmed]
  9. Mutant acetolactate synthase gene is an efficient in vitro selectable marker for the genetic transformation of Brassica juncea (oilseed mustard). Ray, K., Jagannath, A., Gangwani, S.A., Burma, P.K., Pental, D. J. Plant Physiol. (2004) [Pubmed]
  10. Detection of resistance to acetolactate synthase inhibitors in weeds with emphasis on DNA-based techniques: a review. Corbett, C.A., Tardif, F.J. Pest Manag. Sci. (2006) [Pubmed]
  11. Common and distinct gene expression patterns induced by the herbicides 2,4-dichlorophenoxyacetic acid, cinidon-ethyl and tribenuron-methyl in wheat. Pasquer, F., Ochsner, U., Zarn, J., Keller, B. Pest Manag. Sci. (2006) [Pubmed]
  12. Activities of mixtures of soil-applied herbicides with different molecular targets. Kaushik, S., Streibig, J.C., Cedergreen, N. Pest Manag. Sci. (2006) [Pubmed]
  13. Molecular basis for multiple resistance to acetolactate synthase-inhibiting herbicides and atrazine in Amaranthus blitoides (prostrate pigweed). Sibony, M., Rubin, B. Planta (2003) [Pubmed]
  14. Evolution of herbicide resistance in weeds: initial frequency of target site-based resistance to acetolactate synthase-inhibiting herbicides in Lolium rigidum. Preston, C., Powles, S.B. Heredity (2002) [Pubmed]
  15. Cryptococcus neoformans Ilv2p confers resistance to sulfometuron methyl and is required for survival at 37 degrees C and in vivo. Kingsbury, J.M., Yang, Z., Ganous, T.M., Cox, G.M., McCusker, J.H. Microbiology (Reading, Engl.) (2004) [Pubmed]
  16. Pattern recognition analysis of endogenous cell metabolites for high throughput mode of action identification: removing the postscreening dilemma associated with whole-organism high throughput screening. Hole, S.J., Howe, P.W., Stanley, P.D., Hadfield, S.T. Journal of biomolecular screening : the official journal of the Society for Biomolecular Screening. (2000) [Pubmed]
  17. Metabolism-based resistance of a wild mustard (Sinapis arvensis L.) biotype to ethametsulfuron-methyl. Veldhuis, L.J., Hall, L.M., O'Donovan, J.T., Dyer, W., Hall, J.C. J. Agric. Food Chem. (2000) [Pubmed]
  18. A human homolog of bacterial acetolactate synthase genes maps within the CADASIL critical region. Joutel, A., Ducros, A., Alamowitch, S., Cruaud, C., Domenga, V., Maréchal, E., Vahedi, K., Chabriat, H., Bousser, M.G., Tournier-Lasserve, E. Genomics (1996) [Pubmed]
WikiGenes - Universities