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

Olfm1  -  olfactomedin 1

Rattus norvegicus

Synonyms: 1B426B, D2Sut1e, Neuronal olfactomedin-related ER localized protein, Noe1, Noel, ...
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.

High impact information on Olfm1

  • Interestingly, extracellular domain of latrophilin is homologous to olfactomedin, a soluble neuronal protein thought to participate in odorant binding [1].
  • In a recent paper (Brissette, L., and Noël, S.-P. (1986) J. Biol. Chem. 261, 6847-6852), we have demonstrated that human low density lipoproteins and high density lipoproteins-3 can totally prevent the specific binding of rat IDL to the low affinity binding sites [2].
  • Agene encoding olfactomedin-related glycoprotein was isolated from rat glomerulus despite its prior identification as a neuron-specific gene [3].
  • Immunogold electron microscopy revealed selective localization of olfactomedin-related glycoprotein at the Golgi apparatus in podocytes [3].
  • The AMZ and BMZ proteins show significant sequence similarity with olfactomedin, an extracellular matrix protein of bullfrog olfactory epithelium, suggesting the possibility of a matrix-related function for these rat glycoproteins in neurons and neurosecretory cells [4].

Anatomical context of Olfm1


  1. Alpha-latrotoxin receptor, latrophilin, is a novel member of the secretin family of G protein-coupled receptors. Lelianova, V.G., Davletov, B.A., Sterling, A., Rahman, M.A., Grishin, E.V., Totty, N.F., Ushkaryov, Y.A. J. Biol. Chem. (1997) [Pubmed]
  2. The effects of liposome-reconstituted apolipoproteins on the binding of rat intermediate density lipoproteins to rat liver membranes. Brissette, L., Roach, P.D., Noël, S.P. J. Biol. Chem. (1986) [Pubmed]
  3. Localization of olfactomedin-related glycoprotein isoform (BMZ) in the golgi apparatus of glomerular podocytes in rat kidneys. Kondo, D., Yamamoto, T., Yaoita, E., Danielson, P.E., Kobayashi, H., Ohshiro, K., Funaki, H., Koyama, Y., Fujinaka, H., Kawasaki, K., Sutcliffe, J.G., Arakawa, M., Kihara, I. J. Am. Soc. Nephrol. (2000) [Pubmed]
  4. Four structurally distinct neuron-specific olfactomedin-related glycoproteins produced by differential promoter utilization and alternative mRNA splicing from a single gene. Danielson, P.E., Forss-Petter, S., Battenberg, E.L., deLecea, L., Bloom, F.E., Sutcliffe, J.G. J. Neurosci. Res. (1994) [Pubmed]
  5. Analysis of the binding and association of human intermediate density lipoproteins to HepG2 cells. Brissette, L., Falstrault, L. Biochim. Biophys. Acta (1992) [Pubmed]
WikiGenes - Universities