Expression of meltrin-α mRNA is not restricted to fusagenic cells

This publication has 10 references indexed in Scilit:

• ADM-1, a protein with metalloprotease- and disintegrin-like domains, is expressed in syncytial organs, sperm, and sheath cells of sensory organs in Caenorhabditis elegans.
  Molecular Biology of the Cell, 1996
• In situ hybridization analysis of the distribution of neurokinin-3 mRNA in the rat central nervous system
  Journal of Comparative Neurology, 1996
• H+-induced Membrane Insertion of Influenza Virus Hemagglutinin Involves the HA2 Amino-terminal Fusion Peptide but Not the Coiled Coil Region
  Journal of Biological Chemistry, 1996
• ADAM, a novel family of membrane proteins containing A Disintegrin And Metalloprotease domain: multipotential functions in cell-cell and cell-matrix interactions.
  The Journal of cell biology, 1995
• Making one cell from two
  Nature, 1995
• A metalloprotease-disintegrin participating in myoblast fusion
  Nature, 1995
• Identification of a binding site in the disintegrin domain of fertilin required for sperm-egg fusion.
  Proceedings of the National Academy of Sciences, 1994
• The precursor region of a protein active in sperm-egg fusion contains a metalloprotease and a disintegrin domain: structural, functional, and evolutionary implications.
  Proceedings of the National Academy of Sciences, 1993
• A potential fusion peptide and an integrin ligand domain in a protein active in sperm–egg fusion
  Nature, 1992
• Factors that promote progressive development of the osteoblast phenotype in cultured fetal rat calvaria cells
  Journal of Cellular Physiology, 1990