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Purification and complementary-DNA cloning of a receptor for basic fibroblast growth-factor

Academic Article
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Overview

authors

  • Lee, Pauline
  • Johnson, D. E.
  • Cousens, L. S.
  • Fried, V. A.
  • Williams, L. T.

publication date

  • July 1989

journal

  • Science  Journal

abstract

  • Basic fibroblast growth factor (bFGF) participates in many processes including early developmental events, angiogenesis, wound healing, and maintenance of neuronal cell viability. A 130-kilodalton protein was isolated on the basis of its ability to specifically bind to bFGF. A complementary DNA clone was isolated with an oligonucleotide probe corresponding to determined amino acid sequences of tryptic peptide fragments of the purified protein. The putative bFGF receptor encoded by this complementary DNA is a transmembrane protein that contains three extracellular immunoglobulin-like domains, an unusual acidic region, and an intracellular tyrosine kinase domain. These domains are arranged in a pattern that is different from that of any growth factor receptor described.

subject areas

  • Amino Acid Sequence
  • Animals
  • Base Sequence
  • Cells, Cultured
  • Chick Embryo
  • Cloning, Molecular
  • DNA
  • Fibroblast Growth Factors
  • Kinetics
  • Mice
  • Molecular Sequence Data
  • Peptide Fragments
  • Receptors, Cell Surface
  • Receptors, Fibroblast Growth Factor
  • Recombinant Proteins
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Identity

International Standard Serial Number (ISSN)

  • 0036-8075

Digital Object Identifier (DOI)

  • 10.1126/science.2544996

PubMed ID

  • 2544996
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Additional Document Info

start page

  • 57

end page

  • 60

volume

  • 245

issue

  • 4913

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