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- Erratum in:
- Nature 1988 Jul;20(7):442.
Insulin-like growth factor II receptor as a multifunctional binding protein.
The primary structure of human insulin-like growth factor II receptor, predicted from the complementary DNA sequence, reveals a transmembrane receptor molecule with a large extracellular domain made up of fifteen repeat sequences and a small region homologous to the collagen-binding domain of fibronectin. The structural and biochemical features of the IGF-II receptor appear identical to those of the cation-independent mannose-6-phosphate receptor.
PMID: 2957598 [PubMed - indexed for MEDLINE]
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Cited by 82 PubMed Central articles
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ReviewMultifunctional roles of insulin-like growth factor binding protein 5 in breast cancer.
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Up-regulation of cation-independent mannose 6-phosphate receptor and endosomal-lysosomal markers in surviving neurons after 192-IgG-saporin administrations into the adult rat brain.
Hawkes C, Kabogo D, Amritraj A, Kar S.
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[Am J Pathol. 2006]
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Identification of the insulin-like growth factor II receptor as a novel receptor for binding and invasion by Listeria monocytogenes.
Gasanov U, Koina C, Beagley KW, Aitken RJ, Hansbro PM.
Infect Immun. 2006 Jan; 74(1):566-77.
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