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doi: 10.1038/329301a0
pmid: 2957598
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.
Base Sequence, DNA, Recombinant, Membrane Proteins, Receptors, Somatomedin, DNA, Receptor, IGF Type 2, Receptor, Insulin, Rats, Xenopus laevis, Sequence Homology, Nucleic Acid, Oocytes, Animals, Humans, Amino Acid Sequence, Carrier Proteins, Repetitive Sequences, Nucleic Acid
Base Sequence, DNA, Recombinant, Membrane Proteins, Receptors, Somatomedin, DNA, Receptor, IGF Type 2, Receptor, Insulin, Rats, Xenopus laevis, Sequence Homology, Nucleic Acid, Oocytes, Animals, Humans, Amino Acid Sequence, Carrier Proteins, Repetitive Sequences, Nucleic Acid
citations This is an alternative to the "Influence" indicator, which also reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically). | 940 | |
popularity This indicator reflects the "current" impact/attention (the "hype") of an article in the research community at large, based on the underlying citation network. | Top 1% | |
influence This indicator reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically). | Top 0.1% | |
impulse This indicator reflects the initial momentum of an article directly after its publication, based on the underlying citation network. | Top 0.1% |