Subunit structure of the purified human placental insulin receptor. Intramolecular subunit dissociation by sodium dodecyl sulfate-polyacrylamide gel electrophoresis.-Reference-Cited by-同舟云学术

Subunit structure of the purified human placental insulin receptor. Intramolecular subunit dissociation by sodium dodecyl sulfate-polyacrylamide gel electrophoresis.

Published:1985-07 Issue:14 Volume:260 Page:8593-8600
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

Boyle T R,Campana J,Sweet L J,Pessin J E

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference36 articles.

1. Insulin Receptors

2. Molecular Basis of Insulin Action;Pessin,1985

3. Insulin receptor: covalent labeling and identification of subunits.

4. Photoaffinity labeling of insulin receptor proteins of liver plasma membrane preparations

5. The subunit structure of the high affinity insulin receptor. Evidence for a disulfide-linked receptor complex in fat cell and liver plasma membranes.

Cited by 22 articles. 订阅此论文施引文献订阅此论文施引文献，注册后可以免费订阅5篇论文的施引文献，订阅后可以查看论文全部施引文献

1. Transmembrane signaling by the human insulin receptor kinase. Relationship between intramolecular beta subunit trans- and cis-autophosphorylation and substrate kinase activation.;Journal of Biological Chemistry;1992-09

2. Cysteine 647 in the insulin receptor is required for normal covalent interaction between alpha- and beta-subunits and signal transduction.;Journal of Biological Chemistry;1992-04

3. Analysis of the Human Insulin Receptor;Biological Chemistry Hoppe-Seyler;1992-01

4. Evidence supporting a passive role for the insulin receptor transmembrane domain in insulin-dependent signal transduction;Journal of Biological Chemistry;1991-05

5. High affinity insulin binding in the human placenta insulin receptor requires αβ heterodimeric subunit interactions;The Journal of Membrane Biology;1989-06