An N-Linked Glycosylation Motif from the Noncleaving Luteinizing Hormone Receptor Substituted for the Homologous Region (Gly367 to Glu369) of the Thyrotropin Receptor Prevents Cleavage at Its Second, Downstream Site-Reference-Cited by-同舟云学术

An N-Linked Glycosylation Motif from the Noncleaving Luteinizing Hormone Receptor Substituted for the Homologous Region (Gly367 to Glu369) of the Thyrotropin Receptor Prevents Cleavage at Its Second, Downstream Site

Published:1997-11 Issue:45 Volume:272 Page:28296-28300
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

Kakinuma Ayumu,Chazenbalk Gregorio D.,Tanaka Kunihiko,Nagayama Yuji,McLachlan Sandra M.,Rapoport Basil

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference30 articles.

1. Composite structure of the human thyrotropin receptor gene

2. Structural organization of the rat luteinizing hormone (LH) receptor gene

3. Structure of the Luteinizing Hormone Receptor Gene and Multiple Exons of the Coding Sequence*

4. Photoaffinity labelling of the TSH receptor on FRTL5, cells

5. A New Structural Model for the Thyrotropin (TSH) Receptor, as Determined by Covalent Cross-Linking of TSH to the Recombinant Receptor in Intact Cells: Evidence for a Single Polypeptide Chain

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