Solution Structure of a Conformationally Restricted Fully Active Derivative of the Human Relaxin-like Factor-Reference-Cited by-同舟云学术

Solution Structure of a Conformationally Restricted Fully Active Derivative of the Human Relaxin-like Factor

Published:2008-11-20 Issue:50 Volume:47 Page:13308-13317
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Büllesbach Erika E.¹,Hass Mathias A. S.¹,Jensen Malene R.¹,Hansen D. Flemming¹,Kristensen Søren M.¹,Schwabe Christian¹,Led Jens J.¹

Affiliation:

1. Department of Biochemistry and Molecular Biology, Medical University of South Carolina, 173 Ashley Avenue, P.O. Box 250509, Charleston, South Carolina 29425, and Department of Chemistry, University of Copenhagen, Universitetsparken 5, DK-2100 Copenhagen Ø, Denmark

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi801412w

Reference64 articles.

1. The disulphide bonds of insulin

2. The amino acid sequence of human insulin-like growth factor I and its structural homology with proinsulin.

3. Relaxin: A Disulfide Homolog of Insulin

4. Relaxin and its structural relationship to insulin

5. Cloning of a cDNA for a novel insulin-like peptide of the testicular Leydig cells.

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