Fibrillins, Fibulins, and Matrix-Associated Glycoprotein Modulate the Kinetics and Morphology of in Vitro Self-Assembly of a Recombinant Elastin-like Polypeptide-Reference-Cited by-同舟云学术

Fibrillins, Fibulins, and Matrix-Associated Glycoprotein Modulate the Kinetics and Morphology of in Vitro Self-Assembly of a Recombinant Elastin-like Polypeptide

Published:2008-10-31 Issue:47 Volume:47 Page:12601-12613
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Cirulis Judith T.¹,Bellingham Catherine M.¹,Davis Elaine C.¹,Hubmacher Dirk¹,Reinhardt Dieter P.¹,Mecham Robert P.¹,Keeley Fred W.¹

Affiliation:

1. Research Institute, The Hospital for Sick Children, Toronto, Canada, Department of Anatomy and Cell Biology, McGill University, Montréal, Canada, Faculty of Dentistry, McGill University, Montréal, Canada, and Department of Cell Biology and Physiology, Washington University School of Medicine, St. Louis, Missouri 63110

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi8005384

Reference49 articles.

1. Elastin

2. Microfibril-associated glycoprotein binds to the carboxyl-terminal domain of tropoelastin and is a substrate for transglutaminase.

3. Interaction of Tropoelastin with the Amino-terminal Domains of Fibrillin-1 and Fibrillin-2 Suggests a Role for the Fibrillins in Elastic Fiber Assembly

4. Protein Interaction Studies of MAGP-1 with Tropoelastin and Fibrillin-1

5. Fibulin-5/DANCE is essential for elastogenesis in vivo

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