The dimerization mechanism of the N-terminal domain of spider silk proteins is conserved despite extensive sequence divergence-Reference-Cited by-同舟云学术

The dimerization mechanism of the N-terminal domain of spider silk proteins is conserved despite extensive sequence divergence

Published:2022-05 Issue:5 Volume:298 Page:101913
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

Sarr Médoune,Kitoka Kristine,Walsh-White Kellie-Ann,Kaldmäe Margit,Metlāns Rimants,Tārs Kaspar,Mantese Alessandro,Shah Dipen,Landreh Michael,Rising Anna^ORCID,Johansson Jan,Jaudzems Kristaps,Kronqvist Nina

Funder

Center for Innovative Medicine

European Regional Development Fund

VINNOVA

Vetenskapsrådet

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference56 articles.

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3. Changes in fine structure during silk protein production in the ampullate gland of the spider Araneus sericatus;Bell;J. Cell Biol.,1969

4. Ultrastructure of the major ampullate gland of the black widow spider, Latrodectus hesperus;Casem;Tissue Cell,2002

5. Secondary structure transition and critical stress for a model of spider silk assembly;Giesa;Biomacromolecules,2016

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