One short cysteine-rich sequence pattern - two different disulfide-bonded structures - a molecular dynamics simulation study-Reference-Cited by-同舟云学术

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One short cysteine-rich sequence pattern - two different disulfide-bonded structures - a molecular dynamics simulation study

Published:2015-03-17 Issue:6 Volume:21 Page:480-494
ISSN:1075-2617
Container-title:Journal of Peptide Science
language:en
Short-container-title:J. Pept. Sci.

Author:

Dames Sonja A.¹²^ORCID

Affiliation:

1. Biomolecular NMR Spectroscopy, Department of Chemistry; Technische Universität München; 85747 Garching Germany

2. Helmholtz Zentrum München; Germany and Institute of Structural Biology; Ingolstädter Landstr. 1 85764 Neuherberg Germany

Funder

German Research Foundation to S.A.D.

Swiss National Science Foundation

Publisher

Wiley

Subject

Organic Chemistry,Drug Discovery,Pharmacology,Molecular Biology,Molecular Medicine,General Medicine,Biochemistry,Structural Biology

Link

http://onlinelibrary.wiley.com/wol1/doi/10.1002/psc.2765/fullpdf

Reference43 articles.

1. The glycoprotein NOWA and minicollagens are part of a disulfide-linked polymer that forms the cnidarian nematocyst wall;Özbek;J. Biol. Chem.,2004

2. Versatile collagens in invertebrates;Engel;Science,1997

3. Structure/function relationships in the minicollagen of Hydra nematocysts;Özbek;J. Biol. Chem.,2002

4. Determination of a high-precision NMR structure of the minicollagen cysteine rich domain from Hydra and characterization of its disulfide bond formation;Meier;FEBS Lett.,2004

5. Single proline residues can dictate the oxidative folding pathways of cysteine-rich peptides;Boulègue;J. Mol. Biol.,2006

Cited by 1 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. Minicollagen cysteine-rich domains encode distinct modes of polymerization to form stable nematocyst capsules;Scientific Reports;2016-05-11

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