Prolyl hydroxylation in elastin is not random-Reference-Cited by-同舟云学术

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Prolyl hydroxylation in elastin is not random

Published:2016-10 Issue:10 Volume:1860 Page:2169-2177
ISSN:0304-4165
Container-title:Biochimica et Biophysica Acta (BBA) - General Subjects
language:en
Short-container-title:Biochimica et Biophysica Acta (BBA) - General Subjects

Author:

Schmelzer Christian E.H.,Nagel Marcus B.M.,Dziomba Szymon,Merkher Yulia,Sivan Sarit S.,Heinz Andrea

Funder

German Research Foundation (DFG)

Publisher

Elsevier BV

Subject

Molecular Biology,Biochemistry,Biophysics

Reference60 articles.

1. Protein posttranslational modifications: the chemistry of proteome diversifications;Walsh;Angew. Chem. Int. Ed.,2005

2. Proteome-wide post-translational modification statistics: frequency analysis and curation of the swiss-prot database;Khoury;Sci. Rep.,2011

3. Enzymatic and nonenzymatic cross-linking of collagen and elastin;Reiser;FASEB J.,1992

4. Lysyl hydroxylase 2 is a specific telopeptide hydroxylase, while all three isoenzymes hydroxylate collagenous sequences;Takaluoma;Matrix Biol.,2007

5. Location of 3-hydroxyproline residues in collagen types I, II, III, and V/XI implies a role in fibril supramolecular assembly;Weis;J. Biol. Chem.,2010

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