The nature of the conserved basic amino acid sequences found among 437 heparin binding proteins determined by network analysis-Reference-Cited by-同舟云学术

The nature of the conserved basic amino acid sequences found among 437 heparin binding proteins determined by network analysis

Published:2017 Issue:5 Volume:13 Page:852-865
ISSN:1742-206X
Container-title:Molecular BioSystems
language:en
Short-container-title:Mol. BioSyst.

Author:

Rudd Timothy R.¹²³⁴⁵^ORCID,Preston Mark D.¹²³,Yates Edwin A.⁴⁵³

Affiliation:

1. The National Institute for Biological Standards and Control (NIBSC)

2. Hertfordshire EN6 3QG

3. UK

4. Department of Biochemistry, Institute of Integrative Biology, University of Liverpool

5. Liverpool

Abstract

Heparin/HS binding sites on proteins are composed of manifold small and flexible, basic amino acid sequences, that occur in many members of the proteome.

Publisher

Royal Society of Chemistry (RSC)

Subject

Molecular Biology,Biotechnology

Link

http://pubs.rsc.org/en/content/articlepdf/2017/MB/C6MB00857G

Reference56 articles.

1. Heparin and heparan sulfate: structure and function

2. Heparan Sulfate Proteoglycans

3. Proteoglycans: from structural compounds to signaling molecules

4. Nuclear translocation of heparan sulfate proteoglycans and their functional significance

5. Heparan sulfate in the nucleus and its control of cellular functions

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