Get 20M+ Full-Text Papers For Less Than $1.50/day. Start a 14-Day Trial for You or Your Team.

Learn More →

1H, 13C and 15N chemical shift assignments of Ninjurin1 Extracellular N-terminal Domain

1H, 13C and 15N chemical shift assignments of Ninjurin1 Extracellular N-terminal Domain Cell adhesion molecules play a crucial role in fundamental biological processes via regulating cell–cell interactions. Nerve injury induced protein1 (Ninjurin1) is a novel adhesion protein that has no significant homology with other known cell adhesion molecules. Here we present the assignment of an 81 aa construct for human Ninjurin1 Extracellular N-Terminal (ENT) domain, which comprises the critical adhesion domain. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Biomolecular NMR Assignments Springer Journals

1H, 13C and 15N chemical shift assignments of Ninjurin1 Extracellular N-terminal Domain

Loading next page...
 
/lp/springer-journals/1h-13c-and-15n-chemical-shift-assignments-of-ninjurin1-extracellular-n-i7xHxwzv9W

References (19)

Publisher
Springer Journals
Copyright
Copyright © 2012 by Springer Science+Business Media B.V.
Subject
Physics; Biophysics and Biological Physics; Polymer Sciences; Biochemistry, general
ISSN
1874-2718
eISSN
1874-270X
DOI
10.1007/s12104-012-9400-3
pmid
22696136
Publisher site
See Article on Publisher Site

Abstract

Cell adhesion molecules play a crucial role in fundamental biological processes via regulating cell–cell interactions. Nerve injury induced protein1 (Ninjurin1) is a novel adhesion protein that has no significant homology with other known cell adhesion molecules. Here we present the assignment of an 81 aa construct for human Ninjurin1 Extracellular N-Terminal (ENT) domain, which comprises the critical adhesion domain.

Journal

Biomolecular NMR AssignmentsSpringer Journals

Published: Jun 15, 2012

There are no references for this article.