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...

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Published inBiomolecular NMR assignments Vol. 7; no. 2; pp. 159 - 162
Main Authors Lee, In-Gyun, Jang, Sun-Bok, Kim, Ji-Hun, Lee, Ki-Young, Lee, Kyu-Yeon, Cheong, Hae-Kap, Lee, Bong-Jin
Format Journal Article
LanguageEnglish
Published Dordrecht Springer Netherlands 01.10.2013
Springer Nature B.V
Subjects
Biochemistry
Biological and Medical Physics
Biophysics
Carbon Isotopes
Cell adhesion & migration
Cell Adhesion Molecules, Neuronal - chemistry
Homeostasis
Humans
Nerve Growth Factors - chemistry
Nitrogen Isotopes
NMR
Nuclear magnetic resonance
Nuclear Magnetic Resonance, Biomolecular
Physics
Physics and Astronomy
Polymer Sciences
Protein Structure, Secondary
Protein Structure, Tertiary
Proteins
Protons
Ninjurin1
Backbone resonance assignments
Ninjurin1 N-terminal domain
Cell adhesion molecule
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Summary: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.
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ISSN:1874-2718
1874-270X
DOI:10.1007/s12104-012-9400-3