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

In Gyun Lee; Sun Bok Jang; Ji Hun Kim; Ki Young Lee; Kyu Yeon Lee; Hae Kap Cheong; Bong Jin Lee

doi:10.1007/s12104-012-9400-3

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

In Gyun Lee, Sun Bok Jang, Ji Hun Kim, Ki Young Lee, Kyu Yeon Lee, Hae Kap Cheong, Bong Jin Lee

Department of Pharmaceutical Sciences

Research output: Contribution to journal › Article › peer-review

1 Scopus citations

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.

Original language	English
Pages (from-to)	159-162
Number of pages	4
Journal	Biomolecular NMR Assignments
Volume	7
Issue number	2
DOIs	https://doi.org/10.1007/s12104-012-9400-3
State	Published - Oct 2013

Bibliographical note

Funding Information:
Acknowledgments This study was supported by the National Research Foundation of Korea (NRF) grant funded by Korean government (MEST) (Grant number 20110001207). This study was also supported by a grant of the Korea Healthcare technology R&D Project, Ministry for Health, Welfare & Family Affairs, Republic of Korea. (Grant number:A092006). This work was supported in part by 2011 BK21 project for Medicine, Dentistry, and Pharmacy. We thank Korea Basic Science Institute (KBSI) and National Center for Inter-University Research Facilities (NCIRF) for using their NMR machines.

Keywords

Backbone resonance assignments
Cell adhesion molecule
Ninjurin1
Ninjurin1 N-terminal domain

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10.1007/s12104-012-9400-3

Cite this

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

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.",

keywords = "Backbone resonance assignments, Cell adhesion molecule, Ninjurin1, Ninjurin1 N-terminal domain",

author = "Lee, \{In Gyun\} and Jang, \{Sun Bok\} and Kim, \{Ji Hun\} and Lee, \{Ki Young\} and Lee, \{Kyu Yeon\} and Cheong, \{Hae Kap\} and Lee, \{Bong Jin\}",

note = "Funding Information: Acknowledgments This study was supported by the National Research Foundation of Korea (NRF) grant funded by Korean government (MEST) (Grant number 20110001207). This study was also supported by a grant of the Korea Healthcare technology R\&D Project, Ministry for Health, Welfare \& Family Affairs, Republic of Korea. (Grant number:A092006). This work was supported in part by 2011 BK21 project for Medicine, Dentistry, and Pharmacy. We thank Korea Basic Science Institute (KBSI) and National Center for Inter-University Research Facilities (NCIRF) for using their NMR machines.",

year = "2013",

month = oct,

doi = "10.1007/s12104-012-9400-3",

language = "English",

volume = "7",

pages = "159--162",

journal = "Biomolecular NMR Assignments",

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T1 - 1H, 13C and 15N chemical shift assignments of Ninjurin1 Extracellular N-terminal Domain

AU - Lee, In Gyun

AU - Jang, Sun Bok

AU - Kim, Ji Hun

AU - Lee, Ki Young

AU - Lee, Kyu Yeon

AU - Cheong, Hae Kap

AU - Lee, Bong Jin

N1 - Funding Information: Acknowledgments This study was supported by the National Research Foundation of Korea (NRF) grant funded by Korean government (MEST) (Grant number 20110001207). This study was also supported by a grant of the Korea Healthcare technology R&D Project, Ministry for Health, Welfare & Family Affairs, Republic of Korea. (Grant number:A092006). This work was supported in part by 2011 BK21 project for Medicine, Dentistry, and Pharmacy. We thank Korea Basic Science Institute (KBSI) and National Center for Inter-University Research Facilities (NCIRF) for using their NMR machines.

PY - 2013/10

Y1 - 2013/10

N2 - 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.

AB - 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.

KW - Backbone resonance assignments

KW - Cell adhesion molecule

KW - Ninjurin1

KW - Ninjurin1 N-terminal domain

UR - https://www.scopus.com/pages/publications/84883490472

U2 - 10.1007/s12104-012-9400-3

DO - 10.1007/s12104-012-9400-3

M3 - Article

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AN - SCOPUS:84883490472

SN - 1874-2718

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JO - Biomolecular NMR Assignments

JF - Biomolecular NMR Assignments

IS - 2

ER -

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

Abstract

Bibliographical note

Keywords

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