NMR studies reveal a novel mode for hFADD to bind with the unstructured hRTN3 which initiates the ER-stress activated apoptosis

10.1016/j.bbrc.2009.04.024

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Main Authors:	Liu, J., Song, J., Zhu, W., Qin, H.
Other Authors:	BIOCHEMISTRY
Format:	Article
Published:	2011
Subjects:	Apoptosis Circular dichroism (CD) Endoplasmic reticulum (ER) Fas-associated death domain (FADD) Intrinsically unstructured protein Isothermal titration calorimetry (ITC) NMR spectroscopy Reticulon 3 (RTN3) RTN4/Nogo
Online Access:	http://scholarbank.nus.edu.sg/handle/10635/28881
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Institution:	National University of Singapore

id	sg-nus-scholar.10635-28881
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spelling	sg-nus-scholar.10635-288812023-10-27T07:11:08Z NMR studies reveal a novel mode for hFADD to bind with the unstructured hRTN3 which initiates the ER-stress activated apoptosis Liu, J. Song, J. Zhu, W. Qin, H. BIOCHEMISTRY BIOLOGICAL SCIENCES Apoptosis Circular dichroism (CD) Endoplasmic reticulum (ER) Fas-associated death domain (FADD) Intrinsically unstructured protein Isothermal titration calorimetry (ITC) NMR spectroscopy Reticulon 3 (RTN3) RTN4/Nogo 10.1016/j.bbrc.2009.04.024 Biochemical and Biophysical Research Communications 383 4 433-439 BBRCA 2011-11-29T06:10:34Z 2011-11-29T06:10:34Z 2009 Article Liu, J., Song, J., Zhu, W., Qin, H. (2009). NMR studies reveal a novel mode for hFADD to bind with the unstructured hRTN3 which initiates the ER-stress activated apoptosis. Biochemical and Biophysical Research Communications 383 (4) : 433-439. ScholarBank@NUS Repository. https://doi.org/10.1016/j.bbrc.2009.04.024 0006291X 10902104 http://scholarbank.nus.edu.sg/handle/10635/28881 000266227000011 Scopus
institution	National University of Singapore
building	NUS Library
continent	Asia
country	Singapore Singapore
content_provider	NUS Library
collection	ScholarBank@NUS
topic	Apoptosis Circular dichroism (CD) Endoplasmic reticulum (ER) Fas-associated death domain (FADD) Intrinsically unstructured protein Isothermal titration calorimetry (ITC) NMR spectroscopy Reticulon 3 (RTN3) RTN4/Nogo
spellingShingle	Apoptosis Circular dichroism (CD) Endoplasmic reticulum (ER) Fas-associated death domain (FADD) Intrinsically unstructured protein Isothermal titration calorimetry (ITC) NMR spectroscopy Reticulon 3 (RTN3) RTN4/Nogo Liu, J. Song, J. Zhu, W. Qin, H. NMR studies reveal a novel mode for hFADD to bind with the unstructured hRTN3 which initiates the ER-stress activated apoptosis
description	10.1016/j.bbrc.2009.04.024
author2	BIOCHEMISTRY
author_facet	BIOCHEMISTRY Liu, J. Song, J. Zhu, W. Qin, H.
format	Article
author	Liu, J. Song, J. Zhu, W. Qin, H.
author_sort	Liu, J.
title	NMR studies reveal a novel mode for hFADD to bind with the unstructured hRTN3 which initiates the ER-stress activated apoptosis
title_short	NMR studies reveal a novel mode for hFADD to bind with the unstructured hRTN3 which initiates the ER-stress activated apoptosis
title_full	NMR studies reveal a novel mode for hFADD to bind with the unstructured hRTN3 which initiates the ER-stress activated apoptosis
title_fullStr	NMR studies reveal a novel mode for hFADD to bind with the unstructured hRTN3 which initiates the ER-stress activated apoptosis
title_full_unstemmed	NMR studies reveal a novel mode for hFADD to bind with the unstructured hRTN3 which initiates the ER-stress activated apoptosis
title_sort	nmr studies reveal a novel mode for hfadd to bind with the unstructured hrtn3 which initiates the er-stress activated apoptosis
publishDate	2011
url	http://scholarbank.nus.edu.sg/handle/10635/28881
_version_	1781410671766798336

NMR studies reveal a novel mode for hFADD to bind with the unstructured hRTN3 which initiates the ER-stress activated apoptosis

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