[NMR paper] Mechanism of Tau-Promoted Microtubule Assembly As Probed by NMR Spectroscopy.
Mechanism of Tau-Promoted Microtubule Assembly As Probed by NMR Spectroscopy.
Mechanism of Tau-Promoted Microtubule Assembly As Probed by NMR Spectroscopy.
J Am Chem Soc. 2014 Aug 27;
Authors: Gigant B, Landrieu I, Fauquant C, Barbier P, Huvent I, Wieruszeski JM, Knossow M, Lippens G
Abstract
Determining the molecular mechanism of the neuronal Tau protein in the tubulin heterodimer assembly has been a challenge owing to the dynamic character of the complex and the large size of microtubules. We use here defined constructs...
nmrlearner
Journal club
0
08-28-2014 10:09 AM
Correction for Li et al., Mechanism of E-cadherin dimerization probed by NMR relaxation dispersion [Correction]
Correction for Li et al., Mechanism of E-cadherin dimerization probed by NMR relaxation dispersion
...
Date: 2013-11-26
BIOPHYSICS AND COMPUTATIONAL BIOLOGY Correction for “Mechanism of E-cadherin dimerization probed by NMR relaxation dispersion,” by Ying Li, Nicole L. Altorelli, Fabiana Bahna, Barry Honig, Lawrence Shapiro, and Arthur G. Palmer III, which appeared in issue 41, October 8, 2013, of Proc Natl Acad Sci USA (110:16462–16467; first published September... Read More
PNAS:
Number: 48
nmrlearner
Journal club
0
11-27-2013 01:50 AM
[NMR paper] Mechanism of E-cadherin dimerization probed by NMR relaxation dispersion.
Mechanism of E-cadherin dimerization probed by NMR relaxation dispersion.
Mechanism of E-cadherin dimerization probed by NMR relaxation dispersion.
Proc Natl Acad Sci U S A. 2013 Sep 25;
Authors: Li Y, Altorelli NL, Bahna F, Honig B, Shapiro L, Palmer AG
Abstract
Epithelial cadherin (E-cadherin), a member of the classical cadherin family, mediates calcium-dependent homophilic cell-cell adhesion. Crystal structures of classical cadherins reveal an adhesive dimer interface featuring reciprocal exchange of N-terminal ?-strands between two...
nmrlearner
Journal club
0
09-27-2013 05:26 PM
[NMR paper] Proteolytic E-cadherin activation followed by solution NMR and X-ray crystallography.
Proteolytic E-cadherin activation followed by solution NMR and X-ray crystallography.
Related Articles Proteolytic E-cadherin activation followed by solution NMR and X-ray crystallography.
EMBO J. 2004 Apr 21;23(8):1699-708
Authors: Häussinger D, Ahrens T, Aberle T, Engel J, Stetefeld J, Grzesiek S
Cellular adhesion by classical cadherins depends critically on the exact proteolytic removal of their N-terminal prosequences. In this combined solution NMR and X-ray crystallographic study, the consequences of propeptide cleavage of an epithelial...
nmrlearner
Journal club
0
11-24-2010 09:51 PM
[NMR paper] Calcium-dependent homoassociation of E-cadherin by NMR spectroscopy: changes in mobil
Calcium-dependent homoassociation of E-cadherin by NMR spectroscopy: changes in mobility, conformation and mapping of contact regions.
Related Articles Calcium-dependent homoassociation of E-cadherin by NMR spectroscopy: changes in mobility, conformation and mapping of contact regions.
J Mol Biol. 2002 Dec 6;324(4):823-39
Authors: Häussinger D, Ahrens T, Sass HJ, Pertz O, Engel J, Grzesiek S
Cadherins are calcium-dependent cell surface proteins that mediate homophilic cellular adhesion. The calcium-induced oligomerization of the N-terminal two...
nmrlearner
Journal club
0
11-24-2010 08:58 PM
[NMR paper] Internal mobility in the partially folded DNA binding and dimerization domains of GAL
Internal mobility in the partially folded DNA binding and dimerization domains of GAL4: NMR analysis of the N-H spectral density functions.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-acspubs.jpg Related Articles Internal mobility in the partially folded DNA binding and dimerization domains of GAL4: NMR analysis of the N-H spectral density functions.
Biochemistry. 1996 Feb 27;35(8):2674-86
Authors: Lefevre JF, Dayie KT, Peng JW, Wagner G
The DNA binding domain (residues 1--65) of the yeast transcriptional...
nmrlearner
Journal club
0
08-22-2010 02:27 PM
[NMR paper] The dimerization stability of the HLH-LZ transcription protein family is modulated by
The dimerization stability of the HLH-LZ transcription protein family is modulated by the leucine zippers: a CD and NMR study of TFEB and c-Myc.
Related Articles The dimerization stability of the HLH-LZ transcription protein family is modulated by the leucine zippers: a CD and NMR study of TFEB and c-Myc.
Biochemistry. 1994 Sep 20;33(37):11296-306
Authors: Muhle-Goll C, Gibson T, Schuck P, Schubert D, Nalis D, Nilges M, Pastore A
In the HLH-LZ protein family, the helix-loop-helix DNA-binding dimerization domain is followed in the sequence by a...
Mechanism of E-cadherin dimerization probed by NMR RD-Supp
Linear Mode
