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  1. International Journal of Peptide Research and Therapeutics
  2. International Journal of Peptide Research and Therapeutics : Volume 20
  3. International Journal of Peptide Research and Therapeutics : Volume 20, Issue 1, March 2014
  4. Leucine Zipper Motif Drives the Transmembrane Domain Dimerization of E-cadherin
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International Journal of Peptide Research and Therapeutics : Volume 23
International Journal of Peptide Research and Therapeutics : Volume 22
International Journal of Peptide Research and Therapeutics : Volume 21
International Journal of Peptide Research and Therapeutics : Volume 20
International Journal of Peptide Research and Therapeutics : Volume 20, Issue 4, December 2014
International Journal of Peptide Research and Therapeutics : Volume 20, Issue 3, September 2014
International Journal of Peptide Research and Therapeutics : Volume 20, Issue 2, June 2014
International Journal of Peptide Research and Therapeutics : Volume 20, Issue 1, March 2014
Biochemical and Cellular Specificity of Peptide Inhibitors of G Protein-Coupled Receptor Kinases
Discrimination Between Paraffin-Embedded and Frozen Skin Sections Using Synchrotron Infrared Microspectroscopy
Structure–Activity Relationship of a Highly Selective Peptidyl Inhibitor of Kv1.3 Voltage-Gated K$^{+}$-Channel from Scorpion (B. sindicus) Venom
Study of Peptide Mimetics of Hepatitis A Virus Conjugated to Keyhole Limpet Hemocyanin and as Multiple Antigen Peptide System
Why is Substrate Peptide Binding Unsusceptible to Multidrug-Resistant Mutations in HIV-1 Protease? A Structural and Energetic Analysis
Some Mechanistic Aspects on Fmoc Solid Phase Peptide Synthesis
Enhanced Interaction of Shuffled Mutacin IV, an Antimicrobial Peptide of Bacterial Origin, with Surface Protein IsdB of Staphylococcus aureus
Age-Related Changes in the Mechanical Properties of Human Fibroblasts and Its Prospective Reversal After Anti-Wrinkle Tripeptide Treatment
Selection and Characterization of a Peptide Specifically Targeting to Gastric Cancer Cell Line SGC-7901 Using Phage Display
Leucine Zipper Motif Drives the Transmembrane Domain Dimerization of E-cadherin
In silico Structure Modeling and Comparative Analysis of Characterization Properties of Protein Polymers Useful for Protein-Based Nano Particulate Drug Delivery Systems (NPDDS): A Bioinformatics Approach
Inhibition of Proliferation of Non-small Cell Lung Cancer Cells by a bFGF Antagonist Peptide
International Journal of Peptide Research and Therapeutics : Volume 19
International Journal of Peptide Research and Therapeutics : Volume 18
International Journal of Peptide Research and Therapeutics : Volume 17
International Journal of Peptide Research and Therapeutics : Volume 16
International Journal of Peptide Research and Therapeutics : Volume 15
International Journal of Peptide Research and Therapeutics : Volume 14
International Journal of Peptide Research and Therapeutics : Volume 13
International Journal of Peptide Research and Therapeutics : Volume 12
International Journal of Peptide Research and Therapeutics : Volume 11
International Journal of Peptide Research and Therapeutics : Volume 10
International Journal of Peptide Research and Therapeutics : Volume 9
International Journal of Peptide Research and Therapeutics : Volume 8
International Journal of Peptide Research and Therapeutics : Volume 7
International Journal of Peptide Research and Therapeutics : Volume 6
International Journal of Peptide Research and Therapeutics : Volume 5
International Journal of Peptide Research and Therapeutics : Volume 4
International Journal of Peptide Research and Therapeutics : Volume 3

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Leucine Zipper Motif Drives the Transmembrane Domain Dimerization of E-cadherin

Content Provider Springer Nature Link
Author Xu, Lida Hu, Ting Ting Luo, Shi Zhong
Copyright Year 2013
Abstract E-cadherin is a transmembrane glycoprotein which is involved in the Ca$^{2+}$-dependent cell–cell adhesion, and the adhesiveness is heavily dependent on the homodimerization of this molecule. Previous studies have shown that both the extracellular domain and cytoplasmic domain of E-cadherin contribute to its homodimerization. However, the roles of the transmembrane(TM) domain in the E-cadherin homodimerization have not been discussed in detail. In our experiments, SDS-PAGE showed higher molecular weight bands for the synthetic E-cadherin TM peptide, which indicated that the E-cadherin TM peptide is able to dimerize in the SDS micelle. The TOXCAT assay proved that the E-cadherin TM domain can form a moderate homo-oligomer in the Escherichia coli inner membrane. Furthermore, mutational analyses using the TOXCAT assays revealed that, instead of the common GxxxG dimerization motif, the leucine zipper motif is essential for the dimerization of the E-cadherin TM domain. Combining our experiment data and the computational simulation results, we provide insights for understanding the roles of the TM domain in the E-cadherin dimerization.
Starting Page 95
Ending Page 102
Page Count 8
File Format PDF
ISSN 15733149
Journal International Journal of Peptide Research and Therapeutics
Volume Number 20
Issue Number 1
e-ISSN 15733904
Language English
Publisher Springer Netherlands
Publisher Date 2013-09-26
Publisher Place Dordrecht
Access Restriction One Nation One Subscription (ONOS)
Subject Keyword Dimerization E-cadherin GxxxG motif Leucine zipper motif TOXCAT Transmembrane domain Biochemistry Animal Anatomy / Morphology / Histology Polymer Sciences Pharmaceutical Sciences/Technology Pharmacology/Toxicology Molecular Medicine
Content Type Text
Resource Type Article
Subject Analytical Chemistry Drug Discovery Biochemistry Molecular Medicine Bioengineering
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