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Stapling monomeric GCN4 peptides allows for DNA binding and enhanced cellular uptake

Abhishek Iyer (UGent) , Dorien Van Lysebetten (UGent) , Yara Ruiz Garcia (UGent) , Benoit Louage (UGent) , Bruno De Geest (UGent) and Annemieke Madder (UGent)
(2015) ORGANIC & BIOMOLECULAR CHEMISTRY. 13(13). p.3856-3862
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Organization
Abstract
The basic DNA recognition region of the GCN4 protein comprising 23 amino acids has been modified to contain two optimally positioned cysteines which have been linked and stapled using crosslinkers of suitable lengths. This results in stapled peptides with a stabilized alpha-helical conformation which allows for DNA binding and concurrent enhancement of cellular uptake.
Keywords
HELICAL PEPTIDES, PROTEIN, CRYSTAL-STRUCTURE, DIMER, RECOGNITION, SPECIFICITY, INHIBITORS, COMPLEX

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MLA
Iyer, Abhishek et al. “Stapling Monomeric GCN4 Peptides Allows for DNA Binding and Enhanced Cellular Uptake.” ORGANIC & BIOMOLECULAR CHEMISTRY 13.13 (2015): 3856–3862. Print.
APA
Iyer, A., Van Lysebetten, D., Ruiz Garcia, Y., Louage, B., De Geest, B., & Madder, A. (2015). Stapling monomeric GCN4 peptides allows for DNA binding and enhanced cellular uptake. ORGANIC & BIOMOLECULAR CHEMISTRY, 13(13), 3856–3862.
Chicago author-date
Iyer, Abhishek, Dorien Van Lysebetten, Yara Ruiz Garcia, Benoit Louage, Bruno De Geest, and Annemieke Madder. 2015. “Stapling Monomeric GCN4 Peptides Allows for DNA Binding and Enhanced Cellular Uptake.” Organic & Biomolecular Chemistry 13 (13): 3856–3862.
Chicago author-date (all authors)
Iyer, Abhishek, Dorien Van Lysebetten, Yara Ruiz Garcia, Benoit Louage, Bruno De Geest, and Annemieke Madder. 2015. “Stapling Monomeric GCN4 Peptides Allows for DNA Binding and Enhanced Cellular Uptake.” Organic & Biomolecular Chemistry 13 (13): 3856–3862.
Vancouver
1.
Iyer A, Van Lysebetten D, Ruiz Garcia Y, Louage B, De Geest B, Madder A. Stapling monomeric GCN4 peptides allows for DNA binding and enhanced cellular uptake. ORGANIC & BIOMOLECULAR CHEMISTRY. 2015;13(13):3856–62.
IEEE
[1]
A. Iyer, D. Van Lysebetten, Y. Ruiz Garcia, B. Louage, B. De Geest, and A. Madder, “Stapling monomeric GCN4 peptides allows for DNA binding and enhanced cellular uptake,” ORGANIC & BIOMOLECULAR CHEMISTRY, vol. 13, no. 13, pp. 3856–3862, 2015.
@article{5949059,
  abstract     = {The basic DNA recognition region of the GCN4 protein comprising 23 amino acids has been modified to contain two optimally positioned cysteines which have been linked and stapled using crosslinkers of suitable lengths. This results in stapled peptides with a stabilized alpha-helical conformation which allows for DNA binding and concurrent enhancement of cellular uptake.},
  author       = {Iyer, Abhishek and Van Lysebetten, Dorien and Ruiz Garcia, Yara and Louage, Benoit and De Geest, Bruno and Madder, Annemieke},
  issn         = {1477-0520},
  journal      = {ORGANIC & BIOMOLECULAR CHEMISTRY},
  keywords     = {HELICAL PEPTIDES,PROTEIN,CRYSTAL-STRUCTURE,DIMER,RECOGNITION,SPECIFICITY,INHIBITORS,COMPLEX},
  language     = {eng},
  number       = {13},
  pages        = {3856--3862},
  title        = {Stapling monomeric GCN4 peptides allows for DNA binding and enhanced cellular uptake},
  url          = {http://dx.doi.org/10.1039/c4ob02659d},
  volume       = {13},
  year         = {2015},
}

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