@article { ISI:000359951700161,
	title = {RXR-carbamate - a novel molecular transporter for skin},
	journal = {Molecular Therapy},
	volume = {23},
	number = {1},
	year = {2015},
	note = {18th Annual Meeting of the American-Society-of-Gene-and-Cell-Therapy (ASGCT), New Orleans, LA, MAY 13-16, 2015},
	month = {MAY},
	pages = {S64-S64},
	publisher = {Amer Soc Gene \& Cell Therapy},
	address = {75 VARICK ST, 9TH FLR, NEW YORK, NY 10013-1917 USA},
	issn = {1525-0016},
	author = {Natarajan, Poornemaa and Patil, Kiran M. and Vij, Manika and Yadav, Amit K. and Kumar, Vaijayanti A. and Ganguli, Munia and Fernandes, Moneesha}
}
@article {45708,
	title = {(R-X-R)(4)-Motif peptides containing conformationally constrained cyclohexane-derived spacers: effect on cellular uptake},
	journal = {ChemMedChem},
	volume = {12},
	year = {2017},
	month = {NOV },
	pages = {1743-1747},
	type = {Article},
	abstract = {<p>Arginine-rich peptides having the (R-X-R) n motif are among the most effective cell-penetrating peptides (CPPs). Herein we report a several-fold increase in the efficacy of such CPPs if the linear flexible spacer (-X-) in the (R-X-R) motif is replaced by constrained cyclic 1,4-substituted-cyclohexane-derived spacers. Internalization of these oligomers in mammalian cell lines was found to be an energy-dependent process. Incorporation of these constrained, non-proteinogenic amino acid spacers in the CPPs is shown to enhance their proteolytic stability.</p>},
	keywords = {(R-X-R)-motif, cell-penetrating peptides, cellular uptake, protease stability},
	issn = {1860-7179},
	doi = {10.1002/cmdc.201700498},
	author = {Bhosle, Govind S. and Fernandes, Moneesha}
}
@article {47612,
	title = {Replacement of loop residues in TBA by an abasic ethylene glycol spacer: effect on stability, structure and function**},
	journal = {ChemistrySelect},
	volume = {6},
	year = {2021},
	month = {OCT },
	pages = {10648-10650},
	type = {Article},
	abstract = {This article describes the synthesis of ethyleneglycol (E) phosphoramidite and its incorporation into the thrombin binding aptamer (TBA) sequence at loop positions. Circular dichroism (CD) study revealed no major disturbances in the secondary structure of TBA by the abasic E unit and the derived oligomers exhibited a typical antiparallel chair-like conformation similar to that of TBA. UV and CD spectroscopy, together with anti-coagulation and HPLC studies revealed that although nuclease stability was enhanced, and anti-coagulation reasonably good, the thermal stability of the quadruplexes was adversely affected.},
	keywords = {aptamers, clotting time, ethylene glycol spacer, G-quadruplexes, nuclease stability},
	issn = {2365-6549},
	doi = {10.1002/slct.202102269},
	author = {Wagh, Atish A. and Ghalawat, Monika and Fernandes, Moneesha}
}
