Zobrazeno 1 - 10
of 109
pro vyhledávání: '"Shelli R McAlpine"'
Autor:
Nalin Kataria, Chloe-Anne Martinez, Bernadette Kerr, Samantha S. Zaiter, Monica Morgan, Shelli R. McAlpine, Kristina M. Cook
Publikováno v:
Cellular Physiology and Biochemistry, Vol 53, Iss 3, Pp 480-495 (2019)
Externí odkaz:
https://doaj.org/article/08cc13b86d8f465b8d621a35672ff588
Autor:
Yuantao Huo, Laura K. Buckton, Jack L. Bennett, Eloise C. Smith, Frances L. Byrne, Kyle L. Hoehn, Marwa N. Rahimi, Shelli R. McAlpine
Publikováno v:
Journal of Enzyme Inhibition and Medicinal Chemistry, Vol 34, Iss 1, Pp 728-739 (2019)
The most challenging issue facing peptide drug development is producing a molecule with optimal physical properties while maintaining target binding affinity. Masking peptides with protecting groups that can be removed inside the cell, produces a cel
Externí odkaz:
https://doaj.org/article/6788bb62f2ca40478336fde2257a8a2c
Autor:
Jessica Kho, Suhyeon Kwon, Heath Ecroyd, P Chi Pham, Huixin Wang, Shelli R McAlpine, Alana Y Huang, W Alexander Donald, Joel P Rivers
Publikováno v:
ACS Med Chem Lett
[Image: see text] We report the first small molecule peptides based on the N-terminal sequence of heat shock protein 27 (Hsp27, gene HSPB1) that demonstrates chaperone-like activity. The peptide, comprising the SWDPF sequence located at Hsp27’s ami
Autor:
Shelli R. McAlpine, Seong Jong Kim
Publikováno v:
Molecules, Vol 18, Iss 1, Pp 1111-1121 (2013)
Comparing a solution phase route to a solid phase route in the synthesis of the cytotoxic natural product urukthapelstatin A (Ustat A) confirmed that a solid phase method is superior. The solution phase approach was tedious and involved cyclization o
Externí odkaz:
https://doaj.org/article/7398f69fc50843439a41bb6a7f850169
Publikováno v:
Chemistry – A European Journal. 27:1487-1513
Developing macrocyclic peptides that can reach intracellular targets is a significant challenge. This review discusses the most recent strategies used to develop cell permeable cyclic peptides that maintain binding to their biological target inside t
Autor:
Robert Chapman, Shelli R. McAlpine, Shegufta N. Farazi, Raelene Boquiren, Henry Foster, Fan Chen
Publikováno v:
Polymer Chemistry. 11:425-432
Nanogels are attractive delivery vehicles for small hydrophilic cargo, such as peptides, but there is a limited understanding of how the structure of both the nanogel and cargo affect the drug loading and release properties, particularly in biologica
Autor:
Samantha S. Zaiter, Nalin Kataria, Bernadette Kerr, Monica N Morgan, Shelli R. McAlpine, Chloe-Anne Martinez, Kristina M. Cook
Publikováno v:
Cellular Physiology and Biochemistry, Vol 53, Iss 3, Pp 480-495 (2019)
Background/aims Hypoxia Inducible Factor-1α (HIF-1α) is involved in cancer progression and is stabilized by the chaperone HSP90 (Heat Shock Protein 90), preventing degradation. Previously identified HSP90 inhibitors bind to the N-terminal pocket of
Publikováno v:
Chemistry – A European Journal. 27
Publikováno v:
RSC Med Chem
We present the first NMR study of the interaction between heat shock protein 90 (Hsp90) and amino (N)-terminal inhibitors 17-AAG, and AUY922, and carboxy (C)-terminal modulators SM253, and LB51. We show that the two ATP mimics, 17-AAG and AUY922, bin
Autor:
Shelli R. McAlpine, Laura K. Buckton
Publikováno v:
Organic Letters. 20:506-509
The design, synthesis, and cell permeability of 19 hydrophilic macrocyclic peptides is presented. By systematically analyzing the impact of three different approaches (alkylated amino acids, asparagines, and d-amino acids) on the permeability of pola