Zobrazeno 1 - 10
of 13
pro vyhledávání: '"Caitlin N. Kent"'
Autor:
Anuj Khandelwal, Caitlin N. Kent, Maurie Balch, Shuxia Peng, Sanket J. Mishra, Junpeng Deng, Victor W. Day, Weiya Liu, Chitra Subramanian, Mark Cohen, Jeffery M. Holzbeierlein, Robert Matts, Brian S. J. Blagg
Publikováno v:
Nature Communications, Vol 9, Iss 1, Pp 1-7 (2018)
The molecular chaperone Hsp90 oversees the folding of many proteins associated with cancer progression but existing small-molecule inhibitors of this pathway are not isoform-selective. Here, the authors rationally design an Hsp90 inhibitor that displ
Externí odkaz:
https://doaj.org/article/22d6d57dbf0548efa5ef84106a4676a4
Autor:
Samantha J. McClenahan, Caitlin N. Kent, Sujay V. Kharade, Elena Isaeva, Jade C. Williams, Changho Han, Andrew Terker, Robert Gresham, Roman M. Lazarenko, Emily L. Days, Ian M. Romaine, Joshua A. Bauer, Olivier Boutaud, Gary A. Sulikowski, Raymond Harris, C. David Weaver, Alexander Staruschenko, Craig W. Lindsley, Jerod S. Denton
Publikováno v:
Mol Pharmacol
Heteromeric Kir4.1/Kir5.1 (KCNJ10/KCNJ16) inward rectifier potassium (Kir) channels play key roles in the brain and kidney, but pharmacological tools for probing their physiology and therapeutic potential have not been developed. Here, we report the
Autor:
Monimoy Banerjee, Caitlin N. Kent, Penchala Narasimharao Meka, Subhabrata Chaudhury, Brian S. J. Blagg
Publikováno v:
Chemistry
The 90 kDa heat shock proteins (Hsp90) are molecular chaperones that are responsible for the folding and/or trafficking of ~400 client proteins, many of which are directly associated with cancer progression. Consequently, inhibition of Hsp90 can exhi
Autor:
Leonard M. Neckers, John Koren, Kristin Beebe, Vitumbiko Munthali, Jeffrey M. Holzbeierlein, Brian S. J. Blagg, Weiya Liu, Sanket J. Mishra, John A. Taylor, Monimoy Banerjee, Caitlin N. Kent
Publikováno v:
Journal of Medicinal Chemistry. 64:1545-1557
The 90 kD heat shock proteins (Hsp90) are molecular chaperones that are responsible for the folding of select proteins, many of which are directly associated with cancer progression. Consequently, inhibition of the Hsp90 protein folding machinery res
Autor:
Sanket J, Mishra, Weiya, Liu, Kristin, Beebe, Monimoy, Banerjee, Caitlin N, Kent, Vitumbiko, Munthali, John, Koren, John A, Taylor, Leonard M, Neckers, Jeffrey, Holzbeierlein, Brian S J, Blagg
Publikováno v:
J Med Chem
The 90 kD heat shock proteins (Hsp90) are molecular chaperones that are responsible for the folding of select proteins, many of which are directly associated with cancer progression. Consequently, inhibition of the Hsp90 protein folding machinery res
Autor:
Caitlin N, Kent, Mark G, Fulton, Kaylee J, Stillwell, Jonathan W, Dickerson, Matthew T, Loch, Alice L, Rodriguez, Anna L, Blobaum, Olivier, Boutaud, Jerri L, Rook, Colleen M, Niswender, P Jeffrey, Conn, Craig W, Lindsley
Publikováno v:
Bioorganicmedicinal chemistry letters. 37
A high throughput screen (HTS) identified a novel, but weak (EC
Autor:
Chitra Subramanian, Robert L. Matts, Brian S. J. Blagg, Anuj Khandelwal, Weiya Liu, Jeffery M. Holzbeierlein, Junpeng Deng, Mark S. Cohen, Victor W. Day, Sanket J. Mishra, Caitlin N. Kent, Maurie Balch, Shuxia Peng
Publikováno v:
Nature Communications, Vol 9, Iss 1, Pp 1-7 (2018)
Nature Communications
Nature Communications
The 90 kDa heat shock protein (Hsp90) is a molecular chaperone responsible for folding proteins that are directly associated with cancer progression. Consequently, inhibition of the Hsp90 protein folding machinery results in a combinatorial attack on
Publikováno v:
ChemMedChem. 12:2022-2029
The design, synthesis, and biological evaluation of stilbene-based novobiocin analogues is reported. Replacement of the biaryl amide side chain with a triazole side chain produced compounds that exhibited good antiproliferative activities. Heat shock
Autor:
Kaylee J. Stillwell, Jonathan W. Dickerson, Matthew T. Loch, Craig W. Lindsley, Mark G. Fulton, Olivier Boutaud, P. Jeffrey Conn, Colleen M. Niswender, Caitlin N. Kent, Alice L. Rodriguez, Jerri L. Rook, Anna L. Blobaum
Publikováno v:
Bioorganic & Medicinal Chemistry Letters. 37:127838
A high throughput screen (HTS) identified a novel, but weak (EC50 = 6.2 μM, 97% Glu Max) mGlu4 PAM chemotype based on a 1,4-thiazepane core, VU0544412. Reaction development and chemical optimization delivered a potent mGlu4 PAM VU6022296 (EC50 = 32.