PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
23197975-1	2012	KU-32 is a novel, novobiocin-based Hsp90 inhibitor that protects against neuronal glucotoxicity and reverses multiple clinical indices of diabetic peripheral neuropathy in a rodent model.	KU-32	0-5	heat shock protein 90 alpha family class A member 1	Homo sapiens	35-40	
22413817-2	2012	KU-32 is a novobiocin-based, C-terminal inhibitor of the molecular chaperone, heat shock protein 90 (Hsp90).	KU-32	0-5	heat shock protein 90 alpha family class A member 1	Homo sapiens	78-99	
22413817-2	2012	KU-32 is a novobiocin-based, C-terminal inhibitor of the molecular chaperone, heat shock protein 90 (Hsp90).	KU-32	0-5	heat shock protein 90 alpha family class A member 1	Homo sapiens	101-106	
30792306-0	2019	Stimulation of heat shock protein 90 chaperone function through binding of a novobiocin analog KU-32.	KU-32	95-100	heat shock protein 90 alpha family class A member 1	Homo sapiens	15-36	
30792306-4	2019	Here, using biochemical and cell-based assays along with isothermal titration calorimetry, we investigate KU-32, a derivative of the Hsp90 inhibitor novobiocin (NB), for its ability to modulate Hsp90 chaperone function.	KU-32	106-111	heat shock protein 90 alpha family class A member 1	Homo sapiens	133-138	
30792306-4	2019	Here, using biochemical and cell-based assays along with isothermal titration calorimetry, we investigate KU-32, a derivative of the Hsp90 inhibitor novobiocin (NB), for its ability to modulate Hsp90 chaperone function.	KU-32	106-111	heat shock protein 90 alpha family class A member 1	Homo sapiens	194-199	
30792306-5	2019	Although NB and KU-32 differ only slightly in structure, we found that upon binding, they induce completely opposite conformational changes in Hsp90.	KU-32	16-21	heat shock protein 90 alpha family class A member 1	Homo sapiens	143-148	
30792306-6	2019	We observed that NB and KU-32 both bind to the C-terminal domain of Hsp90, but surprisingly, KU-32 stimulated the chaperone functions of Hsp90 via allosteric modulation of its N-terminal domain, responsible for the chaperone"s ATPase activity.	KU-32	24-29	heat shock protein 90 alpha family class A member 1	Homo sapiens	68-73	
30792306-6	2019	We observed that NB and KU-32 both bind to the C-terminal domain of Hsp90, but surprisingly, KU-32 stimulated the chaperone functions of Hsp90 via allosteric modulation of its N-terminal domain, responsible for the chaperone"s ATPase activity.	KU-32	93-98	heat shock protein 90 alpha family class A member 1	Homo sapiens	137-142	
30792306-7	2019	In vitro and in silico studies indicated that upon KU-32 binding, Hsp90 undergoes global structural changes leading to the formation of a "partially closed" intermediate that selectively binds ATP and increases ATPase activity.	KU-32	51-56	heat shock protein 90 alpha family class A member 1	Homo sapiens	66-71	
30792306-8	2019	We also report that KU-32 promotes HeLa cell survival and enhances the refolding of an Hsp90 substrate inside the cell.	KU-32	20-25	heat shock protein 90 alpha family class A member 1	Homo sapiens	87-92	
30792306-9	2019	This discovery explains the effectiveness of KU-32 analogs in the management of neuropathies and may facilitate the design of molecules that promote cell survival by enhancing Hsp90 chaperone function and reducing the load of misfolded proteins in cells.	KU-32	45-50	heat shock protein 90 alpha family class A member 1	Homo sapiens	176-181	
20721818-2	2010	This conference report highlights selected presentations on Hsp90 inhibitors and Hsp70 inducers, such as KU-32 and KU-174 (University of Kansas); natural products in drug design, such as minnelide (University of Minnesota) and tylocrebrine; novel compounds from Merck for metabolic and cardiovascular diseases, such as MK-7725, a series of DDP4 inhibitors and KV1.5 ion channel antagonists; and the discovery of the VEGFR2 kinase inhibitor AMG-429 (Amgen Inc).	KU-32	105-110	heat shock protein 90 alpha family class A member 1	Homo sapiens	60-65