Find your PDFs fast.
Welcome to the Pubget Medical Subject Headings (MESH) browser. Click on a topic or subtopic below to explore related papers. In the gold box is the most recent paper about the current MESH term, and below are 20 related papers.
Protease Inhibitors (5):
Recent article
Protease Inhibitors
Nature Medicine (17)12 2011
Abstract
We describe the small molecule b-AP15 as a previously unidentified class of proteasome inhibitor that abrogates the deubiquitinating activity of the 19S regulatory particle. b-AP15 inhibited the activity of two 19S regulatory-particle-associated deubiquitinases, ubiquitin C-terminal hydrolase 5 (UCH...
|
PMID: 22057347
PDF is available here.
PDF is available here.
| < More recent | Older article > |
Nature Medicine (17)12 2011
Abstract
We describe the small molecule b-AP15 as a previously unidentified class of proteasome inhibitor that abrogates the deubiquitinating activity of the 19S regulatory particle. b-AP15 inhibited the activity of two 19S regulatory-particle-associated deubiquitinases, ubiquitin C-terminal hydrolase 5 (UCH...
|
PMID: 22057347
PDF is available here.
PDF is available here.
Nature Medicine (17)12 2011
Abstract
We describe the small molecule b-AP15 as a previously unidentified class of proteasome inhibitor that abrogates the deubiquitinating activity of the 19S regulatory particle. b-AP15 inhibited the activity of two 19S regulatory-particle-associated deubiquitinases, ubiquitin C-terminal hydrolase 5 (UCH...
|
PMID: 22057347
PDF is available here.
PDF is available here.
Nature Medicine (17)12 2011
Abstract
We describe the small molecule b-AP15 as a previously unidentified class of proteasome inhibitor that abrogates the deubiquitinating activity of the 19S regulatory particle. b-AP15 inhibited the activity of two 19S regulatory-particle-associated deubiquitinases, ubiquitin C-terminal hydrolase 5 (UCH...
|
PMID: 22057347
PDF is available here.
PDF is available here.
Nature Medicine (17)12 2011
Abstract
We describe the small molecule b-AP15 as a previously unidentified class of proteasome inhibitor that abrogates the deubiquitinating activity of the 19S regulatory particle. b-AP15 inhibited the activity of two 19S regulatory-particle-associated deubiquitinases, ubiquitin C-terminal hydrolase 5 (UCH...
|
PMID: 22057347
PDF is available here.
PDF is available here.
Nature Medicine (17)12 2011
Abstract
We describe the small molecule b-AP15 as a previously unidentified class of proteasome inhibitor that abrogates the deubiquitinating activity of the 19S regulatory particle. b-AP15 inhibited the activity of two 19S regulatory-particle-associated deubiquitinases, ubiquitin C-terminal hydrolase 5 (UCH...
|
PMID: 22057347
PDF is available here.
PDF is available here.
Nature Medicine (17)12 2011
Abstract
We describe the small molecule b-AP15 as a previously unidentified class of proteasome inhibitor that abrogates the deubiquitinating activity of the 19S regulatory particle. b-AP15 inhibited the activity of two 19S regulatory-particle-associated deubiquitinases, ubiquitin C-terminal hydrolase 5 (UCH...
|
PMID: 22057347
PDF is available here.
PDF is available here.
Nature Medicine (17)12 2011
Abstract
We describe the small molecule b-AP15 as a previously unidentified class of proteasome inhibitor that abrogates the deubiquitinating activity of the 19S regulatory particle. b-AP15 inhibited the activity of two 19S regulatory-particle-associated deubiquitinases, ubiquitin C-terminal hydrolase 5 (UCH...
|
PMID: 22057347
PDF is available here.
PDF is available here.
Nature Medicine (17)12 2011
Abstract
We describe the small molecule b-AP15 as a previously unidentified class of proteasome inhibitor that abrogates the deubiquitinating activity of the 19S regulatory particle. b-AP15 inhibited the activity of two 19S regulatory-particle-associated deubiquitinases, ubiquitin C-terminal hydrolase 5 (UCH...
|
PMID: 22057347
PDF is available here.
PDF is available here.
Nature Medicine (17)12 2011
Abstract
We describe the small molecule b-AP15 as a previously unidentified class of proteasome inhibitor that abrogates the deubiquitinating activity of the 19S regulatory particle. b-AP15 inhibited the activity of two 19S regulatory-particle-associated deubiquitinases, ubiquitin C-terminal hydrolase 5 (UCH...
|
PMID: 22057347
PDF is available here.
PDF is available here.
Nature Medicine (17)12 2011
Abstract
We describe the small molecule b-AP15 as a previously unidentified class of proteasome inhibitor that abrogates the deubiquitinating activity of the 19S regulatory particle. b-AP15 inhibited the activity of two 19S regulatory-particle-associated deubiquitinases, ubiquitin C-terminal hydrolase 5 (UCH...
|
PMID: 22057347
PDF is available here.
PDF is available here.
Nature Medicine (17)12 2011
Abstract
We describe the small molecule b-AP15 as a previously unidentified class of proteasome inhibitor that abrogates the deubiquitinating activity of the 19S regulatory particle. b-AP15 inhibited the activity of two 19S regulatory-particle-associated deubiquitinases, ubiquitin C-terminal hydrolase 5 (UCH...
|
PMID: 22057347
PDF is available here.
PDF is available here.
Nature Medicine (17)12 2011
Abstract
We describe the small molecule b-AP15 as a previously unidentified class of proteasome inhibitor that abrogates the deubiquitinating activity of the 19S regulatory particle. b-AP15 inhibited the activity of two 19S regulatory-particle-associated deubiquitinases, ubiquitin C-terminal hydrolase 5 (UCH...
|
PMID: 22057347
PDF is available here.
PDF is available here.
Nature Medicine (17)12 2011
Abstract
We describe the small molecule b-AP15 as a previously unidentified class of proteasome inhibitor that abrogates the deubiquitinating activity of the 19S regulatory particle. b-AP15 inhibited the activity of two 19S regulatory-particle-associated deubiquitinases, ubiquitin C-terminal hydrolase 5 (UCH...
|
PMID: 22057347
PDF is available here.
PDF is available here.
Nature Medicine (17)12 2011
Abstract
We describe the small molecule b-AP15 as a previously unidentified class of proteasome inhibitor that abrogates the deubiquitinating activity of the 19S regulatory particle. b-AP15 inhibited the activity of two 19S regulatory-particle-associated deubiquitinases, ubiquitin C-terminal hydrolase 5 (UCH...
|
PMID: 22057347
PDF is available here.
PDF is available here.
Nature Medicine (17)12 2011
Abstract
We describe the small molecule b-AP15 as a previously unidentified class of proteasome inhibitor that abrogates the deubiquitinating activity of the 19S regulatory particle. b-AP15 inhibited the activity of two 19S regulatory-particle-associated deubiquitinases, ubiquitin C-terminal hydrolase 5 (UCH...
|
PMID: 22057347
PDF is available here.
PDF is available here.
Nature Medicine (17)12 2011
Abstract
We describe the small molecule b-AP15 as a previously unidentified class of proteasome inhibitor that abrogates the deubiquitinating activity of the 19S regulatory particle. b-AP15 inhibited the activity of two 19S regulatory-particle-associated deubiquitinases, ubiquitin C-terminal hydrolase 5 (UCH...
|
PMID: 22057347
PDF is available here.
PDF is available here.
Nature Medicine (17)12 2011
Abstract
We describe the small molecule b-AP15 as a previously unidentified class of proteasome inhibitor that abrogates the deubiquitinating activity of the 19S regulatory particle. b-AP15 inhibited the activity of two 19S regulatory-particle-associated deubiquitinases, ubiquitin C-terminal hydrolase 5 (UCH...
|
PMID: 22057347
PDF is available here.
PDF is available here.
Nature Medicine (17)12 2011
Abstract
We describe the small molecule b-AP15 as a previously unidentified class of proteasome inhibitor that abrogates the deubiquitinating activity of the 19S regulatory particle. b-AP15 inhibited the activity of two 19S regulatory-particle-associated deubiquitinases, ubiquitin C-terminal hydrolase 5 (UCH...
|
PMID: 22057347
PDF is available here.
PDF is available here.
Nature Medicine (17)12 2011
Abstract
We describe the small molecule b-AP15 as a previously unidentified class of proteasome inhibitor that abrogates the deubiquitinating activity of the 19S regulatory particle. b-AP15 inhibited the activity of two 19S regulatory-particle-associated deubiquitinases, ubiquitin C-terminal hydrolase 5 (UCH...
|
PMID: 22057347
PDF is available here.
PDF is available here.
Nature Medicine (17)12 2011
Abstract
We describe the small molecule b-AP15 as a previously unidentified class of proteasome inhibitor that abrogates the deubiquitinating activity of the 19S regulatory particle. b-AP15 inhibited the activity of two 19S regulatory-particle-associated deubiquitinases, ubiquitin C-terminal hydrolase 5 (UCH...
|
PMID: 22057347
PDF is available here.
PDF is available here.
Nature Medicine (17)12 2011
Abstract
We describe the small molecule b-AP15 as a previously unidentified class of proteasome inhibitor that abrogates the deubiquitinating activity of the 19S regulatory particle. b-AP15 inhibited the activity of two 19S regulatory-particle-associated deubiquitinases, ubiquitin C-terminal hydrolase 5 (UCH...
|
PMID: 22057347
PDF is available here.
PDF is available here.
Nature Medicine (17)12 2011
Abstract
We describe the small molecule b-AP15 as a previously unidentified class of proteasome inhibitor that abrogates the deubiquitinating activity of the 19S regulatory particle. b-AP15 inhibited the activity of two 19S regulatory-particle-associated deubiquitinases, ubiquitin C-terminal hydrolase 5 (UCH...
|
PMID: 22057347
PDF is available here.
PDF is available here.
Nature Medicine (17)12 2011
Abstract
We describe the small molecule b-AP15 as a previously unidentified class of proteasome inhibitor that abrogates the deubiquitinating activity of the 19S regulatory particle. b-AP15 inhibited the activity of two 19S regulatory-particle-associated deubiquitinases, ubiquitin C-terminal hydrolase 5 (UCH...
|
PMID: 22057347
PDF is available here.
PDF is available here.
Nature Medicine (17)12 2011
Abstract
We describe the small molecule b-AP15 as a previously unidentified class of proteasome inhibitor that abrogates the deubiquitinating activity of the 19S regulatory particle. b-AP15 inhibited the activity of two 19S regulatory-particle-associated deubiquitinases, ubiquitin C-terminal hydrolase 5 (UCH...
|
PMID: 22057347
PDF is available here.
PDF is available here.
Nature Medicine (17)12 2011
Abstract
We describe the small molecule b-AP15 as a previously unidentified class of proteasome inhibitor that abrogates the deubiquitinating activity of the 19S regulatory particle. b-AP15 inhibited the activity of two 19S regulatory-particle-associated deubiquitinases, ubiquitin C-terminal hydrolase 5 (UCH...
|
PMID: 22057347
PDF is available here.
PDF is available here.
Nature Medicine (17)12 2011
Abstract
We describe the small molecule b-AP15 as a previously unidentified class of proteasome inhibitor that abrogates the deubiquitinating activity of the 19S regulatory particle. b-AP15 inhibited the activity of two 19S regulatory-particle-associated deubiquitinases, ubiquitin C-terminal hydrolase 5 (UCH...
|
PMID: 22057347
PDF is available here.
PDF is available here.
Nature Medicine (17)12 2011
Abstract
We describe the small molecule b-AP15 as a previously unidentified class of proteasome inhibitor that abrogates the deubiquitinating activity of the 19S regulatory particle. b-AP15 inhibited the activity of two 19S regulatory-particle-associated deubiquitinases, ubiquitin C-terminal hydrolase 5 (UCH...
|
PMID: 22057347
PDF is available here.
PDF is available here.
Nature Medicine (17)12 2011
Abstract
We describe the small molecule b-AP15 as a previously unidentified class of proteasome inhibitor that abrogates the deubiquitinating activity of the 19S regulatory particle. b-AP15 inhibited the activity of two 19S regulatory-particle-associated deubiquitinases, ubiquitin C-terminal hydrolase 5 (UCH...
|
PMID: 22057347
PDF is available here.
PDF is available here.
Nature Medicine (17)12 2011
Abstract
We describe the small molecule b-AP15 as a previously unidentified class of proteasome inhibitor that abrogates the deubiquitinating activity of the 19S regulatory particle. b-AP15 inhibited the activity of two 19S regulatory-particle-associated deubiquitinases, ubiquitin C-terminal hydrolase 5 (UCH...
|
PMID: 22057347
PDF is available here.
PDF is available here.
Nature Medicine (17)12 2011
Abstract
We describe the small molecule b-AP15 as a previously unidentified class of proteasome inhibitor that abrogates the deubiquitinating activity of the 19S regulatory particle. b-AP15 inhibited the activity of two 19S regulatory-particle-associated deubiquitinases, ubiquitin C-terminal hydrolase 5 (UCH...
|
PMID: 22057347
PDF is available here.
PDF is available here.
Nature Medicine (17)12 2011
Abstract
We describe the small molecule b-AP15 as a previously unidentified class of proteasome inhibitor that abrogates the deubiquitinating activity of the 19S regulatory particle. b-AP15 inhibited the activity of two 19S regulatory-particle-associated deubiquitinases, ubiquitin C-terminal hydrolase 5 (UCH...
|
PMID: 22057347
PDF is available here.
PDF is available here.
Nature Medicine (17)12 2011
Abstract
We describe the small molecule b-AP15 as a previously unidentified class of proteasome inhibitor that abrogates the deubiquitinating activity of the 19S regulatory particle. b-AP15 inhibited the activity of two 19S regulatory-particle-associated deubiquitinases, ubiquitin C-terminal hydrolase 5 (UCH...
|
PMID: 22057347
PDF is available here.
PDF is available here.
Nature Medicine (17)12 2011
Abstract
We describe the small molecule b-AP15 as a previously unidentified class of proteasome inhibitor that abrogates the deubiquitinating activity of the 19S regulatory particle. b-AP15 inhibited the activity of two 19S regulatory-particle-associated deubiquitinases, ubiquitin C-terminal hydrolase 5 (UCH...
|
PMID: 22057347
PDF is available here.
PDF is available here.
Nature Medicine (17)12 2011
Abstract
We describe the small molecule b-AP15 as a previously unidentified class of proteasome inhibitor that abrogates the deubiquitinating activity of the 19S regulatory particle. b-AP15 inhibited the activity of two 19S regulatory-particle-associated deubiquitinases, ubiquitin C-terminal hydrolase 5 (UCH...
|
PMID: 22057347
PDF is available here.
PDF is available here.
Nature Medicine (17)12 2011
Abstract
We describe the small molecule b-AP15 as a previously unidentified class of proteasome inhibitor that abrogates the deubiquitinating activity of the 19S regulatory particle. b-AP15 inhibited the activity of two 19S regulatory-particle-associated deubiquitinases, ubiquitin C-terminal hydrolase 5 (UCH...
|
PMID: 22057347
PDF is available here.
PDF is available here.
Nature Medicine (17)12 2011
Abstract
We describe the small molecule b-AP15 as a previously unidentified class of proteasome inhibitor that abrogates the deubiquitinating activity of the 19S regulatory particle. b-AP15 inhibited the activity of two 19S regulatory-particle-associated deubiquitinases, ubiquitin C-terminal hydrolase 5 (UCH...
|
PMID: 22057347
PDF is available here.
PDF is available here.
Nature Medicine (17)12 2011
Abstract
We describe the small molecule b-AP15 as a previously unidentified class of proteasome inhibitor that abrogates the deubiquitinating activity of the 19S regulatory particle. b-AP15 inhibited the activity of two 19S regulatory-particle-associated deubiquitinases, ubiquitin C-terminal hydrolase 5 (UCH...
|
PMID: 22057347
PDF is available here.
PDF is available here.
Nature Medicine (17)12 2011
Abstract
We describe the small molecule b-AP15 as a previously unidentified class of proteasome inhibitor that abrogates the deubiquitinating activity of the 19S regulatory particle. b-AP15 inhibited the activity of two 19S regulatory-particle-associated deubiquitinases, ubiquitin C-terminal hydrolase 5 (UCH...
|
PMID: 22057347
PDF is available here.
PDF is available here.
Nature Medicine (17)12 2011
Abstract
We describe the small molecule b-AP15 as a previously unidentified class of proteasome inhibitor that abrogates the deubiquitinating activity of the 19S regulatory particle. b-AP15 inhibited the activity of two 19S regulatory-particle-associated deubiquitinases, ubiquitin C-terminal hydrolase 5 (UCH...
|
PMID: 22057347
PDF is available here.
PDF is available here.
Nature Medicine (17)12 2011
Abstract
We describe the small molecule b-AP15 as a previously unidentified class of proteasome inhibitor that abrogates the deubiquitinating activity of the 19S regulatory particle. b-AP15 inhibited the activity of two 19S regulatory-particle-associated deubiquitinases, ubiquitin C-terminal hydrolase 5 (UCH...
|
PMID: 22057347
PDF is available here.
PDF is available here.
Nature Medicine (17)12 2011
Abstract
We describe the small molecule b-AP15 as a previously unidentified class of proteasome inhibitor that abrogates the deubiquitinating activity of the 19S regulatory particle. b-AP15 inhibited the activity of two 19S regulatory-particle-associated deubiquitinases, ubiquitin C-terminal hydrolase 5 (UCH...
|
PMID: 22057347
PDF is available here.
PDF is available here.
Nature Medicine (17)12 2011
Abstract
We describe the small molecule b-AP15 as a previously unidentified class of proteasome inhibitor that abrogates the deubiquitinating activity of the 19S regulatory particle. b-AP15 inhibited the activity of two 19S regulatory-particle-associated deubiquitinases, ubiquitin C-terminal hydrolase 5 (UCH...
|
PMID: 22057347
PDF is available here.
PDF is available here.
Nature Medicine (17)12 2011
Abstract
We describe the small molecule b-AP15 as a previously unidentified class of proteasome inhibitor that abrogates the deubiquitinating activity of the 19S regulatory particle. b-AP15 inhibited the activity of two 19S regulatory-particle-associated deubiquitinases, ubiquitin C-terminal hydrolase 5 (UCH...
|
PMID: 22057347
PDF is available here.
PDF is available here.
Nature Medicine (17)12 2011
Abstract
We describe the small molecule b-AP15 as a previously unidentified class of proteasome inhibitor that abrogates the deubiquitinating activity of the 19S regulatory particle. b-AP15 inhibited the activity of two 19S regulatory-particle-associated deubiquitinases, ubiquitin C-terminal hydrolase 5 (UCH...
|
PMID: 22057347
PDF is available here.
PDF is available here.
Nature Medicine (17)12 2011
Abstract
We describe the small molecule b-AP15 as a previously unidentified class of proteasome inhibitor that abrogates the deubiquitinating activity of the 19S regulatory particle. b-AP15 inhibited the activity of two 19S regulatory-particle-associated deubiquitinases, ubiquitin C-terminal hydrolase 5 (UCH...
|
PMID: 22057347
PDF is available here.
PDF is available here.
Nature Medicine (17)12 2011
Abstract
We describe the small molecule b-AP15 as a previously unidentified class of proteasome inhibitor that abrogates the deubiquitinating activity of the 19S regulatory particle. b-AP15 inhibited the activity of two 19S regulatory-particle-associated deubiquitinases, ubiquitin C-terminal hydrolase 5 (UCH...
|
PMID: 22057347
PDF is available here.
PDF is available here.
Nature Medicine (17)12 2011
Abstract
We describe the small molecule b-AP15 as a previously unidentified class of proteasome inhibitor that abrogates the deubiquitinating activity of the 19S regulatory particle. b-AP15 inhibited the activity of two 19S regulatory-particle-associated deubiquitinases, ubiquitin C-terminal hydrolase 5 (UCH...
|
PMID: 22057347
PDF is available here.
PDF is available here.
Nature Medicine (17)12 2011
Abstract
We describe the small molecule b-AP15 as a previously unidentified class of proteasome inhibitor that abrogates the deubiquitinating activity of the 19S regulatory particle. b-AP15 inhibited the activity of two 19S regulatory-particle-associated deubiquitinases, ubiquitin C-terminal hydrolase 5 (UCH...
|
PMID: 22057347
PDF is available here.
PDF is available here.
Nature Medicine (17)12 2011
Abstract
We describe the small molecule b-AP15 as a previously unidentified class of proteasome inhibitor that abrogates the deubiquitinating activity of the 19S regulatory particle. b-AP15 inhibited the activity of two 19S regulatory-particle-associated deubiquitinases, ubiquitin C-terminal hydrolase 5 (UCH...
|
PMID: 22057347
PDF is available here.
PDF is available here.
Nature Medicine (17)12 2011
Abstract
We describe the small molecule b-AP15 as a previously unidentified class of proteasome inhibitor that abrogates the deubiquitinating activity of the 19S regulatory particle. b-AP15 inhibited the activity of two 19S regulatory-particle-associated deubiquitinases, ubiquitin C-terminal hydrolase 5 (UCH...
|
PMID: 22057347
PDF is available here.
PDF is available here.
Nature Medicine (17)12 2011
Abstract
We describe the small molecule b-AP15 as a previously unidentified class of proteasome inhibitor that abrogates the deubiquitinating activity of the 19S regulatory particle. b-AP15 inhibited the activity of two 19S regulatory-particle-associated deubiquitinases, ubiquitin C-terminal hydrolase 5 (UCH...
|
PMID: 22057347
PDF is available here.
PDF is available here.
Nature Medicine (17)12 2011
Abstract
We describe the small molecule b-AP15 as a previously unidentified class of proteasome inhibitor that abrogates the deubiquitinating activity of the 19S regulatory particle. b-AP15 inhibited the activity of two 19S regulatory-particle-associated deubiquitinases, ubiquitin C-terminal hydrolase 5 (UCH...
|
PMID: 22057347
PDF is available here.
PDF is available here.
Nature Medicine (17)12 2011
Abstract
We describe the small molecule b-AP15 as a previously unidentified class of proteasome inhibitor that abrogates the deubiquitinating activity of the 19S regulatory particle. b-AP15 inhibited the activity of two 19S regulatory-particle-associated deubiquitinases, ubiquitin C-terminal hydrolase 5 (UCH...
|
PMID: 22057347
PDF is available here.
PDF is available here.
Nature Medicine (17)12 2011
Abstract
We describe the small molecule b-AP15 as a previously unidentified class of proteasome inhibitor that abrogates the deubiquitinating activity of the 19S regulatory particle. b-AP15 inhibited the activity of two 19S regulatory-particle-associated deubiquitinases, ubiquitin C-terminal hydrolase 5 (UCH...
|
PMID: 22057347
PDF is available here.
PDF is available here.
Nature Medicine (17)12 2011
Abstract
We describe the small molecule b-AP15 as a previously unidentified class of proteasome inhibitor that abrogates the deubiquitinating activity of the 19S regulatory particle. b-AP15 inhibited the activity of two 19S regulatory-particle-associated deubiquitinases, ubiquitin C-terminal hydrolase 5 (UCH...
|
PMID: 22057347
PDF is available here.
PDF is available here.
Nature Medicine (17)12 2011
Abstract
We describe the small molecule b-AP15 as a previously unidentified class of proteasome inhibitor that abrogates the deubiquitinating activity of the 19S regulatory particle. b-AP15 inhibited the activity of two 19S regulatory-particle-associated deubiquitinases, ubiquitin C-terminal hydrolase 5 (UCH...
|
PMID: 22057347
PDF is available here.
PDF is available here.
Nature Medicine (17)12 2011
Abstract
We describe the small molecule b-AP15 as a previously unidentified class of proteasome inhibitor that abrogates the deubiquitinating activity of the 19S regulatory particle. b-AP15 inhibited the activity of two 19S regulatory-particle-associated deubiquitinases, ubiquitin C-terminal hydrolase 5 (UCH...
|
PMID: 22057347
PDF is available here.
PDF is available here.
Nature Medicine (17)12 2011
Abstract
We describe the small molecule b-AP15 as a previously unidentified class of proteasome inhibitor that abrogates the deubiquitinating activity of the 19S regulatory particle. b-AP15 inhibited the activity of two 19S regulatory-particle-associated deubiquitinases, ubiquitin C-terminal hydrolase 5 (UCH...
|
PMID: 22057347
PDF is available here.
PDF is available here.
Nature Medicine (17)12 2011
Abstract
We describe the small molecule b-AP15 as a previously unidentified class of proteasome inhibitor that abrogates the deubiquitinating activity of the 19S regulatory particle. b-AP15 inhibited the activity of two 19S regulatory-particle-associated deubiquitinases, ubiquitin C-terminal hydrolase 5 (UCH...
|
PMID: 22057347
PDF is available here.
PDF is available here.