Detalhe da pesquisa
1.
Cryo-EM structure determination of small therapeutic protein targets at 3 Å-resolution using a rigid imaging scaffold.
Proc Natl Acad Sci U S A
; 120(37): e2305494120, 2023 09 12.
Artigo
Inglês
| MEDLINE | ID: mdl-37669364
2.
The CCP4 suite: integrative software for macromolecular crystallography.
Acta Crystallogr D Struct Biol
; 79(Pt 6): 449-461, 2023 Jun 01.
Artigo
Inglês
| MEDLINE | ID: mdl-37259835
3.
Handling ligands with Coot.
Acta Crystallogr D Biol Crystallogr
; 68(Pt 4): 425-30, 2012 Apr.
Artigo
Inglês
| MEDLINE | ID: mdl-22505262
4.
The structure of P-TEFb (CDK9/cyclin T1), its complex with flavopiridol and regulation by phosphorylation.
EMBO J
; 27(13): 1907-18, 2008 Jul 09.
Artigo
Inglês
| MEDLINE | ID: mdl-18566585
5.
Kinase domain insertions define distinct roles of CLK kinases in SR protein phosphorylation.
Structure
; 17(3): 352-62, 2009 Mar 11.
Artigo
Inglês
| MEDLINE | ID: mdl-19278650
6.
Cryo-EM: The Resolution Revolution and Drug Discovery.
SLAS Discov
; 26(1): 17-31, 2021 01.
Artigo
Inglês
| MEDLINE | ID: mdl-33016175
7.
Structure of the human protein kinase MPSK1 reveals an atypical activation loop architecture.
Structure
; 16(1): 115-24, 2008 Jan.
Artigo
Inglês
| MEDLINE | ID: mdl-18184589
8.
Structure of the SOCS4-ElonginB/C complex reveals a distinct SOCS box interface and the molecular basis for SOCS-dependent EGFR degradation.
Structure
; 15(11): 1493-504, 2007 Nov.
Artigo
Inglês
| MEDLINE | ID: mdl-17997974
9.
Crystal Structures of the p21-activated kinases PAK4, PAK5, and PAK6 reveal catalytic domain plasticity of active group II PAKs.
Structure
; 15(2): 201-13, 2007 Feb.
Artigo
Inglês
| MEDLINE | ID: mdl-17292838
10.
Structure and characterization of a high affinity C5a monoclonal antibody that blocks binding to C5aR1 and C5aR2 receptors.
MAbs
; 10(1): 104-117, 2018 01.
Artigo
Inglês
| MEDLINE | ID: mdl-28952876
11.
Crystal structures and inhibitor identification for PTPN5, PTPRR and PTPN7: a family of human MAPK-specific protein tyrosine phosphatases.
Biochem J
; 395(3): 483-91, 2006 May 01.
Artigo
Inglês
| MEDLINE | ID: mdl-16441242
12.
Structure-Guided Discovery of Potent and Selective Inhibitors of ERK1/2 from a Modestly Active and Promiscuous Chemical Start Point.
J Med Chem
; 60(8): 3438-3450, 2017 04 27.
Artigo
Inglês
| MEDLINE | ID: mdl-28376306
13.
The crystal structure of human receptor protein tyrosine phosphatase kappa phosphatase domain 1.
Protein Sci
; 15(6): 1500-5, 2006 Jun.
Artigo
Inglês
| MEDLINE | ID: mdl-16672235
14.
Utilization of Structure-Based Design to Identify Novel, Irreversible Inhibitors of EGFR Harboring the T790M Mutation.
ACS Med Chem Lett
; 7(5): 514-9, 2016 May 12.
Artigo
Inglês
| MEDLINE | ID: mdl-27190603
15.
Structural basis of inhibitor specificity of the human protooncogene proviral insertion site in moloney murine leukemia virus (PIM-1) kinase.
J Med Chem
; 48(24): 7604-14, 2005 Dec 01.
Artigo
Inglês
| MEDLINE | ID: mdl-16302800
16.
Discovery and characterization of MAPK-activated protein kinase-2 prevention of activation inhibitors.
J Med Chem
; 58(1): 278-93, 2015 Jan 08.
Artigo
Inglês
| MEDLINE | ID: mdl-25255283
17.
Structure-Guided Design of Highly Selective and Potent Covalent Inhibitors of ERK1/2.
J Med Chem
; 58(11): 4790-801, 2015 Jun 11.
Artigo
Inglês
| MEDLINE | ID: mdl-25977981
18.
Completing the structural family portrait of the human EphB tyrosine kinase domains.
Protein Sci
; 23(5): 627-38, 2014 May.
Artigo
Inglês
| MEDLINE | ID: mdl-24677421
19.
Biochemical and biophysical characterization of four EphB kinase domains reveals contrasting thermodynamic, kinetic and inhibition profiles.
Biosci Rep
; 33(3)2013 Jun 05.
Artigo
Inglês
| MEDLINE | ID: mdl-23627399
20.
Structure- and reactivity-based development of covalent inhibitors of the activating and gatekeeper mutant forms of the epidermal growth factor receptor (EGFR).
J Med Chem
; 56(17): 7025-48, 2013 Sep 12.
Artigo
Inglês
| MEDLINE | ID: mdl-23930994