Detalhe da pesquisa
1.
Dual RING E3 Architectures Regulate Multiubiquitination and Ubiquitin Chain Elongation by APC/C.
Cell
; 165(6): 1440-1453, 2016 Jun 02.
Artigo
em Inglês
| MEDLINE | ID: mdl-27259151
2.
Mechanism for the activation of the anaplastic lymphoma kinase receptor.
Nature
; 600(7887): 153-157, 2021 12.
Artigo
em Inglês
| MEDLINE | ID: mdl-34819673
3.
A bromodomain-independent mechanism of gene regulation by the BET inhibitor JQ1: direct activation of nuclear receptor PXR.
Nucleic Acids Res
; 52(4): 1661-1676, 2024 Feb 28.
Artigo
em Inglês
| MEDLINE | ID: mdl-38084912
4.
Structure-guided approach to modulate small molecule binding to a promiscuous ligand-activated protein.
Proc Natl Acad Sci U S A
; 120(10): e2217804120, 2023 03 07.
Artigo
em Inglês
| MEDLINE | ID: mdl-36848571
5.
Biochemical characterization of the first step in sulfonolipid biosynthesis in Alistipes finegoldii.
J Biol Chem
; 298(8): 102195, 2022 08.
Artigo
em Inglês
| MEDLINE | ID: mdl-35760102
6.
Protein engineering of a ubiquitin-variant inhibitor of APC/C identifies a cryptic K48 ubiquitin chain binding site.
Proc Natl Acad Sci U S A
; 116(35): 17280-17289, 2019 08 27.
Artigo
em Inglês
| MEDLINE | ID: mdl-31350353
7.
The genome of a Bacteroidetes inhabitant of the human gut encodes a structurally distinct enoyl-acyl carrier protein reductase (FabI).
J Biol Chem
; 295(22): 7635-7652, 2020 05 29.
Artigo
em Inglês
| MEDLINE | ID: mdl-32317282
8.
Unraveling the Structural Basis of Selective Inhibition of Human Cytochrome P450 3A5.
J Am Chem Soc
; 143(44): 18467-18480, 2021 11 10.
Artigo
em Inglês
| MEDLINE | ID: mdl-34648292
9.
Structural and functional insights into the interaction between the Cas family scaffolding protein p130Cas and the focal adhesion-associated protein paxillin.
J Biol Chem
; 292(44): 18281-18289, 2017 11 03.
Artigo
em Inglês
| MEDLINE | ID: mdl-28860193
10.
Biochemical Roles for Conserved Residues in the Bacterial Fatty Acid-binding Protein Family.
J Biol Chem
; 291(12): 6292-303, 2016 Mar 18.
Artigo
em Inglês
| MEDLINE | ID: mdl-26774272
11.
Insights into ubiquitin transfer cascades from a structure of a UbcH5B approximately ubiquitin-HECT(NEDD4L) complex.
Mol Cell
; 36(6): 1095-102, 2009 Dec 25.
Artigo
em Inglês
| MEDLINE | ID: mdl-20064473
12.
Structures of SPOP-substrate complexes: insights into molecular architectures of BTB-Cul3 ubiquitin ligases.
Mol Cell
; 36(1): 39-50, 2009 Oct 09.
Artigo
em Inglês
| MEDLINE | ID: mdl-19818708
13.
Structural Basis for the Interaction between Pyk2-FAT Domain and Leupaxin LD Repeats.
Biochemistry
; 55(9): 1332-45, 2016 Mar 08.
Artigo
em Inglês
| MEDLINE | ID: mdl-26866573
14.
Chemical manipulation of an activation/inhibition switch in the nuclear receptor PXR.
Nat Commun
; 15(1): 4054, 2024 May 14.
Artigo
em Inglês
| MEDLINE | ID: mdl-38744881
15.
Selective CK1α degraders exert antiproliferative activity against a broad range of human cancer cell lines.
Nat Commun
; 15(1): 482, 2024 Jan 16.
Artigo
em Inglês
| MEDLINE | ID: mdl-38228616
16.
How the MccB bacterial ancestor of ubiquitin E1 initiates biosynthesis of the microcin C7 antibiotic.
EMBO J
; 28(13): 1953-64, 2009 Jul 08.
Artigo
em Inglês
| MEDLINE | ID: mdl-19494832
17.
Ligand flexibility and binding pocket malleability cooperate to allow selective PXR activation by analogs of a promiscuous nuclear receptor ligand.
Structure
; 31(12): 1545-1555.e9, 2023 12 07.
Artigo
em Inglês
| MEDLINE | ID: mdl-37729916
18.
Biophysical analysis of the Mycobacteria tuberculosis peptide binding protein DppA reveals a stringent peptide binding pocket.
Tuberculosis (Edinb)
; 132: 102157, 2022 01.
Artigo
em Inglês
| MEDLINE | ID: mdl-34894561
19.
Analysis of the Staphylococcus aureus DgkB structure reveals a common catalytic mechanism for the soluble diacylglycerol kinases.
Structure
; 16(7): 1036-46, 2008 Jul.
Artigo
em Inglês
| MEDLINE | ID: mdl-18611377
20.
Structural basis for substrate recognition and chemical inhibition of oncogenic MAGE ubiquitin ligases.
Nat Commun
; 11(1): 4931, 2020 10 01.
Artigo
em Inglês
| MEDLINE | ID: mdl-33004795