Detalhe da pesquisa
1.
Structure and Function of the AAA+ ATPase p97, a Key Player in Protein Homeostasis.
Subcell Biochem
; 93: 221-272, 2019.
Artigo
em Inglês
| MEDLINE | ID: mdl-31939153
2.
Catalysis of a new ribose carbon-insertion reaction by the molybdenum cofactor biosynthetic enzyme MoaA.
Biochemistry
; 52(7): 1134-6, 2013 Feb 19.
Artigo
em Inglês
| MEDLINE | ID: mdl-23286307
3.
The structural and functional basis of the p97/valosin-containing protein (VCP)-interacting motif (VIM): mutually exclusive binding of cofactors to the N-terminal domain of p97.
J Biol Chem
; 286(44): 38679-38690, 2011 Nov 04.
Artigo
em Inglês
| MEDLINE | ID: mdl-21914798
4.
Fragment screening using biolayer interferometry reveals ligands targeting the SHP-motif binding site of the AAA+ ATPase p97.
Commun Chem
; 5(1): 169, 2022 Dec 07.
Artigo
em Inglês
| MEDLINE | ID: mdl-36697690
5.
The yeast E4 ubiquitin ligase Ufd2 interacts with the ubiquitin-like domains of Rad23 and Dsk2 via a novel and distinct ubiquitin-like binding domain.
J Biol Chem
; 285(26): 20390-8, 2010 Jun 25.
Artigo
em Inglês
| MEDLINE | ID: mdl-20427284
6.
Crystal structure of the FeS cluster-containing nucleotide excision repair helicase XPD.
PLoS Biol
; 6(6): e149, 2008 Jun 24.
Artigo
em Inglês
| MEDLINE | ID: mdl-18578568
7.
ENDOR spectroscopy shows that guanine N1 binds to [4Fe-4S] cluster II of the S-adenosylmethionine-dependent enzyme MoaA: mechanistic implications.
J Am Chem Soc
; 131(26): 9184-5, 2009 Jul 08.
Artigo
em Inglês
| MEDLINE | ID: mdl-19566093
8.
The sulfurtransferase activity of Uba4 presents a link between ubiquitin-like protein conjugation and activation of sulfur carrier proteins.
Biochemistry
; 47(24): 6479-89, 2008 Jun 17.
Artigo
em Inglês
| MEDLINE | ID: mdl-18491921
9.
The Interplay of Cofactor Interactions and Post-translational Modifications in the Regulation of the AAA+ ATPase p97.
Front Mol Biosci
; 4: 21, 2017.
Artigo
em Inglês
| MEDLINE | ID: mdl-28451587
10.
Structural Basis of ATP Hydrolysis and Intersubunit Signaling in the AAA+ ATPase p97.
Structure
; 24(1): 127-139, 2016 Jan 05.
Artigo
em Inglês
| MEDLINE | ID: mdl-26712278
11.
Characterization of an Additional Binding Surface on the p97 N-Terminal Domain Involved in Bipartite Cofactor Interactions.
Structure
; 24(1): 140-147, 2016 Jan 05.
Artigo
em Inglês
| MEDLINE | ID: mdl-26712280
12.
Control of p97 function by cofactor binding.
FEBS Lett
; 589(19 Pt A): 2578-89, 2015 Sep 14.
Artigo
em Inglês
| MEDLINE | ID: mdl-26320413
13.
Structural insights into functional modes of proteins involved in ubiquitin family pathways.
Methods Mol Biol
; 832: 547-76, 2012.
Artigo
em Inglês
| MEDLINE | ID: mdl-22350912
14.
The Fe(II)/α-ketoglutarate-dependent taurine dioxygenases from Pseudomonas putida and Escherichia coli are tetramers.
FEBS J
; 279(5): 816-31, 2012 Mar.
Artigo
em Inglês
| MEDLINE | ID: mdl-22221834
15.
Hierarchical binding of cofactors to the AAA ATPase p97.
Structure
; 19(6): 833-43, 2011 Jun 08.
Artigo
em Inglês
| MEDLINE | ID: mdl-21645854
16.
Crystal structure of YnjE from Escherichia coli, a sulfurtransferase with three rhodanese domains.
Protein Sci
; 18(12): 2480-91, 2009 Dec.
Artigo
em Inglês
| MEDLINE | ID: mdl-19798741
17.
Binding of 5'-GTP to the C-terminal FeS cluster of the radical S-adenosylmethionine enzyme MoaA provides insights into its mechanism.
Proc Natl Acad Sci U S A
; 103(18): 6829-34, 2006 May 02.
Artigo
em Inglês
| MEDLINE | ID: mdl-16632608
18.
Crystal structure of the S-adenosylmethionine-dependent enzyme MoaA and its implications for molybdenum cofactor deficiency in humans.
Proc Natl Acad Sci U S A
; 101(35): 12870-5, 2004 Aug 31.
Artigo
em Inglês
| MEDLINE | ID: mdl-15317939
19.
Functionality of alternative splice forms of the first enzymes involved in human molybdenum cofactor biosynthesis.
J Biol Chem
; 277(21): 18303-12, 2002 May 24.
Artigo
em Inglês
| MEDLINE | ID: mdl-11891227
20.
Characterization of MOCS1A, an oxygen-sensitive iron-sulfur protein involved in human molybdenum cofactor biosynthesis.
J Biol Chem
; 279(33): 34721-32, 2004 Aug 13.
Artigo
em Inglês
| MEDLINE | ID: mdl-15180982