Detalhe da pesquisa
1.
The solution structure, binding properties, and dynamics of the bacterial siderophore-binding protein FepB.
J Biol Chem
; 289(42): 29219-34, 2014 Oct 17.
Artigo
em Inglês
| MEDLINE | ID: mdl-25173704
2.
Role of the two structural domains from the periplasmic Escherichia coli histidine-binding protein HisJ.
J Biol Chem
; 288(44): 31409-22, 2013 Nov 01.
Artigo
em Inglês
| MEDLINE | ID: mdl-24036119
3.
NMR solution structure and biophysical characterization of Vibrio harveyi acyl carrier protein A75H: effects of divalent metal ions.
J Biol Chem
; 285(40): 30558-66, 2010 Oct 01.
Artigo
em Inglês
| MEDLINE | ID: mdl-20659901
4.
A structural and functional analysis of type III periplasmic and substrate binding proteins: their role in bacterial siderophore and heme transport.
Biol Chem
; 392(1-2): 39-52, 2011 Jan.
Artigo
em Inglês
| MEDLINE | ID: mdl-21194366
5.
A Novel extracytoplasmic function (ECF) sigma factor regulates virulence in Pseudomonas aeruginosa.
PLoS Pathog
; 5(9): e1000572, 2009 Sep.
Artigo
em Inglês
| MEDLINE | ID: mdl-19730690
6.
Genetic improvement of Saccharomyces cerevisiae for xylose fermentation.
Biotechnol Adv
; 25(5): 425-41, 2007.
Artigo
em Inglês
| MEDLINE | ID: mdl-17524590
7.
FecB, a periplasmic ferric-citrate transporter from E. coli, can bind different forms of ferric-citrate as well as a wide variety of metal-free and metal-loaded tricarboxylic acids.
Metallomics
; 8(1): 125-33, 2016 Jan.
Artigo
em Inglês
| MEDLINE | ID: mdl-26600288
8.
Mutational study of the role of N-terminal amino acid residues in tetrachlorohydroquinone reductive dehalogenase from Sphingomonas sp. UG30.
Res Microbiol
; 160(8): 553-9, 2009 Oct.
Artigo
em Inglês
| MEDLINE | ID: mdl-19682569
9.
Bioinformatic analysis of the TonB protein family.
Biometals
; 20(3-4): 467-83, 2007 Jun.
Artigo
em Inglês
| MEDLINE | ID: mdl-17225063
10.
Investigation of the role of a conserved glycine motif in the Saccharomyces cerevisiae xylose reductase.
Curr Microbiol
; 53(2): 118-23, 2006 Aug.
Artigo
em Inglês
| MEDLINE | ID: mdl-16802208