Detalhe da pesquisa
1.
The ChlD subunit links the motor and porphyrin binding subunits of magnesium chelatase.
Biochem J
; 476(13): 1875-1887, 2019 07 02.
Artigo
em Inglês
| MEDLINE | ID: mdl-31164400
2.
Probing the quality control mechanism of the Escherichia coli twin-arginine translocase with folding variants of a de novo-designed heme protein.
J Biol Chem
; 293(18): 6672-6681, 2018 05 04.
Artigo
em Inglês
| MEDLINE | ID: mdl-29559557
3.
Porphyrin Binding to Gun4 Protein, Facilitated by a Flexible Loop, Controls Metabolite Flow through the Chlorophyll Biosynthetic Pathway.
J Biol Chem
; 290(47): 28477-28488, 2015 Nov 20.
Artigo
em Inglês
| MEDLINE | ID: mdl-26446792
4.
Nanomechanical and Thermophoretic Analyses of the Nucleotide-Dependent Interactions between the AAA(+) Subunits of Magnesium Chelatase.
J Am Chem Soc
; 138(20): 6591-7, 2016 05 25.
Artigo
em Inglês
| MEDLINE | ID: mdl-27133226
5.
Five glutamic acid residues in the C-terminal domain of the ChlD subunit play a major role in conferring Mg(2+) cooperativity upon magnesium chelatase.
Biochemistry
; 54(44): 6659-62, 2015 Nov 10.
Artigo
em Inglês
| MEDLINE | ID: mdl-26513685
6.
Characterization of the magnesium chelatase from Thermosynechococcus elongatus.
Biochem J
; 457(1): 163-70, 2014 Jan 01.
Artigo
em Inglês
| MEDLINE | ID: mdl-24138165
7.
Structural and functional consequences of removing the N-terminal domain from the magnesium chelatase ChlH subunit of Thermosynechococcus elongatus.
Biochem J
; 464(3): 315-22, 2014 Dec 15.
Artigo
em Inglês
| MEDLINE | ID: mdl-25471602
8.
The allosteric role of the AAA+ domain of ChlD protein from the magnesium chelatase of synechocystis species PCC 6803.
J Biol Chem
; 288(40): 28727-32, 2013 Oct 04.
Artigo
em Inglês
| MEDLINE | ID: mdl-23940041
9.
Efficient and Targeted siRNA Delivery to M2 Macrophages by Smart Polymer Blends for M1 Macrophage Repolarization as a Promising Strategy for Future Cancer Treatment.
ACS Biomater Sci Eng
; 10(1): 166-177, 2024 Jan 08.
Artigo
em Inglês
| MEDLINE | ID: mdl-37978912
10.
Chlorophyll biosynthesis under the control of arginine metabolism.
Cell Rep
; 42(11): 113265, 2023 11 28.
Artigo
em Inglês
| MEDLINE | ID: mdl-37864789
11.
Nonequilibrium isotope exchange reveals a catalytically significant enzyme-phosphate complex in the ATP hydrolysis pathway of the AAA(+) ATPase magnesium chelatase.
Biochemistry
; 51(10): 2029-31, 2012 Mar 13.
Artigo
em Inglês
| MEDLINE | ID: mdl-22372406
12.
Spray drying siRNA-lipid nanoparticles for dry powder pulmonary delivery.
J Control Release
; 351: 137-150, 2022 11.
Artigo
em Inglês
| MEDLINE | ID: mdl-36126785
13.
How the O2-dependent Mg-protoporphyrin monomethyl ester cyclase forms the fifth ring of chlorophylls.
Nat Plants
; 7(3): 365-375, 2021 03.
Artigo
em Inglês
| MEDLINE | ID: mdl-33731920
14.
Transporter characterisation reveals aminoethylphosphonate mineralisation as a key step in the marine phosphorus redox cycle.
Nat Commun
; 12(1): 4554, 2021 07 27.
Artigo
em Inglês
| MEDLINE | ID: mdl-34315891
15.
Quantifying the Interaction of Phosphite with ABC Transporters: MicroScale Thermophoresis and a Novel His-Tag Labeling Approach.
Methods Mol Biol
; 2168: 51-62, 2020.
Artigo
em Inglês
| MEDLINE | ID: mdl-33582986
16.
The active site of magnesium chelatase.
Nat Plants
; 6(12): 1491-1502, 2020 12.
Artigo
em Inglês
| MEDLINE | ID: mdl-33257858
17.
Phosphite binding by the HtxB periplasmic binding protein depends on the protonation state of the ligand.
Sci Rep
; 9(1): 10231, 2019 07 15.
Artigo
em Inglês
| MEDLINE | ID: mdl-31308436
18.
The molecular basis of phosphite and hypophosphite recognition by ABC-transporters.
Nat Commun
; 8(1): 1746, 2017 11 23.
Artigo
em Inglês
| MEDLINE | ID: mdl-29170493
19.
The catalytic power of magnesium chelatase: a benchmark for the AAA(+) ATPases.
FEBS Lett
; 590(12): 1687-93, 2016 06.
Artigo
em Inglês
| MEDLINE | ID: mdl-27176620
20.
Synthesis and evaluation of anticancer natural product analogues based on angelmarin: targeting the tolerance towards nutrient deprivation.
ChemMedChem
; 7(5): 766-70, 2012 May.
Artigo
em Inglês
| MEDLINE | ID: mdl-22431333