Detalhe da pesquisa
1.
Macromolecular Crowding, Phase Separation, and Homeostasis in the Orchestration of Bacterial Cellular Functions.
Chem Rev
; 124(4): 1899-1949, 2024 02 28.
Artigo
em Inglês
| MEDLINE | ID: mdl-38331392
2.
Studying Macromolecular Interactions of Cellular Machines by the Combined Use of Analytical Ultracentrifugation, Light Scattering, and Fluorescence Spectroscopy Methods.
Adv Exp Med Biol
; 3234: 89-107, 2024.
Artigo
em Inglês
| MEDLINE | ID: mdl-38507202
3.
Lipid Surfaces and Glutamate Anions Enhance Formation of Dynamic Biomolecular Condensates Containing Bacterial Cell Division Protein FtsZ and Its DNA-Bound Regulator SlmA.
Biochemistry
; 61(22): 2482-2489, 2022 11 15.
Artigo
em Inglês
| MEDLINE | ID: mdl-36315857
4.
Bacterial FtsZ protein forms phase-separated condensates with its nucleoid-associated inhibitor SlmA.
EMBO Rep
; 20(1)2019 01.
Artigo
em Inglês
| MEDLINE | ID: mdl-30523075
5.
A new calmodulin-binding motif for inositol 1,4,5-trisphosphate 3-kinase regulation.
Biochem J
; 463(3): 319-28, 2014 Nov 01.
Artigo
em Inglês
| MEDLINE | ID: mdl-25101901
6.
Control by potassium of the size distribution of Escherichia coli FtsZ polymers is independent of GTPase activity.
J Biol Chem
; 288(38): 27358-27365, 2013 Sep 20.
Artigo
em Inglês
| MEDLINE | ID: mdl-23940054
7.
MinC protein shortens FtsZ protofilaments by preferentially interacting with GDP-bound subunits.
J Biol Chem
; 288(34): 24625-35, 2013 Aug 23.
Artigo
em Inglês
| MEDLINE | ID: mdl-23853099
8.
Combined analytical ultracentrifugation, light scattering and fluorescence spectroscopy studies on the functional associations of the bacterial division FtsZ protein.
Methods
; 59(3): 349-62, 2013 Mar.
Artigo
em Inglês
| MEDLINE | ID: mdl-23296019
9.
Bacterial division ring stabilizing ZapA versus destabilizing SlmA modulate FtsZ switching between biomolecular condensates and polymers.
Open Biol
; 13(3): 220324, 2023 03.
Artigo
em Inglês
| MEDLINE | ID: mdl-36854378
10.
The Uso1 globular head interacts with SNAREs to maintain viability even in the absence of the coiled-coil domain.
Elife
; 122023 May 30.
Artigo
em Inglês
| MEDLINE | ID: mdl-37249218
11.
Benzodioxane-benzamides as promising inhibitors of Escherichia coli FtsZ.
Int J Biol Macromol
; 253(Pt 1): 126398, 2023 Dec 31.
Artigo
em Inglês
| MEDLINE | ID: mdl-37634788
12.
An equilibrium model for the Mg(2+)-linked self-assembly of FtsZ in the presence of GTP or a GTP analogue.
Biochemistry
; 51(31): 6108-13, 2012 Aug 07.
Artigo
em Inglês
| MEDLINE | ID: mdl-22809122
13.
Mg(2+)-linked self-assembly of FtsZ in the presence of GTP or a GTP analogue involves the concerted formation of a narrow size distribution of oligomeric species.
Biochemistry
; 51(22): 4541-50, 2012 Jun 05.
Artigo
em Inglês
| MEDLINE | ID: mdl-22568594
14.
The repeat domain of the melanosome fibril protein Pmel17 forms the amyloid core promoting melanin synthesis.
Proc Natl Acad Sci U S A
; 106(33): 13731-6, 2009 Aug 18.
Artigo
em Inglês
| MEDLINE | ID: mdl-19666488
15.
Development of a homogeneous fluorescence anisotropy assay to monitor and measure FtsZ assembly in solution.
Anal Biochem
; 418(1): 89-96, 2011 Nov 01.
Artigo
em Inglês
| MEDLINE | ID: mdl-21802401
16.
Reconstituting bacterial cell division assemblies in crowded, phase-separated media.
Methods Enzymol
; 646: 19-49, 2021.
Artigo
em Inglês
| MEDLINE | ID: mdl-33453926
17.
FtsZ Interactions and Biomolecular Condensates as Potential Targets for New Antibiotics.
Antibiotics (Basel)
; 10(3)2021 Mar 04.
Artigo
em Inglês
| MEDLINE | ID: mdl-33806332
18.
Assembly of bacterial cell division protein FtsZ into dynamic biomolecular condensates.
Biochim Biophys Acta Mol Cell Res
; 1868(5): 118986, 2021 04.
Artigo
em Inglês
| MEDLINE | ID: mdl-33581219
19.
The Nucleoid Occlusion Protein SlmA Binds to Lipid Membranes.
mBio
; 11(5)2020 09 01.
Artigo
em Inglês
| MEDLINE | ID: mdl-32873767
20.
The Bacterial DNA Binding Protein MatP Involved in Linking the Nucleoid Terminal Domain to the Divisome at Midcell Interacts with Lipid Membranes.
mBio
; 10(3)2019 05 28.
Artigo
em Inglês
| MEDLINE | ID: mdl-31138739