Lista de obras - Silvia Zorrilla - Dominio Público Uruguay

A phospho-sugar binding domain homologous to NagB enzymes regulates the activity of the central glycolytic genes repressor.

artículo científico publicado en 2008

Bacterial FtsZ protein forms phase-separated condensates with its nucleoid-associated inhibitor SlmA

scientific article published on 06 December 2018

Charged Molecules Modulate the Volume Exclusion Effects Exerted by Crowders on FtsZ Polymerization

artículo científico publicado en 2016

Combined Biophysical and Cell-Based Approaches for the Assessment of Ligand Binding to PPARγ

artículo científico publicado en 2013

Combined analytical ultracentrifugation, light scattering and fluorescence spectroscopy studies on the functional associations of the bacterial division FtsZ protein ⬇️

artículo científico publicado el 5 de enero de 2013

Development of a homogeneous fluorescence anisotropy assay to monitor and measure FtsZ assembly in solution.

artículo científico publicado en 2011

Drawbacks of Dialysis Procedures for Removal of EDTA.

artículo científico publicado en 2017

Dynamic interaction of the Escherichia coli cell division ZipA and FtsZ proteins evidenced in nanodiscs.

artículo científico publicado en 2012

Encapsulation of a compartmentalized cytoplasm mimic within a lipid membrane by microfluidics.

artículo científico publicado en 2017

Evidence That Bacteriophage λ Kil Peptide Inhibits Bacterial Cell Division by Disrupting FtsZ Protofilaments and Sequestering Protein Subunits

artículo científico publicado en 2015

Fluorescence anisotropy as a probe to study tracer proteins in crowded solutions.

artículo científico publicado en 2004

Fructose-1,6-bisphosphate acts both as an inducer and as a structural cofactor of the central glycolytic genes repressor (CggR).

artículo científico publicado en 2007

Gbp2 interacts with THO/TREX through a novel type of RRM domain.

artículo científico publicado en 2015

Integrated approaches to unravel the impact of protein lipoxidation on macromolecular interactions

artículo científico publicado en 2019

Isolation, Characterization and Lipid-Binding Properties of the Recalcitrant FtsA Division Protein from Escherichia coli ⬇️

artículo científico publicado el 27 de junio de 2012

Macromolecular interactions of the bacterial division FtsZ protein: from quantitative biochemistry and crowding to reconstructing minimal divisomes in the test tube

artículo científico publicado en 2013

Magnesium-induced linear self-association of the FtsZ bacterial cell division protein monomer. The primary steps for FtsZ assembly

scientific article published on 01 April 2000

Mg2+-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 ⬇️

artículo científico publicado el 22 de mayo de 2012

Microenvironments created by liquid-liquid phase transition control the dynamic distribution of bacterial division FtsZ protein

artículo científico publicado en 2016

MinC protein shortens FtsZ protofilaments by preferentially interacting with GDP-bound subunits

artículo científico publicado en 2013

Molecular basis for group-specific activation of the virulence regulator PlcR by PapR heptapeptides

artículo científico publicado en 2008

Nucleotide and receptor density modulate binding of bacterial division FtsZ protein to ZipA containing lipid-coated microbeads.

artículo científico publicado en 2017

Protein self-association in crowded protein solutions: a time-resolved fluorescence polarization study.

artículo científico publicado en 2004

Quantitative investigation of biomolecular interactions in crowded media by fluorescence spectroscopy, a good choice.

scientific article published on August 2009

Sedimentation equilibrium in a solution containing an arbitrary number of solute species at arbitrary concentrations: theory and application to concentrated solutions of ribonuclease.

artículo científico publicado en 2004

The Bacterial DNA Binding Protein MatP Involved in Linking the Nucleoid Terminal Domain to the Divisome at Midcell Interacts with Lipid Membranes.

artículo científico publicado en 2019

The Nucleoid Occlusion Protein SlmA Binds to Lipid Membranes

artículo científico publicado en 2020

The Nucleoid Occlusion SlmA Protein Accelerates the Disassembly of the FtsZ Protein Polymers without Affecting Their GTPase Activity

artículo científico publicado en 2015

The structure of transcription termination factor Nrd1 reveals an original mode for GUAA recognition.

artículo científico publicado en 2017

Translational and rotational motions of proteins in a protein crowded environment

artículo científico publicado en 2006

Lista de obras de Silvia Zorrilla

A phospho-sugar binding domain homologous to NagB enzymes regulates the activity of the central glycolytic genes repressor.

Bacterial FtsZ protein forms phase-separated condensates with its nucleoid-associated inhibitor SlmA

Charged Molecules Modulate the Volume Exclusion Effects Exerted by Crowders on FtsZ Polymerization

Combined Biophysical and Cell-Based Approaches for the Assessment of Ligand Binding to PPARγ

Combined analytical ultracentrifugation, light scattering and fluorescence spectroscopy studies on the functional associations of the bacterial division FtsZ protein ⬇️

Development of a homogeneous fluorescence anisotropy assay to monitor and measure FtsZ assembly in solution.

Drawbacks of Dialysis Procedures for Removal of EDTA.

Dynamic interaction of the Escherichia coli cell division ZipA and FtsZ proteins evidenced in nanodiscs.

Encapsulation of a compartmentalized cytoplasm mimic within a lipid membrane by microfluidics.

Evidence That Bacteriophage λ Kil Peptide Inhibits Bacterial Cell Division by Disrupting FtsZ Protofilaments and Sequestering Protein Subunits

Fluorescence anisotropy as a probe to study tracer proteins in crowded solutions.

Fructose-1,6-bisphosphate acts both as an inducer and as a structural cofactor of the central glycolytic genes repressor (CggR).

Gbp2 interacts with THO/TREX through a novel type of RRM domain.

Integrated approaches to unravel the impact of protein lipoxidation on macromolecular interactions

Isolation, Characterization and Lipid-Binding Properties of the Recalcitrant FtsA Division Protein from Escherichia coli ⬇️

Macromolecular interactions of the bacterial division FtsZ protein: from quantitative biochemistry and crowding to reconstructing minimal divisomes in the test tube

Magnesium-induced linear self-association of the FtsZ bacterial cell division protein monomer. The primary steps for FtsZ assembly

Mg2+-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 ⬇️

Microenvironments created by liquid-liquid phase transition control the dynamic distribution of bacterial division FtsZ protein

MinC protein shortens FtsZ protofilaments by preferentially interacting with GDP-bound subunits

Molecular basis for group-specific activation of the virulence regulator PlcR by PapR heptapeptides

Nucleotide and receptor density modulate binding of bacterial division FtsZ protein to ZipA containing lipid-coated microbeads.

Protein self-association in crowded protein solutions: a time-resolved fluorescence polarization study.

Quantitative investigation of biomolecular interactions in crowded media by fluorescence spectroscopy, a good choice.

Sedimentation equilibrium in a solution containing an arbitrary number of solute species at arbitrary concentrations: theory and application to concentrated solutions of ribonuclease.

The Bacterial DNA Binding Protein MatP Involved in Linking the Nucleoid Terminal Domain to the Divisome at Midcell Interacts with Lipid Membranes.

The Nucleoid Occlusion Protein SlmA Binds to Lipid Membranes

The Nucleoid Occlusion SlmA Protein Accelerates the Disassembly of the FtsZ Protein Polymers without Affecting Their GTPase Activity

The structure of transcription termination factor Nrd1 reveals an original mode for GUAA recognition.

Translational and rotational motions of proteins in a protein crowded environment