Vanessa Kiraly | Universidade de São Paulo (original) (raw)

Papers by Vanessa Kiraly

Research paper thumbnail of Some Communication Problems of Two Cases in a Suckling Hospital

Pediatric Otorhinolaryngology Japan, 1992

This article is based on a mixed research, whose objective was the use of Phonics Instruction to ... more This article is based on a mixed research, whose objective was the use of Phonics Instruction to improve pronunciation of four sounds /θ/ , /ð/, /I/ and /I:/ in young learners in a private school in Bogotá. In this research, the impact of Phonics Instruction was analyzed in the students' pronunciation. To perform this analysis, Phonics Instruction was implemented in five stages based on Lloyd (2007) six types of sections. The participants were 13 students aged 10 to 12 years old from fifth grade; a mixed method was carried out to analyze collected data through the following instruments: 2 tests (pre-post), recordings and artifacts. This analysis was made using randomly 6 chosen students. At first the students did the pre-test with 20 words containing the sounds

Research paper thumbnail of Structural and functional studies of Leishmania braziliensis Hsp90

Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics, 2013

Research paper thumbnail of New insights on human Hsp70-escort protein 1: Chaperone activity, interaction with liposomes, cellular localizations and HSPA's self-assemblies remodeling

International Journal of Biological Macromolecules

Research paper thumbnail of Biochemical and biophysical characterization of the RVB-1/RVB-2 protein complex, the RuvBL/RVB homologues in Neurospora crassa

The RVB proteins, composed of the conservative paralogs, RVB1 and RVB2, belong to the AAA+ (ATPas... more The RVB proteins, composed of the conservative paralogs, RVB1 and RVB2, belong to the AAA+ (ATPases Associated with various cellular Activities) protein superfamily and are present in archaea and eukaryotes. The most distinct structural features are their ability to interact with each other forming the RVB1/2 complex and their participation in several macromolecular protein complexes leading them to be involved in many biological processes. We report here the biochemical and biophysical characterization of the Neurospora crassa RVB-1/RVB-2 complex. Chromatographic analyses revealed that the complex (APO) predominantly exists as a dimer in solution although hexamers were also observed. Nucleotides influence the oligomerization state, while ATP favors hexamers formation, ADP favors the formation of multimeric states, likely dodecamers, and the Molecular Dynamics (MD) simulations revealed the contribution of certain amino acid residues in the nucleotide stabilization. The complex binds...

Research paper thumbnail of Human HSPA9 (mtHsp70, mortalin) interacts with lipid bilayers containing cardiolipin, a major component of the inner mitochondrial membrane

Biochimica et Biophysica Acta (BBA) - Biomembranes

Research paper thumbnail of Rational design of nanocarriers based on gellan gum/retrograded starch exploiting polyelectrolyte complexation and ionic cross-linking processes: A potential technological platform for oral delivery of bevacizumab

Journal of Drug Delivery Science and Technology

Research paper thumbnail of Interaction of HSPA5 (Grp78, BIP) with negatively charged phospholipid membranes via oligomerization involving the N-terminal end domain

Cell Stress and Chaperones

Heat shock proteins (HSPs) are ubiquitous polypeptides expressed in all living organisms that par... more Heat shock proteins (HSPs) are ubiquitous polypeptides expressed in all living organisms that participate in several basic cellular processes, including protein folding, from which their denomination as molecular chaperones originated. There are several HSPs, including HSPA5, also known as 78-kDa glucose-regulated protein (GRP78) or binding immunoglobulin protein (BIP) that is an ER resident involved in the folding of polypeptides during their translocation into this compartment prior to the transition to the Golgi network. HSPA5 is detected on the surface of cells or secreted into the extracellular environment. Surface HSPA5 has been proposed to have various roles, such as receptor-mediated signal transduction, a co-receptor for soluble ligands, as well as a participant in tumor survival, proliferation, and resistance. Recently, surface HSPA5 has been reported to be a potential receptor of some viruses, including the novel SARS-CoV-2. In spite of these observations, the association of HSPA5 within the plasma membrane is still unclear. To gain information about this process, we studied the interaction of HSPA5 with liposomes made of different phospholipids. We found that HSPA5 has a high affinity for negatively charged phospholipids, such as palmitoyl-oleoyl phosphoserine (POPS) and cardiolipin (CL). The N-terminal and C-terminal domains of HSPA5 were independently capable of interacting with negatively charged phospholipids, but to a lesser extent than the full-length protein, suggesting that both domains are required for the maximum insertion into membranes. Interestingly, we found that the interaction of HSPA5 with negatively charged liposomes promotes an oligomerization process via intermolecular disulfide bonds in which the N-terminus end of the protein plays a critical role.

Research paper thumbnail of Thermal aggregates of human mortalin and Hsp70-1A behave as supramolecular assemblies

International Journal of Biological Macromolecules

Research paper thumbnail of Thermodynamic analysis of interactions of the Hsp90 with adenosine nucleotides: A comparative perspective

International Journal of Biological Macromolecules

Research paper thumbnail of Some Communication Problems of Two Cases in a Suckling Hospital

Pediatric Otorhinolaryngology Japan, 1992

This article is based on a mixed research, whose objective was the use of Phonics Instruction to ... more This article is based on a mixed research, whose objective was the use of Phonics Instruction to improve pronunciation of four sounds /θ/ , /ð/, /I/ and /I:/ in young learners in a private school in Bogotá. In this research, the impact of Phonics Instruction was analyzed in the students' pronunciation. To perform this analysis, Phonics Instruction was implemented in five stages based on Lloyd (2007) six types of sections. The participants were 13 students aged 10 to 12 years old from fifth grade; a mixed method was carried out to analyze collected data through the following instruments: 2 tests (pre-post), recordings and artifacts. This analysis was made using randomly 6 chosen students. At first the students did the pre-test with 20 words containing the sounds

Research paper thumbnail of Structural and functional studies of Leishmania braziliensis Hsp90

Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics, 2013

Research paper thumbnail of New insights on human Hsp70-escort protein 1: Chaperone activity, interaction with liposomes, cellular localizations and HSPA's self-assemblies remodeling

International Journal of Biological Macromolecules

Research paper thumbnail of Biochemical and biophysical characterization of the RVB-1/RVB-2 protein complex, the RuvBL/RVB homologues in Neurospora crassa

The RVB proteins, composed of the conservative paralogs, RVB1 and RVB2, belong to the AAA+ (ATPas... more The RVB proteins, composed of the conservative paralogs, RVB1 and RVB2, belong to the AAA+ (ATPases Associated with various cellular Activities) protein superfamily and are present in archaea and eukaryotes. The most distinct structural features are their ability to interact with each other forming the RVB1/2 complex and their participation in several macromolecular protein complexes leading them to be involved in many biological processes. We report here the biochemical and biophysical characterization of the Neurospora crassa RVB-1/RVB-2 complex. Chromatographic analyses revealed that the complex (APO) predominantly exists as a dimer in solution although hexamers were also observed. Nucleotides influence the oligomerization state, while ATP favors hexamers formation, ADP favors the formation of multimeric states, likely dodecamers, and the Molecular Dynamics (MD) simulations revealed the contribution of certain amino acid residues in the nucleotide stabilization. The complex binds...

Research paper thumbnail of Human HSPA9 (mtHsp70, mortalin) interacts with lipid bilayers containing cardiolipin, a major component of the inner mitochondrial membrane

Biochimica et Biophysica Acta (BBA) - Biomembranes

Research paper thumbnail of Rational design of nanocarriers based on gellan gum/retrograded starch exploiting polyelectrolyte complexation and ionic cross-linking processes: A potential technological platform for oral delivery of bevacizumab

Journal of Drug Delivery Science and Technology

Research paper thumbnail of Interaction of HSPA5 (Grp78, BIP) with negatively charged phospholipid membranes via oligomerization involving the N-terminal end domain

Cell Stress and Chaperones

Heat shock proteins (HSPs) are ubiquitous polypeptides expressed in all living organisms that par... more Heat shock proteins (HSPs) are ubiquitous polypeptides expressed in all living organisms that participate in several basic cellular processes, including protein folding, from which their denomination as molecular chaperones originated. There are several HSPs, including HSPA5, also known as 78-kDa glucose-regulated protein (GRP78) or binding immunoglobulin protein (BIP) that is an ER resident involved in the folding of polypeptides during their translocation into this compartment prior to the transition to the Golgi network. HSPA5 is detected on the surface of cells or secreted into the extracellular environment. Surface HSPA5 has been proposed to have various roles, such as receptor-mediated signal transduction, a co-receptor for soluble ligands, as well as a participant in tumor survival, proliferation, and resistance. Recently, surface HSPA5 has been reported to be a potential receptor of some viruses, including the novel SARS-CoV-2. In spite of these observations, the association of HSPA5 within the plasma membrane is still unclear. To gain information about this process, we studied the interaction of HSPA5 with liposomes made of different phospholipids. We found that HSPA5 has a high affinity for negatively charged phospholipids, such as palmitoyl-oleoyl phosphoserine (POPS) and cardiolipin (CL). The N-terminal and C-terminal domains of HSPA5 were independently capable of interacting with negatively charged phospholipids, but to a lesser extent than the full-length protein, suggesting that both domains are required for the maximum insertion into membranes. Interestingly, we found that the interaction of HSPA5 with negatively charged liposomes promotes an oligomerization process via intermolecular disulfide bonds in which the N-terminus end of the protein plays a critical role.

Research paper thumbnail of Thermal aggregates of human mortalin and Hsp70-1A behave as supramolecular assemblies

International Journal of Biological Macromolecules

Research paper thumbnail of Thermodynamic analysis of interactions of the Hsp90 with adenosine nucleotides: A comparative perspective

International Journal of Biological Macromolecules