Fabiana Avila Carneiro

Instituição:

Universidade Federal do Rio de Janeiro

Centro:

Campus de Xerém

Unidade:

Colegiado de Ensino de Graduação/Xerém

Departamento:

Departamento de Ensino de Graduação/Xerém

ORCID:

https://orcid.org/0000-0002-6584-4875


Formação:

  • Instituto de Medicina Molecular

    | Pós-Doutorado | 2009 - 2009

  • Universidade Federal do Rio de Janeiro

    | Pós-Doutorado | 2008 - 2010

  • Faculdade de Ciências da Universidade de Lisboa

    | Pós-Doutorado | 2008 - 2008

  • Universidade Federal do Rio de Janeiro

    | Pós-Doutorado | 2007 - 2008

  • New York University

    | Pós-Doutorado | 2006 - 2007

  • Universidade Federal do Rio de Janeiro

    | Pós-Doutorado | 2005 - 2006

  • Université Libre de Bruxelles

    Bioquímica | Doutorado | 2003 - 2003

  • Universidade Federal do Rio de Janeiro

    Química Biológica | Doutorado | 2001 - 2004

  • Universidade Federal do Rio de Janeiro

    Química Biológica | Mestrado | 2000 - 2000

  • Universidade Federal do Rio de Janeiro

    Ciências Biológicas | Graduação | 1995 - 1999
Laboratórios:
Nenhum laboratório cadastrado
Nuvens de Palavras:
Artigos:

(96.15% artigos com DOI)

Titulo DOI Ano
Cost-effective 3D lung tissue spheroid as a model for SARS-CoV -2 infection and drug screening 10.1111/aor.14729 2024
Mpox outbreak in Rio de Janeiro, Brazil: A translational approach 10.1002/jmv.29621 2024
Development and assessment of a multiepitope synthetic antigen for the diagnosis of Dengue virus infection 10.1016/j.bjid.2024.103746 2024
Accuracy of a raw saliva-based COVID-19 RT-LAMP diagnostic assay 10.1016/j.bjid.2023.102790 2023
SARS-CoV-2 egress from Vero cells: a morphological approach 10.1007/s00418-023-02239-9 2023
Intracellular host cell membrane remodelling induced by SARS-CoV-2 infection in vitro 10.1111/boc.202000146 2021
How Far Could these New SARS-CoV-2 Variants Take Us? 10.31080/ASMI.2021.04.0853 2021
Acute Toxicological and Biodistribution Aspects of Superparamagnetic Magnetite Nanoparticles In Vitro and on Animal Tissues 10.1007/s12668-021-00914-6 2021
Ultrastructural analysis of SARS-CoV-2 interactions with the host cell via high resolution scanning electron microscopy 10.1038/s41598-020-73162-5 2020
Spheroids and organoids as humanized 3D scaffold-free engineered tissues for SARS-CoV-2 viral infection and drug screening 10.1111/aor.13880 2020
Co-protoporphyrin IX and Sn-protoporphyrin IX inactivate Zika, Chikungunya and other arboviruses by targeting the viral envelope 10.1038/s41598-018-27855-7 2018
Low toxicity superparamagnetic magnetite nanoparticles: one-pot facile green synthesis for biological applications 10.1016/j.msec.2017.04.066 2017
DEVELOPMENT OF STANDARD METHODS FOR ZIKA VIRUS PROPAGATION, TITRATION, AND PURIFICATION 10.1016/j.jviromet.2017.04.011 2017
Dengue Virus Capsid Protein Binding to Hepatic Lipid Droplets (LD) Is Potassium Ion Dependent and Is Mediated by LD Surface Proteins 10.1128/jvi.06796-11 2012
The disordered N-terminal region of dengue virus capsid protein contains a lipid-droplet-binding motif 10.1042/BJ20112219 2012
Viral Inactivation Based on Inhibition of Membrane Fusion: Understanding the Role of Histidine Protonation to Develop New Viral Vaccines 10.2174/092986609788681823 2009
Interaction of the Dengue Virus Fusion Peptide with Membranes Assessed by NMR: The Essential Role of the Envelope Protein Trp101 for Membrane Fusion 10.1016/j.jmb.2009.07.035 2009
Interaction between dengue virus fusion peptide and lipid bilayers depends on peptideo clustering 10.1080/09687680701633091 2008
Inactivation of Vesicular Stomatitis Virus Through Inhibition of Membrane Fusion by Chemical Modification of the Viral Glycoprotein 10.1016/j.antiviral.2006.07.007 2007
Probing the interaction between vesicular stomatitis virus and phosphatidylserine 10.1007/s00249-005-0012-z 2006
Charged residues are involved in membrane fusion mediated by a hydrophilic peptide located in vesicular stomatitis virus G protein 10.1080/09687860600780892 2006
Viral membrane fusion: is glycoprotein G of rhabdoviruses a representative of a new class of viral fusion proteins? 10.1590/s0100-879x2005000600002 2005
Membrane Fusion Induced by Vesicular Stomatitis Virus Depends on Histidine Protonation 10.1074/jbc.m210615200 2003
Multiple Applications of Atomic Force Microscope in Biology 2003
Membrane Recognition by Vesicular Stomatitis Virus Involves Enthalpy-Driven Protein-Lipid Interactions 10.1128/jvi.76.8.3756-3764.2002 2002
Low pH-induced Conformational Changes in Vesicular Stomatitis Virus Glycoprotein Involve Dramatic Structure Reorganization 10.1074/jbc.m008753200 2001
Eventos:

(0.00% eventos com DOI)

Titulo DOI Ano
Vesicular Stomatitis Virus inactivation based on membrane fusion inhibition as a means of vaccine development 2006
Charges Residues are involved in membrane fusion mediated by a hydrophilic peptide located in VSV G protein 2006
Viral-induced Membrane Fusion: from Structural Studies to the Development of a Process of Viral Inactivation 2005
Viral inactivation throught inhibition of virus-induced membrane fusion 2004
Vaccine development for vesicular stomatitis virus based on membrane fusion inhibition 2004
Viral-Induced Membrane Fusion: from Structural Studies to Vaccine Development 2004
Viral inactivation through inhibition of virus-induced membrane fusion 2004
Characterization of a fusion peptide from Vesicular Stomatitis Virus: Phospholipids Dependence and Thermodynamics of Peptide-membrane Interaction and Fusion 2004
Membrane Fusion Induced by Vesicular Stomatitis Vírus: Membrane Interaction d G Protein Structural Changes 2003
Role of Negatively Charged Phospholipids on Protein-Membrane Recognition and Fusion Determined by AFM-Force Spectroscopy 2003
Membrane fusion induced by vesicular stomatitis virus depends on histidine protonation 2003
A Importância de Resíduos de Histidina no Processo de Fusão de Membranas Catalisado Pelo Vírus da Estomatite Vesicular 2003
Membrane recognition by vesicular stomatitis virus involves enthalpy-driven protein-lipid interactions 2002
VSV Lipid Interaction by AFM-Force Spectroscopy 2002
Resíduos de histidina são importantes no processo de fusão de membranas catalisado pela glicoproteína do vírus da estomatite vesicular 2002
Conformational changes in vesicular stomatitis virus glycoprotein during membrane fusion: role of histidines residues 2001
Conformational Changes in Vesicular Stomatitis Virus Glycoprotein during Membrane Fusion: Role of Phospholipids 2001
Mudanças conformacionais na glicoproteína do vírus da estomatite vesicular durante a fusão de membrana: papel dos resíduos de histidina 2001
Membrane recognition by vesicular stomatitis virus involves enthalpy-driven protein-lipid interactions 2001
Structural Studies on Vesicular Stomatitis Virus Glycoprotein at Acidic pH 2000
Publicações:
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