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Marta Filizola

ASSISTANT PROFESSOR  Structural and Chemical Biology

Overview

Gender Female
E-mail marta.filizola@mssm.edu
Education and Training Ph.D., II University of Naples
  B.S., University of Naples 'Federico II'
  M.S., University of Naples 'Federico II'
  Postdoctoral Training, Molecular Research Institute
Awards 2008
The Doctor Harold and Golden Lamport Award for Excellence in Basic Research
Mount Sinai School of Medicine
  2001
National Research Service Award T32 DA07135
National Institute on Drug Abuse (NIDA)
  1999
Title of European Doctor in Biotechnology
European Association for Higher Education in Biotechnology

Dr. Filizola is a dedicated leader in computational biophysics of membrane proteins, with a special focus on the family of cell surface proteins called G protein-coupled receptors (GPCRs), which are the targets for about half of all currently used drugs. Her computational methodologies are closely intertwined with collaborative experimental investigations to provide new and biologically relevant insights about the ligand-induced transmission of the signal from the exterior to the interior of the cell membrane, giving rise to new hypotheses to guide further experimental inquiry. Since the start of her academic appointment in July 2007, Dr. Filizola has been actively engaged in and is continuously making important contributions to academic research and educational activities at Mount Sinai as well as in the scientific community in general. As such, she has recently been elected a worthy recipient of the 2008 Harold and Golden Lamport Award for Excellence in Basic Research, a prestigious award given to tenure-track Assistant Professors at Mount Sinai who demonstrate exceptional potential for making significant contributions in the early stage of their academic career.

Filizola Laboratory

Training

Education and Training Ph.D., II University of Naples
  B.S., University of Naples 'Federico II'
  M.S., University of Naples 'Federico II'
  Postdoctoral Training, Molecular Research Institute

Research

The overall goal of our research is to achieve a detailed mechanistic understanding of signal transduction processes triggered by molecular recognition by means of computational methodologies that range from bioinformatics to modeling and simulation. The strength of our research relies on the deliberate integration of these computational methodologies with collaborative experimental approaches to provide valuable mechanistic interpretations at the molecular level of the ligand-induced transmission of the signal to the inner side of the cell membrane. While our research is driven by the exploration and improvement of computational methods to characterize generalizable mechanisms of molecular recognition and signal transduction, we are excited by the contributions that our computational and modeling efforts make to the experimental field through the generation of new testable hypotheses. Current major research activities in the lab include:

1) Prediction and validation of opioid receptor oligomerization (in collaboration with Dr. Jonathan Javitch at Columbia University);

2) Informatics of GPCRs in drug of abuse mechanisms (in collaboration with Dr. Fabien Campagne at Weill Medical College of Cornell University);

3) Elucidation of integrin allostery and bidirectional signaling (in collaboration with Dr. Barry Coller at Rockefeller University);

4) Structure and function of the 5HT2A/mGluR2 complex in schizophrenia (in collaboration with Drs. Javier Gonzalez-Maeso and Stuart Sealfon at Mount Sinai);

5) Rational design of novel therapeutics for Alzheimer's Disease using a structure guided high-throughput screening approach (in collaboration with Dr. Ubarretxena-Belandia at Mount Sinai).

For more information, please visit the Filizola Laboratory website.

Publications

Guo W, Urizar E, Kralikova M, Mobarec JC, Shi L, Filizola M, Javitch JA. Dopamine D2 Receptors Form Higher Order Oligomers at Physiological Expression Levels. The EMBO Journal 2008; 27(17): 2293-2304.


Gonzalez-Maeso J, Ang R, Yuen T, Chan P, Weisstaub NV, Lopez-Gimenez J, Zhou M, Okawa Y, Callado LF, Milligan G, Gingrich JA, Filizola M, Meana JJ, Sealfon SC. Identification of a Novel Serotonin/Glutamate Receptor Complex Implicated in Psychosis. Nature 2008;.


Mobarec JC, Filizola M. Advances in the Development and Application of Computational Methodologies for Structural Modeling of G-Protein Coupled Receptors. Expert Opinion on Drug Discovery 2008; 3: 343-355.


Taylor MM, Fung HK, Rajgaria R, Filizola M, Weinstein H, Floudas CA. Mutations Affecting the Oligomerization Interface of G-Protein Coupled Receptors Revealed by a Novel De-novo Protein Design Framework. Biophysical Journal 2008 Jan 4; Epub ahead of print.


Murcia M, Jirouskova M, Li JH, Coller BS, Filizola M. Functional and computational studies of the LIgand-associated Metal Binding Site (LIMBS) of beta3 integrins. PROTEINS: Structure, Function, and Bioinformatics 2008 Jan 3; Epub ahead of print.


Niv MY, Filizola M. Influence of Oligomerization on the Dynamics of G-Protein Coupled Receptors as Assessed by Normal Mode Analysis. PROTEINS: Structure, Function, and Bioinformatics 2007 Oct 26; Epub ahead of print.


Skrabanek L, Murcia M, Bouvier M, Devi L, George SR, Lohse MJ, Milligan G, Neubig R, Palczewski K, Parmentier M, Pin JP, Vriend G, Javitch JA, Campagne F, Filizola M. Requirements and Ontology for a G Protein-Coupled Receptor Oligomerization Knowledge Base. BMC Bioinformatics 2007; 8: 177.


Filizola M, Wang SX, Weinstein H. Dynamic Models of G-Protein Coupled Receptors Dimers: Indications of Asymmetry in the Rhodopsin Dimer from Molecular Dynamics Simulations in a POPC Bilayer. Journal of Computer-Aided Molecular Design 2006; 20(7-8): 405-416.


Niv MY, Skrabanek L, Filizola M, Weinstein H. Modeling activated states of GPCRs: the rhodopsin template. Journal of Computer-Aided Molecular Design 2006; 20(7-8): 437-448.


Guo W, Shi L, Filizola M, Weinstein H, Javitch JA. Crosstalk in G protein-coupled receptors: changes at the transmembrane homodimer interface determine activation. Proceedings of the National Academy of Science 2005; 102(48): 17495-17500.


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