Javascript must be enabled to use this form.

View Profile	Home Browse Faculty Facility Research Consortia Training Grants Courses Search Support About rSp Help and FAQ's Contact Us	GCC Home
Faculty Profile Last Modified Time: 09:53:41 AM Fri, 17 Apr 2020   Contact Information Laura Segatori Associated Profiles  Associate Professor, Chemical & Biomolecular Engineering, Rice University   Bioscience Research Collaborative, Room No.: 313    segatori@rice.edu     713-348-3536    Web Link    Lab Webpage    Orthogonal Genetic Circuits, Protein Design and Engineering, Nanotherapeutics, Environmental Health and Safety of Nanotechnology, Engineering the Proteostasis Network    Associated Profiles Research and Expertise Affiliations Appointments  Research and Expertise Research Interests   The flexibility of the polypeptide backbone, combined with the multitude of non-covalent interactions established by amino acid side chains, allows a protein to assume a variety of three-dimensional conformations. Failures of the folding mechanisms to assist in the formation of native protein conformations results in the accumulation of dysfunctional or unstable protein structures; trace amounts of aggregates may also occur spontaneously especially during aging. Therefore, a delicate balance between two main protective strategies –- the repair of damaged proteins and their selective degradation - has evolved in all organisms. Complex interactions among molecular effectors of the chaperone and degradation systems maintain protein homeostasis in eukaryotic cells. These are commonly referred to as protein quality control processes (QC). QC is developed to assist the folding of newly synthesized proteins and refold or degrade polypeptides that fail to attain or maintain a native structure. Its proper function is crucial in preventing the deposition of aggregation-prone, misfolded polypeptides associated with degenerative disorders, such as Alzheimer's and Parkinson diseases. My research interests focus on the relationship between protein folding and disease, the molecular determinants of cellular protein folding, and on the development of cell protein engineering strategies to manipulate the chaperone and degradation capacity. Specifically, we study on loss of function diseases (using patient-derived fibroblasts of lysosomal storage diseases as model system) and gain of function diseases (Parkinson's disease). We are focusing on the development of innovative, system-level strategies based on the integration of chemical genomics and systems biology approaches aimed at identifying modulators of the proteostasis network to restore folding, cellular trafficking and activity of mutated or misfolding prone substrates. Of particular interest to our group is also the development of technologies to measure proteasomal degradation with the objective to discover endogenous cellular factors and small molecules that function as proteasome activators. Our goals are to obtain a broader understanding of the molecular mechanisms involved in cellular protein folding, and to develop methods for manipulating eukaryotic cells, which can be used for therapeutic applications.  Publications/Creative Works Click here to search for this faculty member's publications on PubMed.  Affiliations  Research Consortia GCC Cluster for Cellular and Molecular Biophysics Gulf Coast Cluster for Single Cell Omics  Appointments Title Department / School Institution Associate Professor Chemical & Biomolecular Engineering Rice University

powering - The Partnership
Important Disclaimer: The responsibility for the accuracy of the information contained on these pages lies with the authors and user providing such information.