Anne-Claude Gingras | |
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Born | Île d'Orléans, Quebec, Canada |
Nationality | Canadian |
Alma mater | |
Known for | Quantitative proteomics |
Scientific career | |
Institutions |
Anne-Claude Gingras FRSC is a senior investigator at Lunenfeld-Tanenbaum Research Institute, and a professor in the department of molecular genetics at the University of Toronto. [1] She is an expert in mass spectrometry based proteomics technology that allows identification and quantification of protein from various biological samples.
Gingras was born on Île d'Orléans, Quebec. [2] She earned her undergraduate degree at Université Laval in Quebec. [3] She completed her PhD in biochemistry at McGill University in Montreal, [2] studying how 4E-BP1 regulated translation initiation, under the mentorship of Nahum Sonenberg. [3] After graduating in 2001, she began postdoctoral research in Seattle at the Institute for Systems Biology in the lab of Ruedi Aebersold, where she studied proteomics for three years. [3]
In 2005, Gingras moved to Toronto and joined the Lunenfeld-Tanenbaum Research Institute, and in 2006, she began teaching at the University of Toronto in the department of molecular genetics. [2]
Gingras research focuses on the development of experimental and bioinformatics approaches for functional proteomics, with a focus on protein-protein and proximity interactions. She applies these tools to the study of signaling pathways in health and disease and in mapping the physical organization of the dynamic proteome. Some of her work focuses on the consequence of disease-associated mutations on the interactions established by proteins. [4]
In addition to proteomics, Gingras laboratory has interest in studying human protein phosphatase and their systematic interactions and has now expanded into the field of systems biology.
Gingras has published > 200 articles that have been cited > 35,000 times (Google Scholar; Feb 2020). In 2011, Gingras was named one of Canada's Top 100 Most Powerful Women. [2] [5] In 2015, Gingras was elected a fellow of the Royal Society of Canada. [6] Her work on interaction proteomics, was awarded, alongside John Yates, the Discovery Award in Proteomics from the Human Proteome Organization (2019). She also received the Jeanne Manery Fisher Memorial Lecture award at the 2019 meeting of the Canadian Society for Molecular Biosciences. [7]
Rudolf Aebersold is a Swiss biologist, regarded as a pioneer in the fields of proteomics and systems biology. He has primarily researched techniques for measuring proteins in complex samples, in many cases via mass spectrometry. Ruedi Aebersold is a professor of Systems biology at the Institute of Molecular Systems Biology (IMSB) in ETH Zurich. He was one of the founders of the Institute for Systems Biology in Seattle, Washington, United States where he previously had a research group.
Serine/threonine-protein phosphatase 2A catalytic subunit alpha isoform is an enzyme that is encoded by the PPP2CA gene.
Eukaryotic translation initiation factor 4E-binding protein 1 is a protein that in humans is encoded by the EIF4EBP1 gene. inhibits cap-dependent translation by binding to translation initiation factor eIF4E. Phosphorylation of 4E-BP1 results in its release from eIF4E, thereby allows cap-dependent translation to continue thereby increasing the rate of protein synthesis.
Eukaryotic translation initiation factor 4E, also known as eIF4E, is a protein that in humans is encoded by the EIF4E gene.
Eukaryotic translation initiation factor 4 gamma 2 is a protein that in humans is encoded by the EIF4G2 gene.
Eukaryotic translation initiation factor 4 gamma 1 is a protein that in humans is encoded by the EIF4G1 gene.
MAP kinase-interacting serine/threonine-protein kinase 1 is an enzyme that in humans is encoded by the MKNK1 gene.
Eukaryotic translation initiation factor 4 gamma 3 is a protein that in humans is encoded by the EIF4G3 gene. The gene encodes a protein that functions in translation by aiding the assembly of the ribosome onto the messenger RNA template. Confusingly, this protein is usually referred to as eIF4GII, as although EIF4G3 is the third gene that is similar to eukaryotic translation initiation factor 4 gamma, the second isoform EIF4G2 is not an active translation initiation factor.
Eukaryotic translation initiation factor 4B is a protein that in humans is encoded by the EIF4B gene.
Eukaryotic translation initiation factor 3 subunit B (eIF3b) is a protein that in humans is encoded by the EIF3B gene.
Eukaryotic translation initiation factor 3 subunit C (eIF3c) is a protein that in humans is encoded by the EIF3C gene.
Eukaryotic translation initiation factor 4E type 2 is a protein that in humans is encoded by the EIF4E2 gene. It belongs to the eukaryotic translation initiation factor 4E family.
Immunoglobulin-binding protein 1 is a protein that in humans is encoded by the IGBP1 gene.
CTTNBP2 N-terminal-like protein is a protein that in humans is encoded by the CTTNBP2NL gene. It is a substrate for phosphorylation.
Eukaryotic translation initiation factor 4E-binding protein 2 is a protein that in humans is encoded by the EIF4EBP2 gene.
Serine/threonine-protein phosphatase 4 regulatory subunit 3B is an enzyme that in humans is encoded by the SMEK2 gene.
Protein FAM40A is a protein that is located on chromosome 1 in humans and is encoded by the FAM40A gene.
Serine/threonine-protein phosphatase 4 regulatory subunit 1 is an enzyme that in humans is encoded by the PPP4R1 gene.
Eukaryotic translation initiation factor 4E-binding protein 3 is a protein that in humans is encoded by the EIF4EBP3 gene.
The eukaryotic initiation factor-4A (eIF4A) family consists of 3 closely related proteins EIF4A1, EIF4A2, and EIF4A3. These factors are required for the binding of mRNA to 40S ribosomal subunits. In addition these proteins are helicases that function to unwind double-stranded RNA.