Lori Passmore | |
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Born | Lori Anne Passmore |
Nationality | Canadian/British |
Alma mater |
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Awards |
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Scientific career | |
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Institutions | |
Thesis | Structural and functional studies of the anaphase promoting complex (APC) (2003) |
Doctoral advisor | David Barford |
Other academic advisors | Venki Ramakrishnan Richard Henderson |
Website | www2 |
Lori Anne Passmore FRS is a Canadian/British cryo electron microscopist and structural biologist who works at the Medical Research Council (MRC) Laboratory of Molecular Biology (LMB) at the University of Cambridge. [3] [4] She is known for her work on multiprotein complexes involved in gene expression [5] [6] [7] and development of new supports for cryo-EM. [8]
Lori Passmore graduated from the University of British Columbia, Canada in 1999. [9] She obtained a PhD in 2003 from University of London for research supervised by David Barford at the Institute of Cancer Research. She performed in vitro biochemical characterisation of the activity of the anaphase-promoting complex (APC) [10] and used cryo-EM to study the APC structure. [1] [11]
Passmore worked as a postdoctoral researcher at the MRC-LMB. She worked with Venki Ramakrishnan and Richard Henderson, using cryo-EM to determine the structure of the eukaryotic ribosome bound to initiation factors. [12] Passmore became a group leader at the MRC-LMB in 2009. Her group uses in vitro reconstitution, biochemical assays and cryo-EM to understand the function of multiprotein complexes that regulate gene expression at the level of mRNA. [5] [6] [7] Her group has developed new sample grids for cryo-EM that reduce specimen movement during imaging. [8] In collaboration with Ketan J. Patel, Passmore is also actively studying the molecular mechanisms underlying Fanconi anemia. [13] [14]
Anaphase-promoting complex is an E3 ubiquitin ligase that marks target cell cycle proteins for degradation by the 26S proteasome. The APC/C is a large complex of 11–13 subunit proteins, including a cullin (Apc2) and RING (Apc11) subunit much like SCF. Other parts of the APC/C have unknown functions but are highly conserved.
Transmission electron cryomicroscopy (CryoTEM), commonly known as cryo-EM, is a form of cryogenic electron microscopy, more specifically a type of transmission electron microscopy (TEM) where the sample is studied at cryogenic temperatures. Cryo-EM is gaining popularity in structural biology.
The Medical Research Council (MRC) Laboratory of Molecular Biology (LMB) is a research institute in Cambridge, England, involved in the revolution in molecular biology which occurred in the 1950–60s. Since then it has remained a major medical research laboratory at the forefront of scientific discovery, dedicated to improving the understanding of key biological processes at atomic, molecular and cellular levels using multidisciplinary methods, with a focus on using this knowledge to address key issues in human health.
The cell division cycle protein 20 homolog is an essential regulator of cell division that is encoded by the CDC20 gene in humans. To the best of current knowledge its most important function is to activate the anaphase promoting complex (APC/C), a large 11-13 subunit complex that initiates chromatid separation and entrance into anaphase. The APC/CCdc20 protein complex has two main downstream targets. Firstly, it targets securin for destruction, enabling the eventual destruction of cohesin and thus sister chromatid separation. It also targets S and M-phase (S/M) cyclins for destruction, which inactivates S/M cyclin-dependent kinases (Cdks) and allows the cell to exit from mitosis. A closely related protein, Cdc20homologue-1 (Cdh1) plays a complementary role in the cell cycle.
Fizzy-related protein homolog, also known as hCDH1, is a protein that in humans is encoded by the FZR1 gene.
Cell division cycle protein 16 homolog is a protein that in humans is encoded by the CDC16 gene.
Cell division cycle 23 homolog , also known as CDC23, is a protein that, in humans, is encoded by the CDC23 gene.
Anaphase-promoting complex subunit 2 is an enzyme that in humans is encoded by the ANAPC2 gene.
The tetratricopeptide repeat (TPR) is a structural motif. It consists of a degenerate 34 amino acid tandem repeat identified in a wide variety of proteins. It is found in tandem arrays of 3–16 motifs, which form scaffolds to mediate protein–protein interactions and often the assembly of multiprotein complexes. These alpha-helix pair repeats usually fold together to produce a single, linear solenoid domain called a TPR domain. Proteins with such domains include the anaphase-promoting complex (APC) subunits cdc16, cdc23 and cdc27, the NADPH oxidase subunit p67-phox, hsp90-binding immunophilins, transcription factors, the protein kinase R (PKR), the major receptor for peroxisomal matrix protein import PEX5, protein arginine methyltransferase 9 (PRMT9), and mitochondrial import proteins.
David Barford is a British medical researcher and structural biologist at the MRC Laboratory of Molecular Biology Cambridge, UK.
Ketan Jayakrishna Patel is a British-Kenyan scientist who is Director of the MRC Weatherall Institute of Molecular Medicine and the MRC Molecular Haematology Unit at the University of Oxford. Until 2020 he was a tenured principal investigator at the Medical Research Council (MRC) Laboratory of Molecular Biology (LMB).
Jan Löwe is a German molecular and structural biologist and the Director of the Medical Research Council (MRC) Laboratory of Molecular Biology (LMB) in Cambridge, UK. He became Director of the MRC-LMB in April 2018, succeeding Sir Hugh Pelham. Löwe is known for his contributions to the current understanding of bacterial cytoskeletons.
Sjors Hendrik Willem ScheresFRS is a Dutch scientist at the MRC Laboratory of Molecular Biology Cambridge, UK.
Andrew P. Carter is a British structural biologist who works at the Medical Research Council (MRC) Laboratory of Molecular Biology (LMB) in Cambridge, UK. He is known for his work on the microtubule motor dynein.
Melina Schuh is a German biochemist and Director at the Max Planck Institute for Multidisciplinary Sciences. She is known for her work on meiosis in mammalian oocytes, for her studies on the mechanisms leading to the age-related decline in female fertility, and for the development of the Trim-Away protein depletion method.
Kiyoshi Nagai was a Japanese structural biologist at the MRC Laboratory of Molecular Biology Cambridge, UK. He was known for his work on the mechanism of RNA splicing and structures of the spliceosome.
Anne Bertolotti is a French biochemist and cell biologist who works as Programme Leader at the MRC Laboratory of Molecular Biology in Cambridge, UK. In 2022 she was appointed Head of the MRC LMB's Neurobiology Division. She is known for her research into the cellular defences against misfolded proteins and the mechanisms underlying their deposition, the molecular problem causative of neurodegenerative diseases.
Carbon Catabolite Repression—Negative On TATA-less, or CCR4-Not, is a multiprotein complex that functions in gene expression. The complex has multiple enzymatic activities as both a poly(A) 3′-5′ exonuclease and a ubiquitin ligase. The complex is present both in the nucleus where it regulates transcription and in the cytoplasm where it associates with translating ribosomes and RNA processing bodies.
M. Madan Babu is an Indian-American computational biologist and bioinformatician. He is the endowed chair in biological data science and director of the center of excellence for data-driven discovery at St. Jude Children’s Research Hospital. Previously, he served as a programme leader at the MRC Laboratory of Molecular Biology (LMB).
Nicolas H. Thomä is a German researcher, senior group leader at the Friedrich Miescher Institute for Biomedical Research in Basel, Switzerland. He is a biochemist and structural biologist and a leading researcher in the fields of ubiquitin ligase biology and DNA repair.
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