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Your search keyword '"Lilley, K. S."' showing total 6 results
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6 results on '"Lilley, K. S."'

1. An open invitation to the Understudied Proteins Initiative

Author

Kustatscher, G., Collins, T., Gingras, A. -C, Guo, T., Hermjakob, H., Ideker, T., Lilley, K. S., Lundberg, Emma, Marcotte, E. M., Ralser, M., Rappsilber, J., Kustatscher, G., Collins, T., Gingras, A. -C, Guo, T., Hermjakob, H., Ideker, T., Lilley, K. S., Lundberg, Emma, Marcotte, E. M., Ralser, M., and Rappsilber, J.

Abstract

QC 20230213

Published
2022
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4. A subcellular map of the human proteome

Author

Thul, Peter J., Åkesson, Lovisa, Wiking, Mikaela, Mahdessian, Diana, Geladaki, A., Ait Blal, Hammou, Alm, Tove L., Asplund, A., Björk, Lars, Breckels, L. M., Bäckström, Anna, Danielsson, Frida, Fagerberg, Linn, Fall, Jenny, Gatto, L., Gnann, Christian, Hober, Sophia, Hjelmare, Martin, Johansson, Fredric, Lee, Sunjae, Lindskog, C., Mulder, J., Mulvey, C. M., Nilsson, Peter, Oksvold, Per, Rockberg, Johan, Schutten, Rutger, Schwenk, Jochen M., Sivertsson, Åsa, Sjöstedt, E., Skogs, Marie, Stadler, Charlotte, Sullivan, Devin P., Tegel, Hanna, Winsnes, Casper F., Zhang, Cheng, Zwahlen, Martin, Mardinoglu, Adil, Pontén, F., von Feilitzen, Kalle, Lilley, K. S., Uhlén, Mathias, Lundberg, Emma, Thul, Peter J., Åkesson, Lovisa, Wiking, Mikaela, Mahdessian, Diana, Geladaki, A., Ait Blal, Hammou, Alm, Tove L., Asplund, A., Björk, Lars, Breckels, L. M., Bäckström, Anna, Danielsson, Frida, Fagerberg, Linn, Fall, Jenny, Gatto, L., Gnann, Christian, Hober, Sophia, Hjelmare, Martin, Johansson, Fredric, Lee, Sunjae, Lindskog, C., Mulder, J., Mulvey, C. M., Nilsson, Peter, Oksvold, Per, Rockberg, Johan, Schutten, Rutger, Schwenk, Jochen M., Sivertsson, Åsa, Sjöstedt, E., Skogs, Marie, Stadler, Charlotte, Sullivan, Devin P., Tegel, Hanna, Winsnes, Casper F., Zhang, Cheng, Zwahlen, Martin, Mardinoglu, Adil, Pontén, F., von Feilitzen, Kalle, Lilley, K. S., Uhlén, Mathias, and Lundberg, Emma

Abstract

Resolving the spatial distribution of the human proteome at a subcellular level can greatly increase our understanding of human biology and disease. Here we present a comprehensive image-based map of subcellular protein distribution, the Cell Atlas, built by integrating transcriptomics and antibody-based immunofluorescence microscopy with validation by mass spectrometry. Mapping the in situ localization of 12,003 human proteins at a single-cell level to 30 subcellular structures enabled the definition of the proteomes of 13 major organelles. Exploration of the proteomes revealed single-cell variations in abundance or spatial distribution and localization of about half of the proteins to multiple compartments. This subcellular map can be used to refine existing protein-protein interaction networks and provides an important resource to deconvolute the highly complex architecture of the human cell., QC 20171208

Published
2017
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6. Global analysis of protein-RNA interactions in SARS-CoV-2-infected cells reveals key regulators of infection

Author

Natasha Johnson, Berati Cerikan, Shabaz Mohammed, Manuel Garcia-Moreno, Javier Martinez, Christopher J. Neufeldt, Alfredo Castello, Ralf Bartenschlager, Mohamed Kammoun, Jeffrey Y. Lee, Anna Andrejeva, Mirko Cortese, Marko Noerenberg, Honglin Chen, Kathryn S. Lilley, Ilan Davis, Michael L. Knight, Aino I. Järvelin, Ni Shuai, Wael Kamel, Michael J. Deery, Kamel, W., Noerenberg, M., Cerikan, B., Chen, H., Jarvelin, A. I., Kammoun, M., Lee, J. Y., Shuai, N., Garcia-Moreno, M., Andrejeva, A., Deery, M. J., Johnson, N., Neufeldt, C. J., Cortese, M., Knight, M. L., Lilley, K. S., Martinez, J., Davis, I., Bartenschlager, R., Mohammed, S., and Castello, A.

Subjects
Resource, TRNA Ligase, tRNA ligase, Proteome, RNA-binding protein, viruses, Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2), Computational biology, Biology, Virus Replication, viral ribonucleoprotein, ribonucleoprotein, antiviral response, Viral Proteins, 03 medical and health sciences, 0302 clinical medicine, HSP90, Humans, Molecular Biology, 030304 developmental biology, Ribonucleoprotein, 0303 health sciences, RNA interactome, SARS-CoV-2, host-virus interaction, RIC, COVID-19, RNA-Binding Proteins, virus diseases, RNA, Cell Biology, antiviral, Hsp90, 3. Good health, Viral replication, A549 Cells, biology.protein, viral replication, RNA, Viral, tRNA ligase complex, 030217 neurology & neurosurgery
Abstract

Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) causes COVID-19. SARS-CoV-2 relies on cellular RNA-binding proteins (RBPs) to replicate and spread, although which RBPs control its life cycle remains largely unknown. Here, we employ a multi-omic approach to identify systematically and comprehensively the cellular and viral RBPs that are involved in SARS-CoV-2 infection. We reveal that SARS-CoV-2 infection profoundly remodels the cellular RNA-bound proteome, which includes wide-ranging effects on RNA metabolic pathways, non-canonical RBPs and antiviral factors. Moreover, we apply a new method to identify the proteins that directly interact with viral RNA, uncovering dozens of cellular RBPs and six viral proteins. Amongst them, several components of the tRNA ligase complex, which we show regulate SARS-CoV-2 infection. Furthermore, we discover that available drugs targeting host RBPs that interact with SARS-CoV-2 RNA inhibit infection. Collectively, our results uncover a new universe of host-virus interactions with potential for new antiviral therapies against COVID-19., Graphical Abstract, Kamel, Noerenberg, Cerikan and colleagues apply a multi-omic approach to identify the RNA-binding proteins that regulate SARS-CoV-2 infection. They discovered that the complement of RNA-binding proteins heavily remodels upon SARS-CoV-2 infection. They also show that the viral RNA interacts with dozens of cellular and six viral RNA-binding proteins. These host-virus interactions are fundamental for SARS-CoV-2 infection and have great potential for new therapeutic approaches against COVID-19.

Published
2021
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