Multiplexed protein maps link subcellular organization to cellular states
Gut, G., Herrmann, M. D., Pelkmans, L.
American Association for the Advancement of Science (AAAS)
Published 2018
American Association for the Advancement of Science (AAAS)
Published 2018
Publication Date: |
2018-08-03
|
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Publisher: |
American Association for the Advancement of Science (AAAS)
|
Print ISSN: |
0036-8075
|
Electronic ISSN: |
1095-9203
|
Topics: |
Biology
Chemistry and Pharmacology
Geosciences
Computer Science
Medicine
Natural Sciences in General
Physics
|
Keywords: |
Cell Biology, Techniques
|
Published by: |
_version_ | 1836399021230391296 |
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autor | Gut, G., Herrmann, M. D., Pelkmans, L. |
beschreibung | Obtaining highly multiplexed protein measurements across multiple length scales has enormous potential for biomedicine. Here, we measured, by iterative indirect immunofluorescence imaging (4i), 40-plex protein readouts from biological samples at high-throughput from the millimeter to the nanometer scale. This approach simultaneously captures properties apparent at the population, cellular, and subcellular levels, including microenvironment, cell shape, and cell cycle state. It also captures the detailed morphology of organelles, cytoskeletal structures, nuclear subcompartments, and the fate of signaling receptors in thousands of single cells in situ. We used computer vision and systems biology approaches to achieve unsupervised comprehensive quantification of protein subcompartmentalization within various multicellular, cellular, and pharmacological contexts. Thus, highly multiplexed subcellular protein maps can be used to identify functionally relevant single-cell states. |
citation_standardnr | 6314134 |
datenlieferant | ipn_articles |
feed_id | 25 |
feed_publisher | American Association for the Advancement of Science (AAAS) |
feed_publisher_url | http://www.aaas.org/ |
insertion_date | 2018-08-03 |
journaleissn | 1095-9203 |
journalissn | 0036-8075 |
publikationsjahr_anzeige | 2018 |
publikationsjahr_facette | 2018 |
publikationsjahr_intervall | 7984:2015-2019 |
publikationsjahr_sort | 2018 |
publisher | American Association for the Advancement of Science (AAAS) |
quelle | Science |
relation | http://science.sciencemag.org/cgi/content/short/361/6401/eaar7042?rss=1 |
schlagwort | Cell Biology, Techniques |
search_space | articles |
shingle_author_1 | Gut, G., Herrmann, M. D., Pelkmans, L. |
shingle_author_2 | Gut, G., Herrmann, M. D., Pelkmans, L. |
shingle_author_3 | Gut, G., Herrmann, M. D., Pelkmans, L. |
shingle_author_4 | Gut, G., Herrmann, M. D., Pelkmans, L. |
shingle_catch_all_1 | Multiplexed protein maps link subcellular organization to cellular states Cell Biology, Techniques Obtaining highly multiplexed protein measurements across multiple length scales has enormous potential for biomedicine. Here, we measured, by iterative indirect immunofluorescence imaging (4i), 40-plex protein readouts from biological samples at high-throughput from the millimeter to the nanometer scale. This approach simultaneously captures properties apparent at the population, cellular, and subcellular levels, including microenvironment, cell shape, and cell cycle state. It also captures the detailed morphology of organelles, cytoskeletal structures, nuclear subcompartments, and the fate of signaling receptors in thousands of single cells in situ. We used computer vision and systems biology approaches to achieve unsupervised comprehensive quantification of protein subcompartmentalization within various multicellular, cellular, and pharmacological contexts. Thus, highly multiplexed subcellular protein maps can be used to identify functionally relevant single-cell states. Gut, G., Herrmann, M. D., Pelkmans, L. American Association for the Advancement of Science (AAAS) 0036-8075 00368075 1095-9203 10959203 |
shingle_catch_all_2 | Multiplexed protein maps link subcellular organization to cellular states Cell Biology, Techniques Obtaining highly multiplexed protein measurements across multiple length scales has enormous potential for biomedicine. Here, we measured, by iterative indirect immunofluorescence imaging (4i), 40-plex protein readouts from biological samples at high-throughput from the millimeter to the nanometer scale. This approach simultaneously captures properties apparent at the population, cellular, and subcellular levels, including microenvironment, cell shape, and cell cycle state. It also captures the detailed morphology of organelles, cytoskeletal structures, nuclear subcompartments, and the fate of signaling receptors in thousands of single cells in situ. We used computer vision and systems biology approaches to achieve unsupervised comprehensive quantification of protein subcompartmentalization within various multicellular, cellular, and pharmacological contexts. Thus, highly multiplexed subcellular protein maps can be used to identify functionally relevant single-cell states. Gut, G., Herrmann, M. D., Pelkmans, L. American Association for the Advancement of Science (AAAS) 0036-8075 00368075 1095-9203 10959203 |
shingle_catch_all_3 | Multiplexed protein maps link subcellular organization to cellular states Cell Biology, Techniques Obtaining highly multiplexed protein measurements across multiple length scales has enormous potential for biomedicine. Here, we measured, by iterative indirect immunofluorescence imaging (4i), 40-plex protein readouts from biological samples at high-throughput from the millimeter to the nanometer scale. This approach simultaneously captures properties apparent at the population, cellular, and subcellular levels, including microenvironment, cell shape, and cell cycle state. It also captures the detailed morphology of organelles, cytoskeletal structures, nuclear subcompartments, and the fate of signaling receptors in thousands of single cells in situ. We used computer vision and systems biology approaches to achieve unsupervised comprehensive quantification of protein subcompartmentalization within various multicellular, cellular, and pharmacological contexts. Thus, highly multiplexed subcellular protein maps can be used to identify functionally relevant single-cell states. Gut, G., Herrmann, M. D., Pelkmans, L. American Association for the Advancement of Science (AAAS) 0036-8075 00368075 1095-9203 10959203 |
shingle_catch_all_4 | Multiplexed protein maps link subcellular organization to cellular states Cell Biology, Techniques Obtaining highly multiplexed protein measurements across multiple length scales has enormous potential for biomedicine. Here, we measured, by iterative indirect immunofluorescence imaging (4i), 40-plex protein readouts from biological samples at high-throughput from the millimeter to the nanometer scale. This approach simultaneously captures properties apparent at the population, cellular, and subcellular levels, including microenvironment, cell shape, and cell cycle state. It also captures the detailed morphology of organelles, cytoskeletal structures, nuclear subcompartments, and the fate of signaling receptors in thousands of single cells in situ. We used computer vision and systems biology approaches to achieve unsupervised comprehensive quantification of protein subcompartmentalization within various multicellular, cellular, and pharmacological contexts. Thus, highly multiplexed subcellular protein maps can be used to identify functionally relevant single-cell states. Gut, G., Herrmann, M. D., Pelkmans, L. American Association for the Advancement of Science (AAAS) 0036-8075 00368075 1095-9203 10959203 |
shingle_title_1 | Multiplexed protein maps link subcellular organization to cellular states |
shingle_title_2 | Multiplexed protein maps link subcellular organization to cellular states |
shingle_title_3 | Multiplexed protein maps link subcellular organization to cellular states |
shingle_title_4 | Multiplexed protein maps link subcellular organization to cellular states |
timestamp | 2025-06-30T23:36:20.902Z |
titel | Multiplexed protein maps link subcellular organization to cellular states |
titel_suche | Multiplexed protein maps link subcellular organization to cellular states |
topic | W V TE-TZ SQ-SU WW-YZ TA-TD U |
uid | ipn_articles_6314134 |