Výsledky vyhledávání - "Claire F Dickson"

Akademický článek

IP6 is an HIV pocket factor that prevents capsid collapse and promotes DNA synthesis

Autor: Donna L Mallery, Chantal L Márquez, William A McEwan, Claire F Dickson, David A Jacques, Madhanagopal Anandapadamanaban, Katsiaryna Bichel, Gregory J Towers, Adolfo Saiardi, Till Böcking, Leo C James

Publikováno v: eLife, Vol 7 (2018)

The HIV capsid is semipermeable and covered in electropositive pores that are essential for viral DNA synthesis and infection. Here, we show that these pores bind the abundant cellular polyanion IP6, transforming viral stability from minutes to hours

Externí odkaz: https://doaj.org/article/7c6859948eca463995437484988a1476

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Akademický článek

Trim-Away ubiquitinates and degrades lysine-less and N-terminally acetylated substrates

Autor: Leo Kiss, Tyler Rhinesmith, Jakub Luptak, Claire F. Dickson, Jonas Weidenhausen, Shannon Smyly, Ji-Chun Yang, Sarah L. Maslen, Irmgard Sinning, David Neuhaus, Dean Clift, Leo C. James

Publikováno v: Nature Communications, Vol 14, Iss 1, Pp 1-17 (2023)

Abstract TRIM proteins are the largest family of E3 ligases in mammals. They include the intracellular antibody receptor TRIM21, which is responsible for mediating targeted protein degradation during Trim-Away. Despite their importance, the ubiquitin

Externí odkaz: https://doaj.org/article/9847497c03534f53b81f80ff92484d91

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Akademický článek

A tri-ionic anchor mechanism drives Ube2N-specific recruitment and K63-chain ubiquitination in TRIM ligases

Autor: Leo Kiss, Jingwei Zeng, Claire F. Dickson, Donna L. Mallery, Ji-Chun Yang, Stephen H. McLaughlin, Andreas Boland, David Neuhaus, Leo C. James

Publikováno v: Nature Communications, Vol 10, Iss 1, Pp 1-13 (2019)

The E3 ligase TRIM21 targets a broad range of pathogenic proteins using a unique mechanism. Here, the authors combine structural, biochemical and cell biological approaches to elucidate how TRIM21 selectively recruits its canonical E2 partner enzyme

Externí odkaz: https://doaj.org/article/470293ee22be4d32ba89b9430667e524

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Trim-Away degrades lysine-less substrates without requiring ligase autoubiquitination

Autor: Leo Kiss, Tyler Rhinesmith, Claire F Dickson, Jonas Weidenhausen, Shannon Smyly, Jakub Luptak, Ji-Chun Yang, Sarah L Maslen, Irmgard Sinning, David Neuhaus, Dean Clift, Leo C James

TRIM proteins are the largest family of E3 ligases in mammals. They include the intracellular antibody receptor TRIM21, which is responsible for mediating targeted protein degradation during Trim-Away. Despite their importance, the ubiquitination mec

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::2ff087e88dc61ef593889cbe848b8038
https://doi.org/10.1101/2022.06.29.498105

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Rapid HIV-1 Capsid Interaction Screening Using Fluorescence Fluctuation Spectroscopy

Autor: Vaibhav Shah, Stuart Turville, James C. Walsh, Emma Sierecki, Till Böcking, David A. Jacques, Claire F. Dickson, Derrick Lau, Jeffrey H. Stear, Yann Gambin, Akshay Bhumkar, Dominic J. B. Hunter, Andrew Tuckwell

Publikováno v: Analytical Chemistry. 93:3786-3793

The HIV capsid is a multifunctional protein capsule that mediates the delivery of the viral genetic material into the nucleus of the target cell. Host cell proteins bind to a number of repeating binding sites on the capsid to regulate steps in the re

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::131c18c36f0a5344941ac1891aa0c2a3
https://doi.org/10.1021/acs.analchem.0c04250

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Target-induced clustering activates Trim-Away of pathogens and proteins

Autor: Leo C. James, Aamir S. Mukadam, David A. Jacques, Leo Kiss, William A. McEwan, Christopher M. Johnson, Nadine Renner, Ana Filipa Santos, Eurico Morais-de-Sá, Marina Vaysburd, Claire F. Dickson, Dean Clift, Jingwei Zeng, Jakub Luptak, Mariana Osswald, Stephen H. McLaughlin

Publikováno v: Nat Struct Mol Biol

Trim-Away is a recently developed technology that exploits off-the-shelf antibodies and the RING E3 ligase and cytosolic antibody receptor TRIM21 to carry out rapid protein depletion. How TRIM21 is catalytically activated upon target engagement, eith

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::95319461771d8a5b6e3f5ff62e1a43c8
https://europepmc.org/articles/PMC7611929/

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Substrate-induced clustering activates Trim-Away of pathogens and proteins

Autor: Christopher M. Johnson, Claire F. Dickson, Nadine Renner, Marina Vaysburd, Jakub Luptak, Dean Clift, David A. Jacques, Leo C. James, Ana Filipa Santos, Eurico Morais-de-Sá, Jingwei Zeng, Aamir S. Mukadam, William A. McEwan, Mariana Osswald

SUMMARYTrim-Away is a powerful new technology that exploits off-the-shelf antibodies and the E3 RING ligase and cytosolic antibody receptor TRIM21 to carry out rapid protein depletion. How TRIM21 is catalytically-activated upon substrate engagement d

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::5330dfd9d8ebe28eec060f1b17030504
https://doi.org/10.1101/2020.07.28.225359

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A tri-ionic anchor mechanism drives Ube2N-specific recruitment and K63-chain ubiquitination in TRIM ligases

Autor: Claire F. Dickson, Leo C. James, Leo Kiss, David Neuhaus, Ji-Chun Yang, Jingwei Zeng, Andreas Boland, Donna L. Mallery, Stephen H. McLaughlin

Publikováno v: Nature Communications, Vol 10, Iss 1, Pp 1-13 (2019)
Nature Communications

The cytosolic antibody receptor TRIM21 possesses unique ubiquitination activity that drives broad-spectrum anti-pathogen targeting and underpins the protein depletion technology Trim-Away. This activity is dependent on formation of self-anchored, K63

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::319dfb0128eb74f302b1cae89eeda2d5
https://doi.org/10.1038/s41467-019-12388-y

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