Structural dynamics of AAA + ATPase Drg1 and mechanism of benzo-diazaborine inhibition
Author
Abstract
Suggested Citation
DOI: 10.1038/s41467-022-34511-2
Download full text from publisher
References listed on IDEAS
- Shan Wu & Beril Tutuncuoglu & Kaige Yan & Hailey Brown & Yixiao Zhang & Dan Tan & Michael Gamalinda & Yi Yuan & Zhifei Li & Jelena Jakovljevic & Chengying Ma & Jianlin Lei & Meng-Qiu Dong & John L. Wo, 2016. "Diverse roles of assembly factors revealed by structures of late nuclear pre-60S ribosomes," Nature, Nature, vol. 534(7605), pages 133-137, June.
- Minglei Zhao & Shenping Wu & Qiangjun Zhou & Sandro Vivona & Daniel J. Cipriano & Yifan Cheng & Axel T. Brunger, 2015. "Mechanistic insights into the recycling machine of the SNARE complex," Nature, Nature, vol. 518(7537), pages 61-67, February.
- Yang Xu & Han Han & Ian Cooney & Yuxuan Guo & Noah G. Moran & Nathan R. Zuniga & John C. Price & Christopher P. Hill & Peter S. Shen, 2022. "Active conformation of the p97-p47 unfoldase complex," Nature Communications, Nature, vol. 13(1), pages 1-8, December.
- Alexandrea N. Rizo & JiaBei Lin & Stephanie N. Gates & Eric Tse & Stephen M. Bart & Laura M. Castellano & Frank DiMaio & James Shorter & Daniel R. Southworth, 2019. "Structural basis for substrate gripping and translocation by the ClpB AAA+ disaggregase," Nature Communications, Nature, vol. 10(1), pages 1-12, December.
- Michael Prattes & Irina Grishkovskaya & Victor-Valentin Hodirnau & Ingrid Rössler & Isabella Klein & Christina Hetzmannseder & Gertrude Zisser & Christian C. Gruber & Karl Gruber & David Haselbach & H, 2021. "Structural basis for inhibition of the AAA-ATPase Drg1 by diazaborine," Nature Communications, Nature, vol. 12(1), pages 1-12, December.
Most related items
These are the items that most often cite the same works as this one and are cited by the same works as this one.- Bo Qin & Simon M. Lauer & Annika Balke & Carlos H. Vieira-Vieira & Jörg Bürger & Thorsten Mielke & Matthias Selbach & Patrick Scheerer & Christian M. T. Spahn & Rainer Nikolay, 2023. "Cryo-EM captures early ribosome assembly in action," Nature Communications, Nature, vol. 14(1), pages 1-10, December.
- Lisa Kofler & Lorenz Grundmann & Magdalena Gerhalter & Michael Prattes & Juliane Merl-Pham & Gertrude Zisser & Irina Grishkovskaya & Victor-Valentin Hodirnau & Martin Vareka & Rolf Breinbauer & Stefan, 2024. "The novel ribosome biogenesis inhibitor usnic acid blocks nucleolar pre-60S maturation," Nature Communications, Nature, vol. 15(1), pages 1-17, December.
- Amir Pozner & Li Li & Shiv Prakash Verma & Shuxin Wang & Jared J. Barrott & Mary L. Nelson & Jamie S. E. Yu & Gian Luca Negri & Shane Colborne & Christopher S. Hughes & Ju-Fen Zhu & Sydney L. Lambert , 2024. "ASPSCR1-TFE3 reprograms transcription by organizing enhancer loops around hexameric VCP/p97," Nature Communications, Nature, vol. 15(1), pages 1-21, December.
- Ian Cooney & Heidi L. Schubert & Karina Cedeno & Olivia N. Fisher & Richard Carson & John C. Price & Christopher P. Hill & Peter S. Shen, 2024. "Visualization of the Cdc48 AAA+ ATPase protein unfolding pathway," Nature Communications, Nature, vol. 15(1), pages 1-11, December.
- Harim I. Won & Samuel Zinga & Olga Kandror & Tatos Akopian & Ian D. Wolf & Jessica T. P. Schweber & Ernst W. Schmid & Michael C. Chao & Maya Waldor & Eric J. Rubin & Junhao Zhu, 2024. "Targeted protein degradation in mycobacteria uncovers antibacterial effects and potentiates antibiotic efficacy," Nature Communications, Nature, vol. 15(1), pages 1-14, December.
- Gerald Ryan R. Aquino & Philipp Hackert & Nicolai Krogh & Kuan-Ting Pan & Mariam Jaafar & Anthony K. Henras & Henrik Nielsen & Henning Urlaub & Katherine E. Bohnsack & Markus T. Bohnsack, 2021. "The RNA helicase Dbp7 promotes domain V/VI compaction and stabilization of inter-domain interactions during early 60S assembly," Nature Communications, Nature, vol. 12(1), pages 1-16, December.
- Claudio Mirabello & Björn Wallner & Björn Nystedt & Stavros Azinas & Marta Carroni, 2024. "Unmasking AlphaFold to integrate experiments and predictions in multimeric complexes," Nature Communications, Nature, vol. 15(1), pages 1-16, December.
- Jingyu Zhan & Allison Zeher & Rick Huang & Wai Kwan Tang & Lisa M. Jenkins & Di Xia, 2024. "Conformations of Bcs1L undergoing ATP hydrolysis suggest a concerted translocation mechanism for folded iron-sulfur protein substrate," Nature Communications, Nature, vol. 15(1), pages 1-14, December.
- Kamil Sekulski & Victor Emmanuel Cruz & Christine S. Weirich & Jan P. Erzberger, 2023. "rRNA methylation by Spb1 regulates the GTPase activity of Nog2 during 60S ribosomal subunit assembly," Nature Communications, Nature, vol. 14(1), pages 1-11, December.
Corrections
All material on this site has been provided by the respective publishers and authors. You can help correct errors and omissions. When requesting a correction, please mention this item's handle: RePEc:nat:natcom:v:13:y:2022:i:1:d:10.1038_s41467-022-34511-2. See general information about how to correct material in RePEc.
If you have authored this item and are not yet registered with RePEc, we encourage you to do it here. This allows to link your profile to this item. It also allows you to accept potential citations to this item that we are uncertain about.
If CitEc recognized a bibliographic reference but did not link an item in RePEc to it, you can help with this form .
If you know of missing items citing this one, you can help us creating those links by adding the relevant references in the same way as above, for each refering item. If you are a registered author of this item, you may also want to check the "citations" tab in your RePEc Author Service profile, as there may be some citations waiting for confirmation.
For technical questions regarding this item, or to correct its authors, title, abstract, bibliographic or download information, contact: Sonal Shukla or Springer Nature Abstracting and Indexing (email available below). General contact details of provider: http://www.nature.com .
Please note that corrections may take a couple of weeks to filter through the various RePEc services.