Zobrazeno 1 - 10
of 44
pro vyhledávání: '"Zanlin Yu"'
Autor:
Un Seng Chio, Eugene Palovcak, Anton A. A. Smith, Henriette Autzen, Elise N. Muñoz, Zanlin Yu, Feng Wang, David A. Agard, Jean-Paul Armache, Geeta J. Narlikar, Yifan Cheng
Publikováno v:
Nature Communications, Vol 15, Iss 1, Pp 1-12 (2024)
Abstract Single-particle cryo-EM is widely used to determine enzyme-nucleosome complex structures. However, cryo-EM sample preparation remains challenging and inconsistent due to complex denaturation at the air-water interface (AWI). Here, to address
Externí odkaz:
https://doaj.org/article/27aa364ca261463cb826925799de5972
Publikováno v:
IUCrJ, Vol 7, Iss 6, Pp 1142-1150 (2020)
In cryogenic electron microscopy (cryo-EM) of radiation-sensitive biological samples, both the signal-to-noise ratio (SNR) and the contrast of images are critically important in the image-processing pipeline. Classic methods improve low-frequency ima
Externí odkaz:
https://doaj.org/article/37fafd7cde5d44d08455d9fd1053e30f
Publikováno v:
Nature Communications, Vol 11, Iss 1, Pp 1-11 (2020)
The 26S proteasome is a protein degradation machine composed of a 20S core particle (CP) flanked at one or both ends by a 19S ATPase regulatory particle (RP). Here the authors reconstitute asymmetric archaeal proteasomes and reveal allosteric couplin
Externí odkaz:
https://doaj.org/article/30380c212df8404498d4bb7e427838f4
Autor:
Laylan Bramasole, Abhishek Sinha, Dana Harshuk, Angela Cirigliano, Gurevich Sylvia, Zanlin Yu, Rinat Lift Carmeli, Michael H. Glickman, Teresa Rinaldi, Elah Pick
Publikováno v:
Biomolecules, Vol 9, Iss 9, p 449 (2019)
The class of Cullin−RING E3 ligases (CRLs) selectively ubiquitinate a large portion of proteins targeted for proteolysis by the 26S proteasome. Before degradation, ubiquitin molecules are removed from their conjugated proteins by deubiquitinating e
Externí odkaz:
https://doaj.org/article/fb2309b1301d4e8786277a08077d00d6
Autor:
Arpit Gupta, Alfred M. Lentzsch, Alex Siegel, Zanlin Yu, Un Seng Chio, Yifan Cheng, Shu-ou Shan
Publikováno v:
Science Advances. 9
Ring-forming AAA + chaperones solubilize protein aggregates and protect organisms from proteostatic stress. In metazoans, the AAA + chaperone Skd3 in the mitochondrial intermembrane space (IMS) is critical for human health and efficiently refolds agg
Autor:
Irene P. Chen, James E. Longbotham, Sarah McMahon, Rahul K. Suryawanshi, Mir M. Khalid, Taha Y. Taha, Takako Tabata, Jennifer M. Hayashi, Frank W. Soveg, Jared Carlson-Stevermer, Meghna Gupta, Meng Yao Zhang, Victor L. Lam, Yang Li, Zanlin Yu, Erron W. Titus, Amy Diallo, Jennifer Oki, Kevin Holden, Nevan Krogan, Danica Galonić Fujimori, Melanie Ott
Publikováno v:
Cell reports, vol 40, iss 3
bioRxiv
bioRxiv
Inhibitors of bromodomain and extraterminal domain (BET) proteins are possible anti-severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) prophylactics as they downregulate angiotensin-converting enzyme 2 (ACE2). Here we show that BET proteins
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c5372b20c38023d14b59bc671f5a2a48
https://escholarship.org/uc/item/2pf842c8
https://escholarship.org/uc/item/2pf842c8
Autor:
Nan Zhang, Gira Bhabha, Iris Grossman-Haham, Nicolas Coudray, Ronald D. Vale, Zanlin Yu, Feng Wang
Publikováno v:
Nature structural & molecular biology
Nature structural & molecular biology, vol 28, iss 1
Nature structural & molecular biology, vol 28, iss 1
Motile cilia power cell locomotion and drive extracellular fluid flow by propagating bending waves from their base to tip. The coordinated bending of cilia requires mechanoregulation by the radial spoke (RS) protein complexes and the microtubule cent
Autor:
Zanlin Yu, Junliang Chen, Enzo Takagi, Feng Wang, Bidisha Saha, Xi Liu, Lydia-Marie Joubert, Catherine E. Gleason, Mingliang Jin, Chengmin Li, Carlos Nowotny, David Agard, Yifan Cheng, David Pearce
mTORC2 is a multi-subunit kinase complex that is central to multiple essential signaling pathways. Two core subunits, Rictor and mSin1 distinguish it from its relative, mTORC1 and support context-dependent phosphorylation of its substrates. mTORC2 st
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::55c72a063ae12142da801ad1db253226
https://doi.org/10.1101/2022.02.03.478898
https://doi.org/10.1101/2022.02.03.478898
Publikováno v:
Proceedings of the National Academy of Sciences. 117:5298-5309
The 20S core particle (CP) proteasome is a molecular assembly catalyzing the degradation of misfolded proteins or proteins no longer required for function. It is composed of four stacked heptameric rings that form a barrel-like structure, sequesterin
Autor:
Zanlin Yu, Junliang Chen, Enzo Takagi, Feng Wang, Bidisha Saha, Xi Liu, Lydia-Marie Joubert, Catherine E. Gleason, Mingliang Jin, Chengmin Li, Carlos Nowotny, David Agard, Yifan Cheng, David Pearce
Publikováno v:
The Journal of biological chemistry, vol 298, iss 9
Mechanistic target of rapamycin complex 2 (mTORC2) is a multi-subunit kinase complex, central to multiple essential signaling pathways. Two core subunits, Rictor and mSin1, distinguish it from the related mTORC1 and support context-dependent phosphor