Zobrazeno 1 - 10
of 92
pro vyhledávání: '"Youdong, Mao"'
Autor:
Weize Wang, Ling Liang, Zonglin Dai, Peng Zuo, Shang Yu, Yishuo Lu, Dian Ding, Hongyi Chen, Hui Shan, Yan Jin, Youdong Mao, Yuxin Yin
Publikováno v:
Nature Communications, Vol 15, Iss 1, Pp 1-14 (2024)
Abstract The CUL3-RING E3 ubiquitin ligases (CRL3s) play an essential role in response to extracellular nutrition and stress stimuli. The ubiquitin ligase function of CRL3s is activated through dimerization. However, how and why such a dimeric assemb
Externí odkaz:
https://doaj.org/article/a3fe32b50b3848b2aed23ead80582850
Autor:
Kunyu Wang, Shijian Zhang, Eden P. Go, Haitao Ding, Wei Li Wang, Hanh T. Nguyen, John C. Kappes, Heather Desaire, Joseph Sodroski, Youdong Mao
Publikováno v:
Communications Biology, Vol 6, Iss 1, Pp 1-18 (2023)
Abstract During virus entry, the pretriggered human immunodeficiency virus (HIV-1) envelope glycoprotein (Env) trimer initially transits into a default intermediate state (DIS) that remains structurally uncharacterized. Here, we present cryo-EM struc
Externí odkaz:
https://doaj.org/article/5183390ce11740eba560933fba8b9a2a
Autor:
Shitao Zou, Youdong Mao
Publikováno v:
Clinical and Translational Medicine, Vol 12, Iss 8, Pp n/a-n/a (2022)
Externí odkaz:
https://doaj.org/article/41aa55077a544a0ca5b3241e3bfc8f96
Publikováno v:
BMC Bioinformatics, Vol 20, Iss 1, Pp 1-17 (2019)
Abstract Background The detection of weak signals and selection of single particles from low-contrast micrographs of frozen hydrated biomolecules by cryo-electron microscopy (cryo-EM) represents a major practical bottleneck in cryo-EM data analysis.
Externí odkaz:
https://doaj.org/article/ef20c44775ee4726a93744698ddacd2f
Publikováno v:
Nature Communications, Vol 9, Iss 1, Pp 1-12 (2018)
The 26S proteasome consists of a core particle that is capped at each side by a regulatory particle. Here the authors present cryo-EM structures of the activated human 26S proteasome holoenzyme in three alternative open-gate states, which provides me
Externí odkaz:
https://doaj.org/article/db4b804dc56b4cd2bb2a2dc1b71eeb2d
Publikováno v:
BMC Bioinformatics, Vol 18, Iss 1, Pp 1-10 (2017)
Abstract Background Single-particle cryo-electron microscopy (cryo-EM) has become a mainstream tool for the structural determination of biological macromolecular complexes. However, high-resolution cryo-EM reconstruction often requires hundreds of th
Externí odkaz:
https://doaj.org/article/3e5f9e0751f0432d9fc4c5fa4d6ba225
Publikováno v:
Nature. 605:567-574
Proteasomal degradation of ubiquitylated proteins is tightly regulated at multiple levels1–3. A primary regulatory checkpoint is the removal of ubiquitin chains from substrates by the deubiquitylating enzyme ubiquitin-specific protease 14 (USP14),
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::56557c435ddfc15a2e8b69d1f13f1b49
https://doi.org/10.1038/s41586-022-04671-8
https://doi.org/10.1038/s41586-022-04671-8
Autor:
Shuwen Zhang, Youdong Mao
Publikováno v:
Biomolecules, Vol 10, Iss 4, p 629 (2020)
Adenosine triphosphatases (ATPases) associated with a variety of cellular activities (AAA+), the hexameric ring-shaped motor complexes located in all ATP-driven proteolytic machines, are involved in many cellular processes. Powered by cycles of ATP b
Externí odkaz:
https://doaj.org/article/963b976250ba402d8862a96bfef8a859
Autor:
Jiayi Wu, Yong-Bei Ma, Charles Congdon, Bevin Brett, Shuobing Chen, Yaofang Xu, Qi Ouyang, Youdong Mao
Publikováno v:
PLoS ONE, Vol 12, Iss 8, p e0182130 (2017)
Structural heterogeneity in single-particle cryo-electron microscopy (cryo-EM) data represents a major challenge for high-resolution structure determination. Unsupervised classification may serve as the first step in the assessment of structural hete
Externí odkaz:
https://doaj.org/article/098e06f2fba349da8fd80c7ffac4ff0e
Publikováno v:
International Journal of Molecular Sciences; Volume 23; Issue 16; Pages: 8872
The cellular functions are executed by biological macromolecular complexes in nonequilibrium dynamic processes, which exhibit a vast diversity of conformational states. Solving the conformational continuum of important biomolecular complexes at the a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::de8b19443f39a91bc1bef5f8124e5154