Zobrazeno 1 - 10
of 20
pro vyhledávání: '"Zev A. Ripstein"'
Autor:
Hui Guo, Erik Franken, Yuchen Deng, Samir Benlekbir, Garbi Singla Lezcano, Bart Janssen, Lingbo Yu, Zev A. Ripstein, Yong Zi Tan, John L. Rubinstein
Publikováno v:
IUCrJ, Vol 7, Iss 5, Pp 860-869 (2020)
Direct detector device (DDD) cameras have revolutionized electron cryomicroscopy (cryoEM) with their high detective quantum efficiency (DQE) and output of movie data. A high ratio of camera frame rate (frames per second) to camera exposure rate (elec
Externí odkaz:
https://doaj.org/article/93b68f9a8ca7414db67fd7d935e43bc8
Publikováno v:
eLife, Vol 9 (2020)
The ClpXP degradation machine consists of a hexameric AAA+ unfoldase (ClpX) and a pair of heptameric serine protease rings (ClpP) that unfold, translocate, and subsequently degrade client proteins. ClpXP is an important target for drug development ag
Externí odkaz:
https://doaj.org/article/822beeb8932145e48d5d5f0bd6a2ecf3
Flexible client-dependent cages in the assembly landscape of the periplasmic protease-chaperone DegP
The periplasmic protein DegP, that is implicated in virulence factor transport leading to pathogenicity, is a bi-functional protease and chaperone that maintains protein homeostasis in gram-negative bacteria. To perform these functions, DegP captures
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::dd36d32446f3fd55d3e1d68f7c027b7b
https://doi.org/10.1101/2022.10.17.512556
https://doi.org/10.1101/2022.10.17.512556
Publikováno v:
eLife, Vol 6 (2017)
AAA+ unfoldases are thought to unfold substrate through the central pore of their hexameric structures, but how this process occurs is not known. VAT, the Thermoplasma acidophilum homologue of eukaryotic CDC48/p97, works in conjunction with the prote
Externí odkaz:
https://doaj.org/article/dc3ec99e91454ff5b3deb8e1a5306a02
Publikováno v:
Journal of the American Chemical Society. 142:20519-20523
ClpPs are a conserved family of serine proteases that collaborate with ATP-dependent translocases to degrade protein substrates. Drugs targeting these enzymes have attracted interest for the treatment of cancer and bacterial infections due to their c
Autor:
Huaying Zhao, Yuki Toyama, Zev A Ripstein, Jacob P. Brady, Peter Schuck, Patricia L. Clark, Lewis E. Kay, Robert W. Harkness, Alexander I M Sever, Qing Luan
Publikováno v:
Proc Natl Acad Sci U S A
DegP is an oligomeric protein with dual protease and chaperone activity that regulates protein homeostasis and virulence factor trafficking in the periplasm of gram-negative bacteria. A number of oligomeric architectures adopted by DegP are thought t
Autor:
Ali Haydaroglu, Christopher M. Yip, Hui Guo, Timothy Kwok, Samir Benlekbir, Aaron Au, Zev A Ripstein, Justin M. Di Trani, John L. Rubinstein
Publikováno v:
Acta Crystallographica. Section D, Structural Biology
A method is presented for high-speed low-volume cryo-EM specimen preparation with a device constructed from readily available components.
Although microscopes and image-analysis software for electron cryomicroscopy (cryo-EM) have improved dramat
Although microscopes and image-analysis software for electron cryomicroscopy (cryo-EM) have improved dramat
Publikováno v:
Journal of the American Chemical Society. 142(49)
ClpPs are a conserved family of serine proteases that collaborate with ATP-dependent translocases to degrade protein substrates. Drugs targeting these enzymes have attracted interest for the treatment of cancer and bacterial infections due to their c
Autor:
Eric Wang, Zev A Ripstein, John L. Rubinstein, Alexander E. Conicella, Ai Nguyen, Lewis E. Kay, Peter Schuck, Rui Huang, Thomas Löhr, Michele Vendruscolo
Publikováno v:
Proc Natl Acad Sci U S A
VCP/p97, an enzyme critical to proteostasis, is regulated through interactions with protein adaptors targeting it to specific cellular tasks. One such adaptor, p47, forms a complex with p97 to direct lipid membrane remodeling. Here, we use NMR and ot
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6b2fd7b17e802dc585b5e3535d006476
https://europepmc.org/articles/PMC7585011/
https://europepmc.org/articles/PMC7585011/
Publikováno v:
Angewandte Chemie (International ed. in English). 59(50)
The hexameric p97 enzyme plays an integral role in cellular homeostasis. Large changes to the orientation of its N-terminal domains (NTDs), corresponding to NTD-down (p97-ADP) or NTD-up (p97-ATP), accompany ATP hydrolysis. The NTDs in a series of p97