Zobrazeno 1 - 10
of 40
pro vyhledávání: '"Keith J Mickolajczyk"'
Publikováno v:
eLife, Vol 11 (2022)
Catch bonds are a form of mechanoregulation wherein protein-ligand interactions are strengthened by the application of dissociative tension. Currently, the best-characterized examples of catch bonds are between single protein-ligand pairs. The essent
Externí odkaz:
https://doaj.org/article/1c887fbbda2640e496a009cf2e1c248f
Autor:
Ruifang Guan, Lei Zhang, Qian Peter Su, Keith J. Mickolajczyk, Geng-Yuan Chen, William O. Hancock, Yujie Sun, Yongfang Zhao, Zhucheng Chen
Publikováno v:
Nature Communications, Vol 8, Iss 1, Pp 1-9 (2017)
Kinesins are molecular motors that travel along microtubules through a nucleotide-dependent stepping mechanism. Here the authors present the crystal structure of Zen4 (kinesin-6) in an apo state that sheds light on a key stepping intermediate of kine
Externí odkaz:
https://doaj.org/article/0e277f1467ef49419410cb58269e9820
Autor:
Awani Upadhyay, Aditya Pisupati, Timothy Jegla, Matt Crook, Keith J. Mickolajczyk, Matthew Shorey, Laura E. Rohan, Katherine A. Billings, Melissa M. Rolls, William O. Hancock, Wendy Hanna-Rose
Publikováno v:
Nature Communications, Vol 7, Iss 1, Pp 1-11 (2016)
TRPV are cation channels activated by physical and chemical stimuli. Here the authors show that nicotinamide is a soluble, endogenous agonist for orthologous TRPV channels fromC. elegans and Drosophila, unveiling a metabolic-based regulation for TRPV
Externí odkaz:
https://doaj.org/article/dfd0ef3108b94258be603a05f7ad9bb7
Autor:
Sinduja K. Marx, Keith J. Mickolajczyk, Jonathan M. Craig, Christopher A. Thomas, Akira M. Pfeffer, Sarah J. Abell, Jessica D. Carrasco, Michaela C. Franzi, Jesse R. Huang, Hwanhee C. Kim, Henry D. Brinkerhoff, Tarun M. Kapoor, Jens H. Gundlach, Andrew H. Laszlo
Publikováno v:
bioRxiv : the preprint server for biology.
The genome of SARS-CoV-2 encodes for a helicase called nsp13 that is essential for viral replication and highly conserved across related viruses, making it an attractive antiviral target. Here we use nanopore tweezers, a high-resolution single-molecu
Autor:
Thomas Walz, Nan Chen, Yiming Niu, Sara E. Warrington, Keith J. Mickolajczyk, Paul Dominic B. Olinares, Brian T. Chait, Tarun M. Kapoor, Yusuke Sasaki
Publikováno v:
Proc Natl Acad Sci U S A
Mdn1 is an essential mechanoenzyme that uses the energy from ATP hydrolysis to physically reshape and remodel, and thus mature, the 60S subunit of the ribosome. This massive (>500 kDa) protein has an N-terminal AAA (ATPase associated with diverse cel
Publikováno v:
eLife, Vol 11 (2022)
Catch bonds are a form of mechanoregulation wherein protein-ligand interactions are strengthened by the application of dissociative tension. Currently, the best-characterized examples of catch bonds are between single protein-ligand pairs. The essent
Publikováno v:
Biophys J
High-resolution tracking of gold nanoparticle-labeled proteins has emerged as a powerful technique for measuring the structural kinetics of processive enzymes and other biomacromolecules. These techniques use point spread function (PSF) fitting metho
Autor:
William O. Hancock, Keith J. Mickolajczyk, Allison M. Gicking, Lijun Guo, Pan Wang, Weihong Qiu, Changlin Liu
Publikováno v:
Biophysical Journal. 116:1270-1281
Phragmoplast-associated kinesin-related protein 2 (PAKRP2) is an orphan kinesin in Arabidopsis thaliana that is thought to transport vesicles along phragmoplast microtubules for cell plate formation. Here, using single-molecule fluorescence microscop
Autor:
Tarun M. Kapoor, Xiaocong Cao, Patrick M.M. Shelton, Keith J. Mickolajczyk, Amol Aher, Shixin Liu, Sara E. Warrington, Michael Grasso
Publikováno v:
bioRxiv
Biophysical Journal
Biophysical Journal
The superfamily-1 helicase non-structural protein 13 (nsp13) is required for SARS-CoV-2 replication, making it an important antiviral therapeutic target. The mechanism and regulation of nsp13 has not been explored at the single-molecule level. Specif
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a7e8ec2131c11b51a3e59658b40441ab
https://doi.org/10.1101/2020.07.31.231274
https://doi.org/10.1101/2020.07.31.231274