Zobrazeno 1 - 10
of 369
pro vyhledávání: '"George N. Phillips"'
Autor:
Tom Pan, Chen Dun, Shikai Jin, Mitchell D. Miller, Anastasios Kyrillidis, George N. Phillips Jr.
Publikováno v:
Structural Dynamics, Vol 11, Iss 4, Pp 044701-044701-14 (2024)
Determining the atomic-level structure of a protein has been a decades-long challenge. However, recent advances in transformers and related neural network architectures have enabled researchers to significantly improve solutions to this problem. Thes
Externí odkaz:
https://doaj.org/article/35ebbaec82dd44a9a6ced8b4de52544e
Autor:
Tek Narsingh Malla, Kara Zielinski, Luis Aldama, Sasa Bajt, Denisse Feliz, Brendon Hayes, Mark Hunter, Christopher Kupitz, Stella Lisova, Juraj Knoska, Jose Manuel Martin-Garcia, Valerio Mariani, Suraj Pandey, Ishwor Poudyal, Raymond G. Sierra, Alexandra Tolstikova, Oleksandr Yefanov, Chung Hong Yoon, Abbas Ourmazd, Petra Fromme, Peter Schwander, Anton Barty, Henry N. Chapman, Emina A. Stojkovic, Alexander Batyuk, Sébastien Boutet, George N. Phillips, Lois Pollack, Marius Schmidt
Publikováno v:
Nature Communications, Vol 14, Iss 1, Pp 1-15 (2023)
Abstract For decades, researchers have elucidated essential enzymatic functions on the atomic length scale by tracing atomic positions in real-time. Our work builds on possibilities unleashed by mix-and-inject serial crystallography (MISC) at X-ray f
Externí odkaz:
https://doaj.org/article/50042ef4cec14678ac809352eb19f238
Publikováno v:
IUCrJ, Vol 10, Iss 4, Pp 487-496 (2023)
The general de novo solution of the crystallographic phase problem is difficult and only possible under certain conditions. This paper develops an initial pathway to a deep learning neural network approach for the phase problem in protein crystallogr
Externí odkaz:
https://doaj.org/article/5f4e3dbe014048a3be76cba849b381eb
Publikováno v:
Structural Dynamics, Vol 11, Iss 1, Pp 014702-014702-12 (2024)
Adenylate kinase is a ubiquitous enzyme in living systems and undergoes dramatic conformational changes during its catalytic cycle. For these reasons, it is widely studied by genetic, biochemical, and biophysical methods, both experimental and theore
Externí odkaz:
https://doaj.org/article/452be095b90749f995e0cd79032f1118
Autor:
Suraj Pandey, George Calvey, Andrea M. Katz, Tek Narsingh Malla, Faisal H. M. Koua, Jose M. Martin-Garcia, Ishwor Poudyal, Jay-How Yang, Mohammad Vakili, Oleksandr Yefanov, Kara A. Zielinski, Sasa Bajt, Salah Awel, Katarina Doerner, Matthias Frank, Luca Gelisio, Rebecca Jernigan, Henry Kirkwood, Marco Kloos, Jayanath Koliyadu, Valerio Mariani, Mitchell D. Miller, Grant Mills, Garrett Nelson, Jose L. Olmos Jr, Alireza Sadri, Tokushi Sato, Alexandra Tolstikova, Weijun Xu, Abbas Ourmazd, John C. H. Spence, Peter Schwander, Anton Barty, Henry N. Chapman, Petra Fromme, Adrian P. Mancuso, George N. Phillips Jr, Richard Bean, Lois Pollack, Marius Schmidt
Publikováno v:
IUCrJ, Vol 8, Iss 6, Pp 878-895 (2021)
Here, we illustrate what happens inside the catalytic cleft of an enzyme when substrate or ligand binds on single-millisecond timescales. The initial phase of the enzymatic cycle is observed with near-atomic resolution using the most advanced X-ray s
Externí odkaz:
https://doaj.org/article/fbdbd2a5c401447a974071c858ead28e
Autor:
Zhiwen Liu, Fanglong Zhao, Boyang Zhao, Jie Yang, Joseph Ferrara, Banumathi Sankaran, B. V. Venkataram Prasad, Biki Bapi Kundu, George N. Phillips, Yang Gao, Liya Hu, Tong Zhu, Xue Gao
Publikováno v:
Nature Communications, Vol 12, Iss 1, Pp 1-12 (2021)
Prenylated indole alkaloids contain spirooxindole rings with a 3R or 3S carbon stereocenter, which determines their bioactivities, but the biocatalytic mechanism controlling the 3R- or 3S-spirooxindole formation was unclear. Here, the authors report
Externí odkaz:
https://doaj.org/article/4b7a611c36bc4e4eb026f676456db539
Autor:
Hou-Fu Guo, Neus Bota-Rabassedas, Masahiko Terajima, B. Leticia Rodriguez, Don L. Gibbons, Yulong Chen, Priyam Banerjee, Chi-Lin Tsai, Xiaochao Tan, Xin Liu, Jiang Yu, Michal Tokmina-Roszyk, Roma Stawikowska, Gregg B. Fields, Mitchell D. Miller, Xiaoyan Wang, Juhoon Lee, Kevin N. Dalby, Chad J. Creighton, George N. Phillips, John A. Tainer, Mitsuo Yamauchi, Jonathan M. Kurie
Publikováno v:
Communications Biology, Vol 4, Iss 1, Pp 1-10 (2021)
Guo et al. determine the molecular basis of collagen lysyl hydroxylase 2 (LH2) substrate specificity. They further show that LH2 also functions as a collagen glucosyltransferase to promote lung cancer progression.
Externí odkaz:
https://doaj.org/article/33c609a5058f4848b50950a0e6133563
Autor:
Shikai Jin, Mitchell D. Miller, Mingchen Chen, Nicholas P. Schafer, Xingcheng Lin, Xun Chen, George N. Phillips Jr, Peter G. Wolynes
Publikováno v:
IUCrJ, Vol 7, Iss 6, Pp 1168-1178 (2020)
The phase problem in X-ray crystallography arises from the fact that only the intensities, and not the phases, of the diffracting electromagnetic waves are measured directly. Molecular replacement can often estimate the relative phases of reflections
Externí odkaz:
https://doaj.org/article/1efb0ded5d0d41468fd2c4ad60f1065d
Autor:
Melissa S. Traver, Sarah E. Bradford, Jose Luis Olmos, Zachary J. Wright, Mitchell D. Miller, Weijun Xu, George N. Phillips, Bonnie Bartel
Publikováno v:
Frontiers in Cell and Developmental Biology, Vol 10 (2022)
Peroxisomes are eukaryotic organelles that sequester critical oxidative reactions and process the resulting reactive oxygen species into less toxic byproducts. Peroxisome function and formation are coordinated by peroxins (PEX proteins) that guide pe
Externí odkaz:
https://doaj.org/article/9cdbe4c43d9c41b8b8bcb2221c25eee7
Autor:
George N. Phillips Jr.
Publikováno v:
Structural Dynamics, Vol 8, Iss 2, Pp 020405-020405-1 (2021)
Externí odkaz:
https://doaj.org/article/37cdf270983d4d9d810d033a45cc210f