Zobrazeno 1 - 10
of 619
pro vyhledávání: '"William F. DeGrado"'
Autor:
Gregory E. Merz, Matthew J. Chalkley, Sophia K. Tan, Eric Tse, Joanne Lee, Stanley B. Prusiner, Nick A. Paras, William F. DeGrado, Daniel R. Southworth
Publikováno v:
Nature Communications, Vol 14, Iss 1, Pp 1-11 (2023)
Abstract Accumulation of filamentous aggregates of tau protein in the brain is a pathological hallmark of Alzheimer’s disease (AD) and many other neurodegenerative tauopathies. The filaments adopt disease-specific cross-β amyloid conformations tha
Externí odkaz:
https://doaj.org/article/4d453a94c2d04d8b84481f4520c5fd9e
Autor:
Thaila Fernanda dos Reis, Patrícia Alves de Castro, Rafael Wesley Bastos, Camila Figueiredo Pinzan, Pedro F. N. Souza, Suzanne Ackloo, Mohammad Anwar Hossain, David Harold Drewry, Sondus Alkhazraji, Ashraf S. Ibrahim, Hyunil Jo, Jorge D. Lightfoot, Emily M. Adams, Kevin K. Fuller, William F. deGrado, Gustavo H. Goldman
Publikováno v:
Nature Communications, Vol 14, Iss 1, Pp 1-19 (2023)
Abstract Fungal infections cause more than 1.5 million deaths a year. Due to emerging antifungal drug resistance, novel strategies are urgently needed to combat life-threatening fungal diseases. Here, we identify the host defense peptide mimetic, bri
Externí odkaz:
https://doaj.org/article/95f2a58a934d446abc7358a90c1dec91
Autor:
Alison M. Maxwell, Peng Yuan, Brianna M. Rivera, Wilder Schaaf, Mihovil Mladinov, Vee P. Prasher, Andrew C. Robinson, William F. DeGrado, Carlo Condello
Publikováno v:
Acta Neuropathologica Communications, Vol 9, Iss 1, Pp 1-15 (2021)
Abstract Amyloid beta (Aβ) is thought to play a critical role in the pathogenesis of Alzheimer’s disease (AD). Prion-like Aβ polymorphs, or “strains”, can have varying pathogenicity and may underlie the phenotypic heterogeneity of the disease
Externí odkaz:
https://doaj.org/article/dce996dec328498197f03187eecb924c
Autor:
Bing Yang, Shibing Tang, Cheng Ma, Shang-Tong Li, Guang-Can Shao, Bobo Dang, William F. DeGrado, Meng-Qiu Dong, Peng George Wang, Sheng Ding, Lei Wang
Publikováno v:
Nature Communications, Vol 8, Iss 1, Pp 1-10 (2017)
Proteins associate via weak and transient interactions that are challenging to identify in vivo. Here, the authors use a genetically encoded chemical cross-linker to covalently lock interacting proteins in live cells, allowing them to identify the ca
Externí odkaz:
https://doaj.org/article/780166a230784b39849b98e73164024f
Autor:
Lee Schnaider, Sayanti Brahmachari, Nathan W. Schmidt, Bruk Mensa, Shira Shaham-Niv, Darya Bychenko, Lihi Adler-Abramovich, Linda J. W. Shimon, Sofiya Kolusheva, William F. DeGrado, Ehud Gazit
Publikováno v:
Nature Communications, Vol 8, Iss 1, Pp 1-10 (2017)
Peptide-based supramolecular assemblies are a promising class of nanomaterials with important biomedical applications, but their antibacterial properties can be overlooked. Here the authors show the antibacterial activity of self-assembled diphenylal
Externí odkaz:
https://doaj.org/article/efb41b995bd74dbab61d3ed3bd64f959
Autor:
Kook-Han Kim, Dong-Kyun Ko, Yong-Tae Kim, Nam Hyeong Kim, Jaydeep Paul, Shao-Qing Zhang, Christopher B. Murray, Rudresh Acharya, William F. DeGrado, Yong Ho Kim, Gevorg Grigoryan
Publikováno v:
Nature Communications, Vol 7, Iss 1, Pp 1-9 (2016)
Self-assembly enables complex structures to be fabricated from a few relatively simple components, but requires a detailed understanding of how the constituents may interact. Here, the authors report the rational assembly and crystallographic charact
Externí odkaz:
https://doaj.org/article/6877a1c01f864afab9c66f75013bfad2
Autor:
Ismail A. Ahmed, Arusha Acharyya, Christina M. Eng, Jeffrey M. Rodgers, William F. DeGrado, Hyunil Jo, Feng Gai
Publikováno v:
Molecules, Vol 24, Iss 3, p 602 (2019)
Unnatural nucleosides possessing unique spectroscopic properties that mimic natural nucleobases in both size and chemical structure are ideally suited for spectroscopic measurements of DNA/RNA structure and dynamics in a site-specific manner. However
Externí odkaz:
https://doaj.org/article/8fa2ccf121514fab88623f8f19597618
Autor:
Bruk Mensa, Nicholas F Polizzi, Kathleen S Molnar, Andrew M Natale, Thomas Lemmin, William F DeGrado
Publikováno v:
eLife, Vol 10 (2021)
Transmembrane signaling proteins couple extracytosolic sensors to cytosolic effectors. Here, we examine how binding of Mg2+ to the sensor domain of an E. coli two component histidine kinase (HK), PhoQ, modulates its cytoplasmic kinase domain. We use
Externí odkaz:
https://doaj.org/article/d5bc844519104cae8d3da4e41b6883b8
Autor:
Cristina Arrigoni, Marco Lolicato, David Shaya, Ahmed Rohaim, Felix Findeisen, Lam-Kiu Fong, Claire M. Colleran, Pawel Dominik, Sangwoo S. Kim, Jonathan P. Schuermann, William F. DeGrado, Michael Grabe, Anthony A. Kossiakoff, Daniel L. Minor
Publikováno v:
Nat Struct Mol Biol
Every voltage-gated ion channel (VGIC) has a pore domain (PD) made from four subunits, each comprising an antiparallel transmembrane helix pair bridged by a loop. The extent to which PD subunit structure requires quaternary interactions is unclear. H
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1228e10502809bafbfb88b46afc7f7d4
https://doi.org/10.1038/s41594-022-00775-x
https://doi.org/10.1038/s41594-022-00775-x
Autor:
Barbara Celona, Haifan Wu, Bobo Dang, Huong T. Kratochvil, William F. DeGrado, Brian L. Black
Expansion of intronic GGGGCC repeats in theC9orf72gene causes amyotrophic lateral sclerosis (ALS) and frontotemporal dementia (FTD). Transcription of the expanded repeats results in the formation of RNA-containing nuclear foci and altered RNA metabol
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::5306c4859c701afd627c3012165060cc
https://doi.org/10.1101/2023.03.05.531055
https://doi.org/10.1101/2023.03.05.531055
