Zobrazeno 1 - 10
of 107
pro vyhledávání: '"Arthur, Laganowsky"'
Autor:
Tianqi Zhang, Jixing Lyu, Bowei Yang, Sangho D. Yun, Elena Scott, Minglei Zhao, Arthur Laganowsky
Publikováno v:
Nature Communications, Vol 15, Iss 1, Pp 1-11 (2024)
Abstract The ATP-binding cassette (ABC) transporter, MsbA, plays a pivotal role in lipopolysaccharide (LPS) biogenesis by facilitating the transport of the LPS precursor lipooligosaccharide (LOS) from the cytoplasmic to the periplasmic leaflet of the
Externí odkaz:
https://doaj.org/article/dac16cdee011455f9552a010b74b86ba
Autor:
Lauren Stover, Hanieh Bahramimoghaddam, Lie Wang, Samantha Schrecke, Gaya P. Yadav, Ming Zhou, Arthur Laganowsky
Publikováno v:
Journal of Structural Biology: X, Vol 9, Iss , Pp 100097- (2024)
Aquaporin Z (AqpZ), a bacterial water channel, forms a tetrameric complex and, like many other membrane proteins, activity is regulated by lipids. Various methods have been developed to facilitate structure determination of membrane proteins, such as
Externí odkaz:
https://doaj.org/article/1d7cf849e1b042a19cb46fe7034bb63c
Publikováno v:
Nature Communications, Vol 15, Iss 1, Pp 1-11 (2024)
Abstract Pendrin (SLC26A4) is an anion exchanger that mediates bicarbonate (HCO3 −) exchange for chloride (Cl−) and is crucial for maintaining pH and salt homeostasis in the kidney, lung, and cochlea. Pendrin also exports iodide (I−) in the thy
Externí odkaz:
https://doaj.org/article/6d6b2df95fe74449afcfd24d0974d2dc
Autor:
Yun Zhu, Bo-Ji Peng, Smriti Kumar, Lauren Stover, Jing-Yuan Chang, Jixing Lyu, Tianqi Zhang, Samantha Schrecke, Djavdat Azizov, David H. Russell, Lei Fang, Arthur Laganowsky
Publikováno v:
Nature Communications, Vol 14, Iss 1, Pp 1-9 (2023)
Abstract Native mass spectrometry (MS) is a powerful technique for interrogating membrane protein complexes and their interactions with other molecules. A key aspect of the technique is the ability to preserve native-like structures and noncovalent i
Externí odkaz:
https://doaj.org/article/94436c1d1e2341babb198910d8bb6e06
Publikováno v:
eLife, Vol 12 (2024)
Structural and functional studies of the ATP-binding cassette transporter MsbA have revealed two distinct lipopolysaccharide (LPS) binding sites: one located in the central cavity and the other at a membrane-facing, exterior site. Although these bind
Externí odkaz:
https://doaj.org/article/0eb56b92ad4242ca82726eb840234084
Autor:
Jixing Lyu, Chang Liu, Tianqi Zhang, Samantha Schrecke, Nicklaus P. Elam, Charles Packianathan, Georg K. A. Hochberg, David Russell, Minglei Zhao, Arthur Laganowsky
Publikováno v:
Nature Communications, Vol 13, Iss 1, Pp 1-11 (2022)
The bacterial ABC transporter MsbA is essential for lipopolysaccharide biogenesis. Here, the authors apply native mass spectrometry, X-ray crystallography, cryo-EM and biochemical approaches to characterize the structural basis and functional roles o
Externí odkaz:
https://doaj.org/article/5e9d0f15449143aebe7c810597dff7e1
Autor:
Mia L. Abramsson, Cagla Sahin, Jonathan T. S. Hopper, Rui M. M. Branca, Jens Danielsson, Mingming Xu, Shane A. Chandler, Nicklas Österlund, Leopold L. Ilag, Axel Leppert, Joana Costeira-Paulo, Lisa Lang, Kaare Teilum, Arthur Laganowsky, Justin L. P. Benesch, Mikael Oliveberg, Carol V. Robinson, Erik G. Marklund, Timothy M. Allison, Jakob R. Winther, Michael Landreh
Publikováno v:
JACS Au, Vol 1, Iss 12, Pp 2385-2393 (2021)
Externí odkaz:
https://doaj.org/article/7f0e3b6cb2494cfdaa4cfb5acec6a09a
Autor:
Yaping Pan, Zhenning Ren, Shuai Gao, Jiemin Shen, Lie Wang, Zhichun Xu, Ye Yu, Preetham Bachina, Hanzhi Zhang, Xiao Fan, Arthur Laganowsky, Nieng Yan, Ming Zhou
Publikováno v:
Nature Communications, Vol 11, Iss 1, Pp 1-11 (2020)
Ferroportin is an iron exporter essential for releasing cellular iron into circulation and is inhibited by a peptide hormone, hepcidin. Here authors present cryo-EM structures of the ferroportin from the primate Philippine tarsier (TsFpn) with and wi
Externí odkaz:
https://doaj.org/article/77c24e64d4fc4521bced656e46273ab5
Autor:
Yang Liu, Catherine E. LoCaste, Wen Liu, Michael L. Poltash, David H. Russell, Arthur Laganowsky
Publikováno v:
Nature Communications, Vol 10, Iss 1, Pp 1-9 (2019)
G-protein-gated inward rectifying potassium channels (GIRKs) require Gβγ subunits and phosphorylated phosphatidylinositides (PIPs) for gating. Here authors use native ion mobility mass spectrometry to monitor small molecule binding events to GIRK2
Externí odkaz:
https://doaj.org/article/638c1f32d632456dae3b164c127d399b
Publikováno v:
Journal of the American Society for Mass Spectrometry. 34:790-793
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::a959154df0877df4ead66dce4210fb7d
https://doi.org/10.1021/jasms.2c00352
https://doi.org/10.1021/jasms.2c00352