Zobrazeno 1 - 10
of 24
pro vyhledávání: '"Junyi Jiao"'
Publikováno v:
Materials, Vol 14, Iss 23, p 7385 (2021)
Resistive pressure sensors are appealing due to having several advantages, such as simple reading mechanisms, simple construction, and quick dynamic response. Achieving a constantly changeable microstructure of sensing materials is critical for the f
Externí odkaz:
https://doaj.org/article/012de87997df4b78b87aed2c0bdd69b0
Autor:
Junyi Jiao, Mengze He, Sarah A Port, Richard W Baker, Yonggang Xu, Hong Qu, Yujian Xiong, Yukun Wang, Huaizhou Jin, Travis J Eisemann, Frederick M Hughson, Yongli Zhang
Publikováno v:
eLife, Vol 7 (2018)
Sec1/Munc18-family (SM) proteins are required for SNARE-mediated membrane fusion, but their mechanism(s) of action remain controversial. Using single-molecule force spectroscopy, we found that the SM protein Munc18-1 catalyzes step-wise zippering of
Externí odkaz:
https://doaj.org/article/2f2f2bb0b4e54e3b99b0352811480cc3
Autor:
Lu Ma, Yuhao Kang, Junyi Jiao, Aleksander A. Rebane, Hyo Keun Cha, Zhiqun Xi, Hong Qu, Yongli Zhang
Publikováno v:
Cell Reports, Vol 15, Iss 3, Pp 531-539 (2016)
Intracellular membrane fusion is mediated by dynamic assembly and disassembly of soluble N-ethylmaleimide-sensitive factor (NSF) attachment protein (SNAP) receptors (SNAREs). α-SNAP guides NSF to disassemble SNARE complexes after membrane fusion. Re
Externí odkaz:
https://doaj.org/article/4208b9f7419140b883c7f46f504fa162
Autor:
Lu Ma, Yiying Cai, Yanghui Li, Junyi Jiao, Zhenyong Wu, Ben O'Shaughnessy, Pietro De Camilli, Erdem Karatekin, Yongli Zhang
Publikováno v:
eLife, Vol 6 (2017)
Many biological processes rely on protein–membrane interactions in the presence of mechanical forces, yet high resolution methods to quantify such interactions are lacking. Here, we describe a single-molecule force spectroscopy approach to quantify
Externí odkaz:
https://doaj.org/article/75c12d0c80d841db8a169da342f90e2d
Autor:
Yu Lin, Jane J Long, Fang Huang, Whitney C Duim, Stefanie Kirschbaum, Yongdeng Zhang, Lena K Schroeder, Aleksander A Rebane, Mary Grace M Velasco, Alejandro Virrueta, Daniel W Moonan, Junyi Jiao, Sandy Y Hernandez, Yongli Zhang, Joerg Bewersdorf
Publikováno v:
PLoS ONE, Vol 10, Iss 5, p e0128135 (2015)
Single-molecule switching nanoscopy overcomes the diffraction limit of light by stochastically switching single fluorescent molecules on and off, and then localizing their positions individually. Recent advances in this technique have greatly acceler
Externí odkaz:
https://doaj.org/article/800b51504f3b4364919fe0c4049a6c05
Publikováno v:
Materials, Vol 14, Iss 7385, p 7385 (2021)
Materials; Volume 14; Issue 23; Pages: 7385
Materials
Materials; Volume 14; Issue 23; Pages: 7385
Materials
Resistive pressure sensors are appealing due to having several advantages, such as simple reading mechanisms, simple construction, and quick dynamic response. Achieving a constantly changeable microstructure of sensing materials is critical for the f
Autor:
Travis J Eisemann, Frederick M. Hughson, Junyi Jiao, Yonggang Xu, Yukun Wang, Yujian Xiong, Hong Qu, Sarah A. Port, Mengze He, Richard W. Baker, Yongli Zhang, Huaizhou Jin
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::0f01335a28c0bca196ebe0a40ca24c4e
https://doi.org/10.7554/elife.41771.053
https://doi.org/10.7554/elife.41771.053
Publikováno v:
Methods in Molecular Biology ISBN: 9781493987597
Intracellular membrane fusion mediates material and information exchange among different cells or cellular compartments with high accuracy and spatiotemporal resolution. Fusion is driven by ordered folding and assembly of soluble N-ethylmaleimide-sen
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::105c4a87ceb58425a7e8469360cb65dc
https://doi.org/10.1007/978-1-4939-8760-3_6
https://doi.org/10.1007/978-1-4939-8760-3_6
Autor:
Yanghui Li, Ben O'Shaughnessy, Erdem Karatekin, Lu Ma, Yiying Cai, Zhenyong Wu, Yongli Zhang, Junyi Jiao, Pietro De Camilli
Publikováno v:
eLife
eLife, Vol 6 (2017)
eLife, Vol 6 (2017)
Many biological processes rely on protein-membrane interactions in the presence of mechanical forces, yet high resolution methods to quantify such interactions are lacking. Here, we describe a single-molecule force spectroscopy approach to quantify m