Zobrazeno 1 - 10
of 28
pro vyhledávání: '"Priscilla S-W Yeung"'
Publikováno v:
eLife, Vol 12 (2023)
Ca2+ release-activated Ca2+ (CRAC) channels are activated by direct physical interactions between Orai1, the channel protein, and STIM1, the endoplasmic reticulum Ca2+ sensor. A hallmark of CRAC channels is fast Ca2+-dependent inactivation (CDI) whic
Externí odkaz:
https://doaj.org/article/cbd2b3496b3e40d2952ac2b73ceb4710
Publikováno v:
eLife, Vol 9 (2020)
Sulfur-aromatic interactions occur in the majority of protein structures, yet little is known about their functional roles in ion channels. Here, we describe a novel molecular motif, the M101 gate latch, which is essential for gating of human Orai1 c
Externí odkaz:
https://doaj.org/article/6c73ba37cc954bfc9aeac83928813135
Autor:
Priscilla S.-W. Yeung, Paige Miller, Tran Bao Lai-Nyugen, Phil Cheng, Amira Ibrahim, Run-Zhang Shi, Raffick A.R. Bowen, Ruben Yiqi Luo
Publikováno v:
Journal of Mass Spectrometry and Advances in the Clinical Lab. 28:99-104
Autor:
Megumi Yamashita, Priscilla S.-W. Yeung, Christopher E. Ing, Beth A. McNally, Régis Pomès, Murali Prakriya
Publikováno v:
Nature Communications, Vol 8, Iss 1, Pp 1-13 (2017)
Store-operated Ca2+channels (CRAC) are involved in several cellular functions. Here the authors identify a hydrophobic gate in the CRAC pore and show that CRAC activation by STIM1 involves rotation of the pore helix that hydrates this region to allow
Externí odkaz:
https://doaj.org/article/d822026f02ee422589e1d171ef62a857
Publikováno v:
eLife. 12
Ca2+ release-activated Ca2+ (CRAC) channels are activated by direct physical interactions between Orai1, the channel protein, and STIM1, the endoplasmic reticulum Ca2+ sensor. A hallmark of CRAC channels is fast Ca2+-dependent inactivation (CDI) whic
Autor:
Ruben Yiqi Luo, Christopher Pfaffroth, Samuel Yang, Kevin Hoang, Priscilla S.-W. Yeung, James L. Zehnder, Run-Zhang Shi
BackgroundCerebrospinal fluid (CSF) leak is typically diagnosed by detecting a protein marker β2-transferrin (β2-Tf) in secretion samples. β2-Tf and β1-transferrin (β1-Tf) are glycoforms of human transferrin (Tf). A novel affinity capture techni
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::4655ad0ce650bcb83dea401ef8682d86
https://doi.org/10.1101/2023.01.29.23285161
https://doi.org/10.1101/2023.01.29.23285161
Ca2+ release-activated Ca2+ (CRAC) channels are activated by direct physical interactions between Orai1, the channel protein, and STIM1, the endoplasmic reticulum Ca2+ sensor. A hallmark of CRAC channels is fast Ca2+-dependent inactivation (CDI) whic
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::0eb2bbd250b83c28a675bf7b7ab7e605
https://doi.org/10.1101/2022.08.12.503733
https://doi.org/10.1101/2022.08.12.503733
Autor:
Priscilla S.-W. Yeung, Hannah Wang, Mamdouh Sibai, Daniel Solis, Fumiko Yamamoto, Naomi Iwai, Becky Jiang, Nathan Hammond, Bernadette Truong, Selamawit Bihon, Suzette Santos, Marilyn Mar, Claire Mai, Kenji O. Mfuh, Jacob A. Miller, ChunHong Huang, Malaya K. Sahoo, James L. Zehnder, Benjamin A. Pinsky
Publikováno v:
Journal of Clinical Microbiology. 60
The ability to distinguish between severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) variants of concern (VOCs) is of ongoing interest due to differences in transmissibility, responses to vaccination, clinical prognosis, and therapy. Altho
Autor:
Priscilla S.-W. Yeung, Hannah Wang, Mamdouh Sibai, Daniel Solis, Fumiko Yamamoto, Naomi Iwai, Becky Jiang, Nathan Hammond, Bernadette Truong, Selamawit Bihon, Suzette Santos, Marilyn Mar, Claire Mai, Kenji O. Mfuh, Jacob A. Miller, ChunHong Huang, Malaya K. Sahoo, James L. Zehnder, Benjamin A. Pinsky
The ability to distinguish between SARS-CoV-2 variants of concern (VOCs) is of ongoing interest due to differences in transmissibility, response to vaccination, clinical prognosis, and therapy. Although detailed genetic characterization requires whol
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::cd5d5a60faf65d3d85780359b91e5f8f
https://doi.org/10.1101/2022.02.07.22270629
https://doi.org/10.1101/2022.02.07.22270629