Zobrazeno 1 - 10
of 14
pro vyhledávání: '"Diessel Duan"'
Structural insight into an Arl1–ArfGEF complex involved in Golgi recruitment of a GRIP-domain golgin
Publikováno v:
Nature Communications, Vol 15, Iss 1, Pp 1-13 (2024)
Abstract Arl1 is an Arf-like (Arl) GTP-binding protein that interacts with the guanine nucleotide exchange factor Gea2 to recruit the golgin Imh1 to the Golgi. The Arl1–Gea2 complex also binds and activates the phosphatidylserine flippase Drs2 and
Externí odkaz:
https://doaj.org/article/031bc3b3bd5040bc88b7924b1b607fba
Autor:
Lin Bai, Bhawik K. Jain, Qinglong You, H. Diessel Duan, Mehmet Takar, Todd R. Graham, Huilin Li
Publikováno v:
Nature Communications, Vol 12, Iss 1, Pp 1-12 (2021)
The P4 ATPase lipid flippases play a crucial role in membrane biogenesis. Here the authors report the structure of the monomeric P4B ATPase Neo1 in several states, clarifying the mechanism of substrate transport.
Externí odkaz:
https://doaj.org/article/e2d2a137d08148738412fa8e65ace57a
Autor:
Lin Bai, Qinglong You, Bhawik K Jain, H Diessel Duan, Amanda Kovach, Todd R Graham, Huilin Li
Publikováno v:
eLife, Vol 9 (2020)
The P4 ATPases use ATP hydrolysis to transport large lipid substrates across lipid bilayers. The structures of the endosome- and Golgi-localized phosphatidylserine flippases—such as the yeast Drs2 and human ATP8A1—have recently been reported. How
Externí odkaz:
https://doaj.org/article/acb9322c1c9c48e8a853633cc50a4eed
Publikováno v:
J Biol Chem
A remarkable charge transfer (CT) band is described in the bifurcating electron transfer flavoprotein (Bf-ETF) from Rhodopseudomonas palustris (RpaETF). RpaETF contains two FADs that play contrasting roles in electron bifurcation. The Bf-FAD accepts
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::71a704a902fc490e4f6c3224e1099b1c
https://doi.org/10.1074/jbc.ra120.013174
https://doi.org/10.1074/jbc.ra120.013174
Autor:
H. Diessel Duan, Lin Bai, Huilin Li, Mehmet Takar, Todd R. Graham, Qinglong You, Bhawik Kumar Jain
Publikováno v:
Nature Communications
Nature Communications, Vol 12, Iss 1, Pp 1-12 (2021)
Nature Communications, Vol 12, Iss 1, Pp 1-12 (2021)
P4 ATPases are lipid flippases that are phylogenetically grouped into P4A, P4B and P4C clades. The P4A ATPases are heterodimers composed of a catalytic α-subunit and accessory β-subunit, and the structures of several heterodimeric flippases have be
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::fe461fb21a64153dfde9dc32b38fbb1d
https://doi.org/10.1038/s41467-021-26273-0
https://doi.org/10.1038/s41467-021-26273-0
Autor:
Anne-Frances Miller, Nishya Mohamed-Raseek, Debarati Das, H. Diessel Duan, María González Viegas, Maria-Andrea Mroginski
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Bioenergetics. 1863:148603
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::f3bebb32186d1f71d5bce50de38e1cb8
https://doi.org/10.1016/j.bbabio.2022.148603
https://doi.org/10.1016/j.bbabio.2022.148603
Autor:
Sam Chasen, Diessel Duan, Marisa Gilliam, Rajiv K. Kar, Sharique A. Khan, Anne-Frances Miller, Dallas Bell, Nishya Mohamed-Raseek, Taylor A. Varner
Publikováno v:
The FASEB Journal. 35
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::0fd79c1232bf0f77ceeb4623e5750959
https://doi.org/10.1096/fasebj.2021.35.s1.04129
https://doi.org/10.1096/fasebj.2021.35.s1.04129
P4 ATPases are lipid flippases that are phylogenetically grouped into P4A, P4B and P4C clades. The P4A ATPases are heterodimers composed of a catalytic α-subunit and accessory β-subunit, and the structures of several heterodimeric flippases have be
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::0a5a86328902a7357ea348631b945d68
https://doi.org/10.1101/2021.04.28.441804
https://doi.org/10.1101/2021.04.28.441804
Autor:
Amanda Kovach, Qinglong You, Huilin Li, Todd R. Graham, Lin Bai, Bhawik Kumar Jain, H. Diessel Duan
Publikováno v:
eLife, Vol 9 (2020)
eLife
eLife
The P4 ATPases use ATP hydrolysis to transport large lipid substrates across lipid bilayers. The structures of the endosome- and Golgi-localized phosphatidylserine flippases—such as the yeast Drs2 and human ATP8A1—have recently been reported. How
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3b88e1e9bd85f22b9f67c38dcbb236e8
https://doi.org/10.7554/elife.62163
https://doi.org/10.7554/elife.62163