Zobrazeno 1 - 6
of 6
pro vyhledávání: '"Nnejiuwa U Ibe"'
Autor:
Mark T Lek, Siobanth Cruz, Nnejiuwa U Ibe, Wendy H J Beck, John K Bielicki, Paul M M Weers, Vasanthy Narayanaswami
Publikováno v:
PLoS ONE, Vol 12, Iss 6, p e0178346 (2017)
Apolipoprotein (apo) E3 and apoAI are exchangeable apolipoproteins that play a dominant role in regulating plasma lipoprotein metabolism. ApoE3 (299 residues) is composed of an N-terminal (NT) domain bearing a 4-helix bundle and a C-terminal (CT) dom
Externí odkaz:
https://doaj.org/article/13ed6acafcff45beb0d1ed062e7adf06
Autor:
Yuhui Wang, Hai P. Nguyen, Pengya Xue, Ying Xie, Danielle Yi, Frances Lin, Jennie Dinh, Jose A. Viscarra, Nnejiuwa U. Ibe, Robin E. Duncan, Hei S. Sul
Publikováno v:
Nature Communications, Vol 15, Iss 1, Pp 1-17 (2024)
Abstract Adipose tissue stores triacylglycerol (TAG) in lipid droplets (LD) and release fatty acids upon lipolysis during energy shortage. We identify ApoL6 as a LD-associated protein mainly found in adipose tissue, specifically in adipocytes. ApoL6
Externí odkaz:
https://doaj.org/article/9727d0e5ed68427b834ee202e32bb804
Autor:
Yuhui Wang, Hai P Nguyen, Pengya Xue, Ying Xie, Danielle Yi, Frances Lin, Jose A Viscarra, Nnejiuwa U Ibe, Robin E Duncan, Hei Sook Sul
ApoL6 is a new LD-associated protein containing an apoprotein-like domain, expressed mainly in adipose tissue, specifically in adipocytes. ApoL6 expression is low in fasting but induced upon feeding. ApoL6 knockdown results in smaller LD with lower t
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::2e363904ebcd002e143eafb449db377f
https://doi.org/10.1101/2022.11.10.516022
https://doi.org/10.1101/2022.11.10.516022
Autor:
Nnejiuwa U Ibe, Shaeri Mukherjee
The intracellular bacterial pathogenLegionella pneumophila(L.p.) secretes ~330 effector proteins into the host cell to sculpt an Endoplasmic Reticulum (ER)-derived replicative niche. We previously reported fiveL.p.effectors that inhibit IRE1, a key s
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::da5957487b77548834fb639766b238d8
https://doi.org/10.1101/2020.06.26.174185
https://doi.org/10.1101/2020.06.26.174185
Publikováno v:
Life science alliance, vol 4, iss 12
Life Science Alliance
Life Science Alliance
Legionella pneumophila secretes toxins into the host cell that induce the non-canonical processing and activation of the ER stress sensor and transcription factor ATF6 via a mechanism that is distinct from the canonical pathway activated by unfolded
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::fac889bc41aa36625210f0e97ebd8e52
https://doi.org/10.26508/lsa.202101247
https://doi.org/10.26508/lsa.202101247
Autor:
Edwin E. Jeng, Haley Gause, Michael C. Bassik, Ruiqi Jian, Lihua Jiang, Nevan J. Krogan, Erica Stevenson, Danielle L. Swaney, Michael Snyder, Nnejiuwa U Ibe, Shaeri Mukherjee, David Jimenez-Morales, Varun Bhadkamkar, Joanne Chan
Publikováno v:
Cell Host Microbe
During infection, Legionella pneumophila translocates over 300 effector proteins into the host cytosol, allowing the pathogen to establish an endoplasmic reticulum (ER)-like Legionella-containing vacuole (LCV) that supports bacterial replication. Her
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::cbf9bb4e92f88cb5e6610b654c325f1f
https://pubmed.ncbi.nlm.nih.gov/31540829
https://pubmed.ncbi.nlm.nih.gov/31540829