Zobrazeno 1 - 10
of 30
pro vyhledávání: '"Simin, Rahighi"'
Autor:
Mikhail A. Hameedi, Erica T. Prates, Michael R. Garvin, Irimpan I. Mathews, B. Kirtley Amos, Omar Demerdash, Mark Bechthold, Mamta Iyer, Simin Rahighi, Daniel W. Kneller, Andrey Kovalevsky, Stephan Irle, Van-Quan Vuong, Julie C. Mitchell, Audrey Labbe, Stephanie Galanie, Soichi Wakatsuki, Daniel Jacobson
Publikováno v:
Nature Communications, Vol 13, Iss 1, Pp 1-15 (2022)
The authors report crystallographic and computational studies that detail how SARS-CoV-2 3CLpro cleaves the host NF-κB Essential Modulator in addition to its canonical viral substrates. The association with the high fitness of SARS-CoV-2 in humans i
Externí odkaz:
https://doaj.org/article/f4a60ed5420947fea700b6dd36aeb82f
Publikováno v:
Scientific Reports, Vol 12, Iss 1, Pp 1-9 (2022)
Abstract Ubiquitination of NEMO by the linear ubiquitin chain assembly complex (LUBAC) is essential for activating the canonical NF-κB signaling pathway. While the NZF1 domain of the HOIP subunit of LUBAC recognizes the NEMO substrate, it is unclear
Externí odkaz:
https://doaj.org/article/599646da50f341f790baf88f13792aec
Autor:
Sunhee Hwang, Karen Mruk, Simin Rahighi, Andrew G. Raub, Che-Hong Chen, Lisa E. Dorn, Naoki Horikoshi, Soichi Wakatsuki, James K. Chen, Daria Mochly-Rosen
Publikováno v:
Nature Communications, Vol 9, Iss 1, Pp 1-12 (2018)
Glucose-6-phosphate dehydrogenase (G6PD) deficiency provides insufficient protection from oxidative stress, contributing to diverse human pathologies. Here, the authors identify a small molecule that increases the activity and/or stability of mutant
Externí odkaz:
https://doaj.org/article/1d179241d985451cb9ca3ac72357b58a
Autor:
Nouf Alwadei, Mamunur Rashid, Devaraj Venkatapura Chandrashekar, Simin Rahighi, Jennifer Totonchy, Ajay Sharma, Reza Mehvar
Publikováno v:
International Journal of Molecular Sciences; Volume 24; Issue 9; Pages: 8121
The mechanisms of hepatic ischemia/reperfusion (I/R) injury, which occurs during liver transplantation or surgery, are poorly understood. The purpose of the current study was to generate and characterize a HepG2 cell line with a stable overexpression
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::51c0cb972c4cdaa772d5c1e48400a300
https://doi.org/10.3390/ijms24098121
https://doi.org/10.3390/ijms24098121
Autor:
Soichi Wakatsuki, Stephanie Galanie, B Kirtley Amos, Daniel Jacobson, Stephan Irle, Audrey Labbe, M. A. Hameedi, O. Demerdash, Michael R. Garvin, J. C. Mitchell, Irimpan I. Mathews, Daniel W. Kneller, Erica T. Prates, Van Quan Vuong, M. Iyer, Andrey Kovalevsky, Simin Rahighi, M. Bechthold
Publikováno v:
bioRxiv
article-version (status) pre
article-version (number) 1
article-version (status) pre
article-version (number) 1
In addition to its essential role in viral polyprotein processing, the SARS-CoV-2 3C-like (3CLpro) protease can cleave human immune signaling proteins, like NF-κB Essential Modulator (NEMO) and deregulate the host immune response. Here, in vitro ass
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::73757736e3cecd0aad8b635bcc8529d5
https://pubmed.ncbi.nlm.nih.gov/36075915
https://pubmed.ncbi.nlm.nih.gov/36075915
Autor:
Simin Rahighi, Lina Herhaus, Sean Tang, Innokentiy Maslennikov, Ivan Dikic, H. van den Bedem, Soichi Wakatsuki
Publikováno v:
Journal of Molecular Biology. 431:3146-3156
Although the Ub-binding domain in ABIN proteins and NEMO (UBAN) is highly conserved, UBAN-containing proteins exhibit different Ub-binding properties, resulting in their diverse biological roles. Post-translational modifications further control UBAN
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::33806c527e4361a483e0c0c1945082ab
https://doi.org/10.1016/j.jmb.2019.06.012
https://doi.org/10.1016/j.jmb.2019.06.012
Autor:
Mamta Iyer, Simin Rahighi
Publikováno v:
Acta Crystallographica Section A Foundations and Advances. 78:a275-a275
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::a0d5e578e87ab493c01bfe302bb837cd
https://doi.org/10.1107/s2053273322097248
https://doi.org/10.1107/s2053273322097248
Cyclic Peptides as Protein Kinase Inhibitors: Structure-Activity Relationship and Molecular Modeling
Autor:
Saghar Mozaffari, Samara E Hanna, Rakesh Tiwari, Michel F. Sanner, Simin Rahighi, Keykavous Parang, Khalid Zoghebi
Publikováno v:
J Chem Inf Model
Under-expression or over-expression of protein kinases has been shown to be associated with unregulated cell signal transduction in cancer cells. Therefore, there is a major interest in designing protein kinase inhibitors as anticancer agents. We hav
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1b58f25fcf8a58f8baf732453e55f572
https://europepmc.org/articles/PMC8238896/
https://europepmc.org/articles/PMC8238896/
Autor:
Adam Viegas, Khalid Zoghebi, Simin Rahighi, Keykavous Parang, Razan Orfali, Meng Cui, Young-Woo Nam, Misa Nguyen, Miao Zhang, Eman H M Mohammed
Publikováno v:
Acta Physiologica. 231
Aim Small-conductance Ca2+ -activated potassium (SK) channels are activated exclusively by increases in intracellular Ca2+ that binds to calmodulin constitutively associated with the channel. Wild-type SK2 channels are activated by Ca2+ with an EC50
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::3312b5fde71c7232d3183ccc03e127f3
https://doi.org/10.1111/apha.13552
https://doi.org/10.1111/apha.13552
Autor:
Young-Woo, Nam, Meng, Cui, Razan, Orfali, Adam, Viegas, Misa, Nguyen, Eman H M, Mohammed, Khalid A, Zoghebi, Simin, Rahighi, Keykavous, Parang, Miao, Zhang
Publikováno v:
Acta physiologica (Oxford, England). 231(1)
Small-conductance CaSite-directed mutagenesis, electrophysiological recordings and molecular dynamic (MD) simulations were utilized.Mutations that decrease hydrophobicity at the HA-S4-S5 interface lead to CaThe electrophysiological data and MD simula
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::f60cd66dabee2941bcc7afd96f7f2318
https://pubmed.ncbi.nlm.nih.gov/33119956
https://pubmed.ncbi.nlm.nih.gov/33119956