Zobrazeno 1 - 10
of 15
pro vyhledávání: '"Yair, Gat"'
Publikováno v:
eLife, Vol 10 (2021)
The PI3K-related kinase (PIKK) SMG1 monitors the progression of metazoan nonsense-mediated mRNA decay (NMD) by phosphorylating the RNA helicase UPF1. Previous work has shown that the activity of SMG1 is impaired by small molecule inhibitors, is reduc
Externí odkaz:
https://doaj.org/article/7f597ec2a3aa4b7b9ddb0d4dcef86fd1
Publikováno v:
eLife, Vol 9 (2020)
PI3K-related kinases (PIKKs) are large Serine/Threonine (Ser/Thr)-protein kinases central to the regulation of many fundamental cellular processes. PIKK family member SMG1 orchestrates progression of an RNA quality control pathway, termed nonsense-me
Externí odkaz:
https://doaj.org/article/77c42d6d12404221a6fddbe50a007cf2
Autor:
Mahesh Lingaraju, Fabien Bonneau, Elisabeth Weyher, Yair Gat, Elena Conti, Jan M. Schuller, Michael A. Strauss, Peter J. Murray
Publikováno v:
Nature Structural & Molecular Biology. 26:1089-1093
We report the 3.45-A resolution cryo-EM structure of human SMG1-SMG8-SMG9, a phosphatidylinositol-3-kinase (PI(3)K)-related protein kinase (PIKK) complex central to messenger RNA surveillance. Structural and MS analyses reveal the presence of inosito
Publikováno v:
PLoS ONE, Vol 9, Iss 12, p e113431 (2014)
The widespread thioredoxin superfamily enzymes typically share the following features: a characteristic α-β fold, the presence of a Cys-X-X-Cys (or Cys-X-X-Ser) redox-active motif, and a proline in the cis configuration abutting the redox-active si
Externí odkaz:
https://doaj.org/article/c0f32cfc861947e4b10c75a8bc5fa614
Publikováno v:
eLife
eLife, Vol 9 (2020)
ELIFE
eLife, Vol 9 (2020)
ELIFE
PI3K-related kinases (PIKKs) are large Serine/Threonine (Ser/Thr)-protein kinases central to the regulation of many fundamental cellular processes. PIKK family member SMG1 orchestrates progression of an RNA quality control pathway, termed nonsense-me
Autor:
Gabriel Javitt, Ben Horowitz, Tal Ilani, Yair Gat, Frederic Bard, David Morgenstern, Deborah Fass
Publikováno v:
Glycobiology. 28:580-591
Quiescin sulfhydryl oxidase 1 (QSOX1) catalyzes the formation of disulfide bonds in protein substrates. Unlike other enzymes with related activities, which are commonly found in the endoplasmic reticulum, QSOX1 is localized to the Golgi apparatus or
Autor:
Yair, Gat, Jan Michael, Schuller, Mahesh, Lingaraju, Elisabeth, Weyher, Fabien, Bonneau, Mike, Strauss, Peter J, Murray, Elena, Conti
Publikováno v:
Nature structuralmolecular biology. 26(12)
We report the 3.45-Å resolution cryo-EM structure of human SMG1-SMG8-SMG9, a phosphatidylinositol-3-kinase (PI(3)K)-related protein kinase (PIKK) complex central to messenger RNA surveillance. Structural and MS analyses reveal the presence of inosit
Publikováno v:
FEBS Journal. 282:2746-2757
UNLABELLED The ~ 800 kDa laminin heterotrimer forms a distinctive cross-shaped structure that further self-assembles into networks within the extracellular matrix. The domains at the laminin chain termini, which engage in network formation and cell-s