XBP1 controls diverse cell type- and condition-specific transcriptional regulatory networks.
By D. Acosta-Alvear, Yiming Zhou, A. Blais, M. Tsikitis, Nathan H. Lents, C. Arias, Christen J. Lennon, Yuval Kluger, B. Dynlacht. Molecules and Cells, 2007
842 citations recorded by the source corpus.
Subfields: Biotechnology, Cell Biology, Pollution
View Paper: https://www.semanticscholar.org/paper/74507da083365962cae358a217ffa04132ac9670
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In Biotechnology
- C. Hetz
- Shiyu Wang
- Laurie H. Glimcher
- Ann-Hwee Lee
- J. Cubillos-Ruiz
- R. Kaufman
- F. Papa
- Sarah Bettigole
In Cell Biology
- C. Hetz
- R. Kaufman
- G. Hotamışlıgil
- F. Papa
- Laurie H. Glimcher
- J. Cubillos-Ruiz
- Sarah Bettigole
- Shiyu Wang
In Pollution
Citations in the corpus
- The impact of the unfolded protein response on human disease (2012, background): “Spliced Xbp1 mRNA is translated into a potent transcription factor, XBP1s, which targets a wide variety of genes encoding proteins involved in ER membrane biogenesis, ER protein folding, ERAD, and protein secretion from the cell (Lee et al., 2003; Acosta-Alvear et al., 2007).”
- ER Stress Sensor XBP1 Controls Anti-tumor Immunity by Disrupting Dendritic Cell Homeostasis (2015, positive): “Further, marked upregulation of canonical XBP1 target genes ERdj4 and Sec61a1 (Acosta-Alvear et al., 2007; Lee et al., 2003b) (Figure 1D) and general ER stress response markers Hspa5 (BiP) and Ddit3”
- Endoplasmic Reticulum Stress and the Inflammatory Basis of Metabolic Disease (2010, positive): “For example, genes involved in glucose output and glycogen synthesis such as glycogen synthase 1 are targets of XBP1 (Acosta-Alvear et al., 2007; Lee et al., 2008).”
- ER stress: Autophagy induction, inhibition and selection (2015, background): “The encoded XBP1 protein subsequently translocates to the nucleus where it acts as a potent transcription factor by binding to UPR elements and activating a broad spectrum of UPR-related genes involved in ER membrane biogenesis, ER protein folding, physical expansion of the ER, ERAD, protein entry i”
- A multiplexed single-cell CRISPR screening platform enables systematic dissection of the unfolded protein response (2016, positive): “As expected from previous work (Acosta-Alvear et al., 2007; Han et al., 2013; Lee et al., 2003; Shoulders et al., 2013), epistasis analysis using combinatorial depletions of PERK, ATF6, and IRE1α revealed both distinct and overlapping programs of gene expression.”
- The unfolded protein response: controlling cell fate decisions under ER stress and beyond (2012, background): “This results in the expression of an active and stable transcription factor, termed spliced XBP1 (XBP1s), which translocates to the nucleus to induce the upregulation of its target genes, the protein products of which operate in ER-associated degradation ( ERAD ), the entry of proteins into the ER a”
- Pseudo-temporal ordering of individual cells reveals dynamics and regulators of cell fate decisions (2014, background): “XBP1 was recently reported to inhibit myoblast differentiation in mice, potentially through the mechanisms proposed here 24 .”
- The endoplasmic reticulum stress response in immunity and autoimmunity (2008, background): “In this regard, XBP1 has been linked to myodegenerative disorders, perhaps through a direct activation of the transcriptional regulator Mist1 (Ref”
- XBP1 links ER stress to intestinal inflammation and confers genetic risk for human inflammatory bowel disease (2008, positive): “XBP1s directs transcription of a core group of genes involved in constitutive maintenance of ER function in all cell types, and a remarkably diverse set of tissue- and condition-specific targets (Acosta-Alvear et al., 2007; Lee et al., 2003b; Shaffer et al., 2004).”
- The Unfolded Protein Response and Cell Fate Control. (2017, positive): “XBP1 controls maturation of gastric zymogenic cells by induction of MIST1 and expansion of the rough endoplasmic reticulum.”