D. Minckler
Molecular Biology · 2018
A researcher in the Science corpus: 1 paper; trusts 9 researchers and is trusted by 0 researchers here, as inferred from the citation graph.
Subfields
- Molecular Biology — 18 citations into it
- Cellular and Molecular Neuroscience — 14 citations into it
- Neurology — 14 citations into it
- Epidemiology — 11 citations into it
- Developmental Neuroscience — 9 citations into it
- Cell Biology — 7 citations into it
Whom D. Minckler trusts overall
Their strongest outbound trust, strongest first, inferred from their citations.
- S. Oyadomari
- Masataka Mori
- X. Chen
- M. Sofroniew
- L. Hendershot
- Danzhi Huang
- H. Wässle
- Sidney S. Simon
- J. Sanes
Papers from D. Minckler's perspective
Ordered by how strongly the researchers D. Minckler trusts endorse each paper. Same corpus, a different order for every researcher.
- Activation of ATF6 and an ATF6 DNA binding site by the endoplasmic reticulum stress response. (Journal of Biological Chemistry)
- ER stress regulation of ATF6 localization by dissociation of BiP/GRP78 binding and unmasking of Golgi localization signals. (Developmental Cell)
- Roles of CHOP/GADD153 in endoplasmic reticulum stress (Cell Death and Differentiation)
- IRE1-mediated unconventional mRNA splicing and S2P-mediated ATF6 cleavage merge to regulate XBP1 in signaling the unfolded protein response. (Genes & Development)
- Plasma cell differentiation requires the transcription factor XBP-1 (Nature)
- Regulated translation initiation controls stress-induced gene expression in mammalian cells. (Molecules and Cells)
- ER stress induces cleavage of membrane-bound ATF6 by the same proteases that process SREBPs. (Molecules and Cells)
- XBP1 mRNA is induced by ATF6 and spliced by IRE1 in response to ER stress to produce a highly active transcription factor. (Cell)
- Intracellular signaling from the endoplasmic reticulum to the nucleus: the unfolded protein response in yeast and mammals. (Current Opinion in Cell Biology)
- Coupling of stress in the ER to activation of JNK protein kinases by transmembrane protein kinase IRE1. (Science)
Their papers
- Glaucoma (2018) — 905 citations