UPR, autophagy, and mitochondria crosstalk underlies the ER stress response is a research paper published in Trends in Biochemical Sciences (2015). On theSindex it has a DataRank of 1.1. It has been cited 1,134 times.
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Base Score Contribution
1.1
From this paper's citation signal
Citation Network Contribution
0
Citation network not refreshed for this result
This paper's DataRank is currently driven only by its base citation score. Citation network data was not refreshed for this result.
Learn more about DataRank methodology →NCI NIH HHS
Grant: CA128814
NCI NIH HHS
Grant: P01 CA128814
NCI NIH HHS
Grant: P30 CA030199
FWCI
31.42
Citation Percentile
1.0%
Citation Trend
Fields of Study
MeSH Terms
Keywords
Sustainable Development Goals
Additional file 1 of PERK/NRF2 and autophagy form a resistance mechanism against G9a inhibition in leukemia stem cells
Additional file 1 of PERK/NRF2 and autophagy form a resistance mechanism against G9a inhibition in leukemia stem cells
Additional file 1 of Inhibition of ERAD synergizes with FTS to eradicate pancreatic cancer cells
Additional file 1 of Inhibition of ERAD synergizes with FTS to eradicate pancreatic cancer cells
Additional file 1 of rt269L-Type hepatitis B virus (HBV) in genotype C infection leads to improved mitochondrial dynamics via the PERK–eIF2α–ATF4 axis in an HBx protein-dependent manner
Additional file 1 of rt269L-Type hepatitis B virus (HBV) in genotype C infection leads to improved mitochondrial dynamics via the PERK–eIF2α–ATF4 axis in an HBx protein-dependent manner
Additional file 2 of rt269L-Type hepatitis B virus (HBV) in genotype C infection leads to improved mitochondrial dynamics via the PERK–eIF2α–ATF4 axis in an HBx protein-dependent manner
Additional file 2 of rt269L-Type hepatitis B virus (HBV) in genotype C infection leads to improved mitochondrial dynamics via the PERK–eIF2α–ATF4 axis in an HBx protein-dependent manner
Additional file 3 of rt269L-Type hepatitis B virus (HBV) in genotype C infection leads to improved mitochondrial dynamics via the PERK–eIF2α–ATF4 axis in an HBx protein-dependent manner
Additional file 4 of rt269L-Type hepatitis B virus (HBV) in genotype C infection leads to improved mitochondrial dynamics via the PERK–eIF2α–ATF4 axis in an HBx protein-dependent manner
Additional file 3 of rt269L-Type hepatitis B virus (HBV) in genotype C infection leads to improved mitochondrial dynamics via the PERK–eIF2α–ATF4 axis in an HBx protein-dependent manner
Additional file 4 of rt269L-Type hepatitis B virus (HBV) in genotype C infection leads to improved mitochondrial dynamics via the PERK–eIF2α–ATF4 axis in an HBx protein-dependent manner
Additional file 5 of rt269L-Type hepatitis B virus (HBV) in genotype C infection leads to improved mitochondrial dynamics via the PERK–eIF2α–ATF4 axis in an HBx protein-dependent manner
Additional file 5 of rt269L-Type hepatitis B virus (HBV) in genotype C infection leads to improved mitochondrial dynamics via the PERK–eIF2α–ATF4 axis in an HBx protein-dependent manner
Additional file 6 of rt269L-Type hepatitis B virus (HBV) in genotype C infection leads to improved mitochondrial dynamics via the PERK–eIF2α–ATF4 axis in an HBx protein-dependent manner
Additional file 6 of rt269L-Type hepatitis B virus (HBV) in genotype C infection leads to improved mitochondrial dynamics via the PERK–eIF2α–ATF4 axis in an HBx protein-dependent manner
Additional file 7 of rt269L-Type hepatitis B virus (HBV) in genotype C infection leads to improved mitochondrial dynamics via the PERK–eIF2α–ATF4 axis in an HBx protein-dependent manner
Additional file 7 of rt269L-Type hepatitis B virus (HBV) in genotype C infection leads to improved mitochondrial dynamics via the PERK–eIF2α–ATF4 axis in an HBx protein-dependent manner
Additional file 8 of rt269L-Type hepatitis B virus (HBV) in genotype C infection leads to improved mitochondrial dynamics via the PERK–eIF2α–ATF4 axis in an HBx protein-dependent manner
Additional file 8 of rt269L-Type hepatitis B virus (HBV) in genotype C infection leads to improved mitochondrial dynamics via the PERK–eIF2α–ATF4 axis in an HBx protein-dependent manner