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Frontiers in Microbiology, ISSN 1664-302X, 2014, Volume 5, p. 388
Endoplasmic reticulum (ER) stress is a general term for representing the pathway by which various stimuli affect ER functions. ER stress induces the... 
ER stress | Enterovirus 71 | ATF6 | IRE1 | EIF2a | Unfolded protein response | eIF2 alpha | EIF2-ALPHA KINASE | HEPATITIS-C-VIRUS | MICROBIOLOGY | TRANSLATION INITIATION | ENDOPLASMIC-RETICULUM STRESS | ENVELOPE PROTEINS | CELL-DEATH | unfolded protein response | MESSENGER-RNA | JAPANESE ENCEPHALITIS-VIRUS | enterovirus 71 | MOLECULAR-MECHANISMS | eIF2α | er stress
Journal Article
by Kepp, Oliver and Senovilla, Laura and Vitale, Ilio and Vacchelli, Erika and Adjemian, Sandy and Agostinis, Patrizia and Apetoh, Lionel and Aranda, Fernando and Barnaba, Vincenzo and Bloy, Norma and Bracci, Laura and Breckpot, Karine and Brough, David and Buqué, Aitziber and Castro, Maria G and Cirone, Mara and Colombo, Maria I and Cremer, Isabelle and Demaria, Sandra and Dini, Luciana and Eliopoulos, Aristides G and Faggioni, Alberto and Formenti, Silvia C and Fučíková, Jitka and Gabriele, Lucia and Gaipl, Udo S and Galon, Jérôme and Garg, Abhishek and Ghiringhelli, François and Giese, Nathalia A and Guo, Zong Sheng and Hemminki, Akseli and Herrmann, Martin and Hodge, James W and Holdenrieder, Stefan and Honeychurch, Jamie and Hu, Hong-Min and Huang, Xing and Illidge, Tim M and Kono, Koji and Korbelik, Mladen and Krysko, Dmitri V and Loi, Sherene and Lowenstein, Pedro R and Lugli, Enrico and Ma, Yuting and Madeo, Frank and Manfredi, Angelo A and Martins, Isabelle and Mavilio, Domenico and Menger, Laurie and Merendino, Nicolò and Michaud, Michael and Mignot, Gregoire and Mossman, Karen L and Multhoff, Gabriele and Oehler, Rudolf and Palombo, Fabio and Panaretakis, Theocharis and Pol, Jonathan and Proietti, Enrico and Ricci, Jean-Ehrland and Riganti, Chiara and Rovere-Querini, Patrizia and Rubartelli, Anna and Sistigu, Antonella and Smyth, Mark J and Sonnemann, Juergen and Spisek, Radek and Stagg, John and Sukkurwala, Abdul Qader and Tartour, Eric and Thorburn, Andrew and Thorne, Stephen H and Vandenabeele, Peter and Velotti, Francesca and Workenhe, Samuel T and Yang, Haining and Zong, Wei-Xing and Zitvogel, Laurence and Kroemer, Guido and Galluzzi, Lorenzo
OncoImmunology, ISSN 2162-4011, 09/2014, Volume 3, Issue 9, p. e955691
Apoptotic cells have long been considered as intrinsically tolerogenic or unable to elicit immune responses specific for dead cell-associated antigens.... 
TLR, Toll-like receptor | ATF6, activating transcription factor 6 | HMGB1 | EIF2A, eukaryotic translation initiation factor 2A | H2B, histone 2B | endoplasmic reticulum stress | HMGB1, high mobility group box 1 | APC, antigen-presenting cell | ATP release | immunotherapy | BCL2, B-cell CLL/lymphoma 2 protein | mitochondrial transmembrane potential | DiOC | MOMP, mitochondrial outer membrane permeabilization | RFP, red fluorescent protein | HSV-1, herpes simplex virus type I | ICD, immunogenic cell death | IFN, interferon | XBP1, X-box binding protein 1 | GFP, green fluorescent protein | autophagy | DAMP, damage-associated molecular pattern | PI, propidium iodide | G3BP1, GTPase activating protein (SH3 domain) binding protein 1 | PDIA3, protein disulfide isomerase family A | member 3 | DAPI, 4′,6-diamidino-2-phenylindole | FLT3LG, fms-related tyrosine kinase 3 ligand | BAX, BCL2-associated X protein | CALR, calreticulin | 3,3′-dihexyloxacarbocyanine iodide | CTL, cytotoxic T lymphocyte | IL, interleukin | calreticulin | HSP, heat shock protein | ER, endoplasmic reticulum | BAK1, BCL2-antagonist/killer 1 | Calreticulin | Autophagy | Immunotherapy | Endoplasmic reticulum stress | FLOW-CYTOMETRIC DETECTION | TUMOR-CELLS | IMMUNOLOGY | MOLECULAR-PATTERN | CALRETICULIN EXPOSURE | MITOCHONDRIAL-MEMBRANE PERMEABILIZATION | HEAT-SHOCK PROTEINS | ONCOLOGY | IMMUNE-RESPONSES | APOPTOTIC CELLS | FIND-ME SIGNAL
Journal Article
Biological Trace Element Research, ISSN 0163-4984, 4/2017, Volume 176, Issue 2, pp. 278 - 293
Journal Article
Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 01/2002, Volume 99, Issue 1, pp. 190 - 195
The eIF2α kinases are a family of evolutionarily conserved serine/threonine kinases that regulate stress-induced translational arrest. Here, we demonstrate... 
YEAST | LEGIONELLA-PNEUMOPHILA | MUTANTS | INITIATION FACTOR-2-ALPHA | PROTEIN-KINASE | MULTIDISCIPLINARY SCIENCES | MAMMALIAN HOMOLOG | DEGRADATION | ENDOPLASMIC-RETICULUM | SACCHAROMYCES-CEREVISIAE | TRANSLATIONAL CONTROL | GCN2 gene | eIF2a kinase | GCN4 gene | ICP34.5 protein | Biological Sciences
Journal Article
by Kim, E and Kim, JH and Seo, K and Hong, KY and An, SWA and Kwon, J and Lee, SJV and Jang, SK
CELLULAR AND MOLECULAR LIFE SCIENCES, ISSN 1420-682X, 12/2018, Volume 75, Issue 23, pp. 4287 - 4300
The initiator tRNA (Met-tRNA(i)(Met)) at the P site of the small ribosomal subunit plays an important role in the recognition of an mRNA start codon. In... 
eIF2A | FACTOR 5B | BIOCHEMISTRY & MOLECULAR BIOLOGY | Translation initiation | GUANINE-NUCLEOTIDE EXCHANGE | PROTEIN-SYNTHESIS | CELL BIOLOGY | EUKARYOTIC TRANSLATION INITIATION | COMPLEX-FORMATION | STRESS CONDITIONS | Evolution of initiator tRNA carriers | MESSENGER-RNA | FACTOR IF2 | FACTOR 2A | eIF5B | SUBUNIT | Genetic translation | Codon | Transfer RNA
Journal Article
Autophagy, ISSN 1554-8627, 05/2015, Volume 11, Issue 5, pp. 729 - 739
Autophagy is an evolutionarily conserved process in eukaryotes that eliminates harmful components and maintains cellular homeostasis in response to a series of... 
ATF4, activating transcription factor 4 | HIF1A, hypoxia inducible factor 1, α subunit (basic helix-loop-helix transcription factor) | HDAC3, histone deacetylase 3 | XPO1, exportin 1 | EGF, epidermal growth factor | MAP1LC3A, microtubule-associated protein 1 light chain 3 α | LMP, lysosomal membrane permeabilization | COX8, cytochrome c oxidase subunit VIII | MMP14, matrix metallopeptidase 14 (membrane-inserted) | MLS, mitochondrial localization sequence | EIF2AK2, eukaryotic translation initiation factor 2-α kinase 2 | CuB, cucurbitacin B | autophagy | IMM, inner mitochondrial membrane | CTSL, cathepsin L | IL6, interleukin 6 | miRNA, microRNA | CTSB, cathepsin B | PDGFRB, platelet-derived growth factor receptor, β polypeptide | receptor tyrosine kinases | RTK, receptor tyrosine kinases | PTPN2, protein tyrosine phosphatase, non-receptor type 2 | CNTF, ciliary neurotrophic factor | MAPK1, mitogen-activated protein kinase 1 | ALK, anaplastic lymphoma receptor tyrosine kinase | NES, nuclear export signal | EIF2A, eukaryotic initiation factor 2A, 65kDa | NDUFA13, NADH dehydrogenase (ubiquinone) 1 α subcomplex, 13 | VHL, von Hippel-Lindau tumor suppressor, E3 ubiquitin protein ligase | PTPN6, protein tyrosine phosphatase, non-receptor type 6 | ROS, reactive oxygen species | ETC, electron transport chain | SH2, src homology 2 | targeted therapy | PRKAA2, protein kinase, AMP-activated, α 2 catalytic subunit | STAT3 | BNIP3, BCL2/adenovirus E1B 19kDa interacting protein 3 | NFKB1, nuclear factor of kappa light polypeptide gene enhancer in B-cells 1 | STAT3, signal transducer and activator of transcription 3 (acute-phase response factor) | NLS, nuclear localization signal | FOXO1/3, forkhead box O1/3 | mitoSTAT3, mitochondrial STAT3 | mitophagy | PTPN11, protein tyrosine phosphatase, non-receptor type 11 | KDR, kinase insert domain receptor | cancer | ConA, concanavalin A | CYCS, cytochrome c, somatic | ER, endoplasmic reticulum | Mitophagy | Targeted therapy | Autophagy | Receptor tyrosine kinases | Cancer | CANCER-CELLS | TRANSCRIPTION FACTORS | HEPATOCELLULAR-CARCINOMA CELLS | TYROSINE PHOSPHORYLATION | SERINE PHOSPHORYLATION | CELL BIOLOGY | ELECTRON-TRANSPORT CHAIN | JAK/STAT PATHWAY | MITOCHONDRIAL STAT3 | IN-VIVO | SIGNAL TRANSDUCER | Neoplasms - metabolism | Neoplasms - therapy | Animals | Models, Biological | Humans | Mitochondria - metabolism | STAT3 Transcription Factor - chemistry | Subcellular Fractions - metabolism | STAT3 Transcription Factor - metabolism
Journal Article
Oncotarget, ISSN 1949-2553, 05/2016, Volume 7, Issue 21, pp. 29877 - 29878
Journal Article
BMC Cancer, ISSN 1471-2407, 11/2015, Volume 15, Issue 1, p. 855
Journal Article