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by Klionsky, Daniel J and Abdalla, Fabio C and Abeliovich, Hagai and Abraham, Robert T and Acevedo-Arozena, Abraham and Adeli, Khosrow and Agholme, Lotta and Agnello, Maria and Agostinis, Patrizia and Aguirre-Ghiso, Julio A and Ahn, Hyung Jun and Ait-Mohamed, Ouardia and Ait-Si-Ali, Slimane and Akematsu, Takahiko and Akira, Shizuo and Al-Younes, Hesham M and Al-Zeer, Munir A and Albert, Matthew L and Albin, Roger L and Alegre-Abarrategui, Javier and Aleo, Maria Francesca and Alirezaei, Mehrdad and Almasan, Alexandru and Almonte-Becerril, Maylin and Amano, Atsuo and Amaravadi, Ravi K and Amarnath, Shoba and Amer, Amal O and Andrieu-Abadie, Nathalie and Anantharam, Vellareddy and Ann, David K and Anoopkumar-Dukie, Shailendra and Aoki, Hiroshi and Apostolova, Nadezda and Arancia, Giuseppe and Aris, John P and Asanuma, Katsuhiko and Asare, Nana Y.O and Ashida, Hisashi and Askanas, Valerie and Askew, David S and Auberger, Patrick and Baba, Misuzu and Backues, Steven K and Baehrecke, Eric H and Bahr, Ben A and Bai, Xue-Yuan and Bailly, Yannick and Baiocchi, Robert and Baldini, Giulia and Balduini, Walter and Ballabio, Andrea and Bamber, Bruce A and Bampton, Edward T.W and Juhász, Gábor and Bartholomew, Clinton R and Bassham, Diane C and Bast, Robert C and Batoko, Henri and Bay, Boon-Huat and Beau, Isabelle and Béchet, Daniel M and Begley, Thomas J and Behl, Christian and Behrends, Christian and Bekri, Soumeya and Bellaire, Bryan and Bendall, Linda J and Benetti, Luca and Berliocchi, Laura and Bernardi, Henri and Bernassola, Francesca and Besteiro, Sébastien and Bhatia-Kissova, Ingrid and Bi, Xiaoning and Biard-Piechaczyk, Martine and Blum, Janice S and Boise, Lawrence H and Bonaldo, Paolo and Boone, David L and Bornhauser, Beat C and Bortoluci, Karina R and Bossis, Ioannis and Bost, Frédéric and Bourquin, Jean-Pierre and Boya, Patricia and Boyer-Guittaut, Michaël and Bozhkov, Peter V and Brady, Nathan R and Brancolini, Claudio and Brech, Andreas and Brenman, Jay E and Brennand, Ana and Bresnick, Emery H and Brest, Patrick and Bridges, Dave and Bristol, Molly L and Brookes, Paul S and Brown, Eric J and Brumell, John H and ... and Linköpings universitet and Institutionen för klinisk och experimentell medicin and Geriatrik and Institutionen för medicin och hälsa and Farmakologi and Experimentell patologi and Hälsouniversitetet and Cellbiologi
Autophagy, ISSN 1554-8627, 04/2012, Volume 8, Issue 4, pp. 445 - 544
Journal Article
NATURE COMMUNICATIONS, ISSN 2041-1723, 04/2019, Volume 10, Issue 1, pp. 1729 - 16
RIPK1 regulates cell death and inflammation through kinase-dependent and -independent mechanisms. As a scaffold, RIPK1 inhibits caspase-8-dependent apoptosis... 
APOPTOSIS | COMPLEX | ACTIVATION | NECROPTOSIS | NECROSIS | DOMAIN KINASE | PATHWAY | MULTIDISCIPLINARY SCIENCES | OUTER PROTEIN-P | NF-KAPPA-B | BETA | Molecular machines | Cell culture | Phosphorylation | Phenotypes | Animal models | Cell survival | TAK1 protein | Serine | Mortality | Caspase | Cytotoxicity | Inflammation | Infections | Kinases | Mimicry | Caspase-8 | Tumor necrosis factor | Cell death | Mice | Inhibition | Mutation | Apoptosis
Journal Article
Nature Cell Biology, ISSN 1465-7392, 09/2017, Volume 19, Issue 10, pp. 1248 - 1259
Receptor-interacting protein kinase-1 (RIPK1), a master regulator of cell fate decisions, was identified as a direct substrate of MAPKAP kinase-2 (MK2) by... 
Receptor-Interacting Protein Serine-Threonine Kinases - metabolism | Inflammation - pathology | Protein-Serine-Threonine Kinases - deficiency | Phosphorylation | Apoptosis - drug effects | Humans | Serine | Yersinia Infections - enzymology | Male | Intracellular Signaling Peptides and Proteins - metabolism | Receptors, Tumor Necrosis Factor, Type I - metabolism | Necrosis | Intracellular Signaling Peptides and Proteins - deficiency | Cytosol - enzymology | Transfection | I-kappa B Kinase - metabolism | Time Factors | HEK293 Cells | Female | Membrane Proteins - metabolism | p38 Mitogen-Activated Protein Kinases - metabolism | Intracellular Signaling Peptides and Proteins - genetics | Macrophages - microbiology | Protein-Serine-Threonine Kinases - metabolism | Macrophages - pathology | Signal Transduction | Yersinia Infections - pathology | Yersinia enterocolitica - pathogenicity | Protein-Serine-Threonine Kinases - genetics | Yersinia Infections - microbiology | Genotype | MAP Kinase Kinase Kinases - metabolism | Receptors, Tumor Necrosis Factor, Type I - genetics | Tumor Necrosis Factor-alpha - toxicity | Macrophages - enzymology | Mice, Knockout | Host-Pathogen Interactions | Phenotype | Receptor-Interacting Protein Serine-Threonine Kinases - genetics | Animals | Yersinia enterocolitica - metabolism | Bacterial Proteins - metabolism | Macrophages - drug effects | Cytosol - microbiology | Inflammation - enzymology
Journal Article
Nature Cell Biology, ISSN 1465-7392, 10/2017, Volume 19, Issue 10, pp. 1248 - 1259
Receptor-interacting protein kinase-1 (RIPK1), a master regulator of cell fate decisions, was identified as a direct substrate of MAPKAP kinase-2 (MK2) by... 
Phosphorylation | Integration | Outer protein P | Cytotoxicity | Infections | Inflammation | Embryo fibroblasts | Kinases | Macrophages | Embryos | Screens | Lipopolysaccharides | Yersinia enterocolitica | Signaling | MAPKAP kinase | Cell fate | Protein kinase | Tumor necrosis factor | Fibroblasts | Bacteria | Apoptosis
Journal Article
PLoS Pathogens, ISSN 1553-7366, 06/2016, Volume 12, Issue 6, p. e1005660
Journal Article
PLoS ONE, ISSN 1932-6203, 2010, Volume 5, Issue 10, p. e13165
Journal Article