Mutations that prevent caspase cleavage of RIPK1 cause autoinflammatory disease.

Animals Caspase 3 / metabolism Caspase 8 / metabolism Female Hereditary Autoinflammatory Diseases / genetics Humans MAP Kinase Kinase Kinases / genetics Male Mice Mice, Inbred C57BL Mice, Knockout Mutation Pedigree Receptor-Interacting Protein Serine-Threonine Kinases / deficiency

Journal

Nature
ISSN: 1476-4687
Titre abrégé: Nature
Pays: England
ID NLM: 0410462

Informations de publication

Date de publication:
01 2020
Historique:
received: 05 03 2019
accepted: 17 10 2019
pubmed: 13 12 2019
medline: 9 4 2020
entrez: 13 12 2019
Statut: ppublish

Résumé

RIPK1 is a key regulator of innate immune signalling pathways. To ensure an optimal inflammatory response, RIPK1 is regulated post-translationally by well-characterized ubiquitylation and phosphorylation events, as well as by caspase-8-mediated cleavage

Identifiants

DOI: 10.1038/s41586-019-1828-5 PMID: 31827281 PMC: PMC6930849
pubmed: 31827281
doi: 10.1038/s41586-019-1828-5
pii: 10.1038/s41586-019-1828-5
pmc: PMC6930849
mid: EMS84659
doi:

Substances chimiques

RIPK1 protein, human EC 2.7.11.1
Receptor-Interacting Protein Serine-Threonine Kinases EC 2.7.11.1
Ripk1 protein, mouse EC 2.7.11.1
MAP Kinase Kinase Kinases EC 2.7.11.25
Map3k9 protein, mouse EC 2.7.11.25
Casp3 protein, mouse EC 3.4.22.-
Casp8 protein, mouse EC 3.4.22.-
Caspase 3 EC 3.4.22.-
Caspase 8 EC 3.4.22.-

Types de publication

Journal Article Research Support, N.I.H., Intramural Research Support, Non-U.S. Gov't

Langues

eng

Sous-ensembles de citation

IM

Pagination

103-108

Subventions

Organisme : European Research Council
ID : 787826
Pays : International
Organisme : NIAID NIH HHS
ID : R01 AI137249
Pays : United States
Organisme : NHLBI NIH HHS
ID : R01 HL122533
Pays : United States

Références

Bertrand, M. J. M. et al. cIAP1 and cIAP2 facilitate cancer cell survival by functioning as E3 ligases that promote RIP1 ubiquitination. Mol. Cell 30, 689–700 (2008).
pubmed: 18570872 doi: 10.1016/j.molcel.2008.05.014
Dondelinger, Y. et al. MK2 phosphorylation of RIPK1 regulates TNF-mediated cell death. Nat. Cell Biol. 19, 1237–1247 (2017).
pubmed: 28920952 doi: 10.1038/ncb3608
Dondelinger, Y. et al. NF-κB-independent role of IKKα/IKKβ in preventing RIPK1 kinase-dependent apoptotic and necroptotic cell death during TNF signaling. Mol. Cell 60, 63–76 (2015).
pubmed: 26344099 doi: 10.1016/j.molcel.2015.07.032
Jaco, I. et al. MK2 phosphorylates RIPK1 to prevent TNF-induced cell death. Mol. Cell 66, 698–710.e5 (2017).
pubmed: 28506461 pmcid: 5459754 doi: 10.1016/j.molcel.2017.05.003
Feltham, R. et al. Mind bomb regulates cell death during TNF signaling by suppressing RIPK1’s cytotoxic potential. Cell Reports 23, 470–484 (2018).
pubmed: 29642005 doi: 10.1016/j.celrep.2018.03.054
Menon, M. B. et al. p38
pubmed: 28920954 doi: 10.1038/ncb3614
Lafont, E. et al. TBK1 and IKKε prevent TNF-induced cell death by RIPK1 phosphorylation. Nat. Cell Biol. 20, 1389–1399 (2018).
pubmed: 30420664 pmcid: 6268100 doi: 10.1038/s41556-018-0229-6
Oberst, A. et al. Catalytic activity of the caspase-8–FLIP
pubmed: 21368763 pmcid: 3077893 doi: 10.1038/nature09852
Kim, J. W., Choi, E. J. & Joe, C. O. Activation of death-inducing signaling complex (DISC) by pro-apoptotic C-terminal fragment of RIP. Oncogene 19, 4491–4499 (2000).
pubmed: 11002422 doi: 10.1038/sj.onc.1203796
Lin, Y., Devin, A., Rodriguez, Y. & Liu, Z. G. Cleavage of the death domain kinase RIP by caspase-8 prompts TNF-induced apoptosis. Genes Dev. 13, 2514–2526 (1999).
pubmed: 10521396 pmcid: 317073 doi: 10.1101/gad.13.19.2514
van Raam, B. J., Ehrnhoefer, D. E., Hayden, M. R. & Salvesen, G. S. Intrinsic cleavage of receptor-interacting protein kinase-1 by caspase-6. Cell Death Differ. 20, 86–96 (2013).
pubmed: 22858542 doi: 10.1038/cdd.2012.98
Dillon, C. P. et al. RIPK1 blocks early postnatal lethality mediated by caspase-8 and RIPK3. Cell 157, 1189–1202 (2014).
pubmed: 24813850 pmcid: 4068710 doi: 10.1016/j.cell.2014.04.018
Kaiser, W. J. et al. RIP1 suppresses innate immune necrotic as well as apoptotic cell death during mammalian parturition. Proc. Natl Acad. Sci. USA 111, 7753–7758 (2014).
pubmed: 24821786 doi: 10.1073/pnas.1401857111 pmcid: 4040608
Kelliher, M. A. et al. The death domain kinase RIP mediates the TNF-induced NF-κB signal. Immunity 8, 297–303 (1998).
pubmed: 9529147 doi: 10.1016/S1074-7613(00)80535-X
Rickard, J. A. et al. RIPK1 regulates RIPK3-MLKL-driven systemic inflammation and emergency hematopoiesis. Cell 157, 1175–1188 (2014).
pubmed: 24813849 doi: 10.1016/j.cell.2014.04.019
Moulin, M. et al. IAPs limit activation of RIP kinases by TNF receptor 1 during development. EMBO J. 31, 1679–1691 (2012).
pubmed: 22327219 pmcid: 3321198 doi: 10.1038/emboj.2012.18
Peltzer, N. et al. LUBAC is essential for embryogenesis by preventing cell death and enabling haematopoiesis. Nature 557, 112–117 (2018).
pubmed: 29695863 pmcid: 5947819 doi: 10.1038/s41586-018-0064-8
Peltzer, N. et al. HOIP deficiency causes embryonic lethality by aberrant TNFR1-mediated endothelial cell death. Cell Reports 9, 153–165 (2014).
pubmed: 25284787 doi: 10.1016/j.celrep.2014.08.066
Varfolomeev, E. E. et al. Targeted disruption of the mouse Caspase 8 gene ablates cell death induction by the TNF receptors, Fas/Apo1, and DR3 and is lethal prenatally. Immunity 9, 267–276 (1998).
pubmed: 9729047 doi: 10.1016/S1074-7613(00)80609-3
Yeh, W. C. et al. FADD: essential for embryo development and signaling from some, but not all, inducers of apoptosis. Science 279, 1954–1958 (1998).
pubmed: 9506948 doi: 10.1126/science.279.5358.1954
Yeh, W. C. et al. Requirement for Casper (c-FLIP) in regulation of death receptor-induced apoptosis and embryonic development. Immunity 12, 633–642 (2000).
pubmed: 10894163 doi: 10.1016/S1074-7613(00)80214-9
Kaiser, W. J. et al. RIP3 mediates the embryonic lethality of caspase-8-deficient mice. Nature 471, 368–372 (2011).
pubmed: 21368762 pmcid: 3060292 doi: 10.1038/nature09857
Alvarez-Diaz, S. et al. The pseudokinase MLKL and the kinase RIPK3 have distinct roles in autoimmune disease caused by loss of death-receptor-induced apoptosis. Immunity 45, 513–526 (2016).
pubmed: 27523270 pmcid: 5040700 doi: 10.1016/j.immuni.2016.07.016
Zhang, X., Dowling, J. P. & Zhang, J. RIPK1 can mediate apoptosis in addition to necroptosis during embryonic development. Cell Death Dis. 10, 245 (2019).
pubmed: 30867408 pmcid: 6416317 doi: 10.1038/s41419-019-1490-8
Dondelinger, Y. et al. Serine 25 phosphorylation inhibits RIPK1 kinase-dependent cell death in models of infection and inflammation. Nat. Commun. 10, 1729 (2019).
pubmed: 30988283 pmcid: 6465317 doi: 10.1038/s41467-019-09690-0
Geng, J. et al. Regulation of RIPK1 activation by TAK1-mediated phosphorylation dictates apoptosis and necroptosis. Nat. Commun. 8, 359 (2017).
pubmed: 28842570 pmcid: 5572456 doi: 10.1038/s41467-017-00406-w
Stennicke, H. R. & Salvesen, G. S. Catalytic properties of the caspases. Cell Death Differ. 6, 1054–1059 (1999).
pubmed: 10578173 doi: 10.1038/sj.cdd.4400599
Wong, W. W. et al. RIPK1 is not essential for TNFR1-induced activation of NF-κB. Cell Death Differ. 17, 482–487 (2010).
pubmed: 19927158 doi: 10.1038/cdd.2009.178
Newton, K. et al. RIPK1 inhibits ZBP1-driven necroptosis during development. Nature 540, 129–133 (2016).
pubmed: 27819682 doi: 10.1038/nature20559
Cuchet-Lourenço, D. et al. Biallelic RIPK1 mutations in humans cause severe immunodeficiency, arthritis, and intestinal inflammation. Science 361, 810–813 (2018).
pubmed: 30026316 pmcid: 6529353 doi: 10.1126/science.aar2641
Micheau, O., Lens, S., Gaide, O., Alevizopoulos, K. & Tschopp, J. NF-kappaB signals induce the expression of c-FLIP. Mol. Cell. Biol. 21, 5299–5305 (2001).
pubmed: 11463813 pmcid: 87253 doi: 10.1128/MCB.21.16.5299-5305.2001
Croft, S. N., Walker, E. J. & Ghildyal, R. Human Rhinovirus 3C protease cleaves RIPK1, concurrent with caspase 8 activation. Sci. Rep. 8, 1569 (2018).
pubmed: 29371673 pmcid: 5785518 doi: 10.1038/s41598-018-19839-4
Pearson, J. S. et al. EspL is a bacterial cysteine protease effector that cleaves RHIM proteins to block necroptosis and inflammation. Nat. Microbiol. 2, 16258 (2017).
pubmed: 28085133 doi: 10.1038/nmicrobiol.2016.258
Kim, D., Langmead, B. & Salzberg, S. L. HISAT: a fast spliced aligner with low memory requirements. Nat. Methods 12, 357–360 (2015).
pubmed: 25751142 pmcid: 4655817 doi: 10.1038/nmeth.3317
Anders, S., Pyl, P. T. & Huber, W. HTSeq—a Python framework to work with high-throughput sequencing data. Bioinformatics 31, 166–169 (2015).
doi: 10.1093/bioinformatics/btu638 pubmed: 25260700
Huang, W., Sherman, B. T. & Lempicki, R. A. Systematic and integrative analysis of large gene lists using DAVID bioinformatics resources. Nat. Protocols 4, 44–57 (2009).
doi: 10.1038/nprot.2008.211
Sun, J., Nishiyama, T., Shimizu, K. & Kadota, K. TCC: an R package for comparing tag count data with robust normalization strategies. BMC Bioinformatics 14, 219 (2013).
pubmed: 23837715 pmcid: 3716788 doi: 10.1186/1471-2105-14-219
Robinson, M. D., McCarthy, D. J. & Smyth, G. K. edgeR: a Bioconductor package for differential expression analysis of digital gene expression data. Bioinformatics 26, 139–140 (2010).
pubmed: 19910308 doi: 10.1093/bioinformatics/btp616
Newton, K., Sun, X. & Dixit, V. M. Kinase RIP3 is dispensable for normal NF-κBs, signaling by the B-cell and T-cell receptors, tumor necrosis factor receptor 1, and Toll-like receptors 2 and 4. Mol. Cell. Biol. 24, 1464–1469 (2004).
pubmed: 14749364 pmcid: 344190 doi: 10.1128/MCB.24.4.1464-1469.2004
Murphy, J. M. et al. The pseudokinase MLKL mediates necroptosis via a molecular switch mechanism. Immunity 39, 443–453 (2013).
pubmed: 24012422 doi: 10.1016/j.immuni.2013.06.018
Conos, S. A., Lawlor, K. E., Vaux, D. L., Vince, J. E. & Lindqvist, L. M. Cell death is not essential for caspase-1-mediated interleukin-1β activation and secretion. Cell Death Differ. 23, 1827–1838 (2016).
pubmed: 27419363 pmcid: 5071572 doi: 10.1038/cdd.2016.69
Mandal, P. et al. RIP3 induces apoptosis independent of pronecrotic kinase activity. Mol. Cell 56, 481–495 (2014).
pubmed: 25459880 pmcid: 4512186 doi: 10.1016/j.molcel.2014.10.021
Newton, K. et al. Activity of protein kinase RIPK3 determines whether cells die by necroptosis or apoptosis. Science 343, 1357–1360 (2014).
pubmed: 24557836 doi: 10.1126/science.1249361

Auteurs

Najoua Lalaoui (N)

The Walter and Eliza Hall Institute, Parkville, Victoria, Australia. lalaoui@wehi.edu.au.
Department of Medical Biology, University of Melbourne, Parkville, Victoria, Australia. lalaoui@wehi.edu.au.

Steven E Boyden (SE)

Inflammatory Disease Section, National Human Genome Research Institute, National Institutes of Health, Bethesda, MD, USA. steven.boyden@genetics.utah.edu.

Hirotsugu Oda (H)

Inflammatory Disease Section, National Human Genome Research Institute, National Institutes of Health, Bethesda, MD, USA.

Geryl M Wood (GM)

Inflammatory Disease Section, National Human Genome Research Institute, National Institutes of Health, Bethesda, MD, USA.

Deborah L Stone (DL)

Inflammatory Disease Section, National Human Genome Research Institute, National Institutes of Health, Bethesda, MD, USA.

Diep Chau (D)

The Walter and Eliza Hall Institute, Parkville, Victoria, Australia.

Lin Liu (L)

The Walter and Eliza Hall Institute, Parkville, Victoria, Australia.
Department of Medical Biology, University of Melbourne, Parkville, Victoria, Australia.

Monique Stoffels (M)

Inflammatory Disease Section, National Human Genome Research Institute, National Institutes of Health, Bethesda, MD, USA.

Tobias Kratina (T)

The Walter and Eliza Hall Institute, Parkville, Victoria, Australia.

Kate E Lawlor (KE)

Centre for Innate Immunity and Infectious Diseases, Hudson Institute of Medical Research, Clayton, Victoria, Australia.
Department of Molecular and Translational Science, Monash University, Clayton, Victoria, Australia.

Kristien J M Zaal (KJM)

Light Imaging Section, Office of Science and Technology, National Institute of Arthritis and Musculoskeletal and Skin Diseases, National Institutes of Health, Bethesda, MD, USA.

Patrycja M Hoffmann (PM)

Inflammatory Disease Section, National Human Genome Research Institute, National Institutes of Health, Bethesda, MD, USA.

Nima Etemadi (N)

The Walter and Eliza Hall Institute, Parkville, Victoria, Australia.
Department of Medical Biology, University of Melbourne, Parkville, Victoria, Australia.

Kristy Shield-Artin (K)

The Walter and Eliza Hall Institute, Parkville, Victoria, Australia.
Department of Medical Biology, University of Melbourne, Parkville, Victoria, Australia.

Christine Biben (C)

The Walter and Eliza Hall Institute, Parkville, Victoria, Australia.
Department of Medical Biology, University of Melbourne, Parkville, Victoria, Australia.

Wanxia Li Tsai (WL)

Translational Immunology Section, National Institute of Arthritis and Musculoskeletal and Skin Diseases, National Institutes of Health, Bethesda, MD, USA.

Mary D Blake (MD)

Translational Immunology Section, National Institute of Arthritis and Musculoskeletal and Skin Diseases, National Institutes of Health, Bethesda, MD, USA.

Hye Sun Kuehn (HS)

Department of Laboratory Medicine, Clinical Center, National Institutes of Health, Bethesda, MD, USA.

Dan Yang (D)

Translational Vascular Medicine Branch, National Heart, Lung, and Blood Institute, National Institutes of Health, Bethesda, MD, USA.

Holly Anderton (H)

The Walter and Eliza Hall Institute, Parkville, Victoria, Australia.
Department of Medical Biology, University of Melbourne, Parkville, Victoria, Australia.

Natasha Silke (N)

The Walter and Eliza Hall Institute, Parkville, Victoria, Australia.

Laurens Wachsmuth (L)

Institute for Genetics & Cologne Excellence Cluster on Cellular Stress Responses in Aging-Associated Diseases (CECAD), University of Cologne, Cologne, Germany.
Center for Molecular Medicine (CMMC), University of Cologne, Cologne, Germany.

Lixin Zheng (L)

Molecular Development of the Immune System Section, Laboratory of Immune System Biology; Clinical Genomics Program, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, MD, USA.

Natalia Sampaio Moura (NS)

Inflammatory Disease Section, National Human Genome Research Institute, National Institutes of Health, Bethesda, MD, USA.

David B Beck (DB)

Inflammatory Disease Section, National Human Genome Research Institute, National Institutes of Health, Bethesda, MD, USA.

Gustavo Gutierrez-Cruz (G)

Laboratory of Muscle Stem Cells and Gene Regulation, National Institute of Arthritis and Musculoskeletal and Skin Diseases, National Institutes of Health, Bethesda, MD, USA.

Amanda K Ombrello (AK)

Inflammatory Disease Section, National Human Genome Research Institute, National Institutes of Health, Bethesda, MD, USA.

Gineth P Pinto-Patarroyo (GP)

Inflammatory Disease Section, National Human Genome Research Institute, National Institutes of Health, Bethesda, MD, USA.

Andrew J Kueh (AJ)

The Walter and Eliza Hall Institute, Parkville, Victoria, Australia.
Department of Medical Biology, University of Melbourne, Parkville, Victoria, Australia.

Marco J Herold (MJ)

The Walter and Eliza Hall Institute, Parkville, Victoria, Australia.
Department of Medical Biology, University of Melbourne, Parkville, Victoria, Australia.

Cathrine Hall (C)

The Walter and Eliza Hall Institute, Parkville, Victoria, Australia.

Hongying Wang (H)

Inflammatory Disease Section, National Human Genome Research Institute, National Institutes of Health, Bethesda, MD, USA.

Jae Jin Chae (JJ)

Inflammatory Disease Section, National Human Genome Research Institute, National Institutes of Health, Bethesda, MD, USA.

Natalia I Dmitrieva (NI)

Translational Vascular Medicine Branch, National Heart, Lung, and Blood Institute, National Institutes of Health, Bethesda, MD, USA.

Mark McKenzie (M)

The Walter and Eliza Hall Institute, Parkville, Victoria, Australia.
Department of Medical Biology, University of Melbourne, Parkville, Victoria, Australia.

Amanda Light (A)

The Walter and Eliza Hall Institute, Parkville, Victoria, Australia.

Beverly K Barham (BK)

Inflammatory Disease Section, National Human Genome Research Institute, National Institutes of Health, Bethesda, MD, USA.

Anne Jones (A)

Inflammatory Disease Section, National Human Genome Research Institute, National Institutes of Health, Bethesda, MD, USA.

Tina M Romeo (TM)

Inflammatory Disease Section, National Human Genome Research Institute, National Institutes of Health, Bethesda, MD, USA.

Qing Zhou (Q)

Inflammatory Disease Section, National Human Genome Research Institute, National Institutes of Health, Bethesda, MD, USA.

Ivona Aksentijevich (I)

Inflammatory Disease Section, National Human Genome Research Institute, National Institutes of Health, Bethesda, MD, USA.

James C Mullikin (JC)

NIH Intramural Sequencing Center, National Human Genome Research Institute, National Institutes of Health, Bethesda, MD, USA.

Andrew J Gross (AJ)

Division of Rheumatology, Department of Medicine, University of California San Francisco, San Francisco, CA, USA.

Anthony K Shum (AK)

Division of Pulmonary and Critical Care, Department of Medicine, University of California San Francisco, San Francisco, CA, USA.

Edwin D Hawkins (ED)

The Walter and Eliza Hall Institute, Parkville, Victoria, Australia.
Department of Medical Biology, University of Melbourne, Parkville, Victoria, Australia.

Seth L Masters (SL)

The Walter and Eliza Hall Institute, Parkville, Victoria, Australia.
Department of Medical Biology, University of Melbourne, Parkville, Victoria, Australia.

Michael J Lenardo (MJ)

Molecular Development of the Immune System Section, Laboratory of Immune System Biology; Clinical Genomics Program, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, MD, USA.

Manfred Boehm (M)

Translational Vascular Medicine Branch, National Heart, Lung, and Blood Institute, National Institutes of Health, Bethesda, MD, USA.

Sergio D Rosenzweig (SD)

Department of Laboratory Medicine, Clinical Center, National Institutes of Health, Bethesda, MD, USA.

Manolis Pasparakis (M)

Institute for Genetics & Cologne Excellence Cluster on Cellular Stress Responses in Aging-Associated Diseases (CECAD), University of Cologne, Cologne, Germany.
Center for Molecular Medicine (CMMC), University of Cologne, Cologne, Germany.

Anne K Voss (AK)

The Walter and Eliza Hall Institute, Parkville, Victoria, Australia.
Department of Medical Biology, University of Melbourne, Parkville, Victoria, Australia.

Massimo Gadina (M)

Translational Immunology Section, National Institute of Arthritis and Musculoskeletal and Skin Diseases, National Institutes of Health, Bethesda, MD, USA.

Daniel L Kastner (DL)

Inflammatory Disease Section, National Human Genome Research Institute, National Institutes of Health, Bethesda, MD, USA. kastnerd@mail.nih.gov.

John Silke (J)

The Walter and Eliza Hall Institute, Parkville, Victoria, Australia. silke@wehi.edu.au.
Department of Medical Biology, University of Melbourne, Parkville, Victoria, Australia. silke@wehi.edu.au.

Articles similaires

[Redispensing of expensive oral anticancer medicines: a practical application].

Lisanne N van Merendonk, Kübra Akgöl, Bastiaan Nuijen
1.00
Humans Antineoplastic Agents Administration, Oral Drug Costs Counterfeit Drugs

Smoking Cessation and Incident Cardiovascular Disease.

Jun Hwan Cho, Seung Yong Shin, Hoseob Kim et al.
1.00
Humans Male Smoking Cessation Cardiovascular Diseases Female

Evaluation of Low-Value Services Across Major Medicare Advantage Insurers and Traditional Medicare.

Ciara Duggan, Adam L Beckman, Ishani Ganguli et al.
1.00
Humans United States Aged Cross-Sectional Studies Medicare Part C

Effectiveness of Virtual Yoga for Chronic Low Back Pain: A Randomized Clinical Trial.

Hallie Tankha, Devyn Gaskins, Amanda Shallcross et al.
1.00
Humans Yoga Low Back Pain Female Male

Classifications MeSH

questionsmedicales.fr › Eucaryotes › Animaux › Mutations that prevent caspase cleavage of...
questionsmedicales.fr › Acides aminés, peptides et protéines › Protéines › Protéines et peptides de signalisation intracellulaire › Protéines régulatrices de l'apoptose › Caspases › Caspases effectrices › Caspase-3 › Mutations that prevent caspase cleavage of...
questionsmedicales.fr › Acides aminés, peptides et protéines › Protéines › Protéines et peptides de signalisation intracellulaire › Protéines régulatrices de l'apoptose › Protéines adaptatrices de signalisation des récepteurs à domaine de mort › Caspase 8 › Mutations that prevent caspase cleavage of...
questionsmedicales.fr › Maladies de la peau et du tissu conjonctif › Maladies de la peau › Maladies génétiques de la peau › Maladies auto-inflammatoires héréditaires › Mutations that prevent caspase cleavage of...
questionsmedicales.fr › Eucaryotes › Animaux › Chordés › Vertébrés › Mammifères › Eutheria › Primates › Haplorhini › Catarrhini › Hominidae › Humains › Mutations that prevent caspase cleavage of...
questionsmedicales.fr › Acides aminés, peptides et protéines › Protéines › Protéines et peptides de signalisation intracellulaire › Protein-Serine-Threonine Kinases › MAP Kinase Kinase Kinases › Mutations that prevent caspase cleavage of...
questionsmedicales.fr › Eucaryotes › Animaux › Chordés › Vertébrés › Mammifères › Eutheria › Rodentia › Muridae › Murinae › Souris › Mutations that prevent caspase cleavage of...
questionsmedicales.fr › Eucaryotes › Animaux › Chordés › Vertébrés › Mammifères › Eutheria › Rodentia › Muridae › Murinae › Souris › Lignées consanguines de souris › Souris de lignée C57BL › Mutations that prevent caspase cleavage of...
questionsmedicales.fr › Eucaryotes › Animaux › Chordés › Vertébrés › Mammifères › Eutheria › Rodentia › Muridae › Murinae › Souris › Souris transgéniques › Souris knockout › Mutations that prevent caspase cleavage of...
questionsmedicales.fr › Phénomènes génétiques › Variation génétique › Mutation › Mutations that prevent caspase cleavage of...
questionsmedicales.fr › Techniques d'investigation › Techniques génétiques › Pedigree › Mutations that prevent caspase cleavage of...
questionsmedicales.fr › Acides aminés, peptides et protéines › Protéines › Protéines et peptides de signalisation intracellulaire › Protein-Serine-Threonine Kinases › Receptor-Interacting Protein Serine-Threonine Kinases › Mutations that prevent caspase cleavage of...