About: Loss of autophagy in erythroid cells leads to defective removal of mitochondria and severe anemia in vivo

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About: Loss of autophagy in erythroid cells leads to defective removal of mitochondria and severe anemia in vivo Goto Sponge NotDistinct Permalink

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scientific journal article

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description	artículu científicu espublizáu en 2010 (ast) vědecký článek publikovaný v roce 2010 (cs) 2009年學術文章 (zh) наукова стаття, опублікована в січні 2010 (uk) 2010 թվականի հունվարին հրատարակված գիտական հոդված (hy) 2010 թուականի Յունուարին հրատարակուած գիտական յօդուած (hyw) vedecký článok (publikovaný 2010/01/12) (sk) مقالة علمية (نشرت في 12-1-2010) (ar) im Januar 2010 veröffentlichter wissenschaftlicher Artikel (de) article publié dans les Proceedings of the National Academy of Sciences of the United States of America (fr) scientific journal article (en) wetenschappelijk artikel (gepubliceerd op 2010/01/12) (nl)
publication date	wds:Q28592180-589A0FAF-2E14-4981-BAB4-A74420DB9031
publication date	2009-12-22 00:00:00Z (xsd:dateTime)
language of work or name	wds:Q28592180-A154E4A5-73BD-48AD-B31F-5E3091CBCECA
language of work or name	English
cites work	wds:Q28592180-033CDD36-F3BC-4249-A225-7155585BBD81 wds:Q28592180-09B04C08-B6A3-49B0-AB0E-DC8ABB214F5E wds:Q28592180-0ADA650F-F627-4FD1-A108-7A966E1C15F7 wds:Q28592180-159D39D6-5663-4790-B724-0D20D5A42835 wds:Q28592180-1A5F25F1-FDCD-4197-A873-98C3749A7483 wds:Q28592180-1BF7BFBF-C542-4604-9D7F-25BE41818BE1 wds:Q28592180-309D79E2-4A4E-414C-96D6-0C7BD0678BBE wds:Q28592180-348F20CF-0963-4A8F-B3D5-74D9079CAF40 wds:Q28592180-37F9F58E-BB9B-483D-952C-06CAB7E0C8A6 wds:Q28592180-4855B16E-92E3-443E-A102-BAEA5A036CC6 wds:Q28592180-49B01837-1F44-4B70-BA85-164091DD7ED1 wds:Q28592180-4E75A36B-051A-4A65-B2C7-0E5D6A17B2BF wds:Q28592180-55226428-D39E-4961-B49C-158F9DDEE3E8 wds:Q28592180-612D64D6-56B4-4FB0-93ED-42B974459F8E wds:Q28592180-617DDBAA-5F41-4F12-BD54-2E27253475CA wds:Q28592180-658CF4D8-EFE7-4694-A9D2-61B72B22461D wds:Q28592180-68716601-1AEE-4D5B-9BEB-A196D99F8AC1 wds:Q28592180-69074268-A23A-44C2-8ABD-C732D257E45E wds:Q28592180-6CCC2230-AEAC-4F40-B948-D088FDBC569C wds:Q28592180-8B581F57-8AD2-4582-8B40-6BD6BB5249BC wds:Q28592180-93661610-0351-404C-89B1-ADFDB6914CB3 wds:Q28592180-A8C23620-45F2-4C9A-81FA-AA0BD2AA43B1 wds:Q28592180-AAF3C760-B31D-4B49-82F2-5652CAC520C7 wds:Q28592180-AF3822FF-09A8-47D2-BE89-9EF010B7676C wds:Q28592180-B09050A2-7DB1-4ADB-B8B1-6BBF11425E69 wds:Q28592180-B1B213B7-F996-4CC3-984C-BF8FE0228ED1 wds:Q28592180-B9DFE340-26BD-4A53-85E1-6AB04D403CA6 wds:Q28592180-C1BA6785-6F12-4773-9AF6-D0FAB0FC89E8 wds:Q28592180-C44637EB-70DD-40C3-BCB3-9B1D83AF3010 wds:Q28592180-C756E91A-75AF-40A5-86D8-C2F6DB1469AE wds:Q28592180-C7EC930E-9D86-4F46-BDF7-CF73849F8FA1 wds:Q28592180-D6A1790B-D8A3-4D8C-AD94-0FC577BAD1BC wds:Q28592180-E3402ADA-A7B8-4B0D-858B-A15B0F0BE7D2 wds:Q28592180-E3A8FBEB-6605-4A06-8143-C00BAAB588CB wds:Q28592180-E7ED6785-647B-4EA5-A496-5D2F909FA10D wds:Q28592180-E896D220-F109-433C-9205-1A1FDD1B86D8 wds:Q28592180-F507400F-FADC-404B-89E0-FDF2EB89F04E wds:Q28592180-F84EC552-3496-4997-A7AA-551628D16F4F wds:Q28592180-FEF6AB7A-1398-44C1-B23B-DCD6D211C2F5
cites work	Novel MMP-9 substrates in cancer cells revealed by a label-free quantitative proteomics approach Autophagy of mitochondria in rat bone marrow erythroid cells. Relation to nuclear extrusion. Beclin 1, an autophagy gene essential for early embryonic development, is a haploinsufficient tumor suppressor Self-eating and self-killing: crosstalk between autophagy and apoptosis Calpain-mediated cleavage of Atg5 switches autophagy to apoptosis. How mitochondria produce reactive oxygen species Selective degradation of mitochondria by mitophagy Clathrin light chains function in mannose phosphate receptor trafficking via regulation of actin assembly Autophagy counterbalances endoplasmic reticulum expansion during the unfolded protein response Impairment of starvation-induced and constitutive autophagy in Atg7-deficient mice Essential role for Nix in autophagic maturation of erythroid cells Mitochondrial clearance is regulated by Atg7-dependent and -independent mechanisms during reticulocyte maturation The human homolog of Saccharomyces cerevisiae Apg7p is a Protein-activating enzyme for multiple substrates including human Apg12p, GATE-16, GABARAP, and MAP-LC3 Mouse Apg16L, a novel WD-repeat protein, targets to the autophagic isolation membrane with the Apg12-Apg5 conjugate The role of autophagy during the early neonatal starvation period Mitochondrial fusion, fission and autophagy as a quality control axis: the bioenergetic view The Atg12-Atg5 conjugate has a novel E3-like activity for protein lipidation in autophagy Piecemeal microautophagy of the nucleus requires the core macroautophagy genes. Apg7p/Cvt2p: A novel protein-activating enzyme essential for autophagy Transgenic mice with hematopoietic and lymphoid specific expression of Cre Suppression of basal autophagy in neural cells causes neurodegenerative disease in mice Loss of autophagy in the central nervous system causes neurodegeneration in mice Vacuolar and plasma membrane stripping and autophagic elimination of Toxoplasma gondii in primed effector macrophages The role of autophagy in mammalian development: cell makeover rather than cell death Apoptosis in bone marrow biopsy samples involving stromal and hematopoietic cells in 50 patients with myelodysplastic syndromes Ineffective erythropoiesis in Stat5a(-/-)5b(-/-) mice due to decreased survival of early erythroblasts Promoter elements of vav drive transgene expression in vivo throughout the hematopoietic compartment Ulk1 plays a critical role in the autophagic clearance of mitochondria and ribosomes during reticulocyte maturation Granulocyte colony-stimulating factor inhibits spontaneous cytochrome c release and mitochondria-dependent apoptosis of myelodysplastic syndrome hematopoietic progenitors A critical role for the autophagy gene Atg5 in T cell survival and proliferation Does autophagy have a license to kill mammalian cells? Use of the fluorescent dye 10-N-nonyl acridine orange in quantitative and location assays of cardiolipin: a study on different experimental models Mutations affecting the secretory COPII coat component SEC23B cause congenital dyserythropoietic anemia type II. A mouse model for visualization and conditional mutations in the erythroid lineage Autophagy in organelle homeostasis: peroxisome turnover Assay for apoptosis using the mitochondrial probes, Rhodamine123 and 10-N-nonyl acridine orange Congenital dyserythropoietic anemia type II (CDAII) is caused by mutations in the SEC23B gene. Congenital dyserythropoietic anemia type II: ultrastructural and radioautographic studies of blood and bone marrow Autophagic vacuoles in human red cells
author name string	wds:Q28592180-253B613C-10AD-4C7B-BDB0-F0F3C7B68B3F wds:Q28592180-C3EDAE8B-9053-452A-ADE5-42AB4A1A58E9
OpenCitations bibliographic resource ID	wds:Q28592180-75530673-3520-4986-BB3C-9A9D398AF8BC
OpenCitations bibliographic resource ID	https://w3id.org/oc/corpus/br/1721321
author name string	M Mortensen

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