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000257883 041__ $$aEnglish
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000257883 1001_ $$aStroo, Esther$$b0
000257883 245__ $$aDeletion of SERF2 in mice delays embryonic development and alters amyloid deposit structure in the brain.
000257883 260__ $$aHeidelberg$$bEMBO Press$$c2023
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000257883 520__ $$aIn age-related neurodegenerative diseases, like Alzheimer's and Parkinson's, disease-specific proteins become aggregation-prone and form amyloid-like deposits. Depletion of SERF proteins ameliorates this toxic process in worm and human cell models for diseases. Whether SERF modifies amyloid pathology in mammalian brain, however, has remained unknown. Here, we generated conditional Serf2 knockout mice and found that full-body deletion of Serf2 delayed embryonic development, causing premature birth and perinatal lethality. Brain-specific Serf2 knockout mice, on the other hand, were viable, and showed no major behavioral or cognitive abnormalities. In a mouse model for amyloid-β aggregation, brain depletion of Serf2 altered the binding of structure-specific amyloid dyes, previously used to distinguish amyloid polymorphisms in the human brain. These results suggest that Serf2 depletion changed the structure of amyloid deposits, which was further supported by scanning transmission electron microscopy, but further study will be required to confirm this observation. Altogether, our data reveal the pleiotropic functions of SERF2 in embryonic development and in the brain and support the existence of modifying factors of amyloid deposition in mammalian brain, which offer possibilities for polymorphism-based interventions.
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000257883 650_7 $$2NLM Chemicals$$aAmyloid beta-Peptides
000257883 650_7 $$2NLM Chemicals$$aSERF2 protein, human
000257883 650_7 $$2NLM Chemicals$$aIntracellular Signaling Peptides and Proteins
000257883 650_7 $$2NLM Chemicals$$aSerf2 protein, mouse
000257883 650_2 $$2MeSH$$aBrain: embryology
000257883 650_2 $$2MeSH$$aMice
000257883 650_2 $$2MeSH$$aHumans
000257883 650_2 $$2MeSH$$aAnimals
000257883 650_2 $$2MeSH$$aPlaque, Amyloid: metabolism
000257883 650_2 $$2MeSH$$aBrain: metabolism
000257883 650_2 $$2MeSH$$aAmyloid beta-Peptides: metabolism
000257883 650_2 $$2MeSH$$aMice, Knockout
000257883 650_2 $$2MeSH$$aEmbryonic Development: genetics
000257883 650_2 $$2MeSH$$aMammals: metabolism
000257883 650_2 $$2MeSH$$aIntracellular Signaling Peptides and Proteins: metabolism
000257883 7001_ $$00000-0002-1973-304X$$aJanssen, Leen$$b1
000257883 7001_ $$aSin, Olga$$b2
000257883 7001_ $$aHogewerf, Wytse$$b3
000257883 7001_ $$aKoster, Mirjam$$b4
000257883 7001_ $$aHarkema, Liesbeth$$b5
000257883 7001_ $$aYoussef, Sameh A$$b6
000257883 7001_ $$0P:(DE-HGF)0$$aBeschorner, Natalie$$b7
000257883 7001_ $$aWolters, Anouk Hg$$b8
000257883 7001_ $$00000-0003-3095-7287$$aBakker, Bjorn$$b9
000257883 7001_ $$00000-0002-6890-4984$$aBecker, Lore$$b10
000257883 7001_ $$aGarrett, Lilian$$b11
000257883 7001_ $$00000-0001-5191-7060$$aMarschall, Susan$$b12
000257883 7001_ $$aHoelter, Sabine M$$b13
000257883 7001_ $$0P:(DE-2719)2000028$$aWurst, Wolfgang$$b14
000257883 7001_ $$aFuchs, Helmut$$b15
000257883 7001_ $$aGailus-Durner, Valerie$$b16
000257883 7001_ $$00000-0002-7898-2353$$aHrabe de Angelis, Martin$$b17
000257883 7001_ $$00000-0002-3132-4409$$aThathiah, Amantha$$b18
000257883 7001_ $$00000-0003-0989-3127$$aFoijer, Floris$$b19
000257883 7001_ $$avan de Sluis, Bart$$b20
000257883 7001_ $$avan Deursen, Jan$$b21
000257883 7001_ $$aJucker, Matthias$$b22
000257883 7001_ $$ade Bruin, Alain$$b23
000257883 7001_ $$00000-0003-3740-6373$$aNollen, Ellen Aa$$b24
000257883 773__ $$0PERI:(DE-600)2948687-7$$a10.26508/lsa.202201730$$gVol. 6, no. 7, p. e202201730 -$$n7$$pe202201730$$tLife science alliance$$v6$$x2575-1077$$y2023
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