Spelling suggestions: "subject:"embryonic lethal""
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Acyl CoA Binding Protein (ACBP) Gene Ablation Induces Pre-Implantation Embryonic Lethality in MiceLandrock, Danilo 2010 December 1900 (has links)
Unique among the intracellular lipid binding proteins, acyl CoA binding protein (ACBP)
exclusively binds long chain fatty acyl CoAs (LCFA-CoAs). To test if ACBP is an
essential protein in mammals, the ACBP gene was ablated by homologous
recombination in mice. While ACBP heterozygotes appeared phenotypically normal,
intercrossing of the heterozygotes did not result in any live homozygous deficient (null)
ACBP^(-/-) pups. Heterozygous and wild type embryos were detected at all
postimplantation stages, but no homozygous ACBP null embryos were obtained–
suggesting that an embryonic lethality occurred at a preimplantation stage of
development, or that embryos never formed. While ACBP null embryos were not
detected at any blastocyst stage, ACBP null embryos were detected at the morula (8-
cell), cleavage (2-cell), and zygote (1-cell) preimplantation stages. Two other LCFACoA
binding proteins, sterol carrier protein-2 (SCP-2) and sterol carrier protein-x (SCPx)
were significantly upregulated at these stages. These findings demonstrate for the first
time that ACBP is an essential protein required for embryonic development and its loss
of function may be initially compensated by concomitant upregulation of two other LCFA-CoA binding proteins only at the earliest preimplantation stages. The fact that
ACBP is the first known intracellular lipid binding protein whose deletion results in
embryonic lethality suggests its vital importance in mammals.
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Insights into the ribosomal, extra-ribosomal and developmental role of RP L13a in mammalian modelKour, Ravinder 10 December 2019 (has links)
No description available.
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Hledání biologické role rodiny proteinů podobných Ddi1 / Deciphering the biological role of Ddi1-like protein familySivá, Monika January 2019 (has links)
Ddi1-like protein family has been recently raised into the spotlight by the scientific community due to its important roles in cellular homeostasis maintenance. It represents a specific group among shuttling proteins of the ubiquitin-proteasome system. When compared to other shuttles, Ddi1-like protein family members harbor a unique retroviral-protease like domain besides the conventional ubiquitin-like (UBL) domain and domains interacting with ubiquitin. In addition, a helical domain of Ddi (HDD) has been recently found in most of the orthologs. In this thesis, I focus on characterization of several members of Ddi1-like protein family, both on molecular level using NMR and in model mouse strains via a variety of biological methods. Solution structure of the UBL domain of Ddi1p of S. cerevisiae was solved and its characteristics were compared to those of the UBL domain of its human ortholog. Furthermore, we show that human DDI2 specifically binds to ubiquitin with its terminal domains, both the UBL and the UIM; however, with very low affinity in contrast to binding properties of its yeast counterpart. Our study also show that hDDI2 does not form a head-to-tail homodimer. Based on our structural studies, we hypothesize that human DDI2 might have evolved a different function compared to its yeast...
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Biological functions of microRNA-216 and microRNA-217 during the development of pancreatic cancerAzevedo-Pouly, Ana Clara P. 17 October 2013 (has links)
No description available.
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Biotechnological approaches to fight fruit flies of agricultural importance / Biotechnologische Ansätze zur Fruchfliegen landwirtschaftlicher Bedeutung zu kämpfenOgaugwu, Christian Ejikeme 18 April 2012 (has links)
No description available.
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New molecular technologies to improve the Sterile Insect Technique for the Mediterranean fruitfly <i>Ceratitis capitata</i> (Diptera; Tephritidae) / Neue molekulargenetische Ansätze zur Verbesserung der Sterilen Insekten Technik für die Mittelmeerfruchtfliege <i>Ceratitis capitata</i> (Diptera: Tephritidae)Schetelig, Marc Florian 23 April 2008 (has links)
No description available.
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