UNDERWATER MASKED CARRIER ACOUSTIC COMMUNICATION: MODELING AND ANALYSIS

As naval warfighting capabilities evolve, the need for innovative communication techniques for tactics and command and control increases. Using Navy sonar systems normally reserved for conventional communication in the underwater channel between vessels to transmit a hidden message disguised as ambient ocean noises or biological noise is a possible way to communicate with a low probability of interception or detection. This research applies information hiding via steganography in order to embed and extract bits from an audio file after transmission through a simulated underwater acoustic channel. Specifically, we explore a technique which allows us to communicate such that the transmission appears native to the operating environment. We do this by embedding symbols in an audio source in the frequency domain. We demonstrate the success of our technique via traditional steganography metrics and describe its performance limitations. We find that our scheme can be both imperceptible and robust provided that proper embedding and transmission parameters can be determined.http://archive.org/details/underwatermasked1094559657Outstanding ThesisLieutenant, United States NavyApproved for public release; distribution is unlimited

Underwater Masked Carrier Acoustic Communication

Rohrer, Justin: Principal InvestigatorNavy - FFCNPS-17-N091-

A Specific LSD1/KDM1A Isoform Regulates Neuronal Differentiation through H3K9 Demethylation

Lysine-specific demethylase 1 (LSD1) has been reported to repress and activate transcription by mediating histone H3K4me1/2 and H3K9me1/2 demethylation, respectively. The molecular mechanism that underlies this dual substrate specificity has remained unknown. Here we report that an isoform of LSD1, LSD1+8a, does not have the intrinsic capability to demethylate H3K4me2. Instead, LSD1+8a mediates H3K9me2 demethylation in collaboration with supervillin (SVIL), a new LSD1+8a interacting protein. LSD1+8a knockdown increases H3K9me2, but not H3K4me2, levels at its target promoters and compromises neuronal differentiation. Importantly, SVIL co-localizes to LSD1+8a-bound promoters, and its knockdown mimics the impact of LSD1+8a loss, supporting SVIL as a cofactor for LSD1+8a in neuronal cells. These findings provide insight into mechanisms by which LSD1 mediates H3K9me demethylation and highlight alternative splicing as a means by which LSD1 acquires selective substrate specificities (H3K9 versus H3K4) to differentially control specific gene expression programs in neurons

Phosphatidylinositol 3 kinase contributes to the transformation of hematopoietic cells by the D816V c-Kit mutant

RuJu Chian, Sonia Young, Alla Danilkovitch-Miagkova, Lars Rönnstrand, Edward Leonard, Petranel Ferrao, Leonie Ashman, and Diana Linneki

A Specific LSD1/KDM1A Isoform Regulates Neuronal Differentiation through H3K9 Demethylation

Lysine-specific demethylase 1 (LSD1) has been reported to repress and activate transcription by mediating histone H3K4me1/2 and H3K9me1/2 demethylation, respectively. The molecular mechanism that underlies this dual substrate specificity has remained unknown. Here we report that an isoform of LSD1, LSD1+8a, does not have the intrinsic capability to demethylate H3K4me2. Instead, LSD1+8a mediates H3K9me2 demethylation in collaboration with supervillin (SVIL), a new LSD1+8a interacting protein. LSD1+8a knockdown increases H3K9me2, but not H3K4me2, levels at its target promoters and compromises neuronal differentiation. Importantly, SVIL co-localizes to LSD1+8a-bound promoters, and its knockdown mimics the impact of LSD1+8a loss, supporting SVIL as a cofactor for LSD1+8a in neuronal cells. These findings provide insight into mechanisms by which LSD1 mediates H3K9me demethylation and highlight alternative splicing as a means by which LSD1 acquires selective substrate specificities (H3K9 versus H3K4) to differentially control specific gene expression programs in neurons