Ohjaamon pulpettilaitteiden, kattokonsolien ja näyttöjen keskitetyn himmennysjärjestelmän toteutusvaihtoehtojen kartoitus ja kehitys

Työn tarkoituksena kehittää laivan ohjaamoon keskitetty himmennysjärjestelmä. Himmennysjärjestelmään tulisi liittää pulpettilaitteita, kattokonsoleita ja näyttöjä. Esimerkki laivaksi otettiin NB 1378, Namibiaan toimitettava kalantutkimukseen menevä alus. Työ aloitettiin selvittämällä mitä laitteita aluksen ohjaamo sisältää ja tutkimalla niiden layout-piirustuksia, samalla selvittäen miten laitteet olisi mahdollista liittää uuteen himmennysjärjestelmään.The purpose of this thesis is the development of centralized dimming system for a ship. Dimming system should be connected to booth equipment, roof consoles and monitors. The example ship used in the thesis is NB 1378, fish research vessel. The work began by identifying the equipment that is located in the ship's bridge and deck and studying their layout drawings

Figure S2 from Recognition of a glycosylation substrate by the O-GlcNAc transferase TPR repeats

O-linked <i>N</i>-acetylglucosamine (O-GlcNAc) is an essential and dynamic post-translational modification found on hundreds of nucleocytoplasmic proteins in metazoa. Although a single enzyme, O-GlcNAc transferase (OGT), generates the entire cytosolic O-GlcNAc proteome, it is not understood how it recognizes its protein substrates, targeting only a fraction of serines/threonines in the metazoan proteome for glycosylation. We describe a trapped complex of human OGT with the C-terminal domain of TAB1, a key innate immunity-signalling O-GlcNAc protein, revealing extensive interactions with the tetratricopeptide repeats of OGT. Confirmed by mutagenesis, this interaction suggests that glycosylation substrate specificity is achieved by recognition of a degenerate sequon in the active site combined with an extended conformation C-terminal of the O-GlcNAc target site

Proteome Wide Purification and Identification of <i>O</i>‑GlcNAc-Modified Proteins Using Click Chemistry and Mass Spectrometry

The post-translational modification of proteins with <i>N</i>-acetylglucosamine (<i>O</i>-GlcNAc) is involved in the regulation of a wide variety of cellular processes and associated with a number of chronic diseases. Despite its emerging biological significance, the systematic identification of <i>O</i>-GlcNAc proteins is still challenging. In the present study, we demonstrate a significantly improved <i>O</i>-GlcNAc protein enrichment procedure, which exploits metabolic labeling of cells by azide-modified GlcNAc and copper-mediated Click chemistry for purification of modified proteins on an alkyne-resin. On-resin proteolysis using trypsin followed by LC–MS/MS afforded the identification of around 1500 <i>O</i>-GlcNAc proteins from a single cell line. Subsequent elution of covalently resin bound <i>O</i>-GlcNAc peptides using selective β-elimination enabled the identification of 185 <i>O</i>-GlcNAc modification sites on 80 proteins. To demonstrate the practical utility of the developed approach, we studied the global effects of the <i>O</i>-GlcNAcase inhibitor GlcNAcstatin G on the level of <i>O</i>-GlcNAc modification of cellular proteins. About 200 proteins including several key players involved in the hexosamine signaling pathway showed significantly increased <i>O</i>-GlcNAcylation levels in response to the drug, which further strengthens the link of <i>O</i>-GlcNAc protein modification to cellular nutrient sensing and response

Proteome Wide Purification and Identification of <i>O</i>‑GlcNAc-Modified Proteins Using Click Chemistry and Mass Spectrometry

The post-translational modification of proteins with <i>N</i>-acetylglucosamine (<i>O</i>-GlcNAc) is involved in the regulation of a wide variety of cellular processes and associated with a number of chronic diseases. Despite its emerging biological significance, the systematic identification of <i>O</i>-GlcNAc proteins is still challenging. In the present study, we demonstrate a significantly improved <i>O</i>-GlcNAc protein enrichment procedure, which exploits metabolic labeling of cells by azide-modified GlcNAc and copper-mediated Click chemistry for purification of modified proteins on an alkyne-resin. On-resin proteolysis using trypsin followed by LC–MS/MS afforded the identification of around 1500 <i>O</i>-GlcNAc proteins from a single cell line. Subsequent elution of covalently resin bound <i>O</i>-GlcNAc peptides using selective β-elimination enabled the identification of 185 <i>O</i>-GlcNAc modification sites on 80 proteins. To demonstrate the practical utility of the developed approach, we studied the global effects of the <i>O</i>-GlcNAcase inhibitor GlcNAcstatin G on the level of <i>O</i>-GlcNAc modification of cellular proteins. About 200 proteins including several key players involved in the hexosamine signaling pathway showed significantly increased <i>O</i>-GlcNAcylation levels in response to the drug, which further strengthens the link of <i>O</i>-GlcNAc protein modification to cellular nutrient sensing and response