9 research outputs found

    Spectral Signature Analysis – BIST for RF Front-Ends

    Get PDF
    In this paper, the Spectral Signature Analysis is presented as a concept for an integrable self-test system (Built-In Self-Test – BIST) for RF front-ends is presented. It is based on modelling the whole RF front-end (transmitter and receiver) on system level, on generating of a Spectral Signature and of evaluating of the Signature Response. Because of using multi-carrier signal as the test signature, the concept is especially useful for tests of linearity and frequency response of front-ends. Due to the presented method of signature response evaluation, this concept can be used for Built-In Self-Correction (BISC) at critical building blocks

    Entwurf innovativer Systemarchitekturen fuer Low-Power-Kommunikationsschaltkreise mit fortgeschrittenen IC-Technologien Abschlussbericht

    No full text
    SIGLEAvailable from TIB Hannover: F02B319+a / FIZ - Fachinformationszzentrum Karlsruhe / TIB - Technische InformationsbibliothekSaechsisches Staatsministerium fuer Wissenschaft und Kunst, Dresden (Germany)DEGerman

    Identification of increased amounts of eppin protein complex components in sperm cells of diabetic and obese individuals by difference gel electrophoresis

    No full text
    Metabolic disorders like diabetes mellitus and obesity may compromise the fertility of men and women. To unveil disease-associated proteomic changes potentially affecting male fertility, the proteomes of sperm cells from type-1-diabetic, type-2-diabetic, non-diabetic obese and clinically healthy individuals were comparatively analyzed by differ-ence gel electrophoresis (DIGE). The adaptation of a general protein extraction proce-dure to the solubilization of proteins from sperm cells allowed for the resolution of 3,187 fluorescent spots in the DIGE image of the master gel, which contained the entirety of solubilized sperm proteins. Comparison of the pathological and reference proteomes by applying an average abundance ratio setting of 1.6 and a p≤0.05 criterion resulted in the identification of 79 fluorescent spots containing proteins that were present at significantly changed levels in the sperm cells. Biometric evaluation of the fluorescence data followed by mass spectrometric protein identification revealed altered levels of 12, 71 and 13 pro-tein species in the proteomes of the type-1-diabetic, type-2-diabetic and non-diabetic obese patients, respectively, with considerably enhanced levels of the same set of one molecular form of semenogelin-1, one form of clusterin and two forms of lactotransferrin in each group of pathological samples. Remarkably,galactosidase-1-like protein was the only protein that was detected at decreased levels in all three pathological situations. The former three proteins are part of the eppin (epididymal proteinase inhibitor) protein complex (EPC), which is thought to fulfill fertilization-related functions, such as ejaculate sperm protection, motility regulation and gain of competence for acrosome reaction, while the putative role of the latter protein to function as a glycosyl hydrolase during sperm maturation remains to be explored at the protein/enzyme level. The strikingly similar differences detected in the three groups of pathological sperm proteomes reflect a disease-associated enhanced formation of predominantly proteolytically modified forms of the EPC components, possibly as a response to enduring hyperglycemia and enhanced oxidative stress
    corecore