Refine
Year of publication
Document Type
- Article (58)
- Monograph/Edited Volume (10)
- Postprint (4)
- Part of Periodical (3)
- Other (2)
- Part of a Book (1)
- Conference Proceeding (1)
Keywords
- LPS (2)
- cori cycle (2)
- cytokines (2)
- endotoxin (2)
- human endotoxemia (2)
- inflammation (2)
- lactate (2)
- metabolomics (2)
- pyruvate (2)
- warburg effect (2)
- 3D medical image analysis (1)
- Administrative federalism (1)
- Biological activity (1)
- Biosynthesis (1)
- Brandenburg (1)
- Corpora allata (1)
- Enzyme (1)
- Enzyme inhibitor (1)
- European Union (EU) (1)
- Federal Constitutional Court (1)
- Festschrift (1)
- German administrative system (1)
- German public administration (1)
- ISM: clouds (1)
- ISM: supernova remnants (1)
- In vitro (1)
- Informationsstruktur (1)
- Institut (1)
- Juvenile hormone (1)
- Juvenile hormone analogue (1)
- Kommunalwissenschaft (1)
- Linguistik (1)
- Morphologie (1)
- Open Access (1)
- Orthoptera (1)
- Potsdam (1)
- Syntax (1)
- Universität (1)
- complement (1)
- decentralisation (1)
- errata, addenda (1)
- federal administration (1)
- festschrift (1)
- flow (1)
- gamma rays: general (1)
- glucose (1)
- governance (1)
- information structure (1)
- institutions (1)
- lactate output (1)
- linguistics (1)
- morphology (1)
- multilevel governance (1)
- pQCT (1)
- patient immobilization (1)
- prostaglandin-f2-alpha (1)
- public administration (1)
- reforms (1)
- self-government (1)
- social security (1)
- syntax (1)
- the Basic Law (1)
- the Federal Ministry of the Interior (BMI) (1)
- the German Constitution (1)
- the German federal architecture (1)
- the Länder (1)
- trabecular bone (1)
Institute
- Institut für Biochemie und Biologie (32)
- Institut für Chemie (9)
- Institut für Physik und Astronomie (9)
- Zentrum für Umweltwissenschaften (6)
- Extern (5)
- Historisches Institut (4)
- Department Sport- und Gesundheitswissenschaften (2)
- Institut für Romanistik (2)
- Lehreinheit für Wirtschafts-Arbeit-Technik (2)
- Referat für Presse- und Öffentlichkeitsarbeit (2)
Brandenburgisches Umweltforschungszentrum e.V.:
Arbeitsgruppe: Nachhaltigkeit ; Arbeitsgruppe: Umwelt- und Biotechnologie ; Arbeitsgruppe: Umweltmanagement ; Arbeitsgruppe: Umweltsoziologie ;
Zentrum für Umweltwissenschaften:
Arbeitsgruppe: Betriebliches Umweltmanagement/Umweltbewußtes Konsumentenverhalten ; Arbeitsgruppe: Grüne Bioraffinerie ; Arbeitsgruppe: Integrierter Arten- und Biotopschutz ; Arbeitsgruppe: LIDAR-Inversionen ; Arbeitsgruppe: FG Ökotechnologie ; Arbeitsgruppe: Regenerative Energien ; Arbeitsgruppe: Stoffdynamik in Geosystemen ; Arbeitsgruppe: Umweltbildung
Projekt: Nachhaltiges Brandenburg ; Projekt: Nachhaltige, umweltgerechte Regionalentwicklung in Ostprignitz-Ruppin ; Projekt: Entwicklung nachhaltiger Landnutzung; Projekt: Integrierte Umweltberatung und ökologische Zielsetzungen im Landkreis; Projekt: Fachinformationssystem Naturschutz und Landschaftspflege des Landesumweltamtes Brandenburg ; Projekt: Umweltverträglichkeitsprüfung ; Projekt: Planung und Projektierung der Abwasserentsorgung im Land Brandenburg (1990-1994)
Myriapods (e. g., centipedes and millipedes) display a simple homonomous body plan relative to other arthropods. All members of the class are terrestrial, but they attained terrestriality independently of insects. Myriapoda is the only arthropod class not represented by a sequenced genome. We present an analysis of the genome of the centipede Strigamia maritima. It retains a compact genome that has undergone less gene loss and shuffling than previously sequenced arthropods, and many orthologues of genes conserved from the bilaterian ancestor that have been lost in insects. Our analysis locates many genes in conserved macro-synteny contexts, and many small-scale examples of gene clustering. We describe several examples where S. maritima shows different solutions from insects to similar problems. The insect olfactory receptor gene family is absent from S. maritima, and olfaction in air is likely effected by expansion of other receptor gene families. For some genes S. maritima has evolved paralogues to generate coding sequence diversity, where insects use alternate splicing. This is most striking for the Dscam gene, which in Drosophila generates more than 100,000 alternate splice forms, but in S. maritima is encoded by over 100 paralogues. We see an intriguing linkage between the absence of any known photosensory proteins in a blind organism and the additional absence of canonical circadian clock genes. The phylogenetic position of myriapods allows us to identify where in arthropod phylogeny several particular molecular mechanisms and traits emerged. For example, we conclude that juvenile hormone signalling evolved with the emergence of the exoskeleton in the arthropods and that RR-1 containing cuticle proteins evolved in the lineage leading to Mandibulata. We also identify when various gene expansions and losses occurred. The genome of S. maritima offers us a unique glimpse into the ancestral arthropod genome, while also displaying many adaptations to its specific life history.
The Northeast German Lowland Observatory (TERENO-NE) was established to investigate the regional impact of climate and land use change. TERENO-NE focuses on the Northeast German lowlands, for which a high vulnerability has been determined due to increasing temperatures and decreasing amounts of precipitation projected for the coming decades. To facilitate in-depth evaluations of the effects of climate and land use changes and to separate the effects of natural and anthropogenic drivers in the region, six sites were chosen for comprehensive monitoring. In addition, at selected sites, geoarchives were used to substantially extend the instrumental records back in time. It is this combination of diverse disciplines working across different time scales that makes the observatory TERENO-NE a unique observation platform. We provide information about the general characteristics of the observatory and its six monitoring sites and present examples of interdisciplinary research activities at some of these sites. We also illustrate how monitoring improves process understanding, how remote sensing techniques are fine-tuned by the most comprehensive ground-truthing site DEMMIN, how soil erosion dynamics have evolved, how greenhouse gas monitoring of rewetted peatlands can reveal unexpected mechanisms, and how proxy data provides a long-term perspective of current ongoing changes.
Myofibrillar myopathy (MFM) is a human disease that is characterized by focal myofibrillar destruction and pathological cytoplasmic protein aggregations. In an extended German pedigree with a novel form of MFM characterized by clinical features of a limb-girdle myopathy and morphological features of MFM, we identified a cosegregating, heterozygous nonsense mutation (8130G -> A; W2710X) in the filamin c gene ( FLNC) on chromosome 7q32.1. The mutation is the first found in FLNC and is localized in the dimerization domain of filamin c. Functional studies showed that, in the truncated mutant protein, this domain has a disturbed secondary structure that leads to the inability to dimerize properly. As a consequence of this malfunction, the muscle fibers of our patients display massive cytoplasmic aggregates containing filamin c and several Z-disk-associated and sarcolemmal proteins
Previous work has shown that mutations in muscle LIM protein (MLP) can cause hypertrophic cardiomyopathy (HCM). In order to gain an insight into the molecular basis of the disease phenotype, we analysed the binding characteristics of wild-type MLP and of the (C58G) mutant MLP that causes hypertrophic cardiomyopathy. We show that MLP can form a ternary complex with two of its previously documented myofibrillar ligand proteins, N-RAP and alpha-actinin, which indicates the presence of distinct, non-overlapping binding sites. Our data also show that, in comparison to wild-type MLP, the capacity of the mutated MLP protein to bind both N-RAP and alpha-actinin is significantly decreased. In addition, this single point mutation prevents zinc coordination and proper folding of the second zinc-finger in the first LIM domain, which consequently renders the protein less stable and more susceptible to proteolysis. The molecular basis for HCM-causing mutations in the MLP gene might therefore be an alteration in the equilibrium of interactions of the ternary complex MLP-N-RAP-alpha-actinin. This assumption is supported by the previous observation that in the pathological situation accompanied by MLP down regulation, cardiomyocytes try to compensate for the decreased stability of MLP protein by increasing the expression of its ligand N-RAP, which might finally result in the development of myocyte disarray that is characteristic of this disease
Xin is a protein that is expressed during early developmental stages of cardiac and skeletal muscles. Immunolocalization studies indicated a peripheral localization in embryonic mouse heart, where Xin localizes with beta- catenin and N-cadherin. In adult tissues, Xin is found primarily in the intercalated discs of cardiomyocytes and the myotendinous junctions of skeletal muscle cells, both specialized attachment sites of the myofibrillar ends to the sarcolemma. A large part of the Xin protein consists of unique 16 amino acid repeats with unknown function. We have investigated the characteristics of the Xin repeats by transfection experiments and actin-binding assays and ascertained that, upon expression in cultured cells, these repeats bind to and stabilize the actin-based cytoskeleton. In vitro co- sedimentation assays with skeletal muscle actin indicated that they not only directly bind actin filaments, but also have the capability of arranging microfilaments into networks that sediment upon low-speed centrifugation. Very similar repeats were also found in Xin-repeat protein 2' (XIRP2), a novel protein that seems to be expressed mainly in striated muscles. Human XIRP2 contains 28 Xin repeats with properties identical to those of Xin. We conclude that the Xin repeats define a novel, repetitive actin-binding motif present in at least two different muscle proteins. These Xin- repeat proteins therefore constitute the first two members of a novel family of actin-binding proteins