TY - JOUR
A1 - Goebel, Werner
A1 - Kreft, Jürgen
T1 - Accumulation of replicative intermediates and catenated forms of the colicinogenic factor E\(_1\) in E. coli during the replication at elevated temperatures
N2 - No abstract available
KW - Biologie
Y1 - 1972
U6 - http://nbn-resolving.de/urn/resolver.pl?urn:nbn:de:bvb:20-opus-60625
ER -
TY - JOUR
A1 - Linsenmair, Karl Eduard
T1 - Anemomenotactic orientation in beetles and scorpions
N2 - Scorpions, living in North African semideserts are - in spite of disrupting experimental interferences - able to maintain a certain direction in their natural environment in the dark on a plane surface. Under comparable laboratory conditions, excluding the possibility of light or gravity orientation, they can orient themselves if a directed air current passes over the "arena." In most cases the scorpions do not run necessarily with or against the wind, but rather maintain constant angles to the air current for anywhere from minutes to many hours. They are running anemomenotactically (ref. 1). Under identical conditions many species of beetles also orient themselves to air currents (refs. 2 to 4). The main problems to be solved in the study of anemomenotactic orientation are: (1) Which physical qualities of the air current have an influence on the anemomenotaxis? (2) With which sense organs do beetles and scorpions perceive wind directions? (3) Which physiological mechanism is the basis of anemomenotactic orientation? (4) What is the biological significance of anemomenotaxis in beetles and scorpions? With respect to these problems, more study has been done on beetles than on scorpions. Therefore, due to lack of space, I shall discuss mainly some of the results obtained in experiments with dung beetles (Geotrupes silvaticus, G. ,Stercorarius, G. armifrons, G. niger, Scarabaeus variolosus) and tenebrionid beetles (Tenebrio molitor, Pimelia grossa, P. tenuicomis, Scaurus dubius).
KW - Biologie
KW - Skorpion
KW - Käfer
Y1 - 1972
U6 - http://nbn-resolving.de/urn/resolver.pl?urn:nbn:de:bvb:20-opus-78118
ER -
TY - JOUR
A1 - Kreft, Jürgen
A1 - Burger, Klaus J.
A1 - Goebel, Werner
T1 - Expression of antibiotic resistance genes from Escherichia coli in Bacillus subtilis
N2 - Bifunctional recombinant plasmids were constructed, comprised of the E. coli vectors pBR322, pBR325 and pACYC184 and different plasmids from Gram-positive bacteria, e.g. pBSU161-1 of B. subtilis and pUB110 and pC221 of S. aureus. The beta-lactamase (bla) gene and the chloramphenicol acetyltransferase (cat) gene from the E. coli plasmids were not transcribed and therefore not expressed in B. subtilis. However, tetracycline resistance from the E. coli plasmids was expressed in B. subtilis. Transcription of the tetracycline resistance gene(s) started in B. subtilis at or near the original E. coli promoter, the sequence of which is almost identical with the sequence recognized by σ55 of B. subtilis RNA polymerase.
KW - Biologie
Y1 - 1983
U6 - http://nbn-resolving.de/urn/resolver.pl?urn:nbn:de:bvb:20-opus-60600
ER -
TY - JOUR
A1 - Kreft, Jürgen
A1 - Berger, Harald
A1 - Härtlein, Michael
A1 - Müller, Bodo
A1 - Weidinger, Gerhard
A1 - Goebel, Werner
T1 - Cloning and expression in Escherichia coli and Bacillus subtilis of the hemolysin (cereolysin) determinant from Bacillus cereus
N2 - From a cosmid gene bank of Bacillus cereus GP4 in Escherichia coli we isolated clones which, after several days of incubation, formed hemolysis zones on erythrocyte agar plates. These clones contained recombinant cosmids with B. cereus DNA insertions of varying lengths which shared some common restriction fragments. The smallest insertionwas recloned as aPstl fragment into pJKK3-1, a shuttle vector which repücates in Bacillus subtilis and E. coli. When this recombinant plasmid (pJKK3-1 hly-1) was transformed into E. coli, it caused hemolysis on erythrocyte agar plates, but in liquid assays no extemal or intemal hemolytic activity could be detected with the E. coli transformants. B. subtilis carrying the same plasmid exhibited hemolytic activity at Ievels comparable to those ofthe B. cereus donor strain. The hemolysin produced in B. subtilis seemed to be indistinguishable from cereolysin in its sensitivity to cholesterol, activation by dithiothreitol, and inactivation by antibodies raised against cereolysin. When the recombinant DNA carrying the cereolysin gene was used as a probe in hybridization experiments with chromosomal DNA from a streptolysin 0-producing strain of Streptococcus pyogenes or from üsteriolysin-producing strains of Usteria monoeytogenes, no positive hybridization signals were obtained. These data soggest that the genes for these three SH-activated cytolysins do not have extended sequence homology.
KW - Biologie
Y1 - 1983
U6 - http://nbn-resolving.de/urn/resolver.pl?urn:nbn:de:bvb:20-opus-60596
ER -
TY - JOUR
A1 - Härtlein, Michael
A1 - Schiessl, Sigrid
A1 - Wagner, Wilma
A1 - Rdest, Ursula
A1 - Kreft, Jürgen
A1 - Goebel, Werner
T1 - Transport of hemolysin by Escherichia coli
N2 - No abstract available
KW - Biologie
KW - Hemolysin
KW - Escberichia coli
KW - Gene cloning
KW - Expression
KW - Transport
Y1 - 1983
U6 - http://nbn-resolving.de/urn/resolver.pl?urn:nbn:de:bvb:20-opus-60619
ER -
TY - JOUR
A1 - Hoppe, J.
A1 - Sebald, Walter
T1 - The proton conducting F0-part of bacterial ATP synthases
N2 - No abstract available
KW - Biologie
Y1 - 1984
U6 - http://nbn-resolving.de/urn/resolver.pl?urn:nbn:de:bvb:20-opus-82019
ER -
TY - JOUR
A1 - Goebel, Werner
A1 - Chakraborty, T.
A1 - Kreft, Jürgen
T1 - Bacterial hemolysins as virulence factors
N2 - No abstract available
KW - Biologie
Y1 - 1988
U6 - http://nbn-resolving.de/urn/resolver.pl?urn:nbn:de:bvb:20-opus-60553
ER -
TY - JOUR
A1 - Goebel, Werner
A1 - Kathariou, S.
A1 - Kuhn, M.
A1 - Sokolovic, Z.
A1 - Kreft, Jürgen
A1 - Köhler, S.
A1 - Funke, D.
A1 - Chakraborty, T.
A1 - Leimeister-Wächter, M.
T1 - Hemolysin from Listeria-biochemistry, genetics and function in pathogenesis
N2 - No abstract available
KW - Biologie
Y1 - 1988
U6 - http://nbn-resolving.de/urn/resolver.pl?urn:nbn:de:bvb:20-opus-60563
ER -
TY - JOUR
A1 - Linsenmair, Karl Eduard
A1 - Schmuck, R.
T1 - Adaptations of the reed frog Hyperbolius viridiflavus to its arid environment. III. Aspects of nitrogen metabolism and osmuregulation in the reed frog, H. viridiflavus taeniatus, with special reference to the role of iridophores
N2 - Reed frogs of the superspecies Hyperolius viridiflavus occur throughout the seasonally very dry and hot African savannas. Despite their small size (300-700 mg), estivating reed frogs do not avoid stressful conditions above ground by burrowing into the soil, but endure the inhospitable climate relatively unprotected, clinging to mostly dry grass sterns. They must have emcient mechanisms to enable them to survive e.g. very high temperatures, low relative hurnidities, and high solar radiation loads. Mechanisms must also have developed to prevent poisoning by the nitrogenous wastes that inevitably result from protein and nucleotide turnover. In contrast to fossorial amphibians, estivating reed frogs do not become torpid. Reduction in metabolism is therefore rather Iimited so that nitrogenous wastes accumulate faster in these frogs than in fossorial amphibians. This severely aggravates the osmotic problems caused by dehydration. During dry periods total plasma osmolarity greatly increases, mainly due to urea accumulation. Of the total urea accumulated over 42 days of experimental water deprivation, 30% was produced during the first 7 days. In the next 7 days rise in plasma urea content was negligible. This strong initial increase of urea is seen as a byproduct of elevated amino acid catabolism following the onset of dry conditions. Tbe rise in total plasma osmolarity due to urea accumulation, however, is not totally disadvantageous, but enables fast rehydration when water is available for very short periods only. Voiding of urine and feces eeases once evaporative water loss exceeds 10% of body weight. Tberefore, during continuous water deprivation, nitrogenous end products are not excreted. After 42 days of water deprivation, bladder fluid was substantially depleted, and urea coneentration in the remaining urine (up to 447 mM) was never greater than in plasma fluid. Feces voided at the end of the dry period after water uptake contained only small amounts of nitrogenous end products. DSF (dry season frogs) seemed not to be uricotelic. Instead, up to 35% of the total nitrogenous wastes produced over 42 days of water deprivation were deposited in an osmotically inert and nontoxic form in iridophore crystals. The increase in skin purine content averaged 150 µg/mg dry weight. If urea had been the only nitrogenous waste product during an estivation period of 42 days, lethal limits of total osmolarity (about 700 mOsm) would have been reached 10-14 days earlier. Thus iridophores are not only involved in colour change and in reducing heat load by radiation remission, but are also important in osmoregulation during dry periods. The seIective advantages of deposition of guanine rather than uric acid are discussed.
KW - Biologie
KW - Zoologie
KW - Frosch
KW - Hyperolius viridiflavus
KW - Estivation
KW - Osmoregulation
KW - Nitrogen metabolism
KW - lridophores
Y1 - 1988
U6 - http://nbn-resolving.de/urn/resolver.pl?urn:nbn:de:bvb:20-opus-78108
ER -
TY - JOUR
A1 - Schmuck, R.
A1 - Kobelt, F.
A1 - Linsenmair, Karl Eduard
T1 - Adaptations of the reed frog Hyperbolius viridiflavus (Anura, Hyperbolidae) to its arid environment: V. Iridophores and nitrogen metabolism
N2 - Ofall amphibians living in arid habitats, reed frogs (belonging to the super species Hyperolius viridiflavus) are the most peculiar. Froglets are able to tolerate dry periods of up to 35 days or longer immediately after metamorphosis, in climatically exposed positions. They face similar problems to estivating juveniles, i.e. enduranee of long periods of high temperature and low RH with rather limited energy and water reserves. In addition, they must have had to develop meehanisms to prevent poisoning by nitrogenous wastes that rapidly accumulate during dry periods as a metabolie consequenee of maintaining a non-torpid state. During dry periods, plasma osmolarity of H. v. taeniatus froglets strongly increased, mainly through urea accumulation. Urea accumulation was also observed during metamorphic climax. During postmetamorphic growth, chromatophores develop with the density and morphology typical of the adult pigmentary pattern. The dermal iridophore layer, which is still incomplete at this time, is fully developed within 4-8 days after metamorphosis, irrespective of maintenance conditions. These iridophores mainly contain the purines guanine and hypoxanthine. The ability of these purines to reflect light provides an excellent basis for the role of iridophores in temperature regulation. In individuals experiencing dehydration stress, the initial rate of purine synthesis is doubled in eomparison to specimens continuously maintained under wet season conditions. This increase in synthesis rate leads to a rapid increase in the thiekness of the iridophore layer, thereby effectively reducing radiation absorption. Thus, the danger of overheating is diminished during periods of water shortage when evaporative cooling must be avoided. After the development of an iridophore layer of sufficient thickness for effective radiation reflectance, synthesis of iridophore pigments does not cease. Rather, this pathway is further used during the remaining dry season for solving osmotic problems eaused by accumulation of nitrogenous wastes. During prolonged water deprivation, in spite of reduced metabolic rates, purine pigments are produced at the same rate as in wet season conditions. This leads to a higher relative proportion of nitrogen end products being stored in skin pigments under dry season conditions. At the end of an experimental dry season lasting 35 days, up to 38% of the accrued nitrogen is stored in the form of osmotically inactive purines in thc skin. Thus the osmotic problems caused by evaporative water loss and urea production are greatly reduced.
KW - Biologie
KW - Zoologie
KW - Frosch
Y1 - 1988
U6 - http://nbn-resolving.de/urn/resolver.pl?urn:nbn:de:bvb:20-opus-78094
ER -
TY - JOUR
A1 - Kreft, Jürgen
A1 - Funke, Dorothee
A1 - Haas, Albert
A1 - Lottspeich, Friedrich
A1 - Goebel, Werner
T1 - Production, purification and characterization of hemolysins from Listeria ivanovii and Listeria monocytogenes Sv4b.
N2 - In culture supematants of both Listeria ivanovii and Listeria monocytogenes Sv4b, for the first time a hemolysin of molecular weight 58 kDa was identified, which had all the characteristics of an SH-activated cytolysin, and which was therefore identified as Iisteriolysin 0 (LLO). In the case of L. ivanovii a second major supematant protein of molecular weight 24 kDa co-purified with LLO. However, the function of this protein has to be determined. In culture supematants of L. ivanovii a sphingomyelinase and a Iecithinase activity could be detected, both enzymatic activities together contributing to the pronounced hemolysis caused by L. ivanovii. The N-tenninal amino acid sequences of LLO and the 24 kDa from L. ivanovii are shown.
KW - Biologie
KW - Hemolysin
KW - Listeria
Y1 - 1989
U6 - http://nbn-resolving.de/urn/resolver.pl?urn:nbn:de:bvb:20-opus-60545
ER -
TY - JOUR
A1 - Gilmore, Michael S.
A1 - Cruz-Rodz, Armando L.
A1 - Leimeister-Wächter, Michaela
A1 - Kreft, Jürgen
A1 - Goebel, Werner
T1 - A Bacillus cereus cytolytic determinant, cereolysin AB, which comprises the phospholipase C and sphingomyelinase genes: nucleotide sequence and genetic linkage
N2 - A cloned cytolytic determinant from the genome of Bacillus cereus GP-4 has been characterized at the molecular Ievel. Nucleotide sequence determination revealed the presence of two open reading frames. 8oth open reading frames were found by deletion and complementation analysis to be necessary for expression of the hemolytic phenotype by Bacillus subtilis and Escherichia coli hosts. The 5' open reading frame was found to be nearly identical to a recently reported phospholipase C gene derived from a mutant B. cereus strain which overexpresses the respective protein, and it conferred a lecithinase-positive phenotype to the B. subtilis host. The 3' open reading frame encoded a sphingomyelinase. The two tandemly encoded activities, phospholipase C and sphingomyelinase, constitute a biologically functional cytolytic determinant of B. cereus termed cereolysin AB.
KW - Biologie
Y1 - 1989
U6 - http://nbn-resolving.de/urn/resolver.pl?urn:nbn:de:bvb:20-opus-60588
ER -
TY - JOUR
A1 - Haas, Albert
A1 - Brehm, Klaus
A1 - Kreft, Jürgen
A1 - Goebel, Werner
T1 - Cloning, characterization, and expression in Escherichia coli of a gene encoding Listeria seeligeri catalase, a bacterial enzyme highly homologous to mammalian catalases
N2 - A gene coding for catalase (hydrogen-peroxide:hydrogen-peroxide oxidoreductase; EC 1.11.1.6) of the grain-positive bacterium Listeria seeligeri was cloned from a plasmid library of EcoRI-digested chromosomal DNA, with Escherichia coli DHSa as a host. The recombinant catalase was expressed in E. coli to an enzymatic activity approximately SO times that of the combined E. coli catalases. The nucleutide sequence was determined, and the deduced amino acid sequence revealed 43.2% amino acid sequence identity between bovine liver catalase and L. seeligeri catalase. Most of the amino acid residues which are involved in catalytic activity, the formation of the active center accession channel, and heme binding in bovine liver catalase were also present in L. seeligeri catalase at the corresponding positions. The recombinant protein contained 488 amino acid residues and had a calculated molecular weight of 55,869. The predicted isoelectric point was 5.0. Enzymatic and genetic analyses showed that there is most probably a single catalase of this type in L. seeligeri. A perfect 21-bp inverted repeat, which was highly homologous to previously reported binding sequences of the Fur (ferric uptake regulon) protein of E. coli, was detected next to the putative promoter region of tbe L. seeligeri catalase gene.
KW - Biologie
Y1 - 1991
U6 - http://nbn-resolving.de/urn/resolver.pl?urn:nbn:de:bvb:20-opus-60536
ER -
TY - JOUR
A1 - Schülein, Ralf
A1 - Kreft, Jürgen
A1 - Gonski, Sigrid
A1 - Goebel, Werner
T1 - Preprosubtilisin Carlsberg processing and secretion is blocked after deletion of amino acids 97-101 in the mature part of the enzyme
N2 - During an investigation into the substrate specificity and processing of subtilisin Carlsberg from Bacillus licheniformis, two major independent findings were made: (i) as has been shown previously, a stretch of five amino acids (residues 97-101 of the mature enzyme) that loops out into the binding cleft is involved in substrate binding by subtilisin Carlsberg. In order to see whether this loop element also determines substrate specificity, the coding region for these five amino acids was deleted from the cloned gene for subtilisin Carlsberg by site-directed mutagenesis. Unexpectedly the resulting mutant preproenzyme (P42c, Mr=42 kDa) was not processed to the mature form (Mr = 30 kDa) and was not released into the medium by a proteasedeficient B. subtilis host strain; rather, it accumulated in the cell membrane. This result demonstrates that the integrity of this loop element, which is very distant from the processing cleavage sites in the preproenzyme, is required for secretion of subtilisin Carlsberg. (ii) In culture supernatants from B. subtilis harbouring the cloned wild-type subtilisin Carlsberg gene the transient appearance (at 0-3 h after onset of stationary phase) of a processing intermediate (P38c, Mr = 38 kDa) oftbis protease could be demonstrated. P38c very probably represents a genuine proform of subtilisin Carlsberg.
KW - Biologie
KW - Bacillus
KW - Proenzyme
KW - Subtilisin maturation
KW - Site-directed mutagenesis
KW - Subtilisin Carlsberg
Y1 - 1991
U6 - http://nbn-resolving.de/urn/resolver.pl?urn:nbn:de:bvb:20-opus-60577
ER -
TY - JOUR
A1 - Brehm, Klaus
A1 - Haas, Albert
A1 - Goebel, Werner
A1 - Kreft, Jürgen
T1 - A gene encoding a superoxide dismutase of the facultative intracellular bacterium Listeria monocytogenes
N2 - A gene (Imsod) encoding superoxide dismutase (SOD; EC 1.15.1.1) of the facultative intracellular pathogen, Listeria monocytogenes, was cloned by functional complementation of an SOD-deficient Escherichia coli mutant. The nucleotide sequence was determined and the deduced amino acid (aa) sequence (202 aa) showed close similarity to manganese-containing SOD's from other organisms. Subunits of the recombinant L. monocytogenes SOD (re-SOD) and of both E. coli SODs formed enzymatically active hybrid enzymes in vivo. DNA/DNA-hybridization experiments showed that this type of recombinant re-sod gene is conserved within the genus Listeria.
KW - Biologie
Y1 - 1992
U6 - http://nbn-resolving.de/urn/resolver.pl?urn:nbn:de:bvb:20-opus-60515
ER -
TY - JOUR
A1 - Haas, Albert
A1 - Dumbsky, Martina
A1 - Kreft, Jürgen
T1 - Listeriolysin genes: complete sequence of ilo from Listeria ivanovii and of lso from Listeria seeligeri
N2 - The completc DNA scqucnccs coding for thc thiol-activated cytolysins from Listeria ivanovii, ivanolysin 0 (ILO) and for sccligerolysin 0 (LSO) from Listeria seeligeri have been dctermined. Thc deduced amino acid scquences revealed that: (i) the primary translation products comprise 528 (ILO) and 530 (LSO) amino acids. respectively. (ii) ILO contains two cysteines. LSO has a substitution in the conserved cysteine motif.
KW - Biologie
KW - Thiol-activated cytolysin
KW - Listeriolysin O
KW - Cysteine: motif
KW - ( L. ivanovii )
KW - ( L. selligeri)
Y1 - 1992
U6 - http://nbn-resolving.de/urn/resolver.pl?urn:nbn:de:bvb:20-opus-60529
ER -
TY - JOUR
A1 - Lampidis, Robert
A1 - Gross, Roy
A1 - Sokolovic, Zeljka
A1 - Goebel, Werner
A1 - Kreft, Jürgen
T1 - The virulence regulator protein of Listeria ivanovii is highly homologous to PrfA from Listeria monocytogenes and both belong to the Crp-Fnr family of transcription regulators
N2 - No abstract available
KW - Biologie
Y1 - 1994
U6 - http://nbn-resolving.de/urn/resolver.pl?urn:nbn:de:bvb:20-opus-60503
ER -
TY - JOUR
A1 - Albrecht, Marco
A1 - Sharma, Cynthia M.
A1 - Reinhardt, Richard
A1 - Vogel, Joerg
A1 - Rudel, Thomas
T1 - Deep sequencing-based discovery of the Chlamydia trachomatis transcriptome
N2 - Chlamydia trachomatis is an obligate intracellular pathogenic bacterium that has been refractory to genetic manipulations. Although the genomes of several strains have been sequenced, very little information is available on the gene structure of these bacteria. We used deep sequencing to define the transcriptome of purified elementary bodies (EB) and reticulate bodies (RB) of C. trachomatis L2b, respectively. Using an RNAseq approach, we have mapped 363 transcriptional start sites (TSS) of annotated genes. Semiquantitative analysis of mapped cDNA reads revealed differences in the RNA levels of 84 genes isolated from EB and RB, respectively. We have identified and in part confirmed 42 genome- and 1 plasmid-derived novel non-coding RNAs. The genome encoded non-coding RNA, ctrR0332 was one of the most abundantly and differentially expressed RNA in EB and RB, implying an important role in the developmental cycle of C. trachomatis. The detailed map of TSS in a thus far unprecedented resolution as a complement to the genome sequence will help to understand the organization, control and function of genes of this important pathogen.
KW - Biologie
Y1 - 2010
U6 - http://nbn-resolving.de/urn/resolver.pl?urn:nbn:de:bvb:20-opus-68389
ER -
TY - JOUR
A1 - Koetschan, Christian
A1 - Foerster, Frank
A1 - Keller, Alexander
A1 - Schleicher, Tina
A1 - Ruderisch, Benjamin
A1 - Schwarz, Roland
A1 - Mueller, Tobias
A1 - Wolf, Matthias
A1 - Schultz, Joerg
T1 - The ITS2 Database III-sequences and structures for phylogeny
N2 - The internal transcribed spacer 2 (ITS2) is a widely used phylogenetic marker. In the past, it has mainly been used for species level classifications. Nowadays, a wider applicability becomes apparent. Here, the conserved structure of the RNA molecule plays a vital role. We have developed the ITS2 Database (http://its2.bioapps .biozentrum.uni-wuerzburg.de) which holds information about sequence, structure and taxonomic classification of all ITS2 in GenBank. In the new version, we use Hidden Markov models (HMMs) for the identification and delineation of the ITS2 resulting in a major redesign of the annotation pipeline. This allowed the identification of more than 160 000 correct full ength and more than 50 000 partial structures. In the web interface, these can now be searched with a modified BLAST considering both sequence and structure, enabling rapid taxon sampling. Novel sequences can be annotated using the HMM based approach and modelled according to multiple template structures. Sequences can be searched for known and newly identified motifs. Together, the database and the web server build an exhaustive resource for ITS2 based phylogenetic analyses.
KW - Biologie
Y1 - 2010
U6 - http://nbn-resolving.de/urn/resolver.pl?urn:nbn:de:bvb:20-opus-68390
ER -
TY - JOUR
A1 - Göb, Eva
A1 - Meyer-Natus, Elisabeth
A1 - Benavente, Ricardo
A1 - Alsheimer, Manfred
T1 - Expression of individual mammalian Sun1 isoforms depends on the cell type
N2 - Mammalian Sun1 belongs to an evolutionarily conserved family of inner nuclear membrane proteins, which are known as SUN domain proteins. SUN domain proteins interact with KASH domain partners to form bridging complexes, so-called LINC complexes, that physically connect the nuclear interior to the cytoskeleton. LINC complexes are critical for nuclear integrity and play fundamental roles in nuclear positioning, shaping and movement. The mammalian genome codes for at least five different SUN domain proteins used for the formation of a number of different LINC complexes. Recently, we reported on the identification of everal Sun1 isoforms, which tremendously enlarges the alternatives to form functional LINC complexes. We now confirmed that Sun1 actually exists in at least seven distinct splice variants. Besides that, we observed that expression of individual Sun1 isoforms remarkably depends on the cell type, suggesting a cell type-specific adaption of Sun1 dependent LINC complexes to specific cellular and physiological requirements.
KW - Biologie
KW - Sun1
KW - SUN domain protein
KW - LINC complex
KW - mouse
KW - nuclear envelope
KW - isoform
Y1 - 2011
U6 - http://nbn-resolving.de/urn/resolver.pl?urn:nbn:de:bvb:20-opus-68750
ER -