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  • 1
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    A potentiostat featuring an integrator transimpedance amplifier for the measurement of very low currents—Proof-of-principle application in microfluidic separations and voltammetry (2016)
    American Institute of Physics (AIP)
    Details
    Publication Date: 2016-03-05
    Description: This work reports the design and construction of a novel potentiostat which features an integrator transimpedance amplifier as a current-monitoring unit. The integration approach addresses the limitations of the feedback resistor approach used for current monitoring in conventional potentiostat designs. In the present design, measurement of the current is performed by a precision switched integrator transimpedance amplifier operated in the dual sampling mode which enables sub-pA resolution. The potentiostat is suitable for measuring very low currents (typical dynamic range: 5 pA–4.7 μ A) with a 16 bit resolution, and it can support 2-, 3- and 4-electrode cell configurations. Its operation was assessed by using it as a detection module in a home-made capillary electrophoresis system for the separation and amperometric detection of paracetamol and p -aminophenol at a 3-electrode microfluidic chip. The potential and limitations of the proposed potentiostat to implement fast potential-scan voltammetric techniques were demonstrated for the case of cyclic voltammetry.
    Print ISSN: 0034-6748
    Electronic ISSN: 1089-7623
    Topics: Electrical Engineering, Measurement and Control Technology , Physics
    Published by American Institute of Physics (AIP)
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  • 2
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    Structural biology: Clamour for a kiss (2008)
    Nature Publishing Group (NPG)
    Details
    Publication Date: 2008-10-17
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Economou, Anastassios -- England -- Nature. 2008 Oct 16;455(7215):879-80. doi: 10.1038/455879a.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/18923500" target="_blank"〉PubMed〈/a〉
    Keywords: Adenosine Triphosphatases/*chemistry/*metabolism ; Adenosine Triphosphate/metabolism ; Bacteria/chemistry/cytology/metabolism ; Bacterial Proteins/*chemistry/*metabolism ; Cell Membrane/metabolism ; Crystallography, X-Ray ; Membrane Transport Proteins/*chemistry/*metabolism ; Molecular Motor Proteins/chemistry/metabolism ; Protein Conformation ; Protein Transport
    Print ISSN: 0028-0836
    Electronic ISSN: 1476-4687
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Published by Nature Publishing Group (NPG)
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  • 3
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    Signal peptides are allosteric activators of the protein translocase (2009)
    Nature Publishing Group (NPG)
    Details
    Publication Date: 2009-11-20
    Description: Extra-cytoplasmic polypeptides are usually synthesized as 'preproteins' carrying amino-terminal, cleavable signal peptides and secreted across membranes by translocases. The main bacterial translocase comprises the SecYEG protein-conducting channel and the peripheral ATPase motor SecA. Most proteins destined for the periplasm and beyond are exported post-translationally by SecA. Preprotein targeting to SecA is thought to involve signal peptides and chaperones like SecB. Here we show that signal peptides have a new role beyond targeting: they are essential allosteric activators of the translocase. On docking on their binding groove on SecA, signal peptides act in trans to drive three successive states: first, 'triggering' that drives the translocase to a lower activation energy state; second, 'trapping' that engages non-native preprotein mature domains docked with high affinity on the secretion apparatus; and third, 'secretion' during which trapped mature domains undergo several turnovers of translocation in segments. A significant contribution by mature domains renders signal peptides less critical in bacterial secretory protein targeting than currently assumed. Rather, it is their function as allosteric activators of the translocase that renders signal peptides essential for protein secretion. A role for signal peptides and targeting sequences as allosteric activators may be universal in protein translocases.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2823582/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2823582/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gouridis, Giorgos -- Karamanou, Spyridoula -- Gelis, Ioannis -- Kalodimos, Charalampos G -- Economou, Anastassios -- GM73854/GM/NIGMS NIH HHS/ -- R01 GM073854/GM/NIGMS NIH HHS/ -- R01 GM073854-03/GM/NIGMS NIH HHS/ -- England -- Nature. 2009 Nov 19;462(7271):363-7. doi: 10.1038/nature08559.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institute of Molecular Biology and Biotechnology, Foundation of Research and Technology-Hellas, Iraklio, Crete 71110, Greece.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/19924216" target="_blank"〉PubMed〈/a〉
    Keywords: Adenosine Triphosphatases/metabolism ; Alkaline Phosphatase/metabolism ; Enzyme Activators/*metabolism ; Escherichia coli/*enzymology ; Escherichia coli Proteins/*metabolism ; Periplasmic Proteins/metabolism ; Protein Binding ; Protein Sorting Signals/*physiology ; Protein Transport
    Print ISSN: 0028-0836
    Electronic ISSN: 1476-4687
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Published by Nature Publishing Group (NPG)
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  • 4
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    Structural basis for protein antiaggregation activity of the trigger factor chaperone (2014)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2014-05-09
    Description: Molecular chaperones prevent aggregation and misfolding of proteins, but scarcity of structural data has impeded an understanding of the recognition and antiaggregation mechanisms. We report the solution structure, dynamics, and energetics of three trigger factor (TF) chaperone molecules in complex with alkaline phosphatase (PhoA) captured in the unfolded state. Our data show that TF uses multiple sites to bind to several regions of the PhoA substrate protein primarily through hydrophobic contacts. Nuclear magnetic resonance (NMR) relaxation experiments show that TF interacts with PhoA in a highly dynamic fashion, but as the number and length of the PhoA regions engaged by TF increase, a more stable complex gradually emerges. Multivalent binding keeps the substrate protein in an extended, unfolded conformation. The results show how molecular chaperones recognize unfolded polypeptides and, by acting as unfoldases and holdases, prevent the aggregation and premature (mis)folding of unfolded proteins.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4070327/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4070327/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Saio, Tomohide -- Guan, Xiao -- Rossi, Paolo -- Economou, Anastassios -- Kalodimos, Charalampos G -- GM073854/GM/NIGMS NIH HHS/ -- R01 GM073854/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2014 May 9;344(6184):1250494. doi: 10.1126/science.1250494.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Center for Integrative Proteomics Research and Department of Chemistry and Chemical Biology, Rutgers University, Piscataway, NJ 08854, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/24812405" target="_blank"〉PubMed〈/a〉
    Keywords: Alkaline Phosphatase/*chemistry ; Binding Sites ; Escherichia coli Proteins/*chemistry ; Hydrophobic and Hydrophilic Interactions ; Intrinsically Disordered Proteins/*chemistry ; Molecular Chaperones/*chemistry ; Nuclear Magnetic Resonance, Biomolecular ; Peptides/chemistry ; Peptidylprolyl Isomerase/*chemistry ; Protein Binding ; *Protein Folding ; Protein Structure, Secondary ; Protein Structure, Tertiary
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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  • 5
    Electronic Resource
    Electronic Resource
    Multiple-soliton solutions of Einstein's equations (1989)
    College Park, Md. : American Institute of Physics (AIP)
    Journal of Mathematical Physics 30 (1989), S. 1562-1569 
    Details
    ISSN: 1089-7658
    Source: AIP Digital Archive
    Topics: Mathematics , Physics
    Notes: Using the Belinsky–Zakharov generating technique and a flat metric as a seed, two- and four-soliton solutions of the Einstein vacuum equations for the cases of stationary axisymmetric, cylindrically symmetric, or plane symmetric gravitational fields are considered. Three- and five-parameter classes of exact solutions are obtained, some of which are new.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1063/1.528597
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  • 6
    Electronic Resource
    Electronic Resource
    Molecular characterization of the nodulation gene, nodT, from two biovars of Rhizobium leguminosarum (1990)
    Oxford, UK : Blackwell Publishing Ltd
    Molecular microbiology 4 (1990), S. 0 
    Details
    ISSN: 1365-2958
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology , Medicine
    Notes: DNA sequencing of the nodlJ region from Rhizobium leguminosarum biovar trifolii revealed the nodT gene immediately downstream of nodJ. DNA hybridizations using a nodT-specific probe showed that nodT is present in several R. leguminosarum strains. Interestingly, a flavonoid-inducible nodT gene homologue in R. leguminosarum bv. viciae is not in the nodABCIJ operon but is located downstream of nodMN. The sequence of the nodT gene from bv. viciae was determined and a comparison of the predicted aminoacid sequences of the two nodT genes shows them to be conserved; the predicted protein sequences appear to have a potential transit sequence typical of outer-membrane proteins. Mutations affecting nodT in either biovar had no observed effect on nodulation of the legumes tested.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2958.1990.tb00591.x
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  • 7
    Electronic Resource
    Electronic Resource
    Transcription of rhiA, a gene on a Rhizobium leguminosarum bv. viciae Sym plasmid, requires rhiR and is repressed by flavanoids that induce nod genes (1989)
    Oxford, UK : Blackwell Publishing Ltd
    Molecular microbiology 3 (1989), S. 0 
    Details
    ISSN: 1365-2958
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology , Medicine
    Notes: Strains of Rhizobium leguminosarum biovar viciae specifically make an abundant protein (Rhi) in free-living culture but not in bacteroids. Genes needed for Rhi synthesis are on a Sym plasmid and here we show that one of these genes, rhiA, is the structural gene that specifies this polypeptide. Transcription of rhiA requires a regulatory gene, rhiR, located close to rhiA and to nod genes involved in nodulation. Mutations in rhiA or rhiR do not appear to affect symbiotic nitrogen fixation. Transcription of rhiA is repressed in cells grown in the presence of the flavanone hesperetin or the flavone apigenin, both of which are potent inducers of transcription of nod genes. This was deduced from the use of rhiA-lacZ fusions; however, when the Rhi polypeptide was detected in SDS gels, there was no apparent difference in the intensity of its staining in extracts obtained from cells grown with or without these flavanoid nod gene inducer molecules. However, a mutation in a nodulation gene, nolR, also closely linked to the nod and rhi genes, caused a severe depression in the amount of Rhi (as seen on gels) that was made in cells grown in the presence of inducer flavanoids.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2958.1989.tb00107.x
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  • 8
    Electronic Resource
    Electronic Resource
    Secretion of the Rhizobium leguminosarum nodulation protein NodO by haemolysin-type systems (1992)
    Oxford, UK : Blackwell Publishing Ltd
    Molecular microbiology 6 (1992), S. 0 
    Details
    ISSN: 1365-2958
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology , Medicine
    Notes: The Rhizobium leguminosarum biovar viciae nodulation protein NodO is partially homologous to haemolysin of Escherichia coli and, like haemolysin, is secreted into the growth medium. The NodO protein can be secreted by a strain of E. coli carrying the cloned nodO gene plus the haemolysin secretion genes hlyBD, in a process that also requires the outer membrane protein encoded by tolC. The related protease secretion genes, prtDEF, from Erwinia chrysanthemi also enable E. coli to secrete NodO. The Rhizobium genes encoding the proteins required for NodO secretion are unlinked to nodO and are unlike other nod genes, since they do not require flavonoids or NodO for their expression. Although proteins similar to NodO were not found in rhizobia other than R. leguminosarum bv. viciae, several rhizobia and an Agrobacterium strain containing the cloned nodO gene were found to have the ability to secrete NodO. These observations indicate that a wide range of the Rhizobiaceae have a protein secretion mechanism analogous to that which secretes haemotysin and related toxins and proteases in the Enterobacteriaceae.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2958.1992.tb02004.x
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  • 9
    Electronic Resource
    Electronic Resource
    Reproductive strategies and early development of three freshwater gobies (1993)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of fish biology 42 (1993), S. 0 
    Details
    ISSN: 1095-8649
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Three species of gobiid fish inhabit the freshwater Lake Trichonis of western Greece. Two of these species, Economidichthys pygmaeus and E. trichonis are endemic, and the third is the widespread Knipowitschia caucasica. There are habitat separations between the three species, E. pygmaeus and E. trichonis prefer vegetated areas, the first being fully demersal at all stages of development and the second being semi-demersal. Knipowitschia caucasica prefers sandy bottoms and is distributed in shallower waters. Female E. pygmaeus and E. trichonis spawn in nests prepared by the males in the cavities of broken reeds. The males subsequently guard the eggs until they hatch, with females playing no role in parental care. Economidichthys trichonis is probably the smallest freshwater European species. Its eggs are ovoid, measuring about 0.64 × 0.58 mm, from which tiny, unpigmented and incompletely developed pelagic larvae hatch out after an incubation period lasting less than 1 day at a water temperature of 19.5° C. The eggs of E. pygmaeus are cylindrical and larger, measuring about 2.38 × 0.89 mm, from which relatively large, strongly pigmented and ontogenetically more advanced larvae hatch out after a longer incubation period. Both species reproduce only once in their lifetime, at the age of 1 year, and die shortly after spawning, but the breeding season involves several spawnings by each individual fish. These biological, developmental and reproductive characteristics are discussed in relation to current theories on evolution of life-historics.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1095-8649.1993.tb00382.x
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  • 10
    Electronic Resource
    Electronic Resource
    Freshwater larval fish from Lake Trichonis (Greece) (1994)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of fish biology 45 (1994), S. 0 
    Details
    ISSN: 1095-8649
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: The larvae of 15 freshwater fish species from Lake Trichonis (western Greece) are described from field samples and laboratory-raised fish. Larval morphologies are compared to identify distinguishing characters. The potential utility of these data sets for assessing phylogenetic relationships is discussed.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1095-8649.1994.tb01283.x
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