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  • 1
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    Structure of a glycerol-conducting channel and the basis for its selectivity (2000)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2000-10-20
    Description: Membrane channel proteins of the aquaporin family are highly selective for permeation of specific small molecules, with absolute exclusion of ions and charged solutes and without dissipation of the electrochemical potential across the cell membrane. We report the crystal structure of the Escherichia coli glycerol facilitator (GlpF) with its primary permeant substrate glycerol at 2.2 angstrom resolution. Glycerol molecules line up in an amphipathic channel in single file. In the narrow selectivity filter of the channel the glycerol alkyl backbone is wedged against a hydrophobic corner, and successive hydroxyl groups form hydrogen bonds with a pair of acceptor, and donor atoms. Two conserved aspartic acid-proline-alanine motifs form a key interface between two gene-duplicated segments that each encode three-and-one-half membrane-spanning helices around the channel. This structure elucidates the mechanism of selective permeability for linear carbohydrates and suggests how ions and water are excluded.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Fu, D -- Libson, A -- Miercke, L J -- Weitzman, C -- Nollert, P -- Krucinski, J -- Stroud, R M -- GM24485/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2000 Oct 20;290(5491):481-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry and Biophysics, School of Medicine, University of California, San Francisco, CA 94143-0448, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11039922" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Motifs ; Amino Acid Sequence ; Aquaporins/chemistry/metabolism ; *Bacterial Outer Membrane Proteins/*chemistry/metabolism ; Cell Membrane Permeability ; Conserved Sequence ; Crystallography, X-Ray ; Escherichia coli/*chemistry ; *Escherichia coli Proteins ; Glycerol/chemistry/*metabolism ; Hydrogen Bonding ; Models, Molecular ; Molecular Sequence Data ; Protein Conformation ; Protein Folding ; Protein Structure, Secondary ; Proteolipids/metabolism ; Stereoisomerism ; Sugar Alcohols/metabolism ; Water/metabolism
    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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  • 2
    Electronic Resource
    Electronic Resource
    The effect of cholera toxin on human red cell Ca-ATPase
    Amsterdam : Elsevier
    Biochemical and Biophysical Research Communications 181 (1991), S. 208-212 
    Details
    ISSN: 0006-291X
    Keywords: [abr] CaM; calmodulin ; [abr] EDTA; ethylenediamine tetraacetic acid ; [abr] EGTA; (ethylenebis(oxyethylenenitrilo))tetracetic acid ; [abr] P1; inorganic phosphate ; [abr] Tris; tris-(hydroxymethyl)aminomethane
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Biology , Chemistry and Pharmacology , Physics
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1016/S0006-291X(05)81403-2
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  • 3
    Electronic Resource
    Electronic Resource
    The effect of cholera toxin on human red cell Ca-ATPase
    Amsterdam : Elsevier
    Biochemical and Biophysical Research Communications 181 (1991), S. 208-212 
    Details
    ISSN: 0006-291X
    Keywords: [abr] CaM; calmodulin ; [abr] EDTA; ethylenediamine tetraacetic acid ; [abr] EGTA; (ethylenebis(oxyethylenenitrilo))tetracetic acid ; [abr] P1; inorganic phosphate ; [abr] Tris; tris-(hydroxymethyl)aminomethane
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Biology , Chemistry and Pharmacology , Physics
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1016/S0006-291X(05)81403-2
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  • 4
    Electronic Resource
    Electronic Resource
    Ethanol stimulates the plasma membrane calcium pump from human erythrocytes
    Amsterdam : Elsevier
    Biochimica et Biophysica Acta (BBA)/Biomembranes 1195 (1994), S. 141-148 
    Details
    ISSN: 0005-2736
    Keywords: (Human) ; ATPase, Ca^2^+- ; Alcohol ; Calcium ion transport ; Calmodulin ; Erythrocyte ; Ethanol
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Biology , Chemistry and Pharmacology , Medicine , Physics
    Type of Medium: Electronic Resource
    URL: http://linkinghub.elsevier.com/retrieve/pii/0005-2736(94)90020-5
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  • 5
    Electronic Resource
    Electronic Resource
    Fusion proteins as tools for crystallization: the lactose permease from Escherichia coli (1994)
    Copenhagen : International Union of Crystallography (IUCr)
    Acta crystallographica 50 (1994), S. 375-379 
    Details
    ISSN: 1399-0047
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Chemistry and Pharmacology , Geosciences , Physics
    Notes: A novel strategy is presented for the crystallization of membrane proteins or other proteins with low solubility and/or stability. The method is illustrated with the lactose permease from Escherichia coli, in which a fusion is constructed between the permease and a `carrier' protein. The carrier is a soluble, stable protein with its C and N termini close together in space at the surface of the protein, so that the carrier can be introduced into an internal position of the target protein. The carrier is chosen with convenient spectral or enzymatic properties, making the fusion protein easier to handle than the native molecule. Data are presented for the successful construction, expression and purification of a fusion product between lactose permease and cytochrome b562 from E. coli. The lactose transport activity of the fusion protein is similar to that of wild-type lactose permease, and the fusion product has an absorption spectrum in the visible range which is essentially identical to that of cytochrome b562. The fusion protein has a higher proportional polar surface area than wild-type permease, and should have better possibilities of forming the strong directional intermolecular contacts required of a crystal lattice.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1107/S0907444993014301
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  • 6
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    Host species, pathogens and disease associated with divergent nasal microbial communities in tortoises (2018)
    Royal Society
    Details
    Publication Date: 2018-10-11
    Description: Diverse bacterial communities are found on every surface of macro-organisms, and they play important roles in maintaining normal physiological functions in their hosts. While the study of microbiomes has expanded with the influx of data enabled by recent technological advances, microbiome research in reptiles lags behind other organisms. We sequenced the nasal microbiomes in a sample of four North American tortoise species, and we found differing community compositions among tortoise species and sampling sites, with higher richness and diversity in Texas and Sonoran desert tortoises. Using these data, we investigated the prevalence and operational taxonomic unit (OTU) diversity of the potential pathogen Pasteurella testudinis and found it to be common, abundant and highly diverse. However, the presence of this bacterium was not associated with differences in bacterial community composition within host species. We also found that the presence of nasal discharge from tortoises at the time of sampling was associated with a decline in diversity and a change in microbiome composition, which we posit is due to the harsh epithelial environment associated with immune responses. Repeated sampling across seasons, and at different points of pathogen colonization, should contribute to our understanding of the causes and consequences of different bacterial communities in these long-lived hosts.
    Keywords: microbiology, ecology, health and disease and epidemiology
    Electronic ISSN: 2054-5703
    Topics: Natural Sciences in General
    Published by Royal Society
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  • 7
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    Co-infection does not predict disease signs in Gopherus tortoises (2017)
    Royal Society
    Details
    Publication Date: 2017-10-19
    Description: In disease ecology, the host immune system interacts with environmental conditions and pathogen properties to affect the impact of disease on the host. Within the host, pathogens may interact to facilitate or inhibit each other's growth, and pathogens interact with different hosts differently. We investigated co-infection of two Mycoplasma and the association of infection with clinical signs of upper respiratory tract disease in four congeneric tortoise host species ( Gopherus ) in the United States to detect differences in infection risk and disease dynamics in these hosts. Mojave Desert tortoises had greater prevalence of Mycoplasma agassizii than Texas tortoises and gopher tortoises, while there were no differences in Mycoplasma testudineum prevalence among host species. In some host species, the presence of each pathogen influenced the infection intensity of the other; hence, these two mycoplasmas interact differently within different hosts, and our results may indicate facilitation of these bacteria. Neither infection nor co-infection was associated with clinical signs of disease, which tend to fluctuate across time. From M. agassizii DNA sequences, we detected no meaningful differentiation of haplotypes among hosts. Experimental inoculation studies and recurrent resampling of wild individuals could help to decipher the underlying mechanisms of disease dynamics in this system.
    Keywords: ecology, health and disease and epidemiology
    Electronic ISSN: 2054-5703
    Topics: Natural Sciences in General
    Published by Royal Society
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  • 8
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    The effect of cholera toxin on human red cell Ca-ATPase (1991)
    Elsevier
    Details
    Publication Date: 1991-11-01
    Print ISSN: 0006-291X
    Electronic ISSN: 1090-2104
    Topics: Biology , Chemistry and Pharmacology , Physics
    Published by Elsevier
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  • 9
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    Fusion proteins as tools for crystallization: the lactose permease from Escherichia coli (1994)
    International Union of Crystallography
    Details
    Publication Date: 1994-07-01
    Print ISSN: 0907-4449
    Electronic ISSN: 1399-0047
    Topics: Chemistry and Pharmacology , Geosciences , Physics
    Published by International Union of Crystallography
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