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  • 1
    Monograph available for loan
    Monograph available for loan
    Sitting in the fire : large group transformation using conflict and diversity (2014)
    Florence, California : Deep Democracy Exchange
    Details Availability
    Call number: IASS 19.92868
    Type of Medium: Monograph available for loan
    Pages: x, 267 Seiten , 23 cm
    ISBN: 9781619710245 (pbk.)
    URL: http://www.loc.gov/catdir/enhancements/fy0609/95078176-d.html
    URL: http://www.loc.gov/catdir/enhancements/fy0609/95078176-b.html
    Language: English
    Branch Library: RIFS Library
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  • 2
    Electronic Resource
    Electronic Resource
    Further Studies of the Action of Pancreatic Amylase: Hydrolysis of Waxy Maize Starch1a (1949)
    s.l. : American Chemical Society
    Journal of the American Chemical Society 71 (1949), S. 1779-1781 
    Details
    ISSN: 1520-5126
    Source: ACS Legacy Archives
    Topics: Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1021/ja01173a070
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  • 3
    Electronic Resource
    Electronic Resource
    Structure-function relationships in diphtheria toxin channels: III. Residues which affect the cis pH dependence of channel conductance (1994)
    Springer
    The journal of membrane biology 137 (1994), S. 45-57 
    Details
    ISSN: 1432-1424
    Keywords: Diphtheria toxin ; Site-directed mutagenesis ; Planar lipid bilayers ; Single channel conductance ; Ion selectivity ; pH dependence
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract The conductance of channels formed by diphtheria toxin (DT) in lipid bilayer membranes depends strongly on pH. We have previously shown that a 61 amino acid region of the protein, denoted TH8-9, is sufficient to form channels having the same pH-dependent conductance properties as those of whole toxin channels. One residue in this region, Aspartate 352, is responsible for all the dependence of single channel conductance on trans pH, whereas another, Glutamate 349, has no effect. Here, we report that of the seven remaining charged residues in the TH8-9 region, mutations altering the charge on H322, H323, H372, and R377 have minimal effects on single channel conductance; mutations of Glutamates 326, 327, or 362, however, significantly affect single channel conductance as well as its dependence on cis pH. Moreover, Glutamate 362 is titratable from both the cis and trans sides of the membrane, suggesting that this residue lies within the channel; it is more accessible, however, to cis than to trans protons. These results are consistent with the membrane-spanning topology previously proposed for the TH8-9 region, and suggest a geometric model for the DT channel.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00234997
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  • 4
    Electronic Resource
    Electronic Resource
    Structure function relationships in diphtheria toxin channels: II. A residue responsible for the channel's dependence on trans pH (1994)
    Springer
    The journal of membrane biology 137 (1994), S. 29-44 
    Details
    ISSN: 1432-1424
    Keywords: Diphtheria toxin ; Site-directed mutagenesis ; Planar lipid bilayers ; Single channel conductance ; Ion selectivity ; pH dependence
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract Ion-conducting channels formed in lipid bilayers by diphtheria toxin are highly pH dependent. Among other properties, the channel's single channel conductance and selectivity depend on proton concentrations on either side of the membrane. We have previously shown that a 61 amino acid fragment of DT is sufficient to form a channel having the same pH-dependent single channel properties as that of the intact toxin. This region corresponds to an a-helical hairpin in the recently published crystal structure of DT in solution; the hairpin contains two α-helices, each long enough to span a membrane, connected by a loop of about nine residues. This paper reports on the single channel effects of mutations which alter the two negatively charged residues in this loop. Changing Glutamate 349 to neutral glutamine or to positive lysine has no effect on the DT channel's single channel conductance or selectivity. In contrast, mutations of Aspartate 352 to neutral asparagine (DT-D352N) or positive lysine (DT-D352K) cause progressive reductions in single channel conductance at pH 5.3 cis/7.2 trans (in 1 m KCl), consistent with this group interacting electrostatically with ions in the channel. The cation selectivity of these mutant channels is also reduced from that of wild-type channels, a direction consistent with residue 352 influencing permeant ions via electrostatic forces. When both sides of the membrane are at pH 4, the conductance difference between wild-type and DT-D352N channels is minimal, suggesting that Asp 352 (in the wild type) is neutral at this pH. Differences observed between wild-type and DT-D352N channels at pH 4.0 cis/7.2 trans (with a high concentration of permeant buffer in the cis compartment) imply that residue 352 is on or near the trans side of the membrane. Comparing the conductances of wild-type and DT-D352K channels at large (cis) positive voltages supports this conclusion. The trans location of position 352 severely constrains the number of possible membrane topologies for this region.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00234996
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  • 5
    Electronic Resource
    Electronic Resource
    Structure-function relationships in diphtheria toxin channels: I. Determining a minimal channel-forming domain (1994)
    Springer
    The journal of membrane biology 137 (1994), S. 17-28 
    Details
    ISSN: 1432-1424
    Keywords: Diphtheria toxin ; Site-directed mutagenesis ; Planar lipid bilayers ; Ion channels ; T-domain ; Channel-forming peptides
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract Diphtheria Toxin (DT) is a 535 amino acid exotoxin, whose active form consists of two polypeptide chains linked by an interchain disulphide bond. DT's N-terminal A fragment kills cells by enzymatically inactivating their protein synthetic machinery; its C terminal B chain is required for the binding of toxin to sensitive cells and for the translocation of the A fragment into the cytosol. This B fragment, consisting of its N-terminal T domain (amino acids 191–386) and its C-terminal R domain (amino acids 387–535) is responsible for the ion-conducting channels formed by DT in lipid bilayers and cellular plasma membranes. To further delineate the channel-forming region of DT, we studied channels formed by deletion mutants of DT in lipid bilayer membranes under several pH conditions. Channels formed by mutants containing only the T domain (i.e., lacking the A fragment and/or the R domain), as well as those formed by mutants replacing the R domain with Interleukin-2 (Il–2), have single channel conductances and selectivities essentially identical to those of channels formed by wild-type DT. Furthermore, deleting the N-terminal 118 amino acids of the T domain also has minimal effect on the single channel conductance and selectivity of the mutant channels. Together, these data identify a 61 amino acid stretch of the T domain, corresponding to the region which includes α-helices TH8 and TH9 in the crystal structure of DT, as the channel-forming region of the toxin.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00234995
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  • 6
    Electronic Resource
    Electronic Resource
    Computer modelling of the transmembrane channel formed by a CNBr peptide of diphtheria toxin B fragment (1992)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 105 (1992), S. 0 
    Details
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Abstract Diphtheria toxin (DT) forms transmembrane, voltage-dependent channels in a planar lipid bilayer. Channels with similar characteristics were obtained with CB1, a cyanogen bromide peptide of diphtheria toxin B fragment (DTB) (res 340–459). Tryptophan 398 is in interaction with the hydrophobic core of the lipid bilayer. Using the Eisenberg method in association with the Shiffer-Edmunson wheel representation, we have identified two amphipathic α-helices within CB1 (res 346–364 and 389–406) that could be involved in the interaction with lipids. Bearing this information in mind, we are providing a model for the structure of the CB1 channel.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-6968.1992.tb05893.x
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  • 7
    Electronic Resource
    Electronic Resource
    Devolving training and development to line managers (1995)
    Bradford : Emerald
    Management development review 8 (1995), S. 16-21 
    Details
    ISSN: 0962-2519
    Source: Emerald Fulltext Archive Database 1994-2005
    Topics: Economics
    Notes: Reports that most organizations see training and development as theprovince of the human resource department. Proposes that responsibilityfor this should be placed in the hands of the line manager. Investigateshow the responsibility for training and development can be successfullytransferred to the line manager. Concludes with a series of key learningpoints which help in the implementation of this strategy.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1108/09622519510081993
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  • 8
    Electronic Resource
    Electronic Resource
    Projection structure of a ClC-type chloride channel at 6.5 Å resolution (2001)
    [s.l.] : Macmillian Magazines Ltd.
    Nature 409 (2001), S. 219-223 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] Virtually all cells in all eukaryotic organisms express ion channels of the ClC type, the only known molecular family of chloride-ion-selective channels. The diversity of ClC channels highlights the multitude and range of functions served by gated chloride-ion conduction in biological ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/35051631
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  • 9
    Electronic Resource
    Electronic Resource
    RATES OF MOLECULAR EVOLUTION: Phylogenetic Issues and Applications (1996)
    Palo Alto, Calif. : Annual Reviews
    Annual Review of Ecology, Evolution, and Systematics 27 (1996), S. 279-303 
    Details
    ISSN: 0066-4162
    Source: Annual Reviews Electronic Back Volume Collection 1932-2001ff
    Topics: Biology
    Notes: Abstract The proper relationship between systematics practice and our understanding of evolution has been long debated. Systematists seek to avoid assumptions about evolutionary process in their methods, yet a growing body of evidence indicates that patterns in rates of evolution can be used to reduce effects of homoplasy. We review variable evolutionary rates for molecular characters in the context of constraints on mutation and fixation. Some constraints, like the genetic code for protein-coding genes, are consistent in the direction of their effects, whereas others, like population size and cladogenesis frequency, are historically variable within and among lineages. We review methods for assessing rate variability, and we estimate comparative absolute rates of change for five sets of mitochondrial DNAs in 12 vertebrates for application in phylogenetic analyses. Unequal weights for subsets of mitochondrial DNAs improved congruence with the most highly corroborated tree in many but not all cases. The largest data set (12,120 bases) yielded the same tree under all four weighting alternatives. This is consistent with the notion, echoing the law of large numbers, that as data sets increase in size, homoplasy will tend to cancel itself out. Even if this notion has validity, however, evolutionary biology will remain vital in systematics if we want to: match sets of taxa with characters likely to be historically informative (when data sets are not sufficiently large); avoid comparing characters with different histories due to reticulations, horizontal transfer, or lineage sorting; avoid assuming random distribution of homoplasy; be alerted to the possibility of long-branch attraction problems; and understand the cause of the hierarchy of taxa in nature as inheritance of genetic material and descent with modification.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1146/annurev.ecolsys.27.1.279
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  • 10
    Electronic Resource
    Electronic Resource
    A DECADE OF CLC CHLORIDE CHANNELS: Structure, Mechanism, and Many Unsettled Questions (2000)
    Palo Alto, Calif. : Annual Reviews
    Annual Review of Biophysics and Biomolecular Structure 29 (2000), S. 411-438 
    Details
    ISSN: 1056-8700
    Source: Annual Reviews Electronic Back Volume Collection 1932-2001ff
    Topics: Biology , Physics
    Notes: Abstract ClC-type chloride channels are ubiquitous throughout the biological world. Expressed in nearly every cell type, these proteins have a host of biological functions. With nine distinct homologues known in eukaryotes, the ClCs represent the only molecularly defined family of chloride channels. ClC channels exhibit features of molecular architecture and gating mechanisms unprecedented in other types of ion channels. They form two-pore homodimers, and their voltage-dependence arises not from charged residues in the protein, but rather via coupling of gating to the movement of chloride ions within the pore. Because the functional characteristics of only a few ClC channels have been studied in detail, we are still learning which properties are general to the whole family. New approaches, including structural analyses, will be crucial to an understanding of ClC architecture and function.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1146/annurev.biophys.29.1.411
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