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  • 1
    Keywords: Applied ecology. ; Environmental management. ; Forestry. ; Environmental sciences Social aspects. ; System theory. ; Applied Ecology. ; Environmental Management. ; Forestry. ; Environmental Social Sciences. ; Complex Systems.
    Description / Table of Contents: Introduction -- 1. Chad Oliver and forests as complex systems; Melih Boydak -- Section I. Complex Forest Stand Dynamics -- 2. Principles of stand reconstruction to illuminate stand dynamics of complex forests in Alaska; Bob Deal -- 3: Forest stand dynamics principles used to guide the management of uneven-aged forest in the Missouri Ozarks; Dave Larsen -- 4: Forest stand dynamics and the curious case of the critically endangered Leadbeater’s Possum; Patrick Baker -- 5: Modelling and mapping complex stand structures with airborne LiDAR; John Kershaw -- 6. How might the concepts of traditional stand dynamics be used for more complex stands; Bruce Larson -- Section II. Forests as Complex Ecological Systems -- 7. Integrating effects of climate on temperate montane forests; Pil Sun Park -- 8. Carbon++: integrating non-CO2 forcers in our understanding of forests and climate; Kris Covey -- 9. Understanding post-wildfire fuel dynamics in dry forests of the Pacific Northwest; Morris Johnson -- 10. Understanding forestry through pictures: A journey of graphics, pictures, and visualisations; Jim McCarter -- 11. The inertia of forested landscapes and applications to management; Jeremy Wilson -- Section III. Forests as Complex Social Systems -- 12. Tiger in the woods, elephant in the room; Xuemei Han -- 13. Forests as complex systems: Implications from the perspective of sustainable development; Glenn Galloway -- 14. Securing forest tenure for rural development; Gerardo Segura -- 15. Understanding the dynamics between forests and livelihoods: A case of Central Indian landscapes; Alark Saxena -- 16. Closing comments; Chad Oliver. .
    Abstract: Professor Chadwick Dearing Oliver has made major intellectual contributions to forest science and natural resources management. Over the course of his career he has actively sought to bring research and practice together through synthesis, outreach, and capacity-building. A common thread throughout his career has been complexity and how we as a society understand and manage complex systems. His work on forest stand dynamics, landscape management, and sustainability have all focused on the emergent properties of complex ecological and/or social systems. This volume celebrates a remarkable career through a diverse group of former students and colleagues who work on a wide range of subject areas related to the management of complex natural resource systems. Over the past decade there has been considerable discussion about forests as complex adaptive systems. Advances in remote sensing, social methods, and data collection and processing have enabled more detailed characterisations of complex natural systems across spatial and temporal scales than ever before. Making sense of these data, however, requires conceptual frameworks that are robust to the complexity of the systems and their inherent dynamics, particularly in the context of global change. This volume presents a collection of cutting-edge research on natural ecosystems and their dynamics through the lens of complex adaptive systems. Each chapter offers new insights into how these systems can be made more resilient to ensure that they provide a diversity of ecological and social values well into the future. Together they provide a robust way of thinking about the many challenges that natural ecosystems face and how we as society may best address them.
    Type of Medium: Online Resource
    Pages: XVIII, 334 p. 1 illus. , online resource.
    Edition: 1st ed. 2022.
    ISBN: 9783030885557
    Series Statement: Managing Forest Ecosystems, 41
    DDC: 333.9516
    Language: English
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  • 2
    ISSN: 1399-0047
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Chemistry and Pharmacology , Geosciences , Physics
    Notes: Bacillus stearothermophilus glycerol dehydrogenase (GlyDH) is a 39.5 kDa molecular weight metalloenzyme which catalyzes the oxidation of glycerol to dihydroxyacetone with the concomitant reduction of NAD+ to NADH. Despite its classification as a member of the `iron-containing' polyol dehydrogenase family, studies on recombinant B. stearothermophilus GlyDH have shown this enzyme to be Zn2+-dependent. Crystals of a S305C GlyDH mutant were obtained by the hanging-drop vapour-diffusion method, using ammonium sulfate and PEG 400 as precipitating agents, in the presence and absence of NAD+. The crystals belong to space group I422, with approximate unit-cell parameters a = b = 105, c = 149 Å and one subunit in the asymmetric unit, corresponding to a packing density of 2.6 Å3 Da−1. The crystals diffract X-rays to at least 1.8 Å resolution on a synchrotron-radiation source. Determination of the structure will provide insights into the key determinations of catalytic activity of this class of enzymes, for which no structures are currently available.
    Type of Medium: Electronic Resource
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  • 3
    ISSN: 1399-0047
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Chemistry and Pharmacology , Geosciences , Physics
    Notes: Glucose dehydrogenase (E.C 1.1.1.47; GlcDH) from Haloferax mediterranei has been overexpressed in Escherichia coli, solubilized by the addition of 8 M urea and refolded by rapid dilution. The protein has been purified by conventional techniques and crystallized by the hanging-drop vapour-diffusion method using sodium citrate as the precipitant. Two crystal forms representing the free enzyme and the binary complex with NADP+ grow under these conditions. Crystals of form I diffract to beyond 3.5 Å resolution and belong to the hexagonal space group P622, with unit-cell parameters a = b = 89.1, c = 214.6 Å, α = β = 90, γ = 120°. Crystals of form II diffract to greater than 2.0 Å and belong to the orthorhombic space group I222 or I212121, with unit-cell parameters a = 61.8, b = 110.9, c = 151.7 Å, α = β = γ = 90°. Calculated values for VM and consideration of the packing for both crystal forms suggests that the asymmetric units in both crystal forms contain a monomer.
    Type of Medium: Electronic Resource
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  • 4
    ISSN: 1399-0047
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Chemistry and Pharmacology , Geosciences , Physics
    Notes: Thermotoga maritima maltosyltransferase (MTase) is a 73.7 kDa molecular weight amylolytic enzyme which catalyzes the transfer of maltosyl units from maltodextrins or starch to suitable acceptors. Crystals of recombinant MTase have been obtained by the hanging-drop vapour-diffusion method using ammonium phosphate as a precipitating agent. The crystals belong to space group P4122 or its enantiomorph P4322, with unit-cell parameters a = b = 148.7, c = 106.7 Å. The asymmetric unit appears to contain one subunit, corresponding to a very low packing density of 4.0 Å3 Da−1. The crystals diffract X-rays to at least 2.4 Å resolution on a synchrotron-radiation source.
    Type of Medium: Electronic Resource
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  • 5
    ISSN: 1399-0047
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Chemistry and Pharmacology , Geosciences , Physics
    Notes: Nicotinamide nucleotide transhydrogenase couples the exchange of a hydride-ion equivalent between NAD(H) and NADP(H) to the translocation of protons across an energy-transducing membrane. Peripheral components of 380 and 200 residues bind NAD(H) (dI) and NADP(H) (dIII), respectively, while a third component forms a membrane-spanning region (dII). The NAD(H)-binding component dI of Rhodospirillum rubrum transhydrogenase has been crystallized in a form which diffracts to beyond 3.0 Å resolution and is in space group P2 or P21, with unit-cell parameters a = 69.3, b = 117.8, c = 106.6 Å, β = 107.2° and two dimers in the asymmetric unit. The sequence of the dI component is similar to that of alanine dehydrogenase. A full structure determination will lead to important information on the mode of action of this proton pump and will permit the comparison of the structure–function relationships of dI with those of alanine dehydrogenase.
    Type of Medium: Electronic Resource
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  • 6
    Electronic Resource
    Electronic Resource
    [s.l.] : Nature Publishing Group
    Nature 422 (2003), S. 581-582 
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] For decades, ecologists have struggled to explain how so many tropical tree species can coexist. Kelly and Bowler propose that differences in recruitment fluctuation and competitive abilities among closely related tree species could promote coexistence, and data from a tropical deciduous forest ...
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  • 7
    ISSN: 1072-8368
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Medicine
    Notes: [Auszug] The structure of the hexameric L-alanine dehydrogenase from Phormidium lapideum reveals that the subunit is constructed from two domains, each having the common dinucleotide binding fold. Despite there being no sequence similarity, the fold of alanine dehydrogenase is closely related to that ...
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  • 8
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] Triclosan (5-chloro-2-(2,4-dichlorophenoxy) phenol) has been used for more than 30 years as a general antibacterial and antifungal agent, and is found in formulations as diverse as toothpastes, cosmetics, antiseptic soaps, carpets, plastic kitchenware and toys. It has recently been suggested ...
    Type of Medium: Electronic Resource
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  • 9
    Publication Date: 2015-02-03
    Print ISSN: 1936-0851
    Electronic ISSN: 1936-086X
    Topics: Chemistry and Pharmacology , Physics
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  • 10
    Publication Date: 2018-02-06
    Description: Histidine biosynthesis is an essential process in plants and microorganisms, making it an attractive target for the development of herbicides and antibacterial agents. Imidazoleglycerol-phosphate dehydratase (IGPD), a key enzyme within this pathway, has been biochemically characterized in both Saccharomyces cerevisiae (Sc_IGPD) and Arabidopsis thaliana (At_IGPD). The plant enzyme, having been the focus of in-depth structural analysis as part of an inhibitor development program, has revealed details about the reaction mechanism of IGPD, whereas the yeast enzyme has proven intractable to crystallography studies. The structure–activity relationship of potent triazole-phosphonate inhibitors of IGPD has been determined in both homologs, revealing that the lead inhibitor (C348) is an order of magnitude more potent against Sc_IGPD than At_IGPD; however, the molecular basis of this difference has not been established. Here we have used single-particle electron microscopy (EM) to study structural differences between the At and Sc_IGPD homologs, which could influence the difference in inhibitor potency. The resulting EM maps at ∼3 Å are sufficient to de novo build the protein structure and identify the inhibitor binding site, which has been validated against the crystal structure of the At_IGPD/C348 complex. The structure of Sc_IGPD reveals that a 24-amino acid insertion forms an extended loop region on the enzyme surface that lies adjacent to the active site, forming interactions with the substrate/inhibitor binding loop that may influence inhibitor potency. Overall, this study provides insights into the IGPD family and demonstrates the power of using an EM approach to study inhibitor binding.
    Print ISSN: 0027-8424
    Electronic ISSN: 1091-6490
    Topics: Biology , Medicine , Natural Sciences in General
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