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  • 1
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    Critical Management Studies in the South African context (2021)
    AOSIS | AOSIS
    Details
    Publication Date: 2024-03-30
    Description: The purpose of the book is to establish the first formalised scholarly work on critical management studies (CMS) in the South African context. The book is a collection of seven chapters, six of which employ a conceptual methodology and one of which follows an interpretive paradigm employing qualitative methods of inquiry. CMS is a relatively young school of thought, arising in the early 1990s and still very much being a peripheral movement within the academic discipline of management. South Africa has very little scholarship on CMS as precious few scholars work in this space. Furthermore, publication opportunities are virtually non-existent as CMS is virtually unknown in the South African community of management scholars. Thus, this book represents the first academic work on CMS published in South Africa, written and reviewed by scholars who are familiar with the field. The primary target readership would be management academics, but it could also be a useful reference for postgraduate students in management. A digital similarities index report confirms the originality of the work and that it has not been plagiarised or published elsewhere.
    Keywords: indigenous knowledge ; organisational power relationships ; social structures ; managerialism ; critique ; denaturalisation ; feminism ; critical management studies ; exploitation ; decolonisation ; Epistemology ; Executive compensation ; Paradigm ; Positivism ; South Africa ; thema EDItEUR::K Economics, Finance, Business and Management::KJ Business and Management::KJU Organizational theory and behaviour
    Language: English
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  • 2
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    [Book Review] Form. Function. Fate (2016)
    American Association for the Advancement of Science (AAAS)
    In: Science
    Details
    Publication Date: 2016-06-17
    Description: "This missing science of heredity … is, in simple truth, ten times more important to humanity than all the chemistry and physics, all the technical and industrial science that ever has been or ever will be discovered," wrote H. G. Wells in 1903. Having dedicated more than 500 pages to the topic in his new book, The Gene, Siddhartha Mukherjee would seem to agree. The book examines human genetics, from its philosophical roots in the work of Aristotle, through Gregor Mendel's garden and Thomas Hunt Morgan's work on fruitflies, and including active work in genome editing. Author: Michael A. Goldman
    Keywords: Genetics
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Geosciences , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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  • 3
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    Human glia can both induce and rescue aspects of disease phenotype in Huntington disease (2016)
    Springer Nature
    Details
    Publication Date: 2016-06-09
    Description: Article The contribution of glia to Huntington's disease is unclear. The authors show that human glial progenitor cells (GPCs) expressing mutant huntingtin impair motor performance when engrafted into wild type mice, and wild type human GPCs ameliorate disease phenotypes when engrafted into an HD mouse model. Nature Communications doi: 10.1038/ncomms11758 Authors: Abdellatif Benraiss, Su Wang, Stephanie Herrlinger, Xiaojie Li, Devin Chandler-Militello, Joseph Mauceri, Hayley B. Burm, Michael Toner, Mikhail Osipovitch, Qiwu Jim Xu, Fengfei Ding, Fushun Wang, Ning Kang, Jian Kang, Paul C. Curtin, Daniela Brunner, Martha S. Windrem, Ignacio Munoz-Sanjuan, Maiken Nedergaard, Steven A. Goldman
    Electronic ISSN: 2041-1723
    Topics: Biology , Chemistry and Pharmacology , Natural Sciences in General , Physics
    Published by Springer Nature
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  • 4
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    Systematic Global Analysis of Genes Encoding Protein Phosphatases in Aspergillus fumigatus (2015)
    Genetics Society of America (GSA)
    Details
    Publication Date: 2015-07-16
    Description: Aspergillus fumigatus is a fungal pathogen that causes several invasive and noninvasive diseases named aspergillosis. This disease is generally regarded as multifactorial, considering that several pathogenicity determinants are present during the establishment of this illness. It is necessary to obtain an increased knowledge of how, and which, A. fumigatus signal transduction pathways are engaged in the regulation of these processes. Protein phosphatases are essential to several signal transduction pathways. We identified 32 phosphatase catalytic subunit-encoding genes in A. fumigatus , of which we were able to construct 24 viable deletion mutants. The role of nine phosphatase mutants in the HOG (high osmolarity glycerol response) pathway was evaluated by measuring phosphorylation of the p38 MAPK (SakA) and expression of osmo-dependent genes. We were also able to identify 11 phosphatases involved in iron assimilation, six that are related to gliotoxin resistance, and three implicated in gliotoxin production. These results present the creation of a fundamental resource for the study of signaling in A. fumigatus and its implications in the regulation of pathogenicity determinants and virulence in this important pathogen.
    Electronic ISSN: 2160-1836
    Topics: Biology
    Published by Genetics Society of America (GSA)
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  • 5
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    Genetic technologies. Bioengineered food--safety and labeling (2001)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2001-02-24
    Description: The safety and labeling of genetically engineered foods are two areas that have elicited considerable public concern and debate. This Policy Forum provides a legal analysis of these issues in the context of two bills that have been recently proposed in The U.S. Congress, the Genetically Engineered Food Safety Act and the Genetically Engineered Food Right to Know Act. Most transgenic components of foods currently on the market are plant-incorporated protectants or their inert ingredients. Therefore, they have been evaluated for safety by the Environmental Protection Agency (as well as the Food and Drug Administration), and their disclosure in labeling should not be required. If plant-incorporated protectants are considered safer than chemical pesticides, and chemical pesticides do not have to be disclosed in labels, then bioengineered foods should not be subject to stricter regulation, nor should they be required to be labeled. The two bills are inconsistent, in many respects, with well-established principles of food regulation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Goldman, K A -- New York, N.Y. -- Science. 2000 Oct 20;290(5491):457-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Georgetown University Law Center, Washington, DC 20001, USA. goldmank@law.georgetown.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11183767" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Consumer Product Safety/*legislation & jurisprudence ; Crops, Agricultural/genetics ; Food/*standards ; Food Additives ; Food Labeling/*legislation & jurisprudence ; *Genetic Engineering ; Humans ; *Legislation, Food ; Plants, Genetically Modified ; United States ; United States Environmental Protection Agency ; United States Food and Drug Administration
    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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  • 6
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    Atomic structure of acetylcholinesterase from Torpedo californica: a prototypic acetylcholine-binding protein (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-08-23
    Description: The three-dimensional structure of acetylcholinesterase from Torpedo californica electric organ has been determined by x-ray analysis to 2.8 angstrom resolution. The form crystallized is the glycolipid-anchored homodimer that was purified subsequent to solubilization with a bacterial phosphatidylinositol-specific phospholipase C. The enzyme monomer is an alpha/beta protein that contains 537 amino acids. It consists of a 12-stranded mixed beta sheet surrounded by 14 alpha helices and bears a striking resemblance to several hydrolase structures including dienelactone hydrolase, serine carboxypeptidase-II, three neutral lipases, and haloalkane dehalogenase. The active site is unusual because it contains Glu, not Asp, in the Ser-His-acid catalytic triad and because the relation of the triad to the rest of the protein approximates a mirror image of that seen in the serine proteases. Furthermore, the active site lies near the bottom of a deep and narrow gorge that reaches halfway into the protein. Modeling of acetylcholine binding to the enzyme suggests that the quaternary ammonium ion is bound not to a negatively charged "anionic" site, but rather to some of the 14 aromatic residues that line the gorge.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sussman, J L -- Harel, M -- Frolow, F -- Oefner, C -- Goldman, A -- Toker, L -- Silman, I -- New York, N.Y. -- Science. 1991 Aug 23;253(5022):872-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Structural Chemistry, Weizmann Institute of Science, Rehovot, Israel.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1678899" target="_blank"〉PubMed〈/a〉
    Keywords: Acetylcholine/*metabolism ; Acetylcholinesterase/*chemistry/metabolism ; Amino Acid Sequence ; Animals ; Binding Sites ; Cell Membrane/enzymology ; Chemistry, Physical ; Crystallization ; Electric Organ/*enzymology ; Glutamates ; Glutamic Acid ; Macromolecular Substances ; Molecular Sequence Data ; Molecular Structure ; Phosphatidylinositols/metabolism ; Physicochemical Phenomena ; Protein Conformation ; Sequence Homology, Nucleic Acid ; *Torpedo ; X-Ray Diffraction
    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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  • 7
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    The structure and catalytic cycle of a sodium-pumping pyrophosphatase (2012)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2012-07-28
    Description: Membrane-integral pyrophosphatases (M-PPases) are crucial for the survival of plants, bacteria, and protozoan parasites. They couple pyrophosphate hydrolysis or synthesis to Na(+) or H(+) pumping. The 2.6-angstrom structure of Thermotoga maritima M-PPase in the resting state reveals a previously unknown solution for ion pumping. The hydrolytic center, 20 angstroms above the membrane, is coupled to the gate formed by the conserved Asp(243), Glu(246), and Lys(707) by an unusual "coupling funnel" of six alpha helices. Comparison with our 4.0-angstrom resolution structure of the product complex suggests that helix 12 slides down upon substrate binding to open the gate by a simple binding-change mechanism. Below the gate, four helices form the exit channel. Superimposing helices 3 to 6, 9 to 12, and 13 to 16 suggests that M-PPases arose through gene triplication.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kellosalo, Juho -- Kajander, Tommi -- Kogan, Konstantin -- Pokharel, Kisun -- Goldman, Adrian -- New York, N.Y. -- Science. 2012 Jul 27;337(6093):473-6. doi: 10.1126/science.1222505.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Structural Biology and Biophysics Program, Institute of Biotechnology, Post Office Box 65, University of Helsinki, FIN-00014, Finland.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/22837527" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Bacterial Proteins/chemistry/genetics/metabolism ; Biocatalysis ; Calcium/chemistry ; Catalytic Domain ; Cell Membrane/enzymology ; Crystallography, X-Ray ; Diphosphates/*metabolism ; Hydrolysis ; Hydrophobic and Hydrophilic Interactions ; Ion Channel Gating ; Magnesium/chemistry ; Models, Molecular ; Molecular Sequence Data ; Mutation ; Protein Conformation ; Protein Multimerization ; Protein Structure, Secondary ; Pyrophosphatases/*chemistry/genetics/*metabolism ; Sodium/*metabolism ; Sodium-Potassium-Exchanging ATPase/*chemistry/genetics/metabolism ; Thermotoga maritima/*enzymology
    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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  • 8
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    Dual regulatory switch through interactions of Tcf7l2/Tcf4 with stage-specific partners propels oligodendroglial maturation (2016)
    Springer Nature
    Details
    Publication Date: 2016-03-11
    Description: Article Wnt/β-catenin signaling regulates oligodendrocyte (OL) development. Here the authors show that Tcf7l2, a β-catenin transcriptional partner,sequentially interacts with stage-specific partners to coordinate the transitions of differentiation initiation and maturation during OL development. Nature Communications doi: 10.1038/ncomms10883 Authors: Chuntao Zhao, Yaqi Deng, Lei Liu, Kun Yu, Liguo Zhang, Haibo Wang, Xuelian He, Jincheng Wang, Changqing Lu, Laiman N Wu, Qinjie Weng, Meng Mao, Jianrong Li, Johan H van Es, Mei Xin, Lee Parry, Steven A Goldman, Hans Clevers, Q. Richard Lu
    Electronic ISSN: 2041-1723
    Topics: Biology , Chemistry and Pharmacology , Natural Sciences in General , Physics
    Published by Springer Nature
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  • 9
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    Modulation of tissue repair by regeneration enhancer elements (2016)
    Springer Nature
    In: Nature
    Details
    Publication Date: 2016-04-14
    Description: Modulation of tissue repair by regeneration enhancer elements Nature 532, 7598 (2016). doi:10.1038/nature17644 Authors: Junsu Kang, Jianxin Hu, Ravi Karra, Amy L. Dickson, Valerie A. Tornini, Gregory Nachtrab, Matthew Gemberling, Joseph A. Goldman, Brian L. Black & Kenneth D. Poss How tissue regeneration programs are triggered by injury has received limited research attention. Here we investigate the existence of enhancer regulatory elements that are activated in regenerating tissue. Transcriptomic analyses reveal that leptin b (lepb) is highly induced in regenerating hearts and
    Print ISSN: 0028-0836
    Electronic ISSN: 1476-4687
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Published by Springer Nature
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  • 10
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    Neutron sources: road maps of no use to some physicists (2014)
    Nature Publishing Group (NPG)
    Details
    Publication Date: 2014-03-14
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Matic, Aleksandar -- Boni, Peter -- Goldman, Adrian -- England -- Nature. 2014 Mar 13;507(7491):169. doi: 10.1038/507169c.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Chalmers University of Technology, Gothenburg, Sweden. ; Technische Universitat Munchen, Germany. ; University of Leeds, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/24622190" target="_blank"〉PubMed〈/a〉
    Keywords: Chemistry/*instrumentation/*organization & administration ; Crystallography/*instrumentation/*utilization ; *Policy Making
    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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