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    Emerging infectious diseases: public health issues for the 21st century (1999)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1999-05-21
    Description: Infectious diseases are the third leading cause of death in the United States and the leading cause worldwide. As the new millennium approaches, the public health community must replenish capacity depleted during years of inadequate funding while simultaneously incorporating new technologies and planning for the longer term. Among the challenges facing the public health community is the need for coordinated, global, multisectoral approaches to preventing and controlling complex infectious disease problems.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Binder, S -- Levitt, A M -- Sacks, J J -- Hughes, J M -- New York, N.Y. -- Science. 1999 May 21;284(5418):1311-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Parasitic Diseases, National Center for Infectious Diseases (NCID), Centers for Disease Control and Prevention (CDC), F-22, 4770 Buford Highway, NE, Atlanta, GA 30341, USA. scb1@cdc.gov〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10334978" target="_blank"〉PubMed〈/a〉
    Keywords: *Communicable Disease Control/trends ; *Communicable Diseases/diagnosis/epidemiology/mortality ; Drug Resistance, Microbial ; Environmental Health ; Global Health ; Humans ; Population Surveillance ; *Public Health Practice ; Socioeconomic Factors ; United States/epidemiology ; Vaccination
    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
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    The predicted structure of immunoglobulin D1.3 and its comparison with the crystal structure (1986)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1986-08-15
    Description: Predictions of the structures of the antigen-binding domains of an antibody, recorded before its experimental structure determination and tested subsequently, were based on comparative analysis of known antibody structures or on conformational energy calculations. The framework, the relative positions of the hypervariable regions, and the folds of four of the hypervariable loops were predicted correctly. This portion includes all residues in contact with the antigen, in this case hen egg white lysozyme, implying that the main chain conformation of the antibody combining site does not change upon ligation. The conformations of three residues in each of the other two hypervariable loops are different in the predicted models and the experimental structure.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Chothia, C -- Lesk, A M -- Levitt, M -- Amit, A G -- Mariuzza, R A -- Phillips, S E -- Poljak, R J -- GM25435/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1986 Aug 15;233(4765):755-8.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3090684" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Antibodies, Monoclonal ; *Antigen-Antibody Complex ; Chickens ; Egg White ; Female ; Immunoglobulin Fab Fragments ; *Immunoglobulin G ; Immunoglobulin Heavy Chains ; Immunoglobulin Light Chains ; Immunoglobulin Variable Region ; Models, Molecular ; Muramidase/immunology ; Protein Conformation
    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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