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  • 1
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    Structural investigations of bacteriophage C1 [Biophysics and Computational Biology] (2012)
    National Academy of Sciences
    Details
    Publication Date: 2012-08-29
    Description: The Podoviridae phage C1 was one of the earliest isolated bacteriophages and the first virus documented to be active against streptococci. The icosahedral and asymmetric reconstructions of the virus were calculated using cryo-electron microscopy. The capsid protein has an HK97 fold arranged into a T = 4 icosahedral lattice. The C1 tail...
    Print ISSN: 0027-8424
    Electronic ISSN: 1091-6490
    Topics: Biology , Medicine , Natural Sciences in General
    Published by National Academy of Sciences
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  • 2
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    Rapid killing of Streptococcus pneumoniae with a bacteriophage cell wall hydrolase (2001)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2001-12-12
    Description: Nasopharyngeal carriage is the major reservoir for Streptococcus pneumoniae in the community. Although eliminating this reservoir would greatly reduce disease occurrence, no suitable intervention has been available for this purpose. We show here that seconds after contact, a purified pneumococcal bacteriophage lytic enzyme (Pal) is able to kill 15 common serotypes of pneumococci, including highly penicillin-resistant strains. In vivo, previously colonized mice revealed undetectable pneumococcal titers 5 hours after a single enzyme treatment. Pal enzyme had little or no effect on microorganisms normally found in the human oropharynx, and Pal-resistant pneumococci could not be detected after extensive exposure to the enzyme.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Loeffler, J M -- Nelson, D -- Fischetti, V A -- New York, N.Y. -- Science. 2001 Dec 7;294(5549):2170-2.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Bacterial Pathogenesis, The Rockefeller University, New York, NY 10021, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11739958" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Bacterial Capsules/physiology ; Bacteriolysis ; Cell Membrane/drug effects/ultrastructure ; Cell Wall/drug effects/ultrastructure ; Colony Count, Microbial ; Drug Resistance, Bacterial ; Humans ; Mice ; Mutation ; N-Acetylmuramoyl-L-alanine Amidase/*metabolism/*pharmacology ; Nasopharynx/*microbiology ; Random Allocation ; Streptococcus/drug effects/growth & development ; Streptococcus Phages/*enzymology ; Streptococcus pneumoniae/*drug effects/growth & ; development/physiology/ultrastructure
    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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  • 3
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    Role of alpha-dystroglycan as a Schwann cell receptor for Mycobacterium leprae (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-12-16
    Description: alpha-Dystroglycan (alpha-DG) is a component of the dystroglycan complex, which is involved in early development and morphogenesis and in the pathogenesis of muscular dystrophies. Here, alpha-DG was shown to serve as a Schwann cell receptor for Mycobacterium leprae, the causative organism of leprosy. Mycobacterium leprae specifically bound to alpha-DG only in the presence of the G domain of the alpha2 chain of laminin-2. Native alpha-DG competitively inhibited the laminin-2-mediated M. leprae binding to primary Schwann cells. Thus, M. leprae may use linkage between the extracellular matrix and cytoskeleton through laminin-2 and alpha-DG for its interaction with Schwann cells.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Rambukkana, A -- Yamada, H -- Zanazzi, G -- Mathus, T -- Salzer, J L -- Yurchenco, P D -- Campbell, K P -- Fischetti, V A -- New York, N.Y. -- Science. 1998 Dec 11;282(5396):2076-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Bacterial Pathogenesis and Immunology, Rockefeller University, New York, NY 10021, USA. rambuka@rockvax.rockefeller.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9851927" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Bacterial Adhesion ; Binding Sites ; Calcium/physiology ; Cell Line, Transformed ; Cells, Cultured ; Cytoskeletal Proteins/*metabolism/pharmacology ; Dystroglycans ; Edetic Acid/pharmacology ; Glycosylation ; Humans ; Laminin/chemistry/*metabolism ; Membrane Glycoproteins/*metabolism/pharmacology ; Mycobacterium leprae/*metabolism ; Peripheral Nerves/chemistry ; Rats ; Receptors, Laminin/metabolism ; Recombinant Fusion Proteins/metabolism ; Recombinant Proteins/chemistry/metabolism ; Schwann Cells/metabolism/*microbiology
    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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  • 4
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    Protection against streptococcal pharyngeal colonization with a vaccinia: M protein recombinant (1989)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1989-06-23
    Description: Phagocytosis of group A streptococci requires type-specific antibodies directed against the variable determinants of the bacterial surface M protein molecule. As a step toward developing a broadly protective anti-streptococcal vaccine, a vaccinia virus (VV) recombinant was constructed that expresses the conserved region of the structural gene encoding the M6 molecule (VV:M6'). Mice immunized intranasally with the VV:M6' virus showed markedly reduced pharyngeal colonization by streptococci after intranasal and oral challenge with these bacteria. M protein-specific serum immunoglobulin G was significantly elevated in vaccinated animals and absent in controls. A similar approach may prove useful for the identification of protective determinants present on other bacterial and viral pathogens.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Fischetti, V A -- Hodges, W M -- Hruby, D E -- AI-00666/AI/NIAID NIH HHS/ -- AI-11822/AI/NIAID NIH HHS/ -- AI-26281/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 1989 Jun 23;244(4911):1487-90.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Rockefeller University, New York, NY 10021.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2660266" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antigens, Bacterial/immunology ; *Bacterial Outer Membrane Proteins ; Bacterial Proteins/genetics/*immunology ; *Bacterial Vaccines/immunology ; *Carrier Proteins ; Cloning, Molecular ; *Immunization ; Immunoglobulin A/analysis ; Immunoglobulin G/analysis ; Mice ; Pharyngeal Diseases/etiology/*prevention & control ; Streptococcal Infections/*prevention & control ; Streptococcus pyogenes ; *Vaccines/immunology ; *Vaccines, Synthetic/immunology ; Vaccinia virus/genetics/*immunology
    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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  • 5
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    Expression of streptococcal M protein in Escherichia coli (1983)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1983-08-19
    Description: The structural gene for group A streptococcal M protein, the fibrillar surface molecule enabling the organism to resist phagocytosis, has been cloned into Escherichia coli. The molecule produced by Escherichia coli is slightly larger than the M protein isolated by solubilization of the streptococcal cell wall, but is similar in size to that secreted by streptococcal protoplast and L forms. Immunologically, the molecule synthesized by Escherichia coli has the same type-specific determinants as the streptococcal M protein.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Scott, J R -- Fischetti, V A -- AI11822/AI/NIAID NIH HHS/ -- RR05364/RR/NCRR NIH HHS/ -- New York, N.Y. -- Science. 1983 Aug 19;221(4612):758-60.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6192499" target="_blank"〉PubMed〈/a〉
    Keywords: *Antigens, Bacterial ; *Bacterial Outer Membrane Proteins ; Bacterial Proteins/*genetics/immunology ; *Carrier Proteins ; Cloning, Molecular ; Epitopes ; Escherichia coli/*genetics ; Gene Expression Regulation ; Molecular Weight
    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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    Toxic shock syndrome and lysogeny in Staphylococcus aureus (1983)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1983-04-15
    Description: Lysogeny, or the presence of temperate bacteriophage, was demonstrated, by means of two Staphylococcus aureus indicator strains, in 11 of 12 strains of S. aureus isolated from patients with toxic shock syndrome. Only 1 of 18 strains of S. aureus that were not associated with toxic shock syndrome showed the presence of bacteriophage. A laboratory strain of S. aureus was lysogenized by bacteriophage from two of the toxic shock-associated strains. These results add support to the theory that lysogeny by one or more bacteriophage in certain strains of S. aureus may be responsible for the pathogenesis of toxic shock syndrome.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Schutzer, S E -- Fischetti, V A -- Zabriskie, J B -- New York, N.Y. -- Science. 1983 Apr 15;220(4594):316-8.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6220467" target="_blank"〉PubMed〈/a〉
    Keywords: Bacterial Toxins/metabolism ; Female ; Humans ; *Lysogeny ; Plasmids ; Shock, Septic/etiology/*microbiology ; Staphylococcal Infections/microbiology ; Staphylococcus Phages/isolation & purification ; *Staphylococcus aureus
    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
    Electronic Resource
    Electronic Resource
    Genetic diversity among the T-protein genes of group A streptococci (1991)
    Oxford, UK : Blackwell Publishing Ltd
    Molecular microbiology 5 (1991), S. 0 
    Details
    ISSN: 1365-2958
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology , Medicine
    Notes: T protein is a trypsin- and pepsin-resistant molecule on the surface of group A streptococci used as a serological tool to differentiate streptococci of this group. The purpose of this study was to determine the relatedness among the T protein genes of the 25 known T serotypes. DNA probes were constructed which represented various regions of the structural gene for the T6 protein, tee6. The probes were assayed for their ability to hybridize Hin dlll digests of chromosomal DNA from the 25 different T serotypes. Probe pTEE6.3, coding for the entire T6 protein, and pTEE61–299, coding for the amino-terminal half of T6, displayed the highest amount of homology, each binding to 10 of 25 T serotypes. Probes coding for sequences in the carboxy-terminal half of T6 showed considerably less homology among T serotypes with one probe hybridizing with only three out of 25. A synthetic oligonucleotide coding for the carboxy-terminal hydrophobic domain of T6, an area conserved to some degree among several bacterial surface proteins, showed homology with only seven out of 25 T serotypes. Hybridization with sequences outside the tee6 coding area provided additional information on the relatedness of certain sets of T serotypes according to restriction-fragment size heterogeneity. Clearly, there is considerable diversity among T-serotype genes. The data suggest that two or more families of structurally variant T proteins exist, which share only the property of proteolytic resistance and/or, perhaps, some biological function.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2958.1991.tb01854.x
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  • 8
    Electronic Resource
    Electronic Resource
    An Algorithm for Identifying Similar Amino Acid Clusters among Different Alpha-Helical Coiled-Coil Proteins Using Their Secondary Structure (1999)
    Springer
    Algorithmica 25 (1999), S. 330-346 
    Details
    ISSN: 1432-0541
    Keywords: Key words. Computational biology, Protein structure, Coiled-coil, Epitope, Dynamic programming.
    Source: Springer Online Journal Archives 1860-2000
    Topics: Computer Science , Mathematics
    Notes: Abstract. We describe a simple approach for finding identical amino acid clusters on the outer surface of α -helical coiled-coil proteins by examining the sequence of amino acids that compose the protein. Finding such similarities is an important immunological problem, since these may correspond to cross-reactive epitopes, i.e., sites at which antibodies produced against one protein also bind to another conformationally similar protein. Because of the regularities inherent in a coiled-coil structure the position of each amino acid on the structure is predicted. Based on this prediction, our algorithm finds similarities on the outer surface of the proteins. The matches found by our algorithm serve as an important screening process, intended to indicate which experiments to conduct to determine sites that correspond to cross-reactive epitopes. The location of several cross-reactive epitopes between M proteins and myosins had been verified experimentally. Although our approach makes many simplifying assumptions, these epitopes always correspond to clusters of identical amino acids, which our algorithm predicted to be contiguous on the outer surface. Our algorithm runs in O(n+m+r) time and O(n+m) space, where n and m are the lengths of the protein sequences, and r is the number of matching amino acids that appear in the same structural position of the α -helix in both sequences.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/PL00008281
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  • 9
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    Sortase A localizes to distinct foci on the Streptococcus pyogenes membrane (2008)
    National Academy of Sciences
    Details
    Publication Date: 2008-11-18
    Print ISSN: 0027-8424
    Electronic ISSN: 1091-6490
    Topics: Biology , Medicine , Natural Sciences in General
    Published by National Academy of Sciences
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  • 10
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    Amino acid sequence and physicochemical similarities between streptococcal M protein and mammalian tropomyosin. (1979)
    National Academy of Sciences
    Details
    Publication Date: 1979-08-01
    Print ISSN: 0027-8424
    Electronic ISSN: 1091-6490
    Topics: Biology , Medicine , Natural Sciences in General
    Published by National Academy of Sciences
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