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  • 1
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Science Ltd
    Molecular microbiology 25 (1997), S. 0 
    ISSN: 1365-2958
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology , Medicine
    Notes: slyD encodes a 196 amino acid polypeptide that is a member of the FKBP family of cis–trans peptidyl–prolyl isomerases (PPIases). slyD mutations affect plaque formation by the phage φX174 by blocking the action of the phage lysis protein E. Here we describe the selection of a set of spontaneous slyD mutations conferring resistance to the expression of gene E from a plasmid. These mutations occur disproportionately in residues of SlyD that, based on the structure of the prototype mammalian FKBP12, make ligand contacts with immunosuppressing drug molecules or are conserved in other FKBP proteins. A wide variation in the plating efficiency of φX174 on these E R strains is observed, relative to the parental, indicating that these alleles differ widely in residual SlyD activity. Moreover, it is found that slyD mutations cause significant growth rate defects in Escherichia coli B and C backgrounds. Finally, overexpression of slyD causes filamentation of the host. Thus, among the FKBP genes found in organisms across the evolutionary spectrum, slyD is unique in having three distinct drug-independent phenotypes.
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Springer
    Mycopathologia 78 (1982), S. 47-63 
    ISSN: 1573-0832
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract ‘Without these tools (skin-test and complement fixation antigens for epidemiological, diagnostic, and prognostic use) we are at least 50 years behind in our defining of the disease blastomycosis’ (63). This statement by Rippon et al. emphasizes the need for a well defined antigen or group of antigens from Blastomyces dermatitidis, not only for the two tests named above, but for any serological or immunological test. Several different preparations have been reviewed which are beginning to approach the quality necessary for such a sensitive and specific antigenic tool. All of these require further characterization and, in most instances, purification. One purified fraction isolated from blastomycin, the F fraction, has shown exceptional promise as a skin-test agent in guinea pigs but has not been further studied. A 10–30K molecular weight fraction of the yeast cytoplasm has shown good reactivity, and contains a protein shown by PAGE to be common to several skin-reactive preparations. This fraction has not been further purified. An ASWS preparation has been partially characterized and shown to be especially sensitive and specific in animals, though not yet in humans. Purification of this fraction by PAGE has uncovered a highly reactive protein which may be related to one isolated from the cytoplasm. Investigations using this purified component have not been attempted in humans. The A antigen has been well characterized regarding its applicability to human diagnosis. It has been partially purified and two of its components associated with its reactivity. It also has probably the best possibility as an immediate serologic tool. Even here, though, current preparations contain much extraneous material which could conceivably create cross-reactivity problems in the future. The ethanol-precipitate antigens which have shown such superior results in the past have not been employed recently, nor have they been extensively characterized. This fraction may contain the reactive A antigen or other antigens deserving of study. Hopefully, the use of this technique can be encouraged as one starting point for isolation procedures. The importance and isolation of enzymes and mannose containing antigens have probably not received adequate attention. An almost uniform identification of mannose in reactive preparations argues for purification procedures based on its presence. Finally, use of hybridoma technology to produce antibodies specific for antigens of B. dermatitidis promises to improve our understanding of the organism and to help isolate purer antigenic fractions. The search for antigens of importance in the immunology of B. dermatitidis should not be confined to any one or all of the antigens discussed above. A variety of components will likely be necessary for complete understanding of the disease and for diagnostic use. It has been observed that ‘information of clinical value can be obtained from immunological reactions to several different antigens’ (35), thereby encouraging continuous efforts to obtain as many as possible.
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  • 3
    ISSN: 1432-072X
    Keywords: Key wordsmip Gene ; Mip protein ; FK506-binding proteins ; FKBP ; Legionella pneumophila ; Escherichia coli
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract A newly identified gene in Escherichia coli, fkpA, encodes a protein with extensive similarity to the macrophage infectivity potentiator (Mip) proteins of Legionella pneumophila and Chlamydia trachomatis. The FkpA protein may be a new member of the family of FK506-binding proteins (FKBPs) because its carboxyl domain includes a sequence that matches the consensus FK506-binding motif in 40 of 48 positions, including those amino acids at the active site that form hydrogen bonds with the drug FK506. The amino acid sequence of the 29 kDa FkpA protein is 30–35% identical to the Mip proteins of L. pneumophila, L. micdadei, and C. trachomatis. Of the 270 amino acids of FkpA, 113 (42%) are identical to the sequence of one or another of these Mip proteins. Overexpression of FkpA or deletion of fkpA from the E. coli chromosome had no detrimental effect on bacterial growth, indicating that fkpA is not an essential gene. Hybridization of fkpA-specific DNA probes to genomic blots revealed that similar genes exist in several representatives of the Enterobacteriaceae. Thus, mip-like genes are not found exclusively in bacteria having a predominately intracellular life style, but instead appear to be a new FKBP subfamily that is a common constituent of many bacteria.
    Type of Medium: Electronic Resource
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  • 4
    Electronic Resource
    Electronic Resource
    Springer
    Archives of microbiology 161 (1994), S. 501-507 
    ISSN: 1432-072X
    Keywords: Key words:Escherichia coli–Salmonella typhimurium–murB–rrfB– Repetitive extragenic palindrome – Evolution – Mutation rate
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract. The murB gene of Salmonella typhimurium was cloned and found to be 75% and 82% identical to the DNA and protein sequences, respectively, of the same gene in Escherichia coli. These identities are among the lowest recorded between the two bacteria. Nevertheless, wild-type S. typhimurium murB complemented the known temperature-sensitive E. coli mutant, and wild-type E. coli murB complemented three temperature-sensitive mutants of S. typhimurium. The 5S rRNA gene, rrfB, and the region between murB and rrfB were also cloned and sequenced. The rrfB gene of S. typhimurium differs from rrfB of E. coli in only 2 of 120 nt, but the region between murB and rrfB has diverged greatly and includes a sequence that closely resembles a repetitive extragenic palindrome of the type normally associated with E. coli. Previous comparisons of gene divergence have suggested that the chromosomal mutation rate is lower in the vicinity of the origin of replication. However, the S. typhimurium murB gene, located 6 map minutes from the origin of replication, is highly substituted at synonymous sites and the sequence between murB and rrfB is significantly modified as well. Thus, murB is an exception to the general observation that genes near the origin of replication show less divergence than do genes elsewhere in the bacterial chromosome.
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  • 5
    Publication Date: 1995-05-01
    Print ISSN: 0302-8933
    Electronic ISSN: 1432-072X
    Topics: Biology
    Published by Springer
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  • 6
    Publication Date: 1994-06-01
    Print ISSN: 0302-8933
    Electronic ISSN: 1432-072X
    Topics: Biology
    Published by Springer
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  • 7
    Publication Date: 1990-01-01
    Print ISSN: 0006-3444
    Electronic ISSN: 1464-3510
    Topics: Biology , Mathematics , Medicine
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  • 8
    Publication Date: 2013-08-31
    Description: An unconventional framework is described for the design of decentralized controllers for large flexible structures. In contrast to conventional control system design practice which begins with a model of the open loop plant, the controlled plant is assembled from controlled components in which the modeling phase and the control design phase are integrated at the component level. The developed framework is called controlled component synthesis (CCS) to reflect that it is motivated by the well developed Component Mode Synthesis (CMS) methods which were demonstrated to be effective for solving large complex structural analysis problems for almost three decades. The design philosophy behind CCS is also closely related to that of the subsystem decomposition approach in decentralized control.
    Keywords: SPACECRAFT DESIGN, TESTING AND PERFORMANCE
    Type: NASA, Langley Research Center, NASA(DOD Controls-Structures Interaction Technology 1989; p 151-16
    Format: application/pdf
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