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  • 1
    Electronic Resource
    Electronic Resource
    INVESTORS’PERCEPTION OF RISK: A RE-ASSESSMENT (1979)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of business finance & accounting 6 (1979), S. 0 
    Details
    ISSN: 1468-5957
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Economics
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1468-5957.1979.tb01106.x
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  • 2
    Electronic Resource
    Electronic Resource
    Amino acid sequence changes in the haemagglutinin of A/Hong Kong (H3N2) influenza virus during the period 1968–77 (1980)
    [s.l.] : Nature Publishing Group
    Nature 283 (1980), S. 454-457 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] Haemagglutinin molecules from nine strains of A/Hong Kong/68 (H3N2) influenza virus, isolated between 1968 and 1977, were examined for changes in amino acid sequences. At least 18 changes, 9 of which were located precisely, occurred in the soluble tryptic peptides of the large haemagglutinin ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/283454a0
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  • 3
    Electronic Resource
    Electronic Resource
    Structure and function of the type 1 insulin-like growth factor receptor (2000)
    Springer
    Cellular and molecular life sciences 57 (2000), S. 1050-1093 
    Details
    ISSN: 1420-9071
    Keywords: Key words. Insulin-like growth factor; insulin; receptors; 3D structure; signalling pathways; apoptosis; cancer therapy.
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract. The type 1 insulin-like growth factor receptor (IGF-1R), a transmembrane tyrosine kinase, is widely expressed across many cell types in foetal and postnatal tissues. Activation of the receptor following binding of the secreted growth factor ligands IGF-1 and IGF-2 elicits a repertoire of cellular responses including proliferation, and the protection of cells from programmed cell death or apoptosis. As a result, signalling through the IGF-1R is the principal pathway responsible for somatic growth in foetal mammals, whereas somatic growth in postnatal animals is achieved through the synergistic interaction of growth hormone and the IGFs. Forced overexpression of the IGF-1R results in the malignant transformation of cultured cells; conversely, downregulation of IGF-1R levels can reverse the transformed phenotype of tumour cells, and may render them sensitive to apoptosis in vivo. Elevated levels of IGF-1R are observed in a variety of human tumour types, whereas epidemiological studies implicate the IGF-1 axis as a predisposing factor in the pathogenesis of human breast and prostate cancer. The IGF-1R has thus emerged as a therapeutic target for the development of antitumour agents. Recent progress towards the elucidation of the three-dimensional structure of the extracellular domain of the IGF-1R represents an opportunity for the rational assembly of small molecule antagonists of receptor function for clinical use.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/PL00000744
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  • 4
    Electronic Resource
    Electronic Resource
    Coat protein of Potyviruses (1988)
    Springer
    Archives of virology 102 (1988), S. 207-219 
    Details
    ISSN: 1432-8798
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary Four strains of potato virus Y, PVY-D, PVY-10, PVY-18, and PVY-43, obtained from different Australian sources were compared on the basis of their biological, serological and coat protein structural properties. Each of the strains could be distinguished on the basis of their reactions on selected test plant species. Two of the PVY strains, PVY-D and PVY-10, induced symptoms similar to those produced by the PVYO strain group. The reactions of PVY-18 and PVY-43, although comparable to PVYN in some hosts, did not completely match the description of the PVYN strain group. In contrast to the other three strains, PVY-18 could not be transmitted byMyzus persicae in repeated tests. No difference was observed in the serological properties of the four PVY strains in different assay systems, using polyclonal antisera. The amino acid sequences of the coat proteins of PVY-10, PVY-18, and PVY-43 were obtained and compared with the coat protein sequences of pepper mottle virus (PeMV) [Dougherty WG, Allison RF, Parks TD, Johnston RE, Feild MJ, Armstrong FB (1985) Virology 146: 282–292] and PVY-D [Shukla DD, Inglis AS, McKern NM, Gough KH (1986) Virology 152: 118–125]. The homology between the PVY strains ranged from 96.3 to 99.3% and with the PeMV sequence, 91.4 to 92.9%. Based on this high sequence homology, and the previous observation that coat protein sequences of potyvirus strains are always greater than 90% identical, PeMV could be considered a strain of PVY. However, PVY and PeMV are reported to be only distantly serologically related and on this basis PeMV is currently considered to be an independent member of the Potyvirus group.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01310826
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  • 5
    Electronic Resource
    Electronic Resource
    Coat protein of Potyviruses (1988)
    Springer
    Archives of virology 102 (1988), S. 221-232 
    Details
    ISSN: 1432-8798
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary Three strains of passionfruit woodiness virus, Tip Blight (PWV-TB), Severe (PWV-S) and Mild (PWV-M), were compared on the basis of their biological, serological and coat protein structural properties. Each of the strains could be distinguished on the basis of their reactions on selected test plant species but no differences were observed in the serological properties of the three PWV strains. Molecular weight estimates on SDS-PAGE suggest the PWV coat protein contains 275 amino acid residues and sequence data for 269 of these residues is presented. The amino terminal peptide is blocked and has not been sequenced. The coat proteins of PWV-TB and PWV-S, which cause severe symptoms in infected plants, showed only three sequence differences compared to the eleven or twelve sequence changes between their coat proteins and that of the mild strain. The high sequence homology (96–99%) between the three PWV strains is similar to that previously reported for two strains of tobacco etch virus and three strains of sugarcane mosaic virus. Sequence homology between the three strains of PWV and published sequences for the coat proteins of eight distinct potyviruses ranged from 43–71% (average 57%).
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01310827
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  • 6
    Electronic Resource
    Electronic Resource
    Sequence diversity in the surface-exposed amino-terminal region of the coat proteins of seven strains of sugarcane mosaic virus correlates with their host range (1993)
    Springer
    Archives of virology 132 (1993), S. 399-408 
    Details
    ISSN: 1432-8798
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary The N-terminal region of the coat proteins of five strains (Isis, Brisbane, Sabi, Bundaberg, and BC) of sugarcane mosaic virus (SCMV) isolated from four different plant species (sugarcane, sabi grass, wild sorghum, and blue couch grass) have been compared with the previously published data for SCMV-SC and SCMV-MDB, isolated from sugarcane and maize, respectively. The region, beginning at residue 11 and ending 16 residues beyond the second trypsin cleavage site of the coat protein, varied in size from 68 amino acid residues (Bundaberg) to 115 residues (BC) and contained repeat sequence motifs. Comparisons of the sequence identity and the nature of the repeats in the seven sequences showed that there were five different sequence patterns. These could be grouped further into three subsets which appeared to correlate with the host range of the strains. SCMV-Brisbane, SC, and Isis, isolated from sugarcane, showed almost identical sequence patterns and formed one subset. The other four strains had different sequence patterns and could be grouped further into a Sabi and Bundaberg subset (isolated from sabi grass), and a BC and MDB subset.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01309548
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  • 7
    Electronic Resource
    Electronic Resource
    Cowpea aphid borne mosaic virus-Morocco and South AfricanPassiflora virus are strains of the same potyvirus (1994)
    Springer
    Archives of virology 136 (1994), S. 207-217 
    Details
    ISSN: 1432-8798
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary High performance liquid chromatography (HPLC) profiles of tryptic peptides and partial amino acid sequence analysis have been employed to establish the taxonomic status of the Moroccan isolate of cowpea aphid-borne mosaic virus (CABMV). Some previous reports have suggested CABMV to be very closely related to blackeye cowpea mosaic virus (B1CMV) while other reports have concluded that this relationship is distant. In this report a tryptic digest of the coat protein of CABMV-Morocco was compared with those of the coat proteins of B1CMV-Type, B1CMV-W, the mild mottle strain of peanut stripe virus (PStV-MM) and the NY15 strain of bean common mosaic virus (BCMV-NY15), all of which are now recognised as strains of BCMV. The comparisons also included the NL-3 strain of bean necrosis mosaic virus (BNMV-NL3), which had previously been classified as a strain of BCMV. The HPLC peptide profiles indicated that CABMV-Morocco was distinct from BCMV and BNMV. Amino acid sequence analysis of peptides accounting for more than half of the coat protein confirmed that CABMV-Morocco was not a strain of BNMV or BCMV but was a distinct member of the BCMV subset of viruses that previously has been shown to include BCMV, BNMV, soybean mosaic virus, zucchini yellow mosaic virus, passionfruit woodiness virus and South AfricanPassiflora virus (SAPV). Comparison of the partial sequence data with these and other published sequences revealed that the coat protein of CABMV-Morocco is very similar to that of SAPV suggesting that they are strains of the same virus. Since CABMV was described over 25 years earlier than SAPV, the name CABMV should take precedence and SAPV should be renamed CABMV-SAP, the South AfricanPassiflora strain of CABMV.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01538830
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  • 8
    Electronic Resource
    Electronic Resource
    Nucleotide sequence of the 3′-terminal region of the genome confirms that pea mosaic virus is a strain of bean yellow mosaic potyvirus (1994)
    Springer
    Archives of virology 136 (1994), S. 381-387 
    Details
    ISSN: 1432-8798
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary The 1035 nucleotides at the 3′end of the I strain of pea mosaic potyvirus (PMV-I) genomic RNA, encoding the coat protein, have been cloned and sequenced. A comparison of the derived coat protein sequence with those of the bean yellow mosaic virus (BYMV) strains, CS, S, D and GDD, indicates that PMV-I is a strain of BYMV. Sequence comparisons and hybridisation studies using the 3′-noncoding region support this classification. The nucleotide and protein sequence data also suggest that PMV-I and BYMV-CS form one subset of BYMV strains while the other three strains form another.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01321066
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  • 9
    Electronic Resource
    Electronic Resource
    Insulin and epidermal growth factor receptors contain the cysteine repeat motif found in the tumor necrosis factor receptor (1995)
    New York, NY : Wiley-Blackwell
    Proteins: Structure, Function, and Genetics 22 (1995), S. 141-153 
    Details
    ISSN: 0887-3585
    Keywords: cysteine-rich domains ; disulfide bond predictions ; laminins ; profile searching ; protein structure ; sequence analysis ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Medicine
    Notes: The insulin receptor (INSR) and epidermal growth factor receptor (EGFR) are representatives of two structurally related subfamilies of tyrosine kinase receptors. Using the Wisconsin GCG sequence analysis programs, we have demonstrated that the cysteinerich regions of INSR and EGFR conform to the structural motif found in the tumor necrosis factorreceptor (TNFR) family. The study also revealed that these regions were not composed of simple repeats of eight cysteine residues as previously proposed and that the second Cysrich region of EGFR contained one fewer TNFR repeat than the first. The sequence alignments identified two cysteineresidues in INSR that could be responsible for the additional disulfide bonds known to be involved in dimer formation. The published data on the alignments for the fibronectin type III repeat region of the INSR together with previous cysteine mutagenesis studies indicated that there were two disulfide bonds linking the α and β chains of the INSR, but only one α-β linkage in the insulin-like growth factor 1 receptor (IG 1R). Database searches and sequence alignments showed that the TNFR motif is also found in the cysteine-rich repeats of laminins and the noncatalytic domains of furin-like proteases. If the starting position of the repeat is altered the characteristic laminin repeat of eight cysteine residues can be shown to consist of a TNFR-like motif fused to the last half of an EGF-like repeat. The overlapping regions of these two motifs are known to have identical disulfide bonding patterns and similar protein folds. © 1995 Wiley-Liss, Inc.
    Additional Material: 7 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/prot.340220207
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  • 10
    Electronic Resource
    Electronic Resource
    Coat protein of Potyviruses (1989)
    Springer
    Archives of virology 105 (1989), S. 55-64 
    Details
    ISSN: 1432-8798
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary The amino acid sequence of the coat protein of watermelon mosaic virus 2 (WMV 2) was determined by a combination of peptide and nucleic acid sequencing. The coat protein of WMV 2 contained 281 amino acid residues including a single cysteine at position 132 and a blocked amino terminus. Comparison with the coat protein sequences of 20 strains of ten distinct potyviruses showed sequence homologies ranging from 43% to 69% except for the N strain of soybean mosaic virus (SMV-N), where the sequence homology with WMV 2 was 83%. This degree of homology and the location of sequence differences between WMV 2 and SMV-N is much closer to that observed between strains of the same virus than that found between distinct potyviruses. These data suggest that WMV 2 and SMV-N may be strains of the same virus.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01311116
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