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  • 1
    Electronic Resource
    Electronic Resource
    Mechanism of interaction of O-amino-D-serine with sheep liver serine hydroxymethyltransferase (1989)
    s.l. : American Chemical Society
    Biochemistry 28 (1989), S. 9607-9612 
    Details
    ISSN: 1520-4995
    Source: ACS Legacy Archives
    Topics: Biology , Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1021/bi00451a009
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  • 2
    Electronic Resource
    Electronic Resource
    Mode of interaction of aminooxy compounds with sheep liver serine hydroxymethyltransferase (1989)
    s.l. : American Chemical Society
    Biochemistry 28 (1989), S. 9613-9617 
    Details
    ISSN: 1520-4995
    Source: ACS Legacy Archives
    Topics: Biology , Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1021/bi00451a010
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  • 3
    Electronic Resource
    Electronic Resource
    Symmetry of belladonna mottle virus: rotation function studies (1987)
    Copenhagen : International Union of Crystallography (IUCr)
    Acta crystallographica 43 (1987), S. 376-382 
    Details
    ISSN: 1600-5740
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Chemistry and Pharmacology , Geosciences , Physics
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1107/S0108768187097702
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  • 4
    Electronic Resource
    Electronic Resource
    Molecular characterization and interviral relationships of a flexuous filamentous virus causing mosaic disease of sugarcane (Saccharum officinarum L.) in India (1999)
    Springer
    Archives of virology 144 (1999), S. 479-490 
    Details
    ISSN: 1432-8798
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary.  A virus isolate causing mosaic disease of commercial sugarcane was purified to homogeneity. Electron microscopy revealed flexuous filamentous virus particles of ca 890 × 15 nm. The virus isolate reacted positively with heterologous antiserum to narcissus latent virus form UK, but failed to react with potyvirus group specific antiserum. N-terminal sequencing of the intact coat protein (CP) and the tryptic peptides indicated that the virus was probably a potyvirus but distinct from several reported potyviruses. Comparison of the 3′-terminal 1084 nucleotide sequence of the RNA genome of this virus revealed 93.6% sequence identity in the coat protein coding region with the recently described sugarcane streak mosaic virus (Pakistani isolate). The molecular weight of the coat protein (40 kDa) was higher than that deduced from the amino acid sequence (34 kDa). The apparent increase in size was shown to be due to glycosylation of the coat protein which has not been reported thus far in the family, Potyviridae. This is the first report on the molecular characterization of a virus causing mosaic disease of sugarcane in India and the results demonstrate that the virus is a strain of sugarcane streak mosaic virus, a member of the Tritimovirus genus of the Potyviridae. We have named it sugarcane streak mosaic virus – Andhra Pradesh isolate (SCSMV-AP).
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s007050050519
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  • 5
    Electronic Resource
    Electronic Resource
    Genomic sequence of physalis mottle virus and its evolutionary relationship with other tymoviruses (1998)
    Springer
    Archives of virology 143 (1998), S. 1489-1500 
    Details
    ISSN: 1432-8798
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary.  The genome of physalis mottle tymovirus (PhMV) is 6673 nucleotides long and is rich in cytosine residues (40.58%) like other tymoviruses. The organization of the genes is also similar to that of five other tymoviruses whose sequences are known. However, PhMV has the longest 3 ′ noncoding region as well as the longest replicase (RP) ORF. The RP sequences are similar to those of other tymoviruses (48–60% identity) whereas the coat proteins (CP) and the overlapping proteins (OP) are conserved to a lesser extent (30–50% and 26–34% respectively). A tetra peptide “GILG” was found to be present in all the tymoviral OPs. The PhMV RP also possesses the methyl transferase, polymerase and the helicase motifs found in all the Sindbis-like super group of plant viruses. A phylogenetic analysis of the six tymoviral sequences revealed that they do not have a rigid hierarchical similarity relationship.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s007050050392
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  • 6
    Electronic Resource
    Electronic Resource
    Mutational analysis of the NIa protease from pepper vein banding potyvirus (2000)
    Springer
    Archives of virology 145 (2000), S. 2493-2502 
    Details
    ISSN: 1432-8798
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary.  The nuclear inclusion protein a (NIa) protease plays an important role in the life cycle of potyviruses by processing the viral polyprotein into functional proteins. For functional characterization, the NIa protease from Pepper vein banding potyvirus (PVBV) was overexpressed in Escherichia coli and purified. Using a recombinant polyprotein substrate containing the nuclear inclusion protein b (NIb)-coat protein (CP) cleavage site, a trans-cleavage assay was developed for the NIa protease. The polyprotein substrate also possessed the cleavage site between NIa and NIb, in addition to the NIb-CP site. However, no trans-cleavage by the NIa protease between NIa and NIb was detected indicating that the cleavage between NIa and NIb under natural conditions would be by a cis-cleavage reaction. Site-specific mutations of the conserved residues D81, D90, C110, T146, C151 and H167 were performed to investigate their roles in the catalytic process of the protease. Such an analysis has revealed that D81 and C151 constitute two of the catalytic triad residues in the NIa protease, D90 and C110 are not essential for catalysis, and T146 and H167 are probably involved in binding to Gln at the P1 position of the substrate.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s007050070004
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  • 7
    Electronic Resource
    Electronic Resource
    Determination of 3′-terminal nucleotide sequence of pepper\break vein banding virus RNA and expression of its coat protein in Escherichia coli (1999)
    Springer
    Archives of virology 144 (1999), S. 1679-1687 
    Details
    ISSN: 1432-8798
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary.  Pepper vein banding virus (PVBV) is an important virus infecting chilli pepper in south India. Earlier reports suggested it to be a distinct potyvirus. The nucleotide sequence of PVBV RNA from the 3′-end (3862 nt) was determined. Analysis of the nucleotide and deduced amino acid sequence revealed that it encompasses a partial open reading frame encoding the partial sequence of VPg, NIa-protease, NIb, coat protein (CP) and 3′-untranslated region (UTR). Comparison of the amino acid sequence of CP and the nucleotide sequence of 3′-UTR with those of other potyviruses confirmed an earlier observation that PVBV is a distinct member of the Potyvirus sub-group and it had significant similarity to a recently characterized virus infecting chilli pepper, chilli vein-banding mottle virus (CVbMV), from Thailand. The analysis showed that both PVBV and CVbMV might represent strains of the same virus. Further, the PVBV CP gene was overexpressed in E. coli, which assembled into potyvirus-like particles (PVLPs). The assembled particles were shown to encapsidate the CP mRNA.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s007050050696
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  • 8
    Electronic Resource
    Electronic Resource
    Nucleotide sequence of the 3′ terminal region of belladonna mottle virus-Iowa (renamed Physalis mottle virus) RNA and an analysis of the relationships of tymoviral coat proteins (1992)
    Springer
    Archives of virology 123 (1992), S. 367-377 
    Details
    ISSN: 1432-8798
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary The 3′ terminal 1255nt sequence of Physalis mottle virus (PhMV) genomic RNA has been determined from a set of overlapping cDNA clones. The open reading frame (ORF) at the 3′ terminus corresponds to the amino acid sequence of the coat protein (CP) determined earlier except for the absence of the dipeptide, Lys-Leu, at position 110–111. In addition, the sequence upstream of the CP gene contains the message coding for 178 amino acid residues of the C-terminus of the putative replicase protein (RP). The sequence downstream of the CP gene contains an untranslated region whose terminal 80 nucleotides can be folded into a characteristic tRNA-like structure. A phylogenetic tree constructed after aligning separately the sequence of the CP, the replicase protein (RP) and the tRNA-like structure determined in this study with the corresponding sequences of other tymoviruses shows that PhMV wrongly named belladonna mottle virus [BDMV(I)] is a separate tymovirus and not another strain of BDMV(E) as originally envisaged. The phylogenetic tree in all the three cases is identical showing that any subset of genomic sequence of sufficient length can be used for establishing evolutionary relationships among tymoviruses.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01317270
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  • 9
    Electronic Resource
    Electronic Resource
    Structure-function relationships of icosahedral plant viruses (1989)
    Springer
    Archives of virology 109 (1989), S. 153-172 
    Details
    ISSN: 1432-8798
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary X-ray diffraction studies on single crystals of a few viruses have led to the elucidation of their three dimensional structure at near atomic resolution. Both the tertiary structure of the coat protein subunit and the quaternary organization of the icosahedral capsid in these viruses are remarkably similar. These studies have led to a critical re-examination of the structural principles in the architecture of isometric viruses and suggestions of alternative mechanisms of assembly. Apart from their role in the assembly of the virus particle, the coat proteins of certian viruses have been shown to inhibit the replication of the cognate RNA leading to cross-protection. The coat protein amino acid sequence and the genomic sequence of several spherical plant RNA viruses have been determined in the last decade. Experimental data on the mechanisms of uncoating, gene expression and replication of several classes of viruses have also become available. The function of the non-structural proteins of some viruses have been determined. This rapid progress has provided a wealth of information on several key steps in the life cycle of RNA viruses. The function of the viral coat protein, capsid architecture, assembly and disassembly and replication of isometric RNA plant viruses are discussed in the light of this accumulated knowledge.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01311078
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