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  • 1
    Electronic Resource
    Electronic Resource
    The distributions of nucleotides near bacterial transcription initiation and termination sites show distinct signals that may affect DNA geometry (1987)
    Springer
    Journal of molecular evolution 26 (1987), S. 187-197 
    Details
    ISSN: 1432-1432
    Keywords: Transcription initiation ; Transcription termination ; Sequence signals ; DNA geometry
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary Compilation and analysis of all bacterial sequences which are aligned by their transcription initiation sites show a dramatic behavior of the four nucleotides. Large peaks of T and A are observed. This highly nonrandom distribution is likely to affect the DNA geometry in addition to affecting the strength of binding between the two DNA strands. Following this site, the G and C rise above their overall bacterial mean. Alignment by transcription termination sites indicates that this behavior continues till the mRNA 3′ termini. At this site the concentrations of A and T rise again above the mean. Analysis of the distributions of the 256 quartets in the 1000 nucleotide regions surrounding both transcription initiation and termination sites has been carried out. Some A/T combination sequences may serve as signals to the bacterial transcription machinery, in addition to the well-established T T G A C A and T A T A A T at positions −35 and −10, respectively, and a run of Ts at the transcription termination site. The frequent occurrences of (dA)/(dT) runs in the vicinity of these sites may result in curved DNA structures, affecting recognition and the nature of the interaction between the RNA polymerase and the DNA.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02099851
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  • 2
    Electronic Resource
    Electronic Resource
    PREPARATIVE ELECTROPHORESIS OF PROTEINS IN ACRYLAMIDE GELS (1964)
    Oxford, UK : Blackwell Publishing Ltd
    Annals of the New York Academy of Sciences 121 (1964), S. 0 
    Details
    ISSN: 1749-6632
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Natural Sciences in General
    Notes: (1) A simple apparatus is described for adaption of the “disc” electrophoresis techniques to a preparative procedure that permits analytic and radioactive monitoring of the effluent fractions automatically.(2) The efficiency of the procedure for separating a model system consisting of ribonuclease, trypsin, and chymotrypsin has been demonstrated. In addition, preliminary results concerning the separation of the unexpected multiple proteins of poliovirus are presented.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1749-6632.1964.tb14211.x
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  • 3
    Electronic Resource
    Electronic Resource
    The HIV-1 rev trans -activator acts through a structured target sequence to activate nuclear export of unspliced viral mRNA (1989)
    [s.l.] : Nature Publishing Group
    Nature 338 (1989), S. 254-257 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] In the absence of Rev, the genomic HIV-1 tat gene expression vector pgTAT6 (Fig. la) predominantly expresses a fully spliced cytoplasmic tat mRNA (Fig. 16, lane 9) that encodes the 86-residue form of the HIV-1 Tat protein (Fig. Ic, lane 1). In the presence of Rev, pgTAT produces a high level of an ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/338254a0
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  • 4
    Electronic Resource
    Electronic Resource
    Sequence of reovirus haemagglutinin predicts a coiled-coil structure (1985)
    [s.l.] : Nature Publishing Group
    Nature 315 (1985), S. 421-423 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] Fig. 1 The determined nucleotide of reovirus type 3 SI gene and predicted amino-acid sequences for both open reading frames. The One-letter ammo-acid notation used is recommenced hv the UPAC IUB Commission on Biochemical Nomenclature22. The numbers given above the amino-acid sequence designate the ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/315421a0
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  • 5
    Electronic Resource
    Electronic Resource
    Evolution of a Common Structural Core in the Internal Ribosome Entry Sites of Picornavirus (1998)
    Springer
    Virus genes 16 (1998), S. 25-38 
    Details
    ISSN: 1572-994X
    Keywords: internal ribosome entry site ; initiation of translation ; picornaviridae ; phylogeny ; evolution
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract The translational control involving internal ribosome binding occurs in poliovirus (PV), human rhinoviruses (HRV), encephalomyocarditis virus (EMCV), foot-and-mouth disease virus (FMDV), and hepatitis A virus (HAV). Internal ribosome binding utilizes cis-acting genetic elements of approximately 450 nucleotides (nt) termed the internal ribosome entry sites (IRES) found in these picornaviral 5′-untranslated region (5′UTR). Although these IRES elements are quite different in their primary sequence, a similar folding structure with a conserved 3′ structural core exists in the IRES. Phylogenetic analysis and RNA folding of the 5′ UTR of picornaviruses, including PV types 1–3, coxsackievirus types A and B, swine vesicular disease virus, echoviruses, enteroviruses (human and bovine), HRV, HAV, EMCV, mengovirus, Theiler’s murine encephalomyelitis viruses, FMDV, and equine rhinoviruses, indicates that the predicted conserved structural core is indeed a general structural feature for all members of the picornavirus family. The evolution of a common structural core likely occurred by the gradual addition or deletion of structural domains and elements to preserve a similar tertiary structure that facilitates the utilization of the IRES in specific host-cell environments.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1007941524143
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  • 6
    Electronic Resource
    Electronic Resource
    Phylogenetic Evidence for the Improved RNA Higher-Order Structure in Internal Ribosome Entry Sequences of HCV and Pestiviruses (1998)
    Springer
    Virus genes 17 (1998), S. 279-295 
    Details
    ISSN: 1572-994X
    Keywords: translational control ; internal ribosome entry site ; RNA structure ; phylogenetic comparison ; HCV and pestivirus
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract The strong requirement for a small segment of the 5′-proximal coding sequence of hepatitis C virus (HCV) is one of the most remarkable features in the internal initiation of HCV mRNA translation. Phylogenetic analysis and RNA folding indicate a common RNA structure of the 5′ untranslated region (UTR) of HCV and the animal pestiviruses, including HCV types 1–11, bovine viral diarrhea (BVDV), border disease virus (BDV) and hog cholera (HoCV). Although the common RNA structure shares similar features to that proposed for the internal ribosome entry sequence (IRES) of picornavirus, phylogenetic evidence suggests four new tertiary interactions between conserved terminal hairpin loops and between the terminal hairpin loop of F2b and the short coding sequence for HCV and pestiviruses. We suggest that the higher-order structures of IRES cis-acting elements for HCV and animal pestivirus are composed of stem-loop structures B-C, domains E-H, stem-loop structure J and four additional tertiary interactions. The common structure of IRES elements for these viruses forms a compact structure by these tertiary interactions and stem stacking. The active structural core is centered in the junction domain of E-H that is also conserved in all members of picornaviruses. Our model suggests that the requirement for a small segment of the 5′ coding sequence is to form the distinct tertiary structure that facilitates the cis-acting function of the HCV IRES in the internal initiation of the translational control.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1008073905920
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  • 7
    Electronic Resource
    Electronic Resource
    A common structural core in the internal ribosome entry sites of picornavirus, hepatitis C virus, and pestivirus (1996)
    Springer
    Virus genes 12 (1996), S. 135-147 
    Details
    ISSN: 1572-994X
    Keywords: translation control ; internal ribosome entry site ; phylogenetic comparative analysis ; RNA folding and common structure
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract Cap-independent translations of viral RNAs of enteroviruses and rhinoviruses, cardioviruses and aphthoviruses, hepatitis A and C viruses (HAV and HCV), and pestivirus are initiated by the direct binding of 40S ribosomal subunits to acis-acting genetic element termed theinternal ribosome entry site (IRES) orribosome landing pad (RLP) in the 5′ noncoding region (5′NCR). RNA higher ordered structure models for these IRES elements were derived by a combined approach using thermodynamic RNA folding, Monte Carlo simulation, and phylogenetic comparative analysis. The structural differences among the three groups of picornaviruses arise not only from point mutations, but also from the addition or deletion of structural domains. However, a common core can be identified in the proposed structural models of these IRES elements from enteroviruses and rhinoviruses, cardioviruses and aphthoviruses, and HAV. The common structural core identified within the picornavirus IRES is also conserved in the 5′NCR of the divergent viruses, HCV, and pestiviruses. Furthermore, the proposed structural motif shares a structural feature similar to that observed in the catalytic core of the group I intron. The conserved structural motif from these divergent sequences that looks like the common core region of group I introns is probably a crucial element involved in the IRES-dependent translation.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00572952
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  • 8
    Electronic Resource
    Electronic Resource
    SDS-acrylamide gel electrophoresis and its application to the proteins of poliovirus-and adenovirus-infected human cells (1970)
    New York, NY [u.a.] : Wiley-Blackwell
    Journal of Cellular Physiology 76 (1970), S. 273-287 
    Details
    ISSN: 0021-9541
    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: Sensitive techniques for acrylamide gel electrophoretic analysis have been applied to animal virus systems and have proven generally useful. Estimates of the number of kinds, molecular weights and number of molecules of proteins in almost any biological sample have been made with ease. As applied to the poliovirus-HeLa cell system they reveal four major proteins in the virion and at least ten additional proteins in the infected cell. Some of the intracellular and particulate proteins undergo cleavage reactions following a unique translation in which the genome is apparently translated in toto as one large polypeptide of molecular weight greater than 200,000 daltons. The splits occur at three levels: (a) during synthesis; (b) at intermediate stages; and (c) co-incident with maturation. In vitro studies on protein synthesis, RNA synthesis and virus assembly have substantiated and extended the in vivo observations. The structure of the adenovirion has been established in detail. Hexon, penton base, fiber and core polypeptides and certain relevant subviral structures have been identified. Nearly all of the proteins synthesized in the infected cells after 20 hours are viral. The major structural antigens (hexon and penton) predominate and are made in 10 to 50 fold excess but the internal core polypeptides are not produced in great excess. Studies on the synthesis of polypeptides and their assembly into morphological subunits and virions show that hexon and penton polypeptides are made in about four and two minutes respectively on cytoplasmic polyribosomes, that morphological subunits are formed within five minutes of synthesis of protein, and that there is a delay of greater than one half hour for entry of hexons into virions.
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jcp.1040760307
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