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    • Plusieurs versions

    Erratum to: Linking elements in German: Origin, Change, Functionalization

    Nübling, Damaris, Szczepaniak, Renata
    Morphology, 2013, Vol.23(3), pp.385-385 [Revue évaluée par les pairs]

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    Linking elements--origin, change, and functionalization

    Kurschner, Sebastian, Szczepaniak, Renata
    Morphology, Feb, 2013, Vol.23(1), p.1(6) [Revue évaluée par les pairs]
    Cengage Learning, Inc.
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    Titre: Linking elements--origin, change, and functionalization
    Auteur: Kurschner, Sebastian; Szczepaniak, Renata
    Description: Byline: Sebastian Kurschner (1), Renata Szczepaniak (2) Author Affiliation: (1) Department Germanistik und Komparatistik, University of Erlangen-Nurnberg, Bismarckstrasse 1, 91054, Erlangen, Germany (2) Institut fur Germanistik, Universitat Hamburg, Von-Melle-Park 6, 20146, Hamburg, Germany Article History: Registration Date: 12/06/2013 Online Date: 17/07/2013
    Fait partie de: Morphology, Feb, 2013, Vol.23(1), p.1(6)
    Identifiant: 1871-5621 (ISSN)

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    Linking elements in German Origin, Change, Functionalization.(Report)

    Nubling, Damaris, Szczepaniak, Renata
    Morphology, Feb, 2013, Vol.23(1), p.67(23) [Revue évaluée par les pairs]
    Cengage Learning, Inc.
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    Titre: Linking elements in German Origin, Change, Functionalization.(Report)
    Auteur: Nubling, Damaris; Szczepaniak, Renata
    Sujet: Linking elements ; Compounds ; Grammaticalization ; Exaptation ; Language change;
    Description: Byline: Damaris Nubling (1), Renata Szczepaniak (2) Keywords: Linking elements; Compounds; Grammaticalization; Exaptation; Language change Abstract: Contemporary German is known for its complex system of linking elements. They not only show different degrees of productivity (between unproductive -es- and very productive -s-), but also exhibit functional diversity, with some of them even allowing plural interpretation, e.g. -er- in Volk+er+kunde 'ethnology' vs. Volk+s+kunde 'folklore'. In this paper, we argue that this is due to the complex historical development from two different sources. The first layer of linking elements, which arose out of Germanic primary suffixes, was reduced to one member, the "older" linking -e-, already in Old High German (e.g. in NHG Tag+e+werk 'daily task'). The current functional diversity of the linking elements is primarily due to the later evolution out of inflectional endings. The dissociation from the second source has included a gradual change of the assignment rules from lexical (gender, declension class) to prosodic (formal) level. Thus, the current distribution of the most developed linking -s- is the most formalized one, as it can be directly deduced from the prosodic form of the first constituent. The development of the second layer of linking elements resembles the process of grammaticalization. However, linking elements form part of word formation and therefore are not the typical result of grammaticalization. Author Affiliation: (1) Deutsches Institut, Johannes Gutenberg-Universitat, Jakob Welder-Weg 18, 55099, Mainz, Germany (2) Institut fur Germanistik, Universitat Hamburg, Von-Melle-Park 6, 20146, Hamburg, Germany Article History: Registration Date: 12/06/2013 Online Date: 17/07/2013 Article note: The research for the present article forms part of a larger project on 'Determinants of language variation' funded by the University of Mainz (2010).
    Fait partie de: Morphology, Feb, 2013, Vol.23(1), p.67(23)
    Identifiant: 1871-5621 (ISSN)

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    Telling it straight: a comparison of selected English and Polish idioms from the semantic field of speaking.(Report)

    Szczepaniak, Renata, Adamska - Salaciak, Arleta
    Studia Anglica Posnaniensia: international review of English Studies, Jan, 2010, Vol.46(1), p.71(23) [Revue évaluée par les pairs]

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    Linking elements—origin, change, and functionalization

    Kürschner, Sebastian, Szczepaniak, Renata
    Morphology, 2013, Vol.23(1), pp.1-6 [Revue évaluée par les pairs]
    Springer Science & Business Media B.V.
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    Titre: Linking elements—origin, change, and functionalization
    Auteur: Kürschner, Sebastian; Szczepaniak, Renata
    Sujet: Linguistics ; Linguistics (General) ; Comparative Linguistics ; Phonology ; Sign Language ; Languages & Literatures;
    Fait partie de: Morphology, 2013, Vol.23(1), pp.1-6
    Identifiant: 1871-5621 (ISSN); 1871-5656 (E-ISSN); 10.1007/s11525-013-9215-7 (DOI)

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    Linking elements in German Origin, Change, Functionalization

    Nübling, Damaris, Szczepaniak, Renata
    Morphology, 2013, Vol.23(1), pp.67-89 [Revue évaluée par les pairs]
    Springer Science & Business Media B.V.
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    Titre: Linking elements in German Origin, Change, Functionalization
    Auteur: Nübling, Damaris; Szczepaniak, Renata
    Sujet: Linking elements ; Compounds ; Grammaticalization ; Exaptation ; Language change
    Description: Contemporary German is known for its complex system of linking elements. They not only show different degrees of productivity (between unproductive - es - and very productive - s -), but also exhibit functional diversity, with some of them even allowing plural interpretation, e.g. - er - in Völk + er + kunde ‘ethnology’ vs. Volk + s + kunde ‘folklore’. In this paper, we argue that this is due to the complex historical development from two different sources. The first layer of linking elements, which arose out of Germanic primary suffixes, was reduced to one member, the “older” linking - e -, already in Old High German (e.g. in NHG Tag + e + werk ‘daily task’). The current functional diversity of the linking elements is primarily due to the later evolution out of inflectional endings. The dissociation from the second source has included a gradual change of the assignment rules from lexical (gender, declension class) to prosodic (formal) level. Thus, the current distribution of the most developed linking - s - is the most formalized one, as it can be directly deduced from the prosodic form of the first constituent. The development of the second layer of linking elements resembles the process of grammaticalization. However, linking elements form part of word formation and therefore are not the typical result of grammaticalization.
    Fait partie de: Morphology, 2013, Vol.23(1), pp.67-89
    Identifiant: 1871-5621 (ISSN); 1871-5656 (E-ISSN); 10.1007/s11525-013-9213-9 (DOI)

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    Disulfide bond formation in the herpes simplex virus 1 UL6 protein is required for portal ring formation and genome encapsidation

    Albright, Brandon S, Nellissery, Jacob, Szczepaniak, Renata, Weller, Sandra K
    Journal of virology, September 2011, Vol.85(17), pp.8616-24 [Revue évaluée par les pairs]
    MEDLINE/PubMed (U.S. National Library of Medicine)
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    Titre: Disulfide bond formation in the herpes simplex virus 1 UL6 protein is required for portal ring formation and genome encapsidation
    Auteur: Albright, Brandon S; Nellissery, Jacob; Szczepaniak, Renata; Weller, Sandra K
    Sujet: Protein Multimerization ; Virus Assembly ; Disulfides -- Metabolism ; Herpesvirus 1, Human -- Physiology ; Viral Proteins -- Metabolism
    Description: The herpes simplex virus 1 (HSV-1) UL6 portal protein forms a 12-subunit ring structure at a unique capsid vertex which functions as a conduit for the encapsidation of the viral genome. We have demonstrated previously that the leucine zipper region of UL6 is important for intersubunit interactions and stable ring formation (J. K. Nellissery, R. Szczepaniak, C. Lamberti, and S. K. Weller, J. Virol. 81:8868-8877, 2007). We now demonstrate that intersubunit disulfide bonds exist between monomeric subunits and contribute to portal ring formation and/or stability. Intersubunit disulfide bonds were detected in purified portal rings by SDS-PAGE under nonreducing conditions. Furthermore, the treatment of purified portal rings with dithiothreitol (DTT) resulted in the disruption of the rings, suggesting that disulfide bonds confer stability to this complex structure. The UL6 protein contains nine cysteines that were individually mutated to alanine. Two of these mutants, C166A and C254A, failed to...
    Fait partie de: Journal of virology, September 2011, Vol.85(17), pp.8616-24
    Identifiant: 1098-5514 (E-ISSN); 21593161 Version (PMID); 10.1128/JVI.00123-11 (DOI)

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    Vokalharmonie im Althochdeutschen und im Walserdeutschen. Ein Fall von phonologisch-typologischer Kontinuität

    Szczepaniak, Renata
    Zeitschrift für Dialektologie und Linguistik, 1 January 2007, Vol.74(1), pp.38-60 [Revue évaluée par les pairs]
    Archival Journals (JSTOR)
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    Titre: Vokalharmonie im Althochdeutschen und im Walserdeutschen. Ein Fall von phonologisch-typologischer Kontinuität
    Auteur: Szczepaniak, Renata
    Sujet: Languages & Literatures;
    Description: Processes of vowel assimilation can be observed in Old High German and in the Walser German of Issime (töitschu) in the German-speaking enclave north of Ivrea in Piedmont. We can regard the vowel harmony of Walser German (fümmela > fümmala 'Frau'; süjenwirdschu > süjuwurudschu' suchen wir sie') as a direct continuation and elaboration of a type of vowel assimilation already known from Old High German (wolkan 'Wolke' vs. wolkono [genitive plural]). The Old High German vowel assimilation is confined to the vowel in direct proximity, but in the Walser German of Issime several vowels may be subject to alteration. A further argument for the direct continuity of vowel harmony in Walser German is provided by the phonological typology operating on the level of words and syllables. Old High German shares a number of syllabic features with the Walser German of Issime and the vowel assimilation investigated in the present article is one of these.
    Fait partie de: Zeitschrift für Dialektologie und Linguistik, 1 January 2007, Vol.74(1), pp.38-60
    Identifiant: 00441449 (ISSN)

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    The Exonuclease Activity of Herpes Simplex Virus 1 UL12 Is Required for Production of Viral DNA That Can Be Packaged To Produce Infectious Virus

    Grady, Lorry M, Szczepaniak, Renata, Murelli, Ryan P, Masaoka, Takeshi, Le Grice, Stuart F J, Wright, Dennis L, Weller, Sandra K
    Journal of virology, 01 December 2017, Vol.91(23) [Revue évaluée par les pairs]
    MEDLINE/PubMed (U.S. National Library of Medicine)
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    Titre: The Exonuclease Activity of Herpes Simplex Virus 1 UL12 Is Required for Production of Viral DNA That Can Be Packaged To Produce Infectious Virus
    Auteur: Grady, Lorry M; Szczepaniak, Renata; Murelli, Ryan P; Masaoka, Takeshi; Le Grice, Stuart F J; Wright, Dennis L; Weller, Sandra K
    Sujet: DNA Recombination ; DNA Replication ; Hsv ; Ul12 ; Drug Discovery ; Exonucleases ; Viral DNA ; Mutation ; Virus Assembly ; Deoxyribonucleases -- Metabolism ; Herpesvirus 1, Human -- Pathogenicity ; Viral Proteins -- Metabolism
    Description: The herpes simplex virus (HSV) type I alkaline nuclease, UL12, has 5'-to-3' exonuclease activity and shares homology with nucleases from other members of the family. We previously reported that a UL12-null virus exhibits a severe defect in viral growth. To determine whether the growth defect was a result of loss of nuclease activity or another function of UL12, we introduced an exonuclease-inactivating mutation into the viral genome. The recombinant virus, UL12 D340E (the D340E mutant), behaved identically to the null virus (AN-1) in virus yield experiments, exhibiting a 4-log decrease in the production of infectious virus. Furthermore, both viruses were severely defective in cell-to-cell spread and produced fewer DNA-containing capsids and more empty capsids than wild-type virus. In addition, DNA packaged by the viral mutants was aberrant, as determined by infectivity assays and pulsed-field gel electrophoresis. We conclude that UL12 exonuclease activity is essential for the production...
    Fait partie de: Journal of virology, 01 December 2017, Vol.91(23)
    Identifiant: 1098-5514 (E-ISSN); 28956767 Version (PMID); 10.1128/JVI.01380-17 (DOI)

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    The putative herpes simplex virus 1 chaperone protein UL32 modulates disulfide bond formation during infection

    Albright, Brandon S, Kosinski, Athena, Szczepaniak, Renata, Cook, Elizabeth A, Stow, Nigel D, Conway, James F, Weller, Sandra K
    Journal of virology, January 2015, Vol.89(1), pp.443-53 [Revue évaluée par les pairs]
    MEDLINE/PubMed (U.S. National Library of Medicine)
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    Titre: The putative herpes simplex virus 1 chaperone protein UL32 modulates disulfide bond formation during infection
    Auteur: Albright, Brandon S; Kosinski, Athena; Szczepaniak, Renata; Cook, Elizabeth A; Stow, Nigel D; Conway, James F; Weller, Sandra K
    Sujet: Virus Assembly ; Disulfides -- Metabolism ; Herpesvirus 1, Human -- Physiology ; Viral Proteins -- Metabolism
    Description: During DNA encapsidation, herpes simplex virus 1 (HSV-1) procapsids are converted to DNA-containing capsids by a process involving activation of the viral protease, expulsion of the scaffold proteins, and the uptake of viral DNA. Encapsidation requires six minor capsid proteins (UL6, UL15, UL17, UL25, UL28, and UL33) and one viral protein, UL32, not found to be associated with capsids. Although functions have been assigned to each of the minor capsid proteins, the role of UL32 in encapsidation has remained a mystery. Using an HSV-1 variant containing a functional hemagglutinin-tagged UL32, we demonstrated that UL32 was synthesized with true late kinetics and that it exhibited a previously unrecognized localization pattern. At 6 to 9 h postinfection (hpi), UL32 accumulated in viral replication compartments in the nucleus of the host cell, while at 24 hpi, it was additionally found in the cytoplasm. A newly generated UL32-null mutant was used to confirm that although B capsids containing... Although functions have been assigned to six of the seven required packaging proteins of HSV, the role of UL32 in encapsidation has remained a mystery. UL32 is a cysteine-rich viral protein that contains C-X-X-C motifs reminiscent of those in proteins that participate in the regulation of disulfide bond formation. We have previously demonstrated that disulfide bonds are required for the formation and stability of the viral capsids and are also important for the formation and stability of the UL6 portal ring. In this report, we demonstrate that the disulfide bond profiles of the viral proteins UL6, UL25, and VP19C and the viral protease, VP24, are altered in cells infected with a newly isolated UL32-null mutant virus, suggesting that UL32 acts as a chaperone capable of modulating disulfide bond formation. Furthermore, these results suggest that proper regulation of disulfide bonds is essential for initiating encapsidation.
    Fait partie de: Journal of virology, January 2015, Vol.89(1), pp.443-53
    Identifiant: 1098-5514 (E-ISSN); 25320327 Version (PMID); 10.1128/JVI.01913-14 (DOI)