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Roswitha Löwer

Researcher at Paul Ehrlich Institute

Publications -  37
Citations -  3387

Roswitha Löwer is an academic researcher from Paul Ehrlich Institute. The author has contributed to research in topics: Endogenous retrovirus & Retrovirus. The author has an hindex of 27, co-authored 37 publications receiving 3211 citations.

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The viruses in all of us: characteristics and biological significance of human endogenous retrovirus sequences

TL;DR: The demonstrable and potential roles of HTDV/HERV-K as well as of other human elements in disease and in maintaining genome plasticity are illustrated.
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Identification of human endogenous retroviruses with complex mRNA expression and particle formation.

TL;DR: In this article, the expression pattern of a family of human endogenous retrovirus sequences (HERV-K) in GH cells, a teratocarcinoma cell line producing the human TERATOCCARINoma-derived retrovirirus (HTDV) particles previously described by us, was described.
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Identification of a Rev-related protein by analysis of spliced transcripts of the human endogenous retroviruses HTDV/HERV-K.

TL;DR: The human endogenous retrovirus family HTDV/HERV-K codes for the viral particles observed in teratocarcinoma cell lines, and secondary structure analysis reveals similarities to basic helix-loop-helix proteins.
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Evidence That HERV-K Is the Endogenous Retrovirus Sequence That Codes for the Human Teratocarcinoma-Derived Retrovirus HTDV

TL;DR: Results provide evidence that HERV-K codes for HTDV, an expressed human endogenous retrovirus sequence that is regularly observed by electron microscopy at low frequency in cell lines established from human teratocarcinomas.
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The non-autonomous retrotransposon SVA is trans-mobilized by the human LINE-1 protein machinery

TL;DR: It is demonstrated that SVA elements are mobilized in HeLa cells only in the presence of both L1-encoded proteins, ORF1p and ORF2p, and SVA trans-mobilization rates exceeded pseudogene formation frequencies by 12- to 300-fold in He La-HA cells, indicating that S VA elements represent a preferred substrate for L1 proteins.