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  RNase H activity of HIV reverse transcriptases is confined exclusively to the dimeric forms

Restle, T., Müller, B., & Goody, R. S. (1992). RNase H activity of HIV reverse transcriptases is confined exclusively to the dimeric forms. FEBS Letters, 300(1), 97-100. doi:10.1016/0014-5793(92)80172-D.

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FEBSLett_300_1992_97.pdf (Any fulltext), 462KB
 
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 Creators:
Restle, Tobias1, 2, Author              
Müller, Barbara, Author
Goody, Roger S.1, Author              
Affiliations:
1Emeritus Group Biophysics, Max Planck Institute for Medical Research, Max Planck Society, ou_1497712              
2Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society, ou_1497700              

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Free keywords: HIV; Reverse transcriptase; RNase H; Dimerization
 Abstract: A method for the rapid preparation of a defined substrate to monitor RNase H activity has been developed. Using this substrate, we have investigated the RNase H activities of the different forms of recombinant HIV-1 and HIV-2 reverse transcriptase (RT) in detail. As we report here, RNase H activity is associated only with the dimeric forms (p51/p66 or p66/p66) of the enzymes.

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Language(s): eng - English
 Dates: 1992-01-301992-03-23
 Publication Status: Published in print
 Pages: 4
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 Table of Contents: -
 Rev. Type: Peer
 Degree: -

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Title: FEBS Letters
  Other : FEBS Lett.
Source Genre: Journal
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Publ. Info: Amsterdam : Elsevier
Pages: - Volume / Issue: 300 (1) Sequence Number: - Start / End Page: 97 - 100 Identifier: ISSN: 0014-5793
CoNE: https://pure.mpg.de/cone/journals/resource/954925399501