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Relevant bibliographies by topics / RNases H

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Journal articles

Academic literature on the topic 'RNases H'

Author: Grafiati

Published: 4 May 2024

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Journal articles on the topic "RNases H"

1

Allen, S. J. W., S. H. Krawczyk, L. R. McGee, N. Bischofberger, A. S. Mulato, and J. M. Cherrington. "Inhibition of HIV-1 RNase H Activity by Nucleotide Dimers and Monomers." Antiviral Chemistry and Chemotherapy 7, no. 1 (1996): 37–45. http://dx.doi.org/10.1177/095632029600700107.

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Nucleotide dimers and monomers were shown to inhibit human immunodeficiency virus type 1 (HIV) RNase H activity. Several effective inhibitors were identified and placed into three general groups based on biochemical characterization of their inhibition, The first group (group A) inhibited HIV RNase H and the closely related feline immunodeficiency virus (FIV) RNase H, but did not inhibit less related retroviral or cellular RNases H or HIV reverse transcriptase (RT). The second group (group B) inhibited the RNase H activity of several retroviruses as well as the reverse transcriptase function o

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2

Leich, Franziska, Nadine Stöhr, Anne Rietz, Renate Ulbrich-Hofmann, and Ulrich Arnold. "Endocytotic Internalization as a Crucial Factor for the Cytotoxicity of Ribonucleases." Journal of Biological Chemistry 282, no. 38 (2007): 27640–46. http://dx.doi.org/10.1074/jbc.m702240200.

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The cytotoxic action of ribonucleases (RNases) requires the interaction of the enzyme with the cellular membrane, its internalization, translocation to the cytosol, and the degradation of ribonucleic acid. The interplay of these processes as well as the role of the thermodynamic and proteolytic stability, the catalytic activity, and the evasion from the intracellular ribonuclease inhibitor (RI) has not yet been fully elucidated. As cytosolic internalization is indispensable for the cytotoxicity of extracellular ribonucleases, we investigated the extent of cytosolic internalization of a cytotox

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3

Watkins, Harriet A., and Edward N. Baker. "Structural and Functional Characterization of an RNase HI Domain from the Bifunctional Protein Rv2228c from Mycobacterium tuberculosis." Journal of Bacteriology 192, no. 11 (2010): 2878–86. http://dx.doi.org/10.1128/jb.01615-09.

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ABSTRACT The open reading frame Rv2228c from Mycobacterium tuberculosis is predicted to encode a protein composed of two domains, each with individual functions, annotated through sequence similarity searches. The N-terminal domain is homologous with prokaryotic and eukaryotic RNase H domains and the C-terminal domain with α-ribazole phosphatase (CobC). The N-terminal domain of Rv2228c (Rv2228c/N) and the full-length protein were expressed as fusions with maltose binding protein (MBP). Rv2228c/N was shown to have RNase H activity with a hybrid RNA/DNA substrate as well as double-stranded RNase

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4

Ohtani, Naoto, Mitsuru Haruki, Masaaki Morikawa, and Shigenori Kanaya. "Molecular diversities of RNases H." Journal of Bioscience and Bioengineering 88, no. 1 (1999): 12–19. http://dx.doi.org/10.1016/s1389-1723(99)80168-6.

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5

Hyjek, Malwina, Małgorzata Figiel, and Marcin Nowotny. "RNases H: Structure and mechanism." DNA Repair 84 (December 2019): 102672. http://dx.doi.org/10.1016/j.dnarep.2019.102672.

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6

Goulian, Mehran, and Cheryl J. Heard. "Discrimination between mammalian RNases H-1 and H-2." Analytical Biochemistry 192, no. 2 (1991): 398–402. http://dx.doi.org/10.1016/0003-2697(91)90555-8.

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7

Lim, Shion A., Kathryn M. Hart, Michael J. Harms, and Susan Marqusee. "Evolutionary trend toward kinetic stability in the folding trajectory of RNases H." Proceedings of the National Academy of Sciences 113, no. 46 (2016): 13045–50. http://dx.doi.org/10.1073/pnas.1611781113.

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Proper folding of proteins is critical to producing the biological machinery essential for cellular function. The rates and energetics of a protein’s folding process, which is described by its energy landscape, are encoded in the amino acid sequence. Over the course of evolution, this landscape must be maintained such that the protein folds and remains folded over a biologically relevant time scale. How exactly a protein’s energy landscape is maintained or altered throughout evolution is unclear. To study how a protein’s energy landscape changed over time, we characterized the folding trajecto

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8

Hiller, Bjoern, Martin Achleitner, Silke Glage, Ronald Naumann, Rayk Behrendt, and Axel Roers. "Mammalian RNase H2 removes ribonucleotides from DNA to maintain genome integrity." Journal of Experimental Medicine 209, no. 8 (2012): 1419–26. http://dx.doi.org/10.1084/jem.20120876.

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Ribonucleases H (RNases H) are endonucleases which cleave the RNA moiety of RNA/DNA hybrids. Their function in mammalian cells is incompletely understood. RNase H2 mutations cause Aicardi-Goutières syndrome, an inflammatory condition clinically overlapping with lupus erythematosus. We show that RNase H2 is essential in mouse embryonic development. RNase H2–deficient cells proliferated slower than control cells and accumulated in G2/M phase due to chronic activation of a DNA damage response associated with an increased frequency of single-strand breaks, increased histone H2AX phosphorylation, a

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9

Kirby, Karen A., Bruno Marchand, Yee Tsuey Ong, et al. "Structural and Inhibition Studies of the RNase H Function of Xenotropic Murine Leukemia Virus-Related Virus Reverse Transcriptase." Antimicrobial Agents and Chemotherapy 56, no. 4 (2012): 2048–61. http://dx.doi.org/10.1128/aac.06000-11.

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ABSTRACTRNase H inhibitors (RNHIs) have gained attention as potential HIV-1 therapeutics. Although several RNHIs have been studied in the context of HIV-1 reverse transcriptase (RT) RNase H, there is no information on inhibitors that might affect the RNase H activity of other RTs. We performed biochemical, virological, crystallographic, and molecular modeling studies to compare the RNase H function and inhibition profiles of the gammaretroviral xenotropic murine leukemia virus-related virus (XMRV) and Moloney murine leukemia virus (MoMLV) RTs to those of HIV-1 RT. The RNase H activity of XMRV

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10

Cerritelli, Susana M., and Robert J. Crouch. "RNases H: Multiple roles in maintaining genome integrity." DNA Repair 84 (December 2019): 102742. http://dx.doi.org/10.1016/j.dnarep.2019.102742.

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