نتایج جستجو برای: rnase

تعداد نتایج: 8269  

2001
Chiwook Park Sang-Hyun Park

Salt concentration and pH have dramatic effects on enzymatic catalysis. A quantitative description on these effects is important to elucidate the energetics and mechanisms of catalysis. Here, the effects of salt concentration and pH on binding and catalysis are analyzed with Ribonuclease A (RNase A) as a model system. 11 The effects of pH and mutagenesis on the stability of RNase A-nucleic acid...

2013
Frédéric Sorgeloos Babal Kant Jha Robert H. Silverman Thomas Michiels

Theiler's virus is a neurotropic picornavirus responsible for chronic infections of the central nervous system. The establishment of a persistent infection and the subsequent demyelinating disease triggered by the virus depend on the expression of L*, a viral accessory protein encoded by an alternative open reading frame of the virus. We discovered that L* potently inhibits the interferon-induc...

Journal: :RNA 2001
P R Subbarayan M P Deutscher

RNase M, an enzyme previously purified to homogeneity from Escherichia coli, was suggested to be the RNase responsible for mRNA degradation in this bacterium. Although related to the endoribonuclease, RNase I, its distinct properties led to the conclusion that RNase M was a second, low molecular mass, broad specificity endoribonuclease present in E. coli. However, based on sequence analysis, so...

2014
Elias Tannous Shigenori Kanaya Sompop Bencharit

RNase H1 from Halobacterium sp. NRC-1 (Halo-RNase H1) is characterized by the abundance of acidic residues on the surface, including bi/quad-aspartate site residues. Halo-RNase H1 exists in partially folded (I) and native (N) states in low-salt and high-salt conditions respectively. Its folding is also induced by divalent metal ions. To understand this unique folding mechanism of Halo-RNase H1,...

Journal: :Biochemistry 2005
J Eugene Lee Ronald T Raines

Bovine seminal ribonuclease (BS-RNase) is a homologue of bovine pancreatic ribonuclease (RNase A). Unlike RNase A, BS-RNase has notable toxicity for human tumor cells. Wild-type BS-RNase is a homodimer linked by two intermolecular disulfide bonds. This quaternary structure endows BS-RNase with resistance to inhibition by the cytosolic ribonuclease inhibitor protein (RI), which binds tightly to ...

Journal: :Annual review of biochemistry 2002
Shaohua Xiao Felicia Scott Carol A Fierke David R Engelke

Ribonuclease P (RNase P) is an essential endonuclease that acts early in the tRNA biogenesis pathway. This enzyme catalyzes cleavage of the leader sequence of precursor tRNAs (pre-tRNAs), generating the mature 5' end of tRNAs. RNase P activities have been identified in Bacteria, Archaea, and Eucarya, as well as organelles. Most forms of RNase P are ribonucleoproteins, i.e., they consist of an e...

Journal: :Nucleic acids research 1991
H Nakamura K Katayanagi K Morikawa M Ikehara

Tertiary models of ribonuclease H (RNase H) domains in reverse transcriptases (RTs) from Moloney murine leukemia virus (MuLV) and human immunodeficiency virus (HIV-1) were built based upon the X-ray structure of RNase H from Escherichia coli (E. coli RNase H). In two models of RT-RNase H domains, not only active site residues but also residues, which construct a hydrophobic core and hydrogen bo...

Journal: :Cancer research 1965
R J Wojnar J S Roth

the relationships between RNase activity and cancer, and a review concerning these relationships has been published (14). An understanding of the role of RNase in growth processes has been complicated by dernonstra tions that there is a multiplicity of RNases (14) and of intracellular inhibitors for RNase (9, 11) in animal tissues. Furthermore, the recent discovery that some samples of RNA cont...

Journal: :Antimicrobial agents and chemotherapy 2014
Angela Corona Anna Schneider Kristian Schweimer Paul Rösch Birgitta M Wöhrl Enzo Tramontano

RNase H plays an essential role in the replication of human immunodeficiency virus type 1 (HIV-1). Therefore, it is a promising target for drug development. However, the identification of HIV-1 RNase H inhibitors (RHIs) has been hampered by the open morphology of its active site, the limited number of available RNase H crystal structures in complex with inhibitors, and the fact that, due to the...

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