Ribonuclease T1

Known as: Ribonuclease N1, Guanyloribonuclease, Aspergillus oryzae Ribonuclease 
An enzyme catalyzing the endonucleolytic cleavage of RNA at the 3'-position of a guanylate residue. EC 3.1.27.3.
National Institutes of Health

Papers overview

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Review
1997
Review
1997
During the last decade, protein engineering has been used to identify the residues that contribute to the ribonuclease-T1… (More)
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1994
1994
The energetics of thermal denaturation of two isoforms of ribonuclease T1 (Gln25 and Lys25) in various solvents have been studied… (More)
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1994
1994
In the absence of its two disulfide bonds, ribonuclease T1 can exist in a native-like folded conformation when > or = 2 M NaCl is… (More)
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Highly Cited
1992
Highly Cited
1992
For 30 years, the prevailing view has been that the hydrophobic effect contributes considerably more than hydrogen bonding to the… (More)
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1992
1992
Differential scanning calorimetry has been used to investigate the thermodynamics of denaturation of ribonuclease T1 as a… (More)
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Highly Cited
1992
Highly Cited
1992
Messenger RNA translation initiation and cytoplasmic poly(A) tail shortening require the poly(A)-binding protein (PAB) in yeast… (More)
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1990
1990
To investigate the pH dependence of the conformational stability of ribonucleases A and T1, urea and guanidine hydrochloride… (More)
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1990
1990
The slow refolding of ribonuclease T1 was investigated by different probes. Structural intermediates with secondary structure are… (More)
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Highly Cited
1988
Highly Cited
1988
Ribonuclease T1 has two disulfide bonds linking cysteine residues 2-10 and 6-103. We have prepared a derivative of ribonuclease… (More)
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Review
1964
Review
1964
The effects of various neutral salts on the temperature of the thermally-induced denaturation of the globular protein… (More)
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