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Ribonuclease T1
Known as:
Ribonuclease N1
, Guanyloribonuclease
, Aspergillus oryzae Ribonuclease
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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
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Related topics
Related topics
12 relations
In Blood
Process of secretion
RNase Pch 1
Ribonuclease F1
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Narrower (1)
ribonuclease Po1
Papers overview
Semantic Scholar uses AI to extract papers important to this topic.
Highly Cited
1999
Highly Cited
1999
Buried, charged, non-ion-paired aspartic acid 76 contributes favorably to the conformational stability of ribonuclease T1.
A. Giletto
,
C. Pace
Biochemistry
1999
Corpus ID: 39011070
The side-chain carboxyl of Asp 76 in ribonuclease T1 (RNase T1) is buried, charged, non-ion-paired, and forms three good…
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Highly Cited
1994
Highly Cited
1994
Energetics of ribonuclease T1 structure.
Y. Yu
,
G. Makhatadze
,
C. Pace
,
P. Privalov
Biochemistry
1994
Corpus ID: 46174056
The energetics of thermal denaturation of two isoforms of ribonuclease T1 (Gln25 and Lys25) in various solvents have been studied…
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Highly Cited
1992
Highly Cited
1992
Translation initiation requires the PAB-dependent poly(A) ribonuclease in yeast
A. Sachs
,
Julie A. Deardorff
Cell
1992
Corpus ID: 19684837
Highly Cited
1990
Highly Cited
1990
Folding of ribonuclease T1. 1. Existence of multiple unfolded states created by proline isomerization.
Thomas Kiefhaber
,
R. Quaas
,
Ulrich Hahn
,
Franz X. Schmid
Biochemistry
1990
Corpus ID: 12350798
It is our aim to elucidate molecular aspects of the mechanism of protein folding. We use ribonuclease T1 as a model protein…
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Highly Cited
1990
Highly Cited
1990
Replacement of a cis proline simplifies the mechanism of ribonuclease T1 folding.
Thomas Kiefhaber
,
H. Grunert
,
Ulrich Hahn
,
Franz X. Schmid
Biochemistry
1990
Corpus ID: 21150652
The refolding of ribonuclease T1 is dominated by two major slow kinetic phases that show properties of proline isomerization…
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Highly Cited
1990
Highly Cited
1990
Folding of ribonuclease T1. 2. Kinetic models for the folding and unfolding reactions.
Thomas Kiefhaber
,
R. Quaas
,
Ulrich Hahn
,
Franz X. Schmid
Biochemistry
1990
Corpus ID: 9058107
The slow refolding of ribonuclease T1 was investigated by different probes. Structural intermediates with secondary structure are…
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Highly Cited
1989
Highly Cited
1989
Crystal structure of guanosine-free ribonuclease T1, complexed with vanadate (V), suggests conformational change upon substrate binding.
D. Kostrewa
,
H. Choe
,
U. Heinemann
,
W. Saenger
Biochemistry
1989
Corpus ID: 29465101
Ribonuclease T1 was crystallized in the presence of vanadate(V). The crystal structure was solved by molecular replacement and…
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Highly Cited
1988
Highly Cited
1988
Expression of the chemically synthesized gene for ribonuclease T1 in Escherichia coli using a secretion cloning vector.
R. Quaas
,
Y. McKeown
,
P. Stanssens
,
R. Frank
,
H. Blöcker
,
U. Hahn
European Journal of Biochemistry
1988
Corpus ID: 39907536
The gene for ribonuclease T1 from Aspergillus oryzae has been chemically synthesized using the segmental support technique. An…
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Highly Cited
1971
Highly Cited
1971
Plant Nucleases: III. Polyacrylamide Gel Electrophoresis of Corn Ribonuclease Isoenzymes.
C. M. Wilson
Plant Physiology
1971
Corpus ID: 769634
Isoenzymes of RNase were detected in plant extracts after polyacrylamide gel electrophoresis with a new buffer system. The gels…
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Highly Cited
1955
Highly Cited
1955
Photooxidation of crystalline ribonuclease in the presence of methylene blue.
L. Weil
,
T. S. Seibles
Archives of Biochemistry and Biophysics
1955
Corpus ID: 3190798
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