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Bacillus amyloliquefaciens ribonuclease
Known as:
Bacillus amyloliquefaciens RNase
, RNase ba
, barnase
National Institutes of Health
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Related topics
Related topics
2 relations
Pancreatic ribonuclease
Broader (1)
Ribonucleases
Papers overview
Semantic Scholar uses AI to extract papers important to this topic.
2001
2001
Salt Bridges Stabilize the Folded Structure of Barnase
M. V. and
,
Huan‐Xiang Zhou
2001
Corpus ID: 2135359
Formation of salt bridges entails desolvation, and whether they stabilize protein structures is an open question. In this paper…
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1998
1998
Baculovirus-mediated gene transfer into mammalian cells
Ying Zhu
,
Y. Qi
,
Ziye Liu
,
Gengfu Xiao
Science in China Series C: Life Sciences
1998
Corpus ID: 26055323
A klnd of cytotoxinic gene barnase was cloned downstream of Immediate early promoter from cytomegalovirus (CMV). Rerombinant…
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Highly Cited
1995
Highly Cited
1995
A comparison of the pH, urea, and temperature-denatured states of barnase by heteronuclear NMR: implications for the initiation of protein folding.
V. Arcus
,
S. Vuilleumier
,
S. Freund
,
M. Bycroft
,
A. Fersht
Journal of Molecular Biology
1995
Corpus ID: 269750
The denatured states of barnase that are induced by urea, acid, and high temperature and acid have been assigned and…
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Review
1994
Review
1994
Extrapolation to water of kinetic and equilibrium data for the unfolding of barnase in urea solutions.
A. Matouschek
,
J. Matthews
,
C. Johnson
,
A. Fersht
Protein Engineering
1994
Corpus ID: 23794542
Assumptions about the dependence of protein unfolding on the concentration of urea have been examined by an extensive survey of…
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1993
1993
Local breathing and global unfolding in hydrogen exchange of barnase and its relationship to protein folding pathways.
J. Clarke
,
A. Hounslow
,
M. Bycroft
,
A. Fersht
Proceedings of the National Academy of Sciences…
1993
Corpus ID: 25933982
We have measured the rate constants for exchange of amide protons in 15N-labeled wild-type barnase and a disulfide mutant that is…
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Highly Cited
1992
Highly Cited
1992
The folding of an enzyme. V. H/2H exchange-nuclear magnetic resonance studies on the folding pathway of barnase: complementarity to and agreement with protein engineering studies.
A. Matouschek
,
L. Serrano
,
E. Meiering
,
M. Bycroft
,
A. Fersht
Journal of Molecular Biology
1992
Corpus ID: 21516315
Highly Cited
1992
Highly Cited
1992
An N-terminal fragment of barnase has residual helical structure similar to that in a refolding intermediate.
Javier Sancho
,
José L. Neira
,
A. Fersht
Journal of Molecular Biology
1992
Corpus ID: 19364064
Highly Cited
1991
Highly Cited
1991
Crystal structure of a barnase-d(GpC) complex at 1.9 A resolution.
S. Baudet
,
J. Janin
Journal of Molecular Biology
1991
Corpus ID: 24489769
Highly Cited
1990
Highly Cited
1990
Detection and characterization of a folding intermediate in barnase by NMR
M. Bycroft
,
A. Matouschek
,
J. Kellis
,
L. Serrano
,
A. Fersht
Nature
1990
Corpus ID: 4235781
PROTEIN engineering is being developed for mapping the energetics and pathway of protein folding. From kinetic studies on wild…
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Highly Cited
1972
Highly Cited
1972
Amino-acid sequence of extracellular ribonuclease (barnase) of Bacillus amyloliquefaciens.
R. Hartley
,
E. Barker
Nature: New biology
1972
Corpus ID: 41084312
THE ribonuclease, barnase, produced by Bacillus amyloliquefaciens has a molecular weight of 12,382, consisting of 110 amino-acid…
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