Skip to search formSkip to main contentSkip to account menu

barstar protein, Bacillus amyloliquefaciens

Known as: Nuclease inhibitor, barstar, barstar 
National Institutes of Health

Papers overview

Semantic Scholar uses AI to extract papers important to this topic.
Highly Cited
2006
Highly Cited
2006
We tested the efficacy of an attenuation system developed to preclude the deleterious effects of floral promoter::cytotoxin genes… 
2003
2003
The denaturant-induced unfolding kinetics of the 89-residue protein, barstar, have been examined using fluorescence resonance… 
Highly Cited
2002
Highly Cited
2002
Structural analysis of the initial steps in protein folding is difficult because of the swiftness with which these steps occur… 
1999
1999
The kinetics of the slow folding and unfolding reactions of barstar, a bacterial ribonuclease inhibitor protein, have been… 
Highly Cited
1998
Highly Cited
1998
The dynamic behavior of the ribonuclease inhibitor barstar has been investigated by molecular dynamics (MD) simulations in… 
1997
1997
Barstar an 89-residue protein consisting of four helices and a three-stranded parallel beta-sheet, is the intracellular inhibitor… 
1997
1997
The contributions of the three tryptophan residues of barstar to the spectroscopic properties, stability, and folding of the… 
Highly Cited
1995
Highly Cited
1995
The mechanism of folding of the small protein barstar in the pre-transition zone at pH 7, 25 degrees C has been characterized… 
1995
1995
The temperature-induced unfolding of single, double, and triple mutants of barstar, the specific intracellular protein inhibitor…