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beta-isopropylmalate

Known as: 3-isopropylmalate, butanedioic acid, 2-hydroxy-3-(1-methylethyl)-, (S-(R*,R*))- 
 
National Institutes of Health

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Highly Cited
2012
Highly Cited
2012
Thermophily is thought to be a primitive trait, characteristic of early forms of life on Earth, that has been gradually lost over… Expand
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Highly Cited
2006
Highly Cited
2006
We have recently developed a new method for designing thermostable proteins using phylogenetic trees of enzymes. In this study… Expand
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Highly Cited
2004
Highly Cited
2004
ABSTRACT Since most archaea are extremophilic and difficult to cultivate, our current knowledge of their biology is confined… Expand
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Highly Cited
2001
Highly Cited
2001
3-Isopropylmalate dehydrogenase (IPMDH) from the psychrotrophic bacteriumVibrio sp. I5 has been expressed in Escherichia coli and… Expand
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Highly Cited
1997
Highly Cited
1997
The basis of protein stability has been investigated by the structural comparison of themophilic enzymes with their mesophilic… Expand
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Highly Cited
1994
Highly Cited
1994
We cloned and sequenced the leuB gene encoding 3-isopropylmalate dehydrogenase from Escherichia coli K-12 (JM103). Errors (33… Expand
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Highly Cited
1994
Highly Cited
1994
BACKGROUND The leucine biosynthetic enzyme 3-isopropylmalate dehydrogenase (IMDH) belongs to a unique class of bifunctional… Expand
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Highly Cited
1991
Highly Cited
1991
The three-dimensional structure of the highly thermostable 3-isopropylmalate dehydrogenase (IPMDH) from Thermus thermophilus has… Expand
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Highly Cited
1984
Highly Cited
1984
In studies on the cause of the extreme stability of the macromolecules of Thermus thermophilus HB8, the leuB gene coding for 3… Expand
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Highly Cited
1981
Highly Cited
1981
The gene of an extreme thermophile, Thermus thermophilus HB8, which codes for a leucine biosynthetic enzyme, 3-isopropylmalate (3… Expand
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