R STERNER
Overview
Explore the profile of R STERNER including associated specialties, affiliations and a list of published articles.
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Articles
61
Citations
886
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Recent Articles
1.
Hocker B, Wilmanns M, STERNER R
Biol Chem
. 2001 Nov;
382(9):1315-20.
PMID: 11688714
The (betaalpha)8-barrel is the most versatile and most frequently encountered fold among enzymes. It is an interesting question how the contemporary (betaalpha)8-barrels are evolutionarily related and by which mechanisms they...
2.
Hocker B, Jurgens C, Wilmanns M, STERNER R
Curr Opin Biotechnol
. 2001 Sep;
12(4):376-81.
PMID: 11551466
The (beta alpha)(8)-barrel is a versatile single-domain protein fold that is adopted by a large number of enzymes. The (beta alpha)(8)-barrel fold has been used as a model to elucidate...
3.
4.
STERNER R, Merz A, Thoma R, Kirschner K
Methods Enzymol
. 2001 Mar;
331:270-80.
PMID: 11265469
No abstract available.
5.
STERNER R
J Biol Chem
. 2001 Mar;
276(23):20387-96.
PMID: 11264293
Imidazole glycerol phosphate synthase, which links histidine and de novo purine biosynthesis, is a member of the glutamine amidotransferase family. In bacteria, imidazole glycerol phosphate synthase constitutes a bienzyme complex...
6.
STERNER R, Liebl W
Crit Rev Biochem Mol Biol
. 2001 Mar;
36(1):39-106.
PMID: 11256505
Hyperthermophilic organisms optimally grow close to the boiling point of water. As a consequence, their macromolecules must be much more thermostable than those from mesophilic species. Here, proteins from hyperthermophiles...
7.
Hocker B, Hettwer S, Lustig A, STERNER R
Nat Struct Biol
. 2001 Jan;
8(1):32-6.
PMID: 11135667
The (betaalpha)8-barrel, which is the most frequently encountered protein fold, is generally considered to consist of a single structural domain. However, the X-ray structure of the imidazoleglycerol phosphate synthase (HisF)...
8.
Lang D, Thoma R, STERNER R, Wilmanns M
Science
. 2000 Sep;
289(5484):1546-50.
PMID: 10968789
The atomic structures of two proteins in the histidine biosynthesis pathway consist of beta/alpha barrels with a twofold repeat pattern. It is likely that these proteins evolved by twofold gene...
9.
Jurgens C, Strom A, Wegener D, Hettwer S, Wilmanns M, STERNER R
Proc Natl Acad Sci U S A
. 2000 Aug;
97(18):9925-30.
PMID: 10944186
Enzymes participating in different metabolic pathways often have similar catalytic mechanisms and structures, suggesting their evolution from a common ancestral precursor enzyme. We sought to create a precursor-like enzyme for...
10.
Thoma R, Hennig M, STERNER R, Kirschner K
Structure
. 2000 Apr;
8(3):265-76.
PMID: 10745009
Background: Oligomeric proteins may have been selected for in hyperthermophiles because subunit association provides extra stabilization. Phosphoribosylanthranilate isomerase (PRAI) is monomeric and labile in most mesophilic microorganisms, but dimeric and...