Lactate dehydrogenase from the hyperthermophilic bacterium Thermotoga maritima: the crystal structure at 2.1 å resolution reveals strategies for intrinsic protein stabilization-Reference-Cited by-同舟云学术

Lactate dehydrogenase from the hyperthermophilic bacterium Thermotoga maritima: the crystal structure at 2.1 å resolution reveals strategies for intrinsic protein stabilization

Published:1998-06 Issue:6 Volume:6 Page:769-781
ISSN:0969-2126
Container-title:Structure
language:en
Short-container-title:Structure

Author:

Auerbach Günter,Ostendorp Ralf,Prade Lars,Korndörfer Ingo,Dams Thomas,Huber Robert,Jaenicke Rainer

Publisher

Elsevier BV

Subject

Molecular Biology,Structural Biology

Reference124 articles.

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2. Thermotoga maritima sp. nov. represents a new genus of unique extremely thermophilic eubacteria growing up to 90°C;Huber;Arch. Microbiol,1986

3. Homo-dimeric recombinant dihydrofolate reductase from Thermotoga maritima shows extreme intrinsic stability;Dams;Biol. Chem,1998

4. Octameric enolase from the hyperthermophilic bacterium Thermotoga maritima: purification, characterization, and image processing;Schurig;Protein Sci,1995

5. Sequence, assembly and evolution of a primordial ferredoxin from Thermotoga maritima;Darimont;EMBO J,1994

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