Sterner R - Search Results

1

Structure and function of mutationally generated monomers of dimeric phosphoribosylanthranilate isomerase from Thermotoga maritima.

Thoma R, Hennig M, Sterner R, Kirschner K. Thoma R, et al. Among authors: sterner r. Structure. 2000 Mar 15;8(3):265-76. doi: 10.1016/s0969-2126(00)00106-4. Structure. 2000. PMID: 10745009 Free article.

2

2.0 A structure of indole-3-glycerol phosphate synthase from the hyperthermophile Sulfolobus solfataricus: possible determinants of protein stability.

Hennig M, Darimont B, Sterner R, Kirschner K, Jansonius JN. Hennig M, et al. Among authors: sterner r. Structure. 1995 Dec 15;3(12):1295-306. doi: 10.1016/s0969-2126(01)00267-2. Structure. 1995. PMID: 8747456 Free article.

3

Phosphoribosyl anthranilate isomerase from Thermotoga maritima is an extremely stable and active homodimer.

Sterner R, Kleemann GR, Szadkowski H, Lustig A, Hennig M, Kirschner K. Sterner R, et al. Protein Sci. 1996 Oct;5(10):2000-8. doi: 10.1002/pro.5560051006. Protein Sci. 1996. PMID: 8897600 Free PMC article.

4

Crystal structure at 2.0 A resolution of phosphoribosyl anthranilate isomerase from the hyperthermophile Thermotoga maritima: possible determinants of protein stability.

Hennig M, Sterner R, Kirschner K, Jansonius JN. Hennig M, et al. Among authors: sterner r. Biochemistry. 1997 May 20;36(20):6009-16. doi: 10.1021/bi962718q. Biochemistry. 1997. PMID: 9166771

In contrast to other hyperthermostable enzymes, tPRAI at 25 degrees C is catalytically more efficient than ePRAI, mainly due to its small K(M) value for the substrate [Sterner, R., Kleemann, G. R., Szadkowski, H., Lustig, A., Hennig, M., & Kirschner, K. ( …

In contrast to other hyperthermostable enzymes, tPRAI at 25 degrees C is catalytically more efficient than ePRAI, mainly due to its small K( …

5

A histidine gene cluster of the hyperthermophile Thermotoga maritima: sequence analysis and evolutionary significance.

Thoma R, Schwander M, Liebl W, Kirschner K, Sterner R. Thoma R, et al. Among authors: sterner r. Extremophiles. 1998 Nov;2(4):379-89. doi: 10.1007/s007920050082. Extremophiles. 1998. PMID: 9827326

6

Phosphoribosylanthranilate isomerase and indoleglycerol-phosphate synthase: tryptophan biosynthetic enzymes from Thermotoga maritima.

Sterner R, Merz A, Thoma R, Kirschner K. Sterner R, et al. Methods Enzymol. 2001;331:270-80. doi: 10.1016/s0076-6879(01)31064-9. Methods Enzymol. 2001. PMID: 11265469 No abstract available.

7

(Beta alpha)8-barrel proteins of tryptophan biosynthesis in the hyperthermophile Thermotoga maritima.

Sterner R, Dahm A, Darimont B, Ivens A, Liebl W, Kirschner K. Sterner R, et al. EMBO J. 1995 Sep 15;14(18):4395-402. doi: 10.1002/j.1460-2075.1995.tb00118.x. EMBO J. 1995. PMID: 7556082 Free PMC article.

8

Two (betaalpha)(8)-barrel enzymes of histidine and tryptophan biosynthesis have similar reaction mechanisms and common strategies for protecting their labile substrates.

Henn-Sax M, Thoma R, Schmidt S, Hennig M, Kirschner K, Sterner R. Henn-Sax M, et al. Among authors: sterner r. Biochemistry. 2002 Oct 8;41(40):12032-42. doi: 10.1021/bi026092h. Biochemistry. 2002. PMID: 12356303

9

Role of the N-terminal extension of the (betaalpha)8-barrel enzyme indole-3-glycerol phosphate synthase for its fold, stability, and catalytic activity.

Schneider B, Knöchel T, Darimont B, Hennig M, Dietrich S, Babinger K, Kirschner K, Sterner R. Schneider B, et al. Among authors: sterner r. Biochemistry. 2005 Dec 20;44(50):16405-12. doi: 10.1021/bi051640n. Biochemistry. 2005. PMID: 16342933

10

Efficient expression, purification and crystallisation of two hyperthermostable enzymes of histidine biosynthesis.

Thoma R, Obmolova G, Lang DA, Schwander M, Jenö P, Sterner R, Wilmanns M. Thoma R, et al. Among authors: sterner r. FEBS Lett. 1999 Jul 2;454(1-2):1-6. doi: 10.1016/s0014-5793(99)00757-7. FEBS Lett. 1999. PMID: 10413084 Free article.

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