Krebs B - Search Results

1

Recombinant purple acid phosphatase isoform 3 from sweet potato is an enzyme with a diiron metal center.

Waratrujiwong T, Krebs B, Spener F, Visoottiviseth P. Waratrujiwong T, et al. Among authors: krebs b. FEBS J. 2006 Apr;273(8):1649-59. doi: 10.1111/j.1742-4658.2006.05179.x. FEBS J. 2006. PMID: 16623702 Free article.

2

Heterologous expression and characterization of recombinant purple acid phosphatase from red kidney bean.

Vogel A, Börchers T, Marcus K, Meyer HE, Krebs B, Spener F. Vogel A, et al. Among authors: krebs b. Arch Biochem Biophys. 2002 May 15;401(2):164-72. doi: 10.1016/S0003-9861(02)00046-2. Arch Biochem Biophys. 2002. PMID: 12054466

3

Porcine purple acid phosphatase: heterologous expression, characterization, and proteolytic analysis.

Naseri JI, Truong NT, Hörentrup J, Kuballa P, Vogel A, Rompel A, Spener F, Krebs B. Naseri JI, et al. Among authors: krebs b. Arch Biochem Biophys. 2004 Dec 1;432(1):25-36. doi: 10.1016/j.abb.2004.08.008. Arch Biochem Biophys. 2004. PMID: 15519293

4

Cloning and comparative protein modeling of two purple acid phosphatase isozymes from sweet potatoes (Ipomoea batatas).

Durmus A, Eicken C, Spener F, Krebs B. Durmus A, et al. Among authors: krebs b. Biochim Biophys Acta. 1999 Sep 14;1434(1):202-9. doi: 10.1016/s0167-4838(99)00176-4. Biochim Biophys Acta. 1999. PMID: 10556574

5

Isozymes of Ipomoea batatas catechol oxidase differ in catalase-like activity.

Gerdemann C, Eicken C, Magrini A, Meyer HE, Rompel A, Spener F, Krebs B. Gerdemann C, et al. Among authors: krebs b. Biochim Biophys Acta. 2001 Jul 9;1548(1):94-105. doi: 10.1016/s0167-4838(01)00219-9. Biochim Biophys Acta. 2001. PMID: 11451442

6

Structural relationship between the mammalian Fe(III)-Fe(II) and the Fe(III)-Zn(II) plant purple acid phosphatases.

Klabunde T, Sträter N, Krebs B, Witzel H. Klabunde T, et al. Among authors: krebs b. FEBS Lett. 1995 Jun 19;367(1):56-60. doi: 10.1016/0014-5793(95)00536-i. FEBS Lett. 1995. PMID: 7601285 Free article.

7

Crystal structures of recombinant human purple Acid phosphatase with and without an inhibitory conformation of the repression loop.

Sträter N, Jasper B, Scholte M, Krebs B, Duff AP, Langley DB, Han R, Averill BA, Freeman HC, Guss JM. Sträter N, et al. Among authors: krebs b. J Mol Biol. 2005 Aug 5;351(1):233-46. doi: 10.1016/j.jmb.2005.04.014. Epub 2005 Apr 26. J Mol Biol. 2005. PMID: 15993892

8

Biochemical and spectroscopic characterization of catechol oxidase from sweet potatoes (Ipomoea batatas) containing a type-3 dicopper center.

Eicken C, Zippel F, Büldt-Karentzopoulos K, Krebs B. Eicken C, et al. Among authors: krebs b. FEBS Lett. 1998 Oct 2;436(2):293-9. doi: 10.1016/s0014-5793(98)01113-2. FEBS Lett. 1998. PMID: 9781698 Free article.

9

The active site of purple acid phosphatase from sweet potatoes (Ipomoea batatas) metal content and spectroscopic characterization.

Durmus A, Eicken C, Sift BH, Kratel A, Kappl R, Hüttermann J, Krebs B. Durmus A, et al. Among authors: krebs b. Eur J Biochem. 1999 Mar;260(3):709-16. doi: 10.1046/j.1432-1327.1999.00230.x. Eur J Biochem. 1999. PMID: 10102999 Free article.

10

Structure-function relationships of purple acid phosphatase from red kidney beans based on heterologously expressed mutants.

Truong NT, Naseri JI, Vogel A, Rompel A, Krebs B. Truong NT, et al. Among authors: krebs b. Arch Biochem Biophys. 2005 Aug 1;440(1):38-45. doi: 10.1016/j.abb.2005.05.024. Arch Biochem Biophys. 2005. PMID: 16009331

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