Rudolph R - Search Results

1

The mature part of proNGF induces the structure of its pro-peptide.

Kliemannel M, Rattenholl A, Golbik R, Balbach J, Lilie H, Rudolph R, Schwarz E. Kliemannel M, et al. Among authors: rudolph r. FEBS Lett. 2004 May 21;566(1-3):207-12. doi: 10.1016/j.febslet.2004.04.034. FEBS Lett. 2004. PMID: 15147896 Free article.

2

Biophysical comparison of BMP-2, ProBMP-2, and the free pro-peptide reveals stabilization of the pro-peptide by the mature growth factor.

Hillger F, Herr G, Rudolph R, Schwarz E. Hillger F, et al. Among authors: rudolph r. J Biol Chem. 2005 Apr 15;280(15):14974-80. doi: 10.1074/jbc.M414413200. Epub 2005 Feb 4. J Biol Chem. 2005. PMID: 15695507 Free article.

3

Examination of the slow unfolding of pro-nerve growth factor argues against a loop threading mechanism for nerve growth factor.

Kliemannel M, Weininger U, Balbach J, Schwarz E, Rudolph R. Kliemannel M, et al. Among authors: rudolph r. Biochemistry. 2006 Mar 21;45(11):3517-24. doi: 10.1021/bi051896t. Biochemistry. 2006. PMID: 16533032

4

The pro-peptide of proNGF: structure formation and intramolecular association with NGF.

Kliemannel M, Golbik R, Rudolph R, Schwarz E, Lilie H. Kliemannel M, et al. Among authors: rudolph r. Protein Sci. 2007 Mar;16(3):411-9. doi: 10.1110/ps.062376207. Epub 2007 Jan 22. Protein Sci. 2007. PMID: 17242381 Free PMC article.

5

Oxidative folding of nerve growth factor can be mediated by the pro-peptide of neurotrophin-3.

Hauburger A, Kliemannel M, Madsen P, Rudolph R, Schwarz E. Hauburger A, et al. Among authors: rudolph r. FEBS Lett. 2007 Sep 4;581(22):4159-64. doi: 10.1016/j.febslet.2007.07.063. Epub 2007 Aug 6. FEBS Lett. 2007. PMID: 17698064 Free article.

6

The non-ionic detergent Brij 58P mimics chaperone effects.

Krause M, Rudolph R, Schwarz E. Krause M, et al. Among authors: rudolph r. FEBS Lett. 2002 Dec 4;532(1-2):253-5. doi: 10.1016/s0014-5793(02)03689-x. FEBS Lett. 2002. PMID: 12459500 Free article.

7

Folding of a synthetic parallel beta-roll protein.

Lilie H, Haehnel W, Rudolph R, Baumann U. Lilie H, et al. Among authors: rudolph r. FEBS Lett. 2000 Mar 24;470(2):173-7. doi: 10.1016/s0014-5793(00)01308-9. FEBS Lett. 2000. PMID: 10734229 Free article.

8

Pro-sequence assisted folding and disulfide bond formation of human nerve growth factor.

Rattenholl A, Ruoppolo M, Flagiello A, Monti M, Vinci F, Marino G, Lilie H, Schwarz E, Rudolph R. Rattenholl A, et al. Among authors: rudolph r. J Mol Biol. 2001 Jan 19;305(3):523-33. doi: 10.1006/jmbi.2000.4295. J Mol Biol. 2001. PMID: 11152610

9

The pro-sequence facilitates folding of human nerve growth factor from Escherichia coli inclusion bodies.

Rattenholl A, Lilie H, Grossmann A, Stern A, Schwarz E, Rudolph R. Rattenholl A, et al. Among authors: rudolph r. Eur J Biochem. 2001 Jun;268(11):3296-303. doi: 10.1046/j.1432-1327.2001.02232.x. Eur J Biochem. 2001. PMID: 11389732 Free article.

10

Intradomain disulfide bonds impede formation of the alternatively folded state of antibody chains.

Buchner J, Rudolph R, Lilie H. Buchner J, et al. Among authors: rudolph r. J Mol Biol. 2002 May 3;318(3):829-36. doi: 10.1016/S0022-2836(02)00171-7. J Mol Biol. 2002. PMID: 12054826

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