Rudolph R - Search Results

1

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.

2

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.

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

In vitro folding of inclusion body proteins.

Rudolph R, Lilie H. Rudolph R, et al. FASEB J. 1996 Jan;10(1):49-56. FASEB J. 1996. PMID: 8566547 Review.

7

The effect of molecular chaperones on in vivo and in vitro folding processes.

Schwarz E, Lilie H, Rudolph R. Schwarz E, et al. Among authors: rudolph r. Biol Chem. 1996 Jul-Aug;377(7-8):411-6. Biol Chem. 1996. PMID: 8922274 Review.

8

Advances in refolding of proteins produced in E. coli.

Lilie H, Schwarz E, Rudolph R. Lilie H, et al. Among authors: rudolph r. Curr Opin Biotechnol. 1998 Oct;9(5):497-501. doi: 10.1016/s0958-1669(98)80035-9. Curr Opin Biotechnol. 1998. PMID: 9821278 Review.

9

The N-terminal fragment of human parathyroid hormone receptor 1 constitutes a hormone binding domain and reveals a distinct disulfide pattern.

Grauschopf U, Lilie H, Honold K, Wozny M, Reusch D, Esswein A, Schäfer W, Rücknagel KP, Rudolph R. Grauschopf U, et al. Among authors: rudolph r. Biochemistry. 2000 Aug 1;39(30):8878-87. doi: 10.1021/bi0001426. Biochemistry. 2000. PMID: 10913300

10

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

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