Fabian H - Search Results

1

Antemortem identification of bovine spongiform encephalopathy from serum using infrared spectroscopy.

Lasch P, Schmitt J, Beekes M, Udelhoven T, Eiden M, Fabian H, Petrich W, Naumann D. Lasch P, et al. Among authors: fabian h. Anal Chem. 2003 Dec 1;75(23):6673-8. doi: 10.1021/ac030259a. Anal Chem. 2003. PMID: 14640744

2

Analysis of biofluids in aqueous environment based on mid-infrared spectroscopy.

Fabian H, Lasch P, Naumann D. Fabian H, et al. J Biomed Opt. 2005 May-Jun;10(3):031103. doi: 10.1117/1.1917844. J Biomed Opt. 2005. PMID: 16229628 Free article.

3

Time-resolved FTIR difference spectroscopy as tool for investigating refolding reactions of ribonuclease T1 synchronized with trans --> cis prolyl isomerization.

Moritz R, Reinstädler D, Fabian H, Naumann D. Moritz R, et al. Among authors: fabian h. Biopolymers. 2002;67(3):145-55. doi: 10.1002/bip.10083. Biopolymers. 2002. PMID: 11979593

4

Impact of four (13)C-proline isotope labels on the infrared spectra of ribonuclease T1.

Moritz R, Fabian H, Hahn U, Diem M, Naumann D. Moritz R, et al. Among authors: fabian h. J Am Chem Soc. 2002 Jun 5;124(22):6259-64. doi: 10.1021/ja011749s. J Am Chem Soc. 2002. PMID: 12033852

5

Methods to study protein folding by stopped-flow FT-IR.

Fabian H, Naumann D. Fabian H, et al. Methods. 2004 Sep;34(1):28-40. doi: 10.1016/j.ymeth.2004.03.004. Methods. 2004. PMID: 15283913 Review.

6

Diagnosing benign and malignant lesions in breast tissue sections by using IR-microspectroscopy.

Fabian H, Thi NA, Eiden M, Lasch P, Schmitt J, Naumann D. Fabian H, et al. Biochim Biophys Acta. 2006 Jul;1758(7):874-82. doi: 10.1016/j.bbamem.2006.05.015. Epub 2006 May 23. Biochim Biophys Acta. 2006. PMID: 16814743 Free article.

7

New structural insights into the refolding of ribonuclease T1 as seen by time-resolved Fourier-transform infrared spectroscopy.

Reinstädler D, Fabian H, Naumann D. Reinstädler D, et al. Among authors: fabian h. Proteins. 1999 Feb 15;34(3):303-16. doi: 10.1002/(sici)1097-0134(19990215)34:3<303::aid-prot4>3.0.co;2-h. Proteins. 1999. PMID: 10024018

8

IR spectroscopic analyses of amyloid fibril formation of β2-microglobulin using a simplified procedure for its in vitro generation at neutral pH.

Fabian H, Gast K, Laue M, Jetzschmann KJ, Naumann D, Ziegler A, Uchanska-Ziegler B. Fabian H, et al. Biophys Chem. 2013 Sep;179:35-46. doi: 10.1016/j.bpc.2013.05.001. Epub 2013 May 7. Biophys Chem. 2013. PMID: 23727989

9

Temperature-jump-induced refolding of ribonuclease A: a time-resolved FTIR spectroscopic study.

Backmann J, Fabian H, Naumann D. Backmann J, et al. Among authors: fabian h. FEBS Lett. 1995 May 8;364(2):175-8. doi: 10.1016/0014-5793(95)00387-o. FEBS Lett. 1995. PMID: 7750565 Free article.

10

Refolding of thermally and urea-denatured ribonuclease A monitored by time-resolved FTIR spectroscopy.

Reinstädler D, Fabian H, Backmann J, Naumann D. Reinstädler D, et al. Among authors: fabian h. Biochemistry. 1996 Dec 10;35(49):15822-30. doi: 10.1021/bi961810j. Biochemistry. 1996. PMID: 8961946

Therefore, our kinetic infrared studies provide evidence for a high structural similarity of urea-denatured and heat-denatured RNase A, corroborating the conclusions derived from the direct comparison of the infrared spectra of thermally and chemically denatured RNase A under equ …

Therefore, our kinetic infrared studies provide evidence for a high structural similarity of urea-denatured and heat-denatured RNase A, corr …

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