Barth A - Search Results

1

Structural changes in the catalytic cycle of the Na+,K+-ATPase studied by infrared spectroscopy.

Stolz M, Lewitzki E, Bergbauer R, Mäntele W, Grell E, Barth A. Stolz M, et al. Among authors: barth a. Biophys J. 2009 Apr 22;96(8):3433-42. doi: 10.1016/j.bpj.2009.01.010. Biophys J. 2009. PMID: 19383486 Free PMC article.

2

Fourier transform infrared (FTIR) spectroscopic investigation of the nicotinic acetylcholine receptor (nAChR). Investigation of agonist binding and receptor conformational changes by flash-induced release of 'caged' carbamoylcholine.

Görne-Tschelnokow U, Hucho F, Naumann D, Barth A, Mäntele W. Görne-Tschelnokow U, et al. Among authors: barth a. FEBS Lett. 1992 Sep 7;309(2):213-7. doi: 10.1016/0014-5793(92)81097-6. FEBS Lett. 1992. PMID: 1505686 Free article.

3

Infrared spectroscopic signals arising from ligand binding and conformational changes in the catalytic cycle of sarcoplasmic reticulum calcium ATPase.

Barth A, Mäntele W, Kreutz W. Barth A, et al. Biochim Biophys Acta. 1991 Mar 1;1057(1):115-23. doi: 10.1016/s0005-2728(05)80091-x. Biochim Biophys Acta. 1991. PMID: 1826215

4

Molecular changes in the sarcoplasmic reticulum calcium ATPase during catalytic activity. A Fourier transform infrared (FTIR) study using photolysis of caged ATP to trigger the reaction cycle.

Barth A, Kreutz W, Mäntele W. Barth A, et al. FEBS Lett. 1990 Dec 17;277(1-2):147-50. doi: 10.1016/0014-5793(90)80830-c. FEBS Lett. 1990. PMID: 2148528 Free article.

5

Structural changes of sarcoplasmic reticulum Ca(2+)-ATPase upon Ca2+ binding studied by simultaneous measurement of infrared absorbance changes and changes of intrinsic protein fluorescence.

Georg H, Barth A, Kreutz W, Siebert F, Mäntele W. Georg H, et al. Among authors: barth a. Biochim Biophys Acta. 1994 Nov 1;1188(1-2):139-50. doi: 10.1016/0005-2728(94)90032-9. Biochim Biophys Acta. 1994. PMID: 7947901

6

Changes of protein structure, nucleotide microenvironment, and Ca(2+)-binding states in the catalytic cycle of sarcoplasmic reticulum Ca(2+)-ATPase: investigation of nucleotide binding, phosphorylation and phosphoenzyme conversion by FTIR difference spectroscopy.

Barth A, Kreutz W, Mäntele W. Barth A, et al. Biochim Biophys Acta. 1994 Aug 24;1194(1):75-91. doi: 10.1016/0005-2736(94)90205-4. Biochim Biophys Acta. 1994. PMID: 8075144

7

Time-resolved infrared spectroscopy of the Ca2+-ATPase. The enzyme at work.

Barth A, von Germar F, Kreutz W, Mäntele W. Barth A, et al. J Biol Chem. 1996 Nov 29;271(48):30637-46. doi: 10.1074/jbc.271.48.30637. J Biol Chem. 1996. PMID: 8940039 Free article.

8

Ca2+ release from the phosphorylated and the unphosphorylated sarcoplasmic reticulum Ca2+ ATPase results in parallel structural changes. An infrared spectroscopic study.

Barth A, Kreutz W, Mäntele W. Barth A, et al. J Biol Chem. 1997 Oct 10;272(41):25507-10. doi: 10.1074/jbc.272.41.25507. J Biol Chem. 1997. PMID: 9325264 Free article.

9

ATP-Induced phosphorylation of the sarcoplasmic reticulum Ca2+ ATPase: molecular interpretation of infrared difference spectra.

Barth A, Mäntele W. Barth A, et al. Biophys J. 1998 Jul;75(1):538-44. doi: 10.1016/S0006-3495(98)77543-5. Biophys J. 1998. PMID: 9649416 Free PMC article.

10

Structural changes of the sarcoplasmic reticulum Ca(2+)-ATPase upon nucleotide binding studied by fourier transform infrared spectroscopy.

von Germar F, Barth A, Mäntele W. von Germar F, et al. Among authors: barth a. Biophys J. 2000 Mar;78(3):1531-40. doi: 10.1016/S0006-3495(00)76705-1. Biophys J. 2000. PMID: 10692337 Free PMC article.

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