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Items: 10


Na,K-ATPase in skeletal muscle: two populations of beta-spectrin control localization in the sarcolemma but not partitioning between the sarcolemma and the transverse tubules.

Williams MW, Resneck WG, Kaysser T, Ursitti JA, Birkenmeier CS, Barker JE, Bloch RJ.

J Cell Sci. 2001 Feb;114(Pt 4):751-62. Erratum in: J Cell Sci. 2010 Jun;123(Pt 11):1970.


Identification of a stable semiquinone intermediate in the purified and membrane bound ubiquinol oxidase-cytochrome bd from Escherichia coli.

Hastings SF, Kaysser TM, Jiang F, Salerno JC, Gennis RB, Ingledew WJ.

Eur J Biochem. 1998 Jul 1;255(1):317-23.


Resonance Raman spectroscopic identification of a histidine ligand of b595 and the nature of the ligation of chlorin d in the fully reduced Escherichia coli cytochrome bd oxidase.

Sun J, Kahlow MA, Kaysser TM, Osborne JP, Hill JJ, Rohlfs RJ, Hille R, Gennis RB, Loehr TM.

Biochemistry. 1996 Feb 20;35(7):2403-12.


Methionine-393 is an axial ligand of the heme b558 component of the cytochrome bd ubiquinol oxidase from Escherichia coli.

Kaysser TM, Ghaim JB, Georgiou C, Gennis RB.

Biochemistry. 1995 Oct 17;34(41):13491-501.


Resonance Raman studies of Escherichia coli cytochrome bd oxidase. Selective enhancement of the three heme chromophores of the "as-isolated" enzyme and characterization of the cyanide adduct.

Sun J, Osborne JP, Kahlow MA, Kaysser TM, Hil JJ, Gennis RB, Loehr TM.

Biochemistry. 1995 Sep 26;34(38):12144-51. Erratum in: Biochemistry 1996 Jan 16;35(2):666.


The haem b558 component of the cytochrome bd quinol oxidase complex from Escherichia coli has histidine-methionine axial ligation.

Spinner F, Cheesman MR, Thomson AJ, Kaysser T, Gennis RB, Peng Q, Peterson J.

Biochem J. 1995 Jun 1;308 ( Pt 2):641-4.


The murine mutation jaundiced is caused by replacement of an arginine with a stop codon in the mRNA encoding the ninth repeat of beta-spectrin.

Bloom ML, Kaysser TM, Birkenmeier CS, Barker JE.

Proc Natl Acad Sci U S A. 1994 Oct 11;91(21):10099-103.


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