Watching the uniformly accelerated reference frame

Rothenstein, Bernhard; Rothenstein, Albert

doi:10.1088/0143-0807/12/5/005

Cited by 2 publications

(1 citation statement)

References 2 publications

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“…Disruption of p30 Gene-Deletion of most of the p30 gene was carried out by a one-step replacement (28). A targeting vector for yeast p30 cDNA was constructed as follows.…”

Section: Methodsmentioning

confidence: 99%

p32 Protein, a Splicing Factor 2-associated Protein, Is Localized in Mitochondrial Matrix and Is Functionally Important in Maintaining Oxidative Phosphorylation

Muta¹,

Kang²,

Kitajima³

et al. 1997

Journal of Biological Chemistry

205

214

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Human p32, originally cloned as a splicing factor 2-associated protein, has been reported to interact with a variety of molecules including human immunodeficiency virus Tat and complement 1q (C1q). p32 protein is supposed to be in the nucleus and on the plasma membrane for the association with human immunodeficiency virus Tat and C1q, respectively. None of the interactions, however, is proven to have a physiological role. To investigate the physiological function of p32, we determined the intracellular localization of p32. The fractionation of cells, fluorescent immunocytochemistry, and electron microscopic immunostaining show that p32 is exclusively localized in the mitochondrial matrix. We cloned a Saccharomyces cerevisiae homologue of human p32 gene, referred to yeast p30 gene. The yeast p30 protein is also localized in the mitochondrial matrix. The disruption of the p30 gene caused the growth retardation of yeast cells in a glycerol medium but not in a glucose medium, i.e. the impairment of the mitochondrial ATP synthesis. The growth impairment was restored by the introduction of the human p32 cDNA, indicating that p30 is a functional yeast counterpart of human p32. Taken together, both p32 and p30 reside in mitochondrial matrix and play an important role in maintaining mitochondrial oxidative phosphorylation.

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“…Disruption of p30 Gene-Deletion of most of the p30 gene was carried out by a one-step replacement (28). A targeting vector for yeast p30 cDNA was constructed as follows.…”

Section: Methodsmentioning

confidence: 99%

p32 Protein, a Splicing Factor 2-associated Protein, Is Localized in Mitochondrial Matrix and Is Functionally Important in Maintaining Oxidative Phosphorylation

Muta¹,

Kang²,

Kitajima³

et al. 1997

Journal of Biological Chemistry

205

214

View full text Add to dashboard Cite

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Special relativity with television techniques

Rothenstein¹,

Tamasdan²

1994

Eur. J. Phys.

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The main purpose of this paper is to show that if the student has understood special relativity with Einstein synchronized clocks knowing that the times tE and t'E which appear in the Lorentz transformations are times measured with such clocks, then the teacher can obtain the Lorentz transformations with non-Einstein-synchronized clocks simply by replacing tE and t'E with a relationship which relates them to the times measured on this new set of clocks. All the relativistic effects which are a consequence of the manner in which simultaneity is ensured, are interpreted as an attempt of an inertial observer to measure the proper length of a moving rod or the proper time of a moving rod.

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Watching the uniformly accelerated reference frame

Abstract: The apparent shape and colour of objects moving at a constant proper acceleration is presented.

Cited by 2 publications

References 2 publications

p32 Protein, a Splicing Factor 2-associated Protein, Is Localized in Mitochondrial Matrix and Is Functionally Important in Maintaining Oxidative Phosphorylation

p32 Protein, a Splicing Factor 2-associated Protein, Is Localized in Mitochondrial Matrix and Is Functionally Important in Maintaining Oxidative Phosphorylation

Special relativity with television techniques

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