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Contents: December 1996, Volume 1, Issue 12   [Index by Author]       Other Issues:  
       Original Articles
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To see an article, click its [Full Text] link. To review many abstracts, check the boxes to the left of the titles you want, and click the 'Get All Checked Abstract(s)' button. To see one abstract at a time, click its [Abstract] link.

Original Articles:

H Kawase, M Okuwaki, M Miyaji, R Ohba, H Handa, Y Ishimi, T Fujii-Nakata, A Kikuchi, and K Nagata
NAP-I is a functional homologue of TAF-I that is required for replication and transcription of the adenovirus genome in a chromatin-like structure
Genes to Cells (1996) 1, 1045-1056. [Abstract] [PDF]  

K Maeshima, K Morimatsu, and T Horii
Purification and characterization of XRad51.1 protein, Xenopus RAD51 homologue: recombinant XRad51.1 promotes strand exchange reaction
Genes to Cells (1996) 1, 1057-1068. [Abstract] [PDF]  

T Yokochi, J Kato, and H Ikeda
DNA nicking by Escherichia coli topoisomerase IV with a substitution mutation from tyrosine to histidine at the active site
Genes to Cells (1996) 1, 1069-1075. [Abstract] [PDF]  

M Suzuki, K Abe, K Yoshinaga, M Obinata, M Furusawa, and K Abe
Specific arrest of spermatogenesis caused by apoptotic cell death in transgenic mice
Genes to Cells (1996) 1, 1077-1086. [Abstract] [PDF]  

K Fukushima, S Motomura, A Kuraoka, H Nakano, and T Nishimoto
A single point mutation of hamster aminoacyl-tRNA synthetase causes apoptosis by deprivation of cognate amino acid residue
Genes to Cells (1996) 1, 1087-1099. [Abstract] [PDF]  

S Motomura, K Fukushima, H Nishitani, H Nawata, and T Nishimoto
A hamster temperature-sensitive G1 mutant, tsBN250 has a single point mutation in histidyl-tRNA synthetase that inhibits an accumulation of cyclin D1
Genes to Cells (1996) 1, 1101-1112. [Abstract] [PDF]  

To see an article, click its [Full Text] link. To review many abstracts, check the boxes to the left of the titles you want, and click the 'Get All Checked Abstract(s)' button. To see one abstract at a time, click its [Abstract] link.


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