scholarly journals Evolution of tRNA nucleotidyltransferases: A small deletion generated CC-adding enzymes

2008 ◽  
Vol 105 (23) ◽  
pp. 7953-7958 ◽  
Author(s):  
A. Neuenfeldt ◽  
A. Just ◽  
H. Betat ◽  
M. Morl
Keyword(s):  
PLoS ONE ◽  
2008 ◽  
Vol 3 (8) ◽  
pp. e3104 ◽  
Author(s):  
Adam J. de Smith ◽  
Robin G. Walters ◽  
Lachlan J. M. Coin ◽  
Israel Steinfeld ◽  
Zohar Yakhini ◽  
...  
Keyword(s):  

Virology ◽  
1992 ◽  
Vol 189 (2) ◽  
pp. 556-567 ◽  
Author(s):  
Philippe Dezélée ◽  
Jean Vianney Barnier ◽  
Annie Hampe ◽  
Danielle Laugier ◽  
Maria Marx ◽  
...  

1985 ◽  
Vol 5 (2) ◽  
pp. 422-426
Author(s):  
J S Verbeek ◽  
A J Roebroek ◽  
A M van den Ouweland ◽  
H P Bloemers ◽  
W J Van de Ven

The organization of the human c-fms proto-oncogene has been determined and compared with an abnormal allele. The human v-fms homologous genetic sequences are dispersed discontinuously and colinearly with the viral oncogene over a DNA region of ca. 32 kilobase pairs. The abnormal c-fms locus contains a small deletion in its 3' portion. DNA sequencing analysis indicated that it was 426 base pairs in size and located in close proximity to a putative c-fms exon.


2019 ◽  
Vol 09 (02) ◽  
pp. 114-116
Author(s):  
Esra Nagehan Akyol Onder ◽  
Mine Ozkol ◽  
Nalan Nese ◽  
Can Taneli ◽  
Osman Orkun Cankorur ◽  
...  

AbstractXanthogranulomatous pyelonephritis (XGP) is characterized by destruction of the renal parenchyma and granulomatous inflammation with lipid-laden foamy macrophages as well as inflammatory infiltration and intensive renal fibrosis. It generally occurs in adults, especially those in the fifth and sixth decades of life, but is occasionally seen in children as well. Brachydactyly mental retardation (BDMR) syndrome (OMIM 600430) is caused by a small deletion of chromosome 2q37 and is a rare condition, with roughly 100 cases reported worldwide. Here, we describe the case of a patient with deletion of chromosome 2q37, which is known as the BDMR syndrome, and XGP.


2000 ◽  
Vol 8 (4) ◽  
pp. 248-257 ◽  
Author(s):  
A.-M.K Säämänen ◽  
H.J Salminen ◽  
P.B Dean ◽  
B De Crombrugghe ◽  
E.I Vuorio ◽  
...  

2008 ◽  
Vol 38 (8) ◽  
pp. 781-787 ◽  
Author(s):  
E.G. Kakani ◽  
I.M. Ioannides ◽  
J.T. Margaritopoulos ◽  
N.A. Seraphides ◽  
P.J. Skouras ◽  
...  

Author(s):  
Chunhui Chen ◽  
Yin Wang ◽  
Hidemasa Nakaminami ◽  
Eu Suk Kim ◽  
George A. Jacoby ◽  
...  

The Qnr pentapeptide repeat proteins interact with DNA gyrase and protect it from quinolone inhibition. The two external loops, particularly the larger loop B, of Qnr proteins are essential for quinolone protection of DNA gyrase. The specific QnrB1 interaction sites on DNA gyrase are not known. In this study, we investigated the interaction between GyrA and QnrB1 using site-specific photo crosslinking of QnrB1 loop B combined with mass spectrometry. We found that amino acid residues 286-298 on the Tower domain of GyrA interact with QnrB1 and play a key role in QnrB1 protection of gyrase from quinolone inhibition. Alanine replacement of arginine at residue 293 and a small deletion of amino acids 286-289 of GyrA resulted in a decrease in the QnrB1-mediated increase in quinolone MICs and also abolished the QnrB1 protection of purified DNA gyrase from ciprofloxacin inhibition.


Sign in / Sign up

Export Citation Format

Share Document