Zobrazeno 1 - 10
of 11
pro vyhledávání: '"Janet S. Hankins"'
Autor:
Stephen M. Garrey, Jenna L. Riffell, Janet S. Hankins, Ying-Han Roger Hsu, George A. Mackie, Melinda M. Diver, Michaela Blech, Vitharani Kunanithy, Leigh M. Stickney
Publikováno v:
Journal of Biological Chemistry. 284:31843-31850
The paralogous endoribonucleases, RNase E and RNase G, play major roles in intracellular RNA metabolism in Escherichia coli and related organisms. To assay the relative importance of the principal RNA binding sites identified by crystallographic anal
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::afc2c31468b4234e17d75213fd38c37b
https://doi.org/10.1074/jbc.m109.063263
https://doi.org/10.1074/jbc.m109.063263
Publikováno v:
Journal of Bacteriology. 189:4353-4358
Degradation of the cspA mRNA in vivo is very rapid at temperatures greater than 30°C and is moderately dependent on RNase E. Investigations in vitro show that degradosomes prepared from normal or cold-shocked cultures cleave the cspA mRNA preferenti
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::af574ff98154a5ac7a06f7c193eaac47
https://doi.org/10.1128/jb.00193-07
https://doi.org/10.1128/jb.00193-07
Publikováno v:
Journal of Bacteriology. 187:7214-7221
We have examined the roles of the conserved S1 and KH RNA binding motifs in the widely dispersed prokaryotic exoribonuclease polynucleotide phosphorylase (PNPase). These domains can be released from the enzyme by mild proteolysis or by truncation of
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4b5620b496d9dd28c2582a555cd31b8f
https://doi.org/10.1128/jb.187.21.7214-7221.2005
https://doi.org/10.1128/jb.187.21.7214-7221.2005
Publikováno v:
Molecular Microbiology. 50:1381-1390
RNase G is the endoribonuclease responsible for forming the mature 5' end of 16S rRNA. This enzyme shares 35% identity with and 50% similarity to the N-terminal 470 amino acids encompassing the catalytic domain of RNase E, the major endonuclease in E
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::24a1f36d4b57a512473626f1f3a928ee
https://doi.org/10.1046/j.1365-2958.2003.03775.x
https://doi.org/10.1046/j.1365-2958.2003.03775.x
Autor:
Dora K. Lee, Laura Sekirov, Ljiljana D. Kojic, Steven M. Ansell, Anthony Boey, Nancy Dos Santos, Sandra K. Klimuk, Troy Harasym, Sean C. Semple, Janet S. Hankins, Athena R. Bennett
Publikováno v:
Bioconjugate Chemistry. 10:653-666
Lipid conjugates of oligo-(14-amino-3,6,9,12-tetraoxatetradecanoic acid) (ATTAn) were synthesized as monodisperse analogues of poly(ethylene glycol) (PEG) derivatives used in liposomal drug delivery systems. The new lipids were shown to be at least e
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::41bcd4c1209c8326a9a52fb0ba51f4ae
https://doi.org/10.1021/bc990005p
https://doi.org/10.1021/bc990005p
Publikováno v:
Journal of bacteriology. 192(10)
Differential mRNA stability is an important means of achieving posttranscriptional regulation of gene expression in Escherichia coli and many other organisms (1, 5). CspA, a small cold shock protein (11, 16, 17, 28), is an excellent case in point. Du
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::46864c9a752505b5d6ec0855ab05a57d
https://pubmed.ncbi.nlm.nih.gov/20233932
https://pubmed.ncbi.nlm.nih.gov/20233932
Autor:
Stephen M, Garrey, Michaela, Blech, Jenna L, Riffell, Janet S, Hankins, Leigh M, Stickney, Melinda, Diver, Ying-Han Roger, Hsu, Vitharani, Kunanithy, George A, Mackie
Publikováno v:
The Journal of biological chemistry. 284(46)
The paralogous endoribonucleases, RNase E and RNase G, play major roles in intracellular RNA metabolism in Escherichia coli and related organisms. To assay the relative importance of the principal RNA binding sites identified by crystallographic anal
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::a9d3ebeb688a67e6a7991c979810f676
https://pubmed.ncbi.nlm.nih.gov/19778900
https://pubmed.ncbi.nlm.nih.gov/19778900
Autor:
George A, Mackie, Glen A, Coburn, Xin, Miao, Douglas J, Briant, Annie, Prud'homme-Généreux, Leigh M, Stickney, Janet S, Hankins
Publikováno v:
Methods in enzymology. 447
The RNA degradosome is a multienzyme complex that plays a key role in the processing of stable RNAs, the degradation of mRNAs, and the action of small regulatory RNAs. Initially discovered in Escherichia coli, similar or related complexes are found i
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::13ac0623faf4d4d11d5654834bff254d
https://pubmed.ncbi.nlm.nih.gov/19161845
https://pubmed.ncbi.nlm.nih.gov/19161845
Autor:
Janet S. Hankins, Annie Prud’Homme-Genereux, George A. Mackie, Leigh M. Stickney, Douglas J. Briant, Xin Miao, Glen A. Coburn
The RNA degradosome is a multienzyme complex that plays a key role in the processing of stable RNAs, the degradation of mRNAs, and the action of small regulatory RNAs. Initially discovered in Escherichia coli , similar or related complexes are found
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::45cb8e72c6b47f82e87d2d0cba79e5b9
https://doi.org/10.1016/s0076-6879(08)02211-8
https://doi.org/10.1016/s0076-6879(08)02211-8
Publikováno v:
Molecular microbiology. 50(4)
RNase G is the endoribonuclease responsible for forming the mature 5' end of 16S rRNA. This enzyme shares 35% identity with and 50% similarity to the N-terminal 470 amino acids encompassing the catalytic domain of RNase E, the major endonuclease in E
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::4150a967f4c1c95ead47d44522209578
https://pubmed.ncbi.nlm.nih.gov/14622423
https://pubmed.ncbi.nlm.nih.gov/14622423