Zobrazeno 1 - 7
of 7
pro vyhledávání: '"Hermann Hämmerle"'
Publikováno v:
PLoS ONE, Vol 9, Iss 6, p e98661 (2014)
The RNA chaperone Hfq acts as a central player in post-transcriptional gene regulation in several Gram-negative Bacteria, whereas comparatively little is known about its role in Gram-positive Bacteria. Here, we studied the function of Hfq in Bacillus
Externí odkaz:
https://doaj.org/article/abc469ee12564f399c2138999f431a00
Autor:
Hermann Hämmerle, Mads Beich-Frandsen, Branislav Večerek, Lukas Rajkowitsch, Oliviero Carugo, Kristina Djinović-Carugo, Udo Bläsi
Publikováno v:
PLoS ONE, Vol 7, Iss 11, p e50892 (2012)
In Escherichia coli the RNA chaperone Hfq is involved in riboregulation by assisting base-pairing between small regulatory RNAs (sRNAs) and mRNA targets. Several structural and biochemical studies revealed RNA binding sites on either surface of the d
Externí odkaz:
https://doaj.org/article/39b5024d3dec4894884480f53637362d
Autor:
Branislav Večerek, Herwig Peterlik, Dmitri I. Svergun, Udo Bläsi, Euripedes de Almeida Ribeiro, Hermann Hämmerle, Mads Beich-Frandsen, Petr V. Konarev, Weifeng Shang, Kristina Djinović-Carugo, Georg Kontaxis
Publikováno v:
Nucleic Acids Research
Nucleic acids research 40(16), 8072-8084 (2012). doi:10.1093/nar/gks510
Nucleic acids research 40(16), 8072-8084 (2012). doi:10.1093/nar/gks510
In enteric bacteria, many small regulatory RNAs (sRNAs) associate with the RNA chaperone host factor Q (Hfq) and often require the protein for regulation of target mRNAs. Previous studies suggested that the hexameric Escherichia coli Hfq (Hfq(Ec)) bi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3a2fd3c3991f45b1c0f8f8b77c43641b
https://doi.org/10.1093/nar/gks510
https://doi.org/10.1093/nar/gks510
Autor:
Udo Bläsi, Kristina Djinović-Carugo, Hermann Hämmerle, Robert Konrat, Dimitri I. Svergun, Björn Sjöblom, Georg Kontaxis, Petr V. Konarev, Bonnie A. Wallace, Karin Kloiber, Andrew J. Miles, Mads Beich-Frandsen, Branislav Večerek, Lukas Rajkowitsch
Publikováno v:
Nucleic Acids Research
Nucleic acids research 39(11), 4900-4915 (2011). doi:10.1093/nar/gkq1346
Nucleic acids research 39(11), 4900-4915 (2011). doi:10.1093/nar/gkq1346
The hexameric Escherichia coli RNA chaperone Hfq (Hfq(Ec)) is involved in riboregulation of target mRNAs by small trans-encoded RNAs. Hfq proteins of different bacteria comprise an evolutionarily conserved core, whereas the C-terminus is variable in
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3f8f41b298bf6899f1a6c682a22105ef
https://doi.org/10.1093/nar/gkq1346
https://doi.org/10.1093/nar/gkq1346
Publikováno v:
PLoS ONE
PLoS ONE, Vol 9, Iss 6, p e98661 (2014)
PLoS ONE, Vol 9, Iss 6, p e98661 (2014)
The RNA chaperone Hfq acts as a central player in post-transcriptional gene regulation in several Gram-negative Bacteria, whereas comparatively little is known about its role in Gram-positive Bacteria. Here, we studied the function of Hfq in Bacillus
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::95172a2d6649abb35a6046c3c13cb6e1
https://pubmed.ncbi.nlm.nih.gov/24932523
https://pubmed.ncbi.nlm.nih.gov/24932523
Publikováno v:
RNA biology. 10(12)
At low temperatures the Escherichia coli rpoS mRNA, encoding the stationary phase sigma factor RpoS, forms an intramolecular secondary structure (iss) that impedes translation initiation. Under these conditions the small RNA DsrA, which is stabilzed
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::ef8fda728a3b5be218fb52ef59365288
https://pubmed.ncbi.nlm.nih.gov/24448230
https://pubmed.ncbi.nlm.nih.gov/24448230
Autor:
Mads Beich-Frandsen, Oliviero Carugo, Udo Bläsi, Hermann Hämmerle, Kristina Djinović-Carugo, Branislav Večerek, Lukas Rajkowitsch
Publikováno v:
PLoS ONE, Vol 7, Iss 11, p e50892 (2012)
PLoS ONE
PLoS ONE
In Escherichia coli the RNA chaperone Hfq is involved in riboregulation by assisting base-pairing between small regulatory RNAs (sRNAs) and mRNA targets. Several structural and biochemical studies revealed RNA binding sites on either surface of the d
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::cc6fc5edf5d979d3011c88dc36d5e5c9
https://doi.org/10.1371/journal.pone.0050892
https://doi.org/10.1371/journal.pone.0050892