Difference between revisions of "Paper"
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== Jan Gundlach== | == Jan Gundlach== | ||
− | <pubmed></pubmed> | + | <pubmed> 25215494 15968460 9787636 </pubmed> |
== für Master-Seminar == | == für Master-Seminar == |
Revision as of 12:54, 14 October 2014
Contents
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POTM
Kimihiro Abe, Yuta Kawano, Keito Iwamoto, Kenji Arai, Yuki Maruyama, Patrick Eichenberger, Tsutomu Sato
Developmentally-regulated excision of the SPβ prophage reconstitutes a gene required for spore envelope maturation in Bacillus subtilis.
PLoS Genet: 2014, 10(10);e1004636
[PubMed:25299644]
[WorldCat.org]
[DOI]
(I e)
Nils Jäger
Jan Lüddecke, Karl Forchhammer
From PII signaling to metabolite sensing: a novel 2-oxoglutarate sensor that details PII-NAGK complex formation.
PLoS One: 2013, 8(12);e83181
[PubMed:24349456]
[WorldCat.org]
[DOI]
(I e)
Rebecca M Corrigan, Ivan Campeotto, Tharshika Jeganathan, Kevin G Roelofs, Vincent T Lee, Angelika Gründling
Systematic identification of conserved bacterial c-di-AMP receptor proteins.
Proc Natl Acad Sci U S A: 2013, 110(22);9084-9
[PubMed:23671116]
[WorldCat.org]
[DOI]
(I p)
Felix M P Mehne, Katrin Gunka, Hinnerk Eilers, Christina Herzberg, Volkhard Kaever, Jörg Stülke
Cyclic di-AMP homeostasis in bacillus subtilis: both lack and high level accumulation of the nucleotide are detrimental for cell growth.
J Biol Chem: 2013, 288(3);2004-17
[PubMed:23192352]
[WorldCat.org]
[DOI]
(I p)
Jan Gundlach
Kamakshi Sureka, Philip H Choi, Mimi Precit, Matthieu Delince, Daniel A Pensinger, TuAnh Ngoc Huynh, Ashley R Jurado, Young Ah Goo, Martin Sadilek, Anthony T Iavarone, John-Demian Sauer, Liang Tong, Joshua J Woodward
The cyclic dinucleotide c-di-AMP is an allosteric regulator of metabolic enzyme function.
Cell: 2014, 158(6);1389-1401
[PubMed:25215494]
[WorldCat.org]
[DOI]
(I p)
L Tong
Acetyl-coenzyme A carboxylase: crucial metabolic enzyme and attractive target for drug discovery.
Cell Mol Life Sci: 2005, 62(16);1784-803
[PubMed:15968460]
[WorldCat.org]
[DOI]
(P p)
T Dandekar, B Snel, M Huynen, P Bork
Conservation of gene order: a fingerprint of proteins that physically interact.
Trends Biochem Sci: 1998, 23(9);324-8
[PubMed:9787636]
[WorldCat.org]
[DOI]
(P p)