Joern Krausze
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Explore the profile of Joern Krausze including associated specialties, affiliations and a list of published articles.
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Articles
26
Citations
386
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0
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Recent Articles
1.
Karanth M, Kirkpatrick J, Krausze J, Schmelz S, Scrima A, Carlomagno T
Sci Adv
. 2024 Jun;
10(25):eadm9404.
PMID: 38896613
In the quest for new bioactive substances, nonribosomal peptide synthetases (NRPS) provide biodiversity by synthesizing nonproteinaceous peptides with high cellular activity. NRPS machinery consists of multiple modules, each catalyzing a...
2.
Probst C, Yang J, Krausze J, Hercher T, Richers C, Spatzal T, et al.
Nat Chem
. 2021 Jun;
13(8):758-765.
PMID: 34183818
The molybdenum cofactor (Moco) is found in the active site of numerous important enzymes that are critical to biological processes. The bidentate ligand that chelates molybdenum in Moco is the...
3.
Diwo M, Michel W, Aurass P, Kuhle-Keindorf K, Pippel J, Krausze J, et al.
Proc Natl Acad Sci U S A
. 2021 Jun;
118(23).
PMID: 34074754
The virulence factor PlaB promotes lung colonization, tissue destruction, and intracellular replication of , the causative agent of Legionnaires' disease. It is a highly active phospholipase exposed at the bacterial...
4.
Hercher T, Krausze J, Yang J, Kirk M, Kruse T
Biosci Rep
. 2020 Oct;
40(11).
PMID: 33084886
The molybdenum cofactor (Moco) is a redox active prosthetic group found in the active site of Moco-dependent enzymes (Mo-enzymes). As Moco and its intermediates are highly sensitive towards oxidative damage,...
5.
Krausze J, Hercher T, Archna A, Kruse T
Acta Crystallogr F Struct Biol Commun
. 2020 Sep;
76(Pt 9):453-463.
PMID: 32880594
The molybdenum cofactor (Moco) is the prosthetic group of all molybdenum-dependent enzymes except for nitrogenase. The multistep biosynthesis pathway of Moco and its function in molybdenum-dependent enzymes are already well...
6.
Massmig M, Reijerse E, Krausze J, Laurich C, Lubitz W, Jahn D, et al.
J Biol Chem
. 2020 Jul;
295(37):13065-13078.
PMID: 32694223
Bacterial formation of trimethylamine (TMA) from carnitine in the gut microbiome has been linked to cardiovascular disease. During this process, the two-component carnitine monooxygenase (CntAB) catalyzes the oxygen-dependent cleavage of...
7.
Hercher T, Krausze J, Hoffmeister S, Zwerschke D, Lindel T, Blankenfeldt W, et al.
Biosci Rep
. 2019 Dec;
40(1).
PMID: 31860061
Molybdenum insertases (Mo-insertases) catalyze the final step of molybdenum cofactor (Moco) biosynthesis, an evolutionary old and highly conserved multi-step pathway. In the first step of the pathway, GTP serves as...
8.
Lambertz R, Pippel J, Gerhauser I, Kollmus H, Anhlan D, Hrincius E, et al.
J Gen Virol
. 2018 Aug;
99(9):1187-1198.
PMID: 30084768
The haemagglutinin (HA) of H1N1 and H3N2 influenza A virus (IAV) subtypes has to be activated by host proteases. Previous studies showed that H1N1 virus cannot replicate efficiently in Tmprss2...
9.
Krausze J, Hercher T, Zwerschke D, Kirk M, Blankenfeldt W, Mendel R, et al.
Biochem J
. 2018 May;
475(10):1739-1753.
PMID: 29717023
The molybdenum cofactor (Moco) is a redox-active prosthetic group found in the active site of Moco-dependent enzymes, which are vitally important for life. Moco biosynthesis involves several enzymes that catalyze...
10.
Layer G, Krausze J, Moser J
Adv Exp Med Biol
. 2016 Dec;
925:147-161.
PMID: 27957709
The sophisticated biochemistry of nitrogenase plays a fundamental role for the biosynthesis of tetrapyrrole molecules, acting as key components of photosynthesis and methanogenesis. Three nitrogenase-like metalloenzymes have been characterized to...