Match!
Michael W. Risør
Aarhus University
ChemistryVenus flytrapBiochemistryBiologyAmyloid
16Publications
7H-index
146Citations
What is this?
Publications 16
Newest
#1Marina Linova (University of Southern Denmark)H-Index: 1
#2Michael W. Risør (AU: Aarhus University)H-Index: 7
Last. Henrik Karring (University of Southern Denmark)H-Index: 17
view all 8 authors...
Abstract The SUMO fusion system is widely used to facilitate recombinant expression and production of difficult-to-express proteins. After purification of the recombinant fusion protein, removal of the SUMO-tag is accomplished by the yeast cysteine protease, SUMO protease 1 (Ulp1), which specifically recognizes the tertiary fold of the SUMO domain. At present, the expression of the catalytic domain, residues 403–621, is used for obtaining soluble and biologically active Ulp1. However, we have ob...
1 CitationsSource
#1Mengjun Xue (AU: Aarhus University)H-Index: 3
#2Takuro Wakamoto (Rits: Ritsumeikan University)H-Index: 2
Last. Frans A. A. Mulder (AU: Aarhus University)H-Index: 35
view all 9 authors...
Although many proteins possess a distinct folded structure lying at a minimum in a funneled free energy landscape, thermal energy causes any protein to continuously access lowly populated excited states. The existence of excited states is an integral part of biological function. Although transitions into the excited states may lead to protein misfolding and aggregation, little structural information is currently available for them. Here, we show how NMR spectroscopy, coupled with pressure pertur...
5 CitationsSource
#1Ebbe Toftgaard Poulsen (AU: Aarhus University)H-Index: 12
#2Nadia Sukusu Nielsen (AU: Aarhus University)H-Index: 6
Last. Jan J. Enghild (AU: Aarhus University)H-Index: 59
view all 12 authors...
: The serine protease high-temperature requirement protein A1 (HtrA1) is associated with protein-misfolding disorders such as Alzheimer's disease and transforming growth factor β-induced protein (TGFBIp)-linked corneal dystrophy. In this study, using several biochemical and biophysical approaches, including recombinant protein expression, LC-MS/MS and 2DE analyses, and thioflavin T (ThT) fluorescence assays for amyloid fibril detection, and FTIR assays, we investigated the role of HtrA1 both in ...
3 CitationsSource
#1Dennis Wilkens Juhl (AU: Aarhus University)H-Index: 3
#2Michael W. Risør (AU: Aarhus University)H-Index: 7
Last. Jan J. Enghild (AU: Aarhus University)H-Index: 59
view all 7 authors...
Several human proteins cause disease by misfolding and aggregating into amyloid fibril deposits affecting the surrounding tissues. Multiple other proteins co-associate with the diseased deposits but little is known about how this association is influenced by the nature of the amyloid aggregate and the properties of the amyloid-forming protein. In this study, we investigated the co-aggregation of plasma and cerebrospinal proteins in the presence of pre-formed amyloid fibrils. We evaluated the fib...
4 CitationsSource
#1Nadia Sukusu Nielsen (AU: Aarhus University)H-Index: 6
#2Dennis Wilkens Juhl (AU: Aarhus University)H-Index: 3
Last. Jan J. Enghild (AU: Aarhus University)H-Index: 59
view all 8 authors...
Mutations in the transforming growth factor β-induced protein (TGFBIp) cause phenotypically diverse corneal dystrophies, where protein aggregation in the cornea leads to severe visual impairment. Previous studies have shown a relationship between mutant-specific corneal dystrophy phenotypes and the thermodynamic stability of TGFBIp. Using liquid chromatography–tandem mass spectrometry and nuclear magnetic resonance (NMR), we investigated correlations between the structural integrity of disease-r...
3 CitationsSource
#1Michael W. Risør (AU: Aarhus University)H-Index: 7
#2Dennis Wilkens Juhl (AU: Aarhus University)H-Index: 3
Last. Daniel E. Otzen (AU: Aarhus University)H-Index: 60
view all 7 authors...
Abstract Many proteins and peptides self-associate into highly ordered and structurally similar amyloid cross- β aggregates. This fibrillation is critically dependent on properties of the protein and the surrounding environment that alter kinetic and thermodynamic equilibria. Here, we report on dominating surface and solution effects on the fibrillogenic behavior and amyloid assembly of the C-36 peptide, a circulating bioactive peptide from the α 1 -antitrypsin serine protease inhibitor. C-36 co...
5 CitationsSource
#1Ole Juul Andersen (AU: Aarhus University)H-Index: 4
#2Michael W. Risør (AU: Aarhus University)H-Index: 7
Last. Birgit Schiøtt (AU: Aarhus University)H-Index: 30
view all 7 authors...
Protease inhibition by metastable serine protease inhibitors (serpins) is mediated by one of the largest functional intradomain conformational changes known in biology. In this extensive structural rearrangement, protease–serpin complex formation triggers cleavage of the serpin reactive center loop (RCL), its subsequent insertion into central β-sheet A, and covalent trapping of the target protease. In this study, we present the first detailed accelerated molecular dynamics simulation of the inse...
14 CitationsSource
#1Nadia Sukusu Nielsen (AU: Aarhus University)H-Index: 6
#2Ebbe Toftgaard Poulsen (AU: Aarhus University)H-Index: 12
Last. Jan J. Enghild (AU: Aarhus University)H-Index: 59
view all 8 authors...
1 Citations
#1Michael W. Risør (AU: Aarhus University)H-Index: 7
#2Line R. Thomsen (AU: Aarhus University)H-Index: 5
Last. Jan J. Enghild (AU: Aarhus University)H-Index: 59
view all 13 authors...
Carnivorous plants primarily use aspartic proteases during digestion of captured prey. In contrast, the major endopeptidases in the digestive fluid of the Venus flytrap (Dionaea muscipula) are cysteine proteases (dionain-1 to -4). Here, we present the crystal structure of mature dionain-1 in covalent complex with inhibitor E-64 at 1.5 A resolution. The enzyme exhibits an overall protein fold reminiscent of other plant cysteine proteases. The inactive glycosylated pro-form undergoes autoprocessin...
9 CitationsSource
#1Michael W. RisørH-Index: 7
#2Line R. ThomsenH-Index: 5
Last. Jan J. EnghildH-Index: 59
view all 13 authors...
Source
12