Zobrazeno 1 - 9
of 9
pro vyhledávání: '"Marie-Kristin von Wrisberg"'
Autor:
Shu-Yu Chen, Michaela K. Fiedler, Thomas F. Gronauer, Olesia Omelko, Marie-Kristin von Wrisberg, Tao Wang, Sabine Schneider, Stephan A. Sieber, Martin Zacharias
Publikováno v:
Communications Biology, Vol 7, Iss 1, Pp 1-11 (2024)
Abstract Staphylococcus aureus signal peptidase IB (SpsB) is an essential enzyme for protein secretion. While inhibition of its activity by small molecules is a well-precedented mechanism to kill bacteria, the mode of activation is however less under
Externí odkaz:
https://doaj.org/article/29fa57a779a04f2d86a49e6cf38e078d
Publikováno v:
Communications Biology, Vol 5, Iss 1, Pp 1-9 (2022)
The structure of the Cas13a RNase from the purple bacterium R. capsulatus in complex with its crRNA is reported here. The study reveals that the enzyme combines shape and sequence-specific readout to recognize its crRNA.
Externí odkaz:
https://doaj.org/article/759a217191e64654b991a7b315e63116
Autor:
Shirley Tremel, Yohei Ohashi, Dustin R. Morado, Jessie Bertram, Olga Perisic, Laura T. L. Brandt, Marie-Kristin von Wrisberg, Zhuo A. Chen, Sarah L. Maslen, Oleksiy Kovtun, Mark Skehel, Juri Rappsilber, Kathrin Lang, Sean Munro, John A. G. Briggs, Roger L. Williams
Publikováno v:
Nature Communications, Vol 12, Iss 1, Pp 1-15 (2021)
The phosphatidylinositol-3-phosphate (PI3P) is generated by the lipid kinase VPS34, in the context of VPS34 complex I on autophagosomes or complex II on endosomes. Biochemical and structural analyses provide insights into the mechanism of both VPS34
Externí odkaz:
https://doaj.org/article/d0b77c3d6f3f4cfcbbaf6326c8d008f3
Autor:
Jiqing Du, Marie-Kristin von Wrisberg, Burak Gulen, Matthias Stahl, Christian Pett, Christian Hedberg, Kathrin Lang, Sabine Schneider, Aymelt Itzen
Publikováno v:
Nature Communications, Vol 12, Iss 1, Pp 1-16 (2021)
The Legionella effector DrrA AMPylates the host protein Rab1 during infection, but the mechanism is still under debate. Here, the authors provide structural insights into the low-affinity DrrA:Rab1 interaction, showing that Rab1 allosterically activa
Externí odkaz:
https://doaj.org/article/db46eaf2179e4b49abbf39b105a93816
Autor:
Anton Murnauer, Kathrin Lang, Susanne V. Mayer, Marie-Lena Jokisch, Marie-Kristin von Wrisberg
Publikováno v:
Angewandte Chemie (International Ed. in English)
Inverse electron‐demand Diels–Alder cycloadditions (iEDDAC) between tetrazines and strained alkenes/alkynes have emerged as essential tools for studying and manipulating biomolecules. A light‐triggered version of iEDDAC (photo‐iEDDAC) is pres
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2ec6ae0226a0201d7304789bb8b37af0
https://doi.org/10.1002/anie.201908209
https://doi.org/10.1002/anie.201908209
Autor:
Marie-Kristin von Wrisberg, Juri Rappsilber, Olga Perisic, Roger L. Williams, Sarah L. Maslen, Dustin R. Morado, John A. G. Briggs, Kathrin Lang, Jessie Bertram, Shirley Tremel, Sean Munro, Mark Skehel, Oleksiy Kovtun, Yohei Ohashi, Zhuo A. Chen, Laura T L Brandt
Publikováno v:
Nature Communications, 12
Tremel, S, Ohashi, Y, Morado, D R, Bertram, J, Perisic, O, Brandt, L T L, von Wrisberg, M K, Chen, Z A, Maslen, S L, Kovtun, O, Skehel, M, Rappsilber, J, Lang, K, Munro, S, Briggs, J A G & Williams, R L 2021, ' Structural basis for VPS34 kinase activation by Rab1 and Rab5 on membranes ', Nature Communications, vol. 12, 1564 . https://doi.org/10.1038/s41467-021-21695-2
Nature Communications, Vol 12, Iss 1, Pp 1-15 (2021)
Nature Communications
Tremel, S, Ohashi, Y, Morado, D R, Bertram, J, Perisic, O, Brandt, L T L, von Wrisberg, M K, Chen, Z A, Maslen, S L, Kovtun, O, Skehel, M, Rappsilber, J, Lang, K, Munro, S, Briggs, J A G & Williams, R L 2021, ' Structural basis for VPS34 kinase activation by Rab1 and Rab5 on membranes ', Nature Communications, vol. 12, 1564 . https://doi.org/10.1038/s41467-021-21695-2
Nature Communications, Vol 12, Iss 1, Pp 1-15 (2021)
Nature Communications
The lipid phosphatidylinositol-3-phosphate (PI3P) is a regulator of two fundamental but distinct cellular processes, endocytosis and autophagy, so its generation needs to be under precise temporal and spatial control. PI3P is generated by two complex
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f817ee0df381ae701383613316007446
https://hdl.handle.net/20.500.11850/529518
https://hdl.handle.net/20.500.11850/529518
Autor:
Christian Hedberg, Kathrin Lang, Jiqing Du, Burak Gulen, Marie Kristin von Wrisberg, Christian Pett, Matthias Stahl, Sabine Schneider, Aymelt Itzen
Publikováno v:
Nature Communications, Vol 12, Iss 1, Pp 1-16 (2021)
Nature Communications, 12 (1)
Nature Communications
'Nature Communications ', vol: 12, pages: 460-1-460-16 (2021)
Nature Communications, 12 (1)
Nature Communications
'Nature Communications ', vol: 12, pages: 460-1-460-16 (2021)
Legionella pneumophila infects eukaryotic cells by forming a replicative organelle – the Legionella containing vacuole. During this process, the bacterial protein DrrA/SidM is secreted and manipulates the activity and post-translational modificatio
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::bf16b711f2a76093fb12749be949f141
https://doi.org/10.1038/s41467-020-20702-2
https://doi.org/10.1038/s41467-020-20702-2
Autor:
Aymelt Itzen, Kathrin Lang, Maximilian Fottner, Thorsten G. Müller, Roger S. Goody, Daniel Horn-Ghetko, Matthias P. Müller, Marko Cigler, Marie-Kristin von Wrisberg
Publikováno v:
Angewandte Chemie. 129:15943-15947
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::30590e847271aa32af3b99e5d280a51b
https://doi.org/10.1002/ange.201706927
https://doi.org/10.1002/ange.201706927
Autor:
Marko Cigler, Matthias P. Müller, Kathrin Lang, Maximilian Fottner, Thorsten G. Müller, Roger S. Goody, Marie-Kristin von Wrisberg, Aymelt Itzen, Daniel Horn-Ghetko
Publikováno v:
Angewandte Chemie International Edition. 56:15737-15741
The characterization of low-affinity protein complexes is challenging due to their dynamic nature. Here, we present a method to stabilize transient protein complexes in vivo by generating a covalent and conformationally flexible bridge between the in
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1d32962e67ce31a6560cb4b2153bf12f
https://doi.org/10.1002/anie.201706927
https://doi.org/10.1002/anie.201706927