Zobrazeno 1 - 10
of 22
pro vyhledávání: '"Annette, Duelli"'
Autor:
Yihong Chen, Chrysostomi Gialeli, Junyan Shen, Pontus Dunér, Björn Walse, Annette Duelli, Rhawnie Caing-Carlsson, Anna M. Blom, John R. Zibert, Anna Hultgårdh Nilsson, Jan Alenfall, Chun Liang, Jan Nilsson
Publikováno v:
Pharmacological Research, Vol 205, Iss , Pp 107259- (2024)
The osteopontin-derived peptide FOL-005 stimulates hair growth. Using ligand-receptor glyco-capture technology we identified neuropilin-1 (NRP-1), a known co-receptor for vascular endothelial growth factor (VEGF) receptors, as the most probable recep
Externí odkaz:
https://doaj.org/article/d07c8358d1374cfe9015cbdecd1009ab
Autor:
Christina Grønberg, Qiaoxia Hu, Dhani Ram Mahato, Elena Longhin, Nina Salustros, Annette Duelli, Pin Lyu, Viktoria Bågenholm, Jonas Eriksson, Komal Umashankar Rao, Domhnall Iain Henderson, Gabriele Meloni, Magnus Andersson, Tristan Croll, Gabriela Godaly, Kaituo Wang, Pontus Gourdon
Publikováno v:
eLife, Vol 10 (2021)
Transition metals, such as zinc, are essential micronutrients in all organisms, but also highly toxic in excessive amounts. Heavy-metal transporting P-type (PIB) ATPases are crucial for homeostasis, conferring cellular detoxification and redistributi
Externí odkaz:
https://doaj.org/article/d573c39425cc4d7a8882ae41e7785cee
Autor:
Christina Grønberg, Qiaoxia Hu, Dhani Ram Mahato, Elena Longhin, Nina Salustros, Annette Duelli, Pin Lyu, Viktoria Bågenholm, Jonas Eriksson, Komal Umashankar Rao, Domhnall Iain Henderson, Gabriele Meloni, Magnus Andersson, Tristan Croll, Gabriela Godaly, Kaituo Wang, Pontus Gourdon
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::f6765f5a4f3feacf4c697c47b77838fa
https://doi.org/10.7554/elife.73124.sa2
https://doi.org/10.7554/elife.73124.sa2
Autor:
Qiaoxia Hu, Domhnall Iain Henderson, Komal Umashankar Rao, Magnus Andersson, Gabriela Godaly, Elena Longhin, Kaituo Wang, Gabriele Meloni, Annette Duelli, Jonas Eriksson, Tristan I. Croll, Christina Grønberg, Dhani Ram Mahato, Pontus Gourdon, Nina Salustros
Transition metals, such as zinc, are essential micronutrients in all organisms, but also highly toxic in excessive amounts. Heavy-metal transporting P-type (PIB) ATPases are crucial for homeostasis, conferring cellular detoxification and redistributi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::c4b5460f39121fc23a9c1ae30dd146e9
https://doi.org/10.1101/2021.09.01.458532
https://doi.org/10.1101/2021.09.01.458532
Autor:
Ida V. Lundholm, Helena Rodilla, Weixiao Y. Wahlgren, Annette Duelli, Gleb Bourenkov, Josip Vukusic, Ran Friedman, Jan Stake, Thomas Schneider, Gergely Katona
Publikováno v:
Structural Dynamics, Vol 2, Iss 5, Pp 054702-054702-12 (2015)
Whether long-range quantum coherent states could exist in biological systems, and beyond low-temperature regimes where quantum physics is known to be applicable, has been the subject to debate for decades. It was proposed by Fröhlich that vibrationa
Externí odkaz:
https://doaj.org/article/8ffd172668914c6588cfc6c9b74401cd
Autor:
Annette Duelli, Bence Kiss, Ida Lundholm, Andrea Bodor, Maxim V Petoukhov, Dmitri I Svergun, László Nyitray, Gergely Katona
Publikováno v:
PLoS ONE, Vol 9, Iss 5, p e97654 (2014)
S100A4 interacts with many binding partners upon Ca2+ activation and is strongly associated with increased metastasis formation. In order to understand the role of the C-terminal random coil for the protein function we examined how small angle X-ray
Externí odkaz:
https://doaj.org/article/32964cdd12d0482fb447a06672f31334
Autor:
Matteo Levantino, Martin Nors Pedersen, Chenge Li, Magnus Andersson, Mattias Eklund, Michael Wulff, Andreas Barth, Aljona Sitsel, Annette Duelli, Poul Nissen, Claus Olesen, Harsha Ravishankar
Publikováno v:
Ravishankar, H, Pedersen, M N, Eklund, M, Sitsel, A, Li, C, Duelli, A, Levantino, M, Wulff, M, Barth, A, Olesen, C, Nissen, P & Andersson, M 2020, ' Tracking Ca 2+ ATPase intermediates in real time by x-ray solution scattering ', Science Advances, vol. 6, no. 12, eaaz0981 . https://doi.org/10.1126/sciadv.aaz0981
'Science Advances ', vol: 6, pages: aaz0981-1-aaz0981-11 (2020)
'Science Advances ', vol: 6, pages: aaz0981-1-aaz0981-11 (2020)
Sarco/endoplasmic reticulum Ca2+ ATPase (SERCA) transporters regulate calcium signaling by active calcium ion reuptake to internal stores. Structural transitions associated with transport have been characterized by x-ray crystallography, but critical
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::dd20dc81064942645b3b496ce9815625
http://urn.kb.se/resolve?urn=urn:nbn:se:umu:diva-169875
http://urn.kb.se/resolve?urn=urn:nbn:se:umu:diva-169875
Autor:
Maria Skovager Jensen, Annette Duelli, T. Günther Pomorski, Rosa L. López-Marqués, Michael G. Palmgren, Lisbeth R. Poulsen, Lyubomir Dimitrov Stanchev, P. A. Andersen, Pontus Gourdon, Sara Rute Costa
Publikováno v:
Scientific Reports, Vol 7, Iss 1, Pp 1-13 (2017)
Scientific Reports
Jensen, M S, Costa, S, Duelli, A S, Andersen, P A, Poulsen, L R, Stanchev, L D, Gourdon, P E, Palmgren, M B, Günther-Pomorski, T & Lopez Marques, R L 2017, ' Phospholipid flipping involves a central cavity in P4 ATPases ', Scientific Reports, vol. 7, 17621 . https://doi.org/10.1038/s41598-017-17742-y
Scientific Reports
Jensen, M S, Costa, S, Duelli, A S, Andersen, P A, Poulsen, L R, Stanchev, L D, Gourdon, P E, Palmgren, M B, Günther-Pomorski, T & Lopez Marques, R L 2017, ' Phospholipid flipping involves a central cavity in P4 ATPases ', Scientific Reports, vol. 7, 17621 . https://doi.org/10.1038/s41598-017-17742-y
P4 ATPase flippases translocate phospholipids across biomembranes, thus contributing to the establishment of transmembrane lipid asymmetry, a feature important for multiple cellular processes. The mechanism by which such phospholipid flipping occurs
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0c42b1686f6136495902595fc413cab7
http://link.springer.com/article/10.1038/s41598-017-17742-y
http://link.springer.com/article/10.1038/s41598-017-17742-y
Autor:
Harsha, Ravishankar, Martin Nors, Pedersen, Mattias, Eklund, Aljona, Sitsel, Chenge, Li, Annette, Duelli, Matteo, Levantino, Michael, Wulff, Andreas, Barth, Claus, Olesen, Poul, Nissen, Magnus, Andersson
Publikováno v:
Science Advances
We characterize thus-far elusive domain rearrangements of a calcium-transporting ATPase in the native membrane.
Sarco/endoplasmic reticulum Ca2+ ATPase (SERCA) transporters regulate calcium signaling by active calcium ion reuptake to internal st
Sarco/endoplasmic reticulum Ca2+ ATPase (SERCA) transporters regulate calcium signaling by active calcium ion reuptake to internal st
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::bcea9f241be8c5237ffc6b7e775e51c2
https://pubmed.ncbi.nlm.nih.gov/32219166
https://pubmed.ncbi.nlm.nih.gov/32219166
Autor:
Jack Goodman, Harsha Ravishankar, Matteo Levantino, Annette Duelli, Per Rogne, Michael Wulff, Fredrik Orädd, Lars Backman, Martin Nors Pedersen, Magnus Andersson, Magnus Wolf-Watz
Publikováno v:
'Science Advances ', vol: 7, pages: eabi5514-1-eabi5514-12 (2021)
Science Advances
Orädd, F, Ravishankar, H, Goodman, J, Rogne, P, Backman, L, Duelli, A, Pedersen, M N, Levantino, M, Wulff, M, Wolf-Watz, M & Andersson, M 2021, ' Tracking the ATP-binding response in adenylate kinase in real time ', Science Advances, vol. 7, no. 47, eabi5514, pp. 1-13 . https://doi.org/10.1126/sciadv.abi5514
Science Advances
Orädd, F, Ravishankar, H, Goodman, J, Rogne, P, Backman, L, Duelli, A, Pedersen, M N, Levantino, M, Wulff, M, Wolf-Watz, M & Andersson, M 2021, ' Tracking the ATP-binding response in adenylate kinase in real time ', Science Advances, vol. 7, no. 47, eabi5514, pp. 1-13 . https://doi.org/10.1126/sciadv.abi5514
Description
Time-resolved x-ray solution scattering identifies cooperative structural dynamics in the adenylate kinase enzymatic reaction.
The biological function of proteins is critically dependent on dynamics inherent to the native struct
Time-resolved x-ray solution scattering identifies cooperative structural dynamics in the adenylate kinase enzymatic reaction.
The biological function of proteins is critically dependent on dynamics inherent to the native struct
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::97ba9bbce39e9258c0eb261b4a886664
https://epn-library.esrf.fr/flora/jsp/index_view_direct_anonymous.jsp?record=doc:PUB_ESRF:58892
https://epn-library.esrf.fr/flora/jsp/index_view_direct_anonymous.jsp?record=doc:PUB_ESRF:58892