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Autor:
Rüdiger, S.G.D., Ferrari, L., Asea, Alexzander A. A., Kaur, Punit, Sub Cellular Protein Chemistry, Cellular Protein Chemistry
Publikováno v:
Heat Shock Protein 90 in Human Diseases and Disorders, 19(1), 473. Springer Cham
Heat Shock Proteins ISBN: 9783030231576
Heat Shock Proteins ISBN: 9783030231576
The molecular chaperone Hsp90 is at the heart of protein homeostasis control. A wide range of pathologies disturbs protein homeostasis, thus placing Hsp90 at the crossroads of many diseases. Here, we evaluate the impact of recent progress in understa
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f3cd1a0f700d7017f92cde907e8a48d9
https://dspace.library.uu.nl/handle/1874/388310
https://dspace.library.uu.nl/handle/1874/388310
Autor:
Morán Luengo, T., Kityk, R., Mayer, Matthias, Rüdiger, S.G.D., Cellular Protein Chemistry, Sub Cellular Protein Chemistry
Publikováno v:
Molecular Cell, 70(3), 545. Cell Press
Protein folding in the cell requires ATP-driven chaperone machines such as the conserved Hsp70 and Hsp90. It is enigmatic how these machines fold proteins. Here, we show that Hsp90 takes a key role in protein folding by breaking an Hsp70-inflicted fo
The molecular chaperone Hsp90 plays a crucial role in folding and maturation of regulatory proteins. Key aspects of Hsp90's molecular mechanism and its adenosine-5'-triphosphate (ATP)-controlled active cycle remain elusive. In particular the role of
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=od_______101::13d3ecf9d0da4af95145fc5a0ddd6772
https://dspace.library.uu.nl/handle/1874/235187
https://dspace.library.uu.nl/handle/1874/235187
Autor:
Karagöz, G.E., Sinnige, T, Hsieh, O., Rüdiger, S.G.D., Cellular Protein Chemistry, NMR Spectroscopy, Sub NMR Spectroscopy, Sub Cellular Protein Chemistry
Publikováno v:
Protein Engineering, Design & Selection, 24(6), 495. NLM (Medline)
Expressed protein ligation (EPL) is a protein engineering tool for post-translational ligation of protein or peptide fragments. This technique allows modification of specific parts of proteins, opening possibilities for incorporating probes for bioph
Autor:
Karagöz, G.E., dos santos Duarte, A.M., Ippel, J.H., Uetrecht, C., Sinnige, T., van Rosmalen, M., Hausmann, J., Heck, A.J.R., Boelens, R., Rüdiger, S.G.D., Biomolecular Mass Spectrometry and Proteomics, Cellular Protein Chemistry, NMR Spectroscopy, Sub Cellular Protein Chemistry, Sub NMR Spectroscopy, Sub Biomol.Mass Spect. and Proteomics, Dep Scheikunde, Sub Biomol.Mass Spectrometry & Proteom.
Publikováno v:
Proceedings of the National Academy of Sciences of the United States of America, 108(2), 580. National Academy of Sciences
The molecular chaperone Hsp90 is a protein folding machine that is conserved from bacteria to man. Human, cytosolic Hsp90 is dedicated to folding of chiefly signal transduction components. The chaperoning mechanism of Hsp90 is controlled by ATP and v
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f2cd8fda8e33b0d9cf28a61e16da1074
https://dspace.library.uu.nl/handle/1874/200583
https://dspace.library.uu.nl/handle/1874/200583
Autor:
Rodriguez, Fernanda, Arsène-Ploetze, F., Rist, W., Rüdiger, S.G.D., Schneider-Mergener, J., Mayer, M.P., Bukau, B., Eiwitvouwing en cellulaire factoren, Dep Scheikunde
Publikováno v:
Molecular Cell, 32, 347. Cell Press
Central to the transcriptional control of the Escherichia coli heat shock regulon is the stress-dependent inhibition of the s32 subunit of RNA polymerase by reversible association with the DnaK chaperone, mediated by the DnaJ cochaperone. Here we ide
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=narcis______::027dc5b10c834565bc640e3677f075ad
https://dspace.library.uu.nl/handle/1874/33029
https://dspace.library.uu.nl/handle/1874/33029
Autor:
Rotem, S., Katz, C., Benyamini, H., Lebendiker, M., Veprintsev, D., Rüdiger, S.G.D., Danieli, T., Friedler, A., Eiwitvouwing en cellulaire factoren, Dep Scheikunde
Publikováno v:
Journal of Biological Chemistry, 283(27), 18990. American Society for Biochemistry and Molecular Biology Inc.
ASPP2 is a pro-apoptotic protein that stimulates the p53-mediated apoptotic response. The C terminus of ASPP2 contains ankyrin (Ank) repeats and a SH3 domain, which mediate its interactions with numerous partner proteins such as p53,NF B, and Bcl-2.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=narcis______::1140eb26d44a723698ce6bbfaf7e9a85
https://dspace.library.uu.nl/handle/1874/33026
https://dspace.library.uu.nl/handle/1874/33026
Autor:
Katz, C., Benyamini, H., Rotem, S., Lebendiker, M., Danieli, T., Iosub, A., Refaely, H., Dines, M., Bronner, V., Bravman, T., Shalev, D.E., Rüdiger, S.G.D., Friedler, A., Eiwitvouwing en cellulaire factoren, Dep Scheikunde
Publikováno v:
Proceedings of the National Academy of Sciences of the United States of America, 105(34), 12277. National Academy of Sciences
We have characterized the molecular basis of the interaction between ASPP2 and Bcl-2, which are key proteins in the apoptotic pathway. The C-terminal ankyrin repeats and SH3 domain of ASPP2 (ASPP2Ank-SH3) mediate its interactions with the antiapoptot
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=narcis______::e0c5e02972aa19c6f0fb71eada917188
https://dspace.library.uu.nl/handle/1874/33027
https://dspace.library.uu.nl/handle/1874/33027
The amount of folded functional protein in a cell is controlled by a number of factors, including the relative rates of its biosynthetic and specific degradation processes, and its intrinsic thermodynamic stability. Mutationinduced loss of stability
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=od_______101::4568e2e06d1da330bef1ffd24fcb06e9
https://dspace.library.uu.nl/handle/1874/26804
https://dspace.library.uu.nl/handle/1874/26804