Zobrazeno 1 - 9
of 9
pro vyhledávání: '"Andreas C. Woerner"'
Autor:
Christian Behl, Christian Haass, Petra Goldmann, Nikolas Furthmann, Jens Meschede, Konstanze F. Winklhofer, Alina Blusch, Dietrich Trümbach, Kohji Mori, Mark S. Hipp, Cathrin Schnack, Wolfgang Wurst, Verian Bader, Jörg Tatzelt, Joseph Longworth, Cathrin Showkat, Elisabeth Petrasch-Parwez, Maria Patra, Carsten Saft, Thomas Arzberger, Dominik A. Sehr, Albrecht M. Clement, Lena A. Berlemann, Lena Angersbach, F. Ulrich Hartl, Ana Sánchez-Vicente, Andreas C. Woerner, Gisa Ellrichmann, Eva M van Well, Ralf Gold, Gunnar Dittmar
Publikováno v:
The EMBO journal 38(9), e100730 (2019). doi:10.15252/embj.2018100730
Neurodegenerative diseases are characterized by the accumulation of misfolded proteins in the brain. Insights into protein quality control mechanisms to prevent neuronal dysfunction and cell death are crucial in developing causal therapies. Here, we
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9026497cb3304040f80c960a7bcdd512
https://pub.dzne.de/record/140707
https://pub.dzne.de/record/140707
Autor:
Konstanze F. Winklhofer, Frédéric Frottin, Andreas C. Woerner, Maria Patra, Daniel Hornburg, Mark S. Hipp, F. Ulrich Hartl, Felix Meissner, Matthias Mann, Li Rebekah Feng, Jörg Tatzelt
Publikováno v:
Science. 351:173-176
Location, location, location Aggregates of certain disease-associated proteins are involved in neurodegeneration. Woerner et al. now show that the exact location of these aggregates in the cell may be the key to their pathology (see the Perspective b
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::de10e28c9395f63484e6e445744e4017
https://doi.org/10.1126/science.aad2033
https://doi.org/10.1126/science.aad2033
Autor:
F. Ulrich Hartl, Andreas C. Woerner, Gerd Multhaup, Anja Harmeier, Konstanze F. Winklhofer, Susan Lindquist, Ulrike K. Resenberger, Veronika Müller, Rajaraman Krishnan, R. Martin Vabulas, Jörg Tatzelt, Hans A. Kretzschmar, Jessica L. Goodman
Publikováno v:
The EMBO Journal. 30:2057-2070
Formation of aberrant protein conformers is a common pathological denominator of different neurodegenerative disorders, such as Alzheimer's disease or prion diseases. Moreover, increasing evidence indicates that soluble oligomers are associated with
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::fc02148aedfb9aea113517b554b6fc6d
https://doi.org/10.1038/emboj.2011.86
https://doi.org/10.1038/emboj.2011.86
Autor:
Clemens Glaubitz, Nicole Pfleger, Josef Wachtveitl, Thomas Köhler, Andreas C. Woerner, Sarah-Anna Fiedler, Mirka-Kristin Verhoefen, Franziska Hempelmann, Soraya Hölper
Publikováno v:
Journal of the American Chemical Society. 133:4645-4654
The proteorhodopsin (PR) family found in bacteria near the ocean's surface consists of hundreds of PR variants color-tuned to their environment. PR contains a highly conserved single histidine at position 75, which is not found in most other retinal
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::90fa522835c6cbf764b043979c646e70
https://doi.org/10.1021/ja111116a
https://doi.org/10.1021/ja111116a
Autor:
Sonya M. Schermann, Manajit Hayer-Hartl, F. Ulrich Hartl, Michael H. Hecht, Heidi Olzscha, Michele Vendruscolo, R. Martin Vabulas, Stefan Pinkert, Andreas C. Woerner, Gian Gaetano Tartaglia
Publikováno v:
Cell; Vol 144
Cell
Cell
SummaryProtein aggregation is linked with neurodegeneration and numerous other diseases by mechanisms that are not well understood. Here, we have analyzed the gain-of-function toxicity of artificial β sheet proteins that were designed to form amyloi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::af5590885129943d31641581cb7807b2
Publikováno v:
Journal of Biomolecular NMR. 40:15-21
The proteorhodopsin family consists of hundreds of homologous retinal containing membrane proteins found in bacteria in the photic zone of the oceans. They are colour tuned to their environment and act as light-driven proton pumps with a potential en
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::38fced6fb08a849c5d497f619305077c
https://doi.org/10.1007/s10858-007-9203-5
https://doi.org/10.1007/s10858-007-9203-5
Autor:
Ulrike K, Resenberger, Anja, Harmeier, Andreas C, Woerner, Jessica L, Goodman, Veronika, Müller, Rajaraman, Krishnan, R Martin, Vabulas, Hans A, Kretzschmar, Susan, Lindquist, F Ulrich, Hartl, Gerd, Multhaup, Konstanze F, Winklhofer, Jörg, Tatzelt
Publikováno v:
The EMBO journal. 30(10)
Formation of aberrant protein conformers is a common pathological denominator of different neurodegenerative disorders, such as Alzheimer's disease or prion diseases. Moreover, increasing evidence indicates that soluble oligomers are associated with
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::aad586a3b872c41147c0d107c7bc259b
https://pubmed.ncbi.nlm.nih.gov/21593729
https://pubmed.ncbi.nlm.nih.gov/21593729
Autor:
Clemens Glaubitz, Ernst Bamberg, Andreas C. Woerner, Éva Lörinczi, Josef Wachtveitl, Martin Engelhard, Mirka-Kristin Verhoefen, Thomas Friedrich
Publikováno v:
Journal of molecular biology. 393(2)
Proteorhodopsin (PR), a light-driven proton pump from marine proteobacteria, exhibits photocycle characteristics similar to bacteriorhodopsin (BR) at neutral pH, including an M-like photointermediate. However, at acidic pH, spectroscopic evidence for
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d91168ab44943bd893784a4e58911f80
https://pubmed.ncbi.nlm.nih.gov/19631661
https://pubmed.ncbi.nlm.nih.gov/19631661
Publikováno v:
Photochemistry and photobiology. 83(2)
The first steps of the photocycle of the D97N mutant of proteorhodopsin (PR) have been investigated by means of ultrafast transient absorption spectroscopy. A comparison with the primary dynamics of native PR and D85N mutant of bacteriorhodopsin is g
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::10383b8ec26a080b5c94422e52237c5e
https://pubmed.ncbi.nlm.nih.gov/16808594
https://pubmed.ncbi.nlm.nih.gov/16808594