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Sevil Weinkauf

Showing results (21-30 of 30) with videos related to

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Proceedings of the National Academy of Sciences of the United States of America|December 7, 2011
Multiple molecular architectures of the eye lens chaperone αB-crystallin elucidated by a triple hybrid approachNathalie Braun, Martin Zacharias, Jirka Peschek, et al.
Nature Communications|November 19, 2021
Phosphorylation activates the yeast small heat shock protein Hsp26 by weakening domain contacts in the oligomer ensembleMoritz Mühlhofer, Carsten Peters, Thomas Kriehuber, et al.
Nature Structural & Molecular Biology|October 13, 2015
The chaperone αB-crystallin uses different interfaces to capture an amorphous and an amyloid clientAndi Mainz, Jirka Peschek, Maria Stavropoulou, et al.
Molecular Cell|May 27, 2015
The Chaperone Activity of the Developmental Small Heat Shock Protein Sip1 Is Regulated by pH-Dependent Conformational ChangesTilly Fleckenstein, Andreas Kastenmüller, Martin Lorenz Stein, et al.
The Journal of Biological Chemistry|November 28, 2022
The permanently chaperone-active small heat shock protein Hsp17 from Caenorhabditis elegans exhibits topological separation of its N-terminal regionsAnnika Strauch, Benjamin Rossa, Fabian Köhler, et al.
Journal of Molecular Biology|October 26, 2005
The oligomeric distribution of SecYEG is altered by SecA and translocation ligandsJohannes Scheuring, Nathalie Braun, Lars Nothdurft, et al.
Molecular Cell|August 28, 2010
Hsp12 is an intrinsically unstructured stress protein that folds upon membrane association and modulates membrane functionSylvia Welker, Birgit Rudolph, Elke Frenzel, et al.
Nature Structural & Molecular Biology|December 4, 2019
The structure and oxidation of the eye lens chaperone αA-crystallinChristoph J O Kaiser, Carsten Peters, Philipp W N Schmid, et al.
Nature Structural & Molecular Biology|January 12, 2021
Imbalances in the eye lens proteome are linked to cataract formationPhilipp W N Schmid, Nicole C H Lim, Carsten Peters, et al.
Molecular and Cellular Biology|April 2, 2014
Leucine-rich repeat kinase 2 binds to neuronal vesicles through protein interactions mediated by its C-terminal WD40 domainGiovanni Piccoli, Franco Onofri, Maria Daniela Cirnaru, et al.
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Showing results (21-30 of 30) with videos related to

Sort By:
Pageof 3
You have reached the last page of results.This site can display upto 30 results.
Proceedings of the National Academy of Sciences of the United States of America|December 7, 2011
Multiple molecular architectures of the eye lens chaperone αB-crystallin elucidated by a triple hybrid approachNathalie Braun, Martin Zacharias, Jirka Peschek, et al.
Nature Communications|November 19, 2021
Phosphorylation activates the yeast small heat shock protein Hsp26 by weakening domain contacts in the oligomer ensembleMoritz Mühlhofer, Carsten Peters, Thomas Kriehuber, et al.
Nature Structural & Molecular Biology|October 13, 2015
The chaperone αB-crystallin uses different interfaces to capture an amorphous and an amyloid clientAndi Mainz, Jirka Peschek, Maria Stavropoulou, et al.
Molecular Cell|May 27, 2015
The Chaperone Activity of the Developmental Small Heat Shock Protein Sip1 Is Regulated by pH-Dependent Conformational ChangesTilly Fleckenstein, Andreas Kastenmüller, Martin Lorenz Stein, et al.
The Journal of Biological Chemistry|November 28, 2022
The permanently chaperone-active small heat shock protein Hsp17 from Caenorhabditis elegans exhibits topological separation of its N-terminal regionsAnnika Strauch, Benjamin Rossa, Fabian Köhler, et al.
Journal of Molecular Biology|October 26, 2005
The oligomeric distribution of SecYEG is altered by SecA and translocation ligandsJohannes Scheuring, Nathalie Braun, Lars Nothdurft, et al.
Molecular Cell|August 28, 2010
Hsp12 is an intrinsically unstructured stress protein that folds upon membrane association and modulates membrane functionSylvia Welker, Birgit Rudolph, Elke Frenzel, et al.
Nature Structural & Molecular Biology|December 4, 2019
The structure and oxidation of the eye lens chaperone αA-crystallinChristoph J O Kaiser, Carsten Peters, Philipp W N Schmid, et al.
Nature Structural & Molecular Biology|January 12, 2021
Imbalances in the eye lens proteome are linked to cataract formationPhilipp W N Schmid, Nicole C H Lim, Carsten Peters, et al.
Molecular and Cellular Biology|April 2, 2014
Leucine-rich repeat kinase 2 binds to neuronal vesicles through protein interactions mediated by its C-terminal WD40 domainGiovanni Piccoli, Franco Onofri, Maria Daniela Cirnaru, et al.
Pageof 3