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International Journal of Biological Macromolecules
|
April 22, 2006
Matrix-assisted refolding of oligomeric small heat-shock protein Hsp26
Titus M Franzmann
The Journal of Biological Chemistry
|
June 21, 2018
Prion-like low-complexity sequences: Key regulators of protein solubility and phase behavior
Titus M Franzmann, Simon Alberti
Cold Spring Harbor Perspectives in Biology
|
January 9, 2019
Protein Phase Separation as a Stress Survival Strategy
Titus M Franzmann, Simon Alberti
The Journal of Biological Chemistry
|
April 2, 2011
Regulatory circuits of the AAA+ disaggregase Hsp104
Titus M Franzmann, Anna Czekalla, Stefan G Walter
Molecular Cell
|
February 5, 2008
Activation of the chaperone Hsp26 is controlled by the rearrangement of its thermosensor domain
Titus M Franzmann, Petra Menhorn, Stefan Walter, et al.
Journal of Molecular Biology
|
June 22, 2005
The activation mechanism of Hsp26 does not require dissociation of the oligomer
Titus M Franzmann, Martin Wühr, Klaus Richter, et al.
Biochemistry
|
April 1, 2011
The crystal structure of Escherichia coli group 4 capsule protein GfcC reveals a domain organization resembling that of Wza
Karthik Sathiyamoorthy, Erez Mills, Titus M Franzmann, et al.
Journal of Molecular Biology
|
February 23, 2010
Regions outside the alpha-crystallin domain of the small heat shock protein Hsp26 are required for its dimerization
Jin Chen, Matthias J Feige, Titus M Franzmann, et al.
Journal of Molecular Biology
|
July 3, 2010
Structural and mechanical hierarchies in the alpha-crystallin domain dimer of the hyperthermophilic small heat shock protein Hsp16.5
Morten Bertz, Jin Chen, Matthias J Feige, et al.
Proceedings of the National Academy of Sciences of the United States of America
|
January 19, 2010
Protein refolding by pH-triggered chaperone binding and release
Timothy L Tapley, Titus M Franzmann, Sumita Chakraborty, et al.
Page
of 5
Search research articles
Search
Showing results (1-10 of 44) with videos related to
Sort By:
Page
of 5
International Journal of Biological Macromolecules
|
April 22, 2006
Matrix-assisted refolding of oligomeric small heat-shock protein Hsp26
Titus M Franzmann
The Journal of Biological Chemistry
|
June 21, 2018
Prion-like low-complexity sequences: Key regulators of protein solubility and phase behavior
Titus M Franzmann, Simon Alberti
Cold Spring Harbor Perspectives in Biology
|
January 9, 2019
Protein Phase Separation as a Stress Survival Strategy
Titus M Franzmann, Simon Alberti
The Journal of Biological Chemistry
|
April 2, 2011
Regulatory circuits of the AAA+ disaggregase Hsp104
Titus M Franzmann, Anna Czekalla, Stefan G Walter
Molecular Cell
|
February 5, 2008
Activation of the chaperone Hsp26 is controlled by the rearrangement of its thermosensor domain
Titus M Franzmann, Petra Menhorn, Stefan Walter, et al.
Journal of Molecular Biology
|
June 22, 2005
The activation mechanism of Hsp26 does not require dissociation of the oligomer
Titus M Franzmann, Martin Wühr, Klaus Richter, et al.
Biochemistry
|
April 1, 2011
The crystal structure of Escherichia coli group 4 capsule protein GfcC reveals a domain organization resembling that of Wza
Karthik Sathiyamoorthy, Erez Mills, Titus M Franzmann, et al.
Journal of Molecular Biology
|
February 23, 2010
Regions outside the alpha-crystallin domain of the small heat shock protein Hsp26 are required for its dimerization
Jin Chen, Matthias J Feige, Titus M Franzmann, et al.
Journal of Molecular Biology
|
July 3, 2010
Structural and mechanical hierarchies in the alpha-crystallin domain dimer of the hyperthermophilic small heat shock protein Hsp16.5
Morten Bertz, Jin Chen, Matthias J Feige, et al.
Proceedings of the National Academy of Sciences of the United States of America
|
January 19, 2010
Protein refolding by pH-triggered chaperone binding and release
Timothy L Tapley, Titus M Franzmann, Sumita Chakraborty, et al.
Page
of 5