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Rebecca B Berlow

Showing results (1-10 of 24) with videos related to

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Biophysical Journal|April 12, 2018
A Dual Regulatory Role for the Disordered C-Terminus of Protein Kinase CαRebecca B Berlow
Nature|February 26, 2020
Tight complexes from disordered proteinsRebecca B Berlow, Peter E Wright
Nature|March 2, 2018
Tight complexes from disordered proteinsRebecca B Berlow, Peter E Wright
Biochemistry|April 8, 2009
Role of loop-loop interactions in coordinating motions and enzymatic function in triosephosphate isomeraseYan Wang, Rebecca B Berlow, J Patrick Loria
FEBS Letters|June 16, 2015
Functional advantages of dynamic protein disorderRebecca B Berlow, H Jane Dyson, Peter E Wright
Accounts of Chemical Research|February 20, 2008
Characterization of enzyme motions by solution NMR relaxation dispersionJ Patrick Loria, Rebecca B Berlow, Eric D Watt
Nature|March 9, 2017
Hypersensitive termination of the hypoxic response by a disordered protein switchRebecca B Berlow, H Jane Dyson, Peter E Wright
Biochemistry|April 26, 2007
Value of a hydrogen bond in triosephosphate isomerase loop motionRebecca B Berlow, Tatyana I Igumenova, J Patrick Loria
Proceedings of the National Academy of Sciences of the United States of America|January 11, 2022
Multivalency enables unidirectional switch-like competition between intrinsically disordered proteinsRebecca B Berlow, H Jane Dyson, Peter E Wright
Current Opinion in Structural Biology|December 14, 2023
Multivalency emerges as a common feature of intrinsically disordered protein interactionsEmily L Sipko, Garrett F Chappell, Rebecca B Berlow
Pageof 3

Showing results (1-10 of 24) with videos related to

Sort By:
Pageof 3
Biophysical Journal|April 12, 2018
A Dual Regulatory Role for the Disordered C-Terminus of Protein Kinase CαRebecca B Berlow
Nature|February 26, 2020
Tight complexes from disordered proteinsRebecca B Berlow, Peter E Wright
Nature|March 2, 2018
Tight complexes from disordered proteinsRebecca B Berlow, Peter E Wright
Biochemistry|April 8, 2009
Role of loop-loop interactions in coordinating motions and enzymatic function in triosephosphate isomeraseYan Wang, Rebecca B Berlow, J Patrick Loria
FEBS Letters|June 16, 2015
Functional advantages of dynamic protein disorderRebecca B Berlow, H Jane Dyson, Peter E Wright
Accounts of Chemical Research|February 20, 2008
Characterization of enzyme motions by solution NMR relaxation dispersionJ Patrick Loria, Rebecca B Berlow, Eric D Watt
Nature|March 9, 2017
Hypersensitive termination of the hypoxic response by a disordered protein switchRebecca B Berlow, H Jane Dyson, Peter E Wright
Biochemistry|April 26, 2007
Value of a hydrogen bond in triosephosphate isomerase loop motionRebecca B Berlow, Tatyana I Igumenova, J Patrick Loria
Proceedings of the National Academy of Sciences of the United States of America|January 11, 2022
Multivalency enables unidirectional switch-like competition between intrinsically disordered proteinsRebecca B Berlow, H Jane Dyson, Peter E Wright
Current Opinion in Structural Biology|December 14, 2023
Multivalency emerges as a common feature of intrinsically disordered protein interactionsEmily L Sipko, Garrett F Chappell, Rebecca B Berlow
Pageof 3