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T B Topping

Showing results (1-10 of 13) with videos related to

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Protein Science : a Publication of the Protein Society|May 1, 1994
Determination of the binding frame within a physiological ligand for the chaperone SecBT B Topping, L L Randall
The Journal of Biological Chemistry|August 1, 1997
Chaperone SecB from Escherichia coli mediates kinetic partitioning via a dynamic equilibrium with its ligandsT B Topping, L L Randall
Proceedings of the National Academy of Sciences of the United States of America|December 1, 1989
Physiological role during export for the retardation of folding by the leader peptide of maltose-binding proteinG Liu, T B Topping, L L Randall
Science (New York, N.Y.)|May 18, 1990
No specific recognition of leader peptide by SecB, a chaperone involved in protein exportL L Randall, T B Topping, S J Hardy
Protein Science : a Publication of the Protein Society|May 30, 1998
Calorimetric analyses of the interaction between SecB and its ligandsL L Randall, T B Topping, D Suciu, et al.
The Journal of Biological Chemistry|October 15, 1988
Retardation of folding as a possible means of suppression of a mutation in the leader sequence of an exported proteinG P Liu, T B Topping, W H Cover, et al.
Science (New York, N.Y.)|February 26, 1988
Modulation of folding pathways of exported proteins by the leader sequenceS Park, G Liu, T B Topping, et al.
The Journal of Biological Chemistry|June 26, 1999
Mutational alterations in the homotetrameric chaperone SecB that implicate the structure as dimer of dimersE M Murén, D Suciu, T B Topping, et al.
The Journal of Biological Chemistry|December 9, 2000
Direct demonstration that homotetrameric chaperone SecB undergoes a dynamic dimer-tetramer equilibriumT B Topping, R L Woodbury, D L Diamond, et al.
Methods in Enzymology|April 16, 1998
SecB: a chaperone from Escherichia coliL L Randall, T B Topping, V F Smith, et al.
Pageof 2

Showing results (1-10 of 13) with videos related to

Sort By:
Pageof 2
Protein Science : a Publication of the Protein Society|May 1, 1994
Determination of the binding frame within a physiological ligand for the chaperone SecBT B Topping, L L Randall
The Journal of Biological Chemistry|August 1, 1997
Chaperone SecB from Escherichia coli mediates kinetic partitioning via a dynamic equilibrium with its ligandsT B Topping, L L Randall
Proceedings of the National Academy of Sciences of the United States of America|December 1, 1989
Physiological role during export for the retardation of folding by the leader peptide of maltose-binding proteinG Liu, T B Topping, L L Randall
Science (New York, N.Y.)|May 18, 1990
No specific recognition of leader peptide by SecB, a chaperone involved in protein exportL L Randall, T B Topping, S J Hardy
Protein Science : a Publication of the Protein Society|May 30, 1998
Calorimetric analyses of the interaction between SecB and its ligandsL L Randall, T B Topping, D Suciu, et al.
The Journal of Biological Chemistry|October 15, 1988
Retardation of folding as a possible means of suppression of a mutation in the leader sequence of an exported proteinG P Liu, T B Topping, W H Cover, et al.
Science (New York, N.Y.)|February 26, 1988
Modulation of folding pathways of exported proteins by the leader sequenceS Park, G Liu, T B Topping, et al.
The Journal of Biological Chemistry|June 26, 1999
Mutational alterations in the homotetrameric chaperone SecB that implicate the structure as dimer of dimersE M Murén, D Suciu, T B Topping, et al.
The Journal of Biological Chemistry|December 9, 2000
Direct demonstration that homotetrameric chaperone SecB undergoes a dynamic dimer-tetramer equilibriumT B Topping, R L Woodbury, D L Diamond, et al.
Methods in Enzymology|April 16, 1998
SecB: a chaperone from Escherichia coliL L Randall, T B Topping, V F Smith, et al.
Pageof 2