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L L Randall

Showing results (31-40 of 71) with videos related to

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Nature Structural Biology|December 2, 2000
The promiscuous and specific sides of SecBL L Randall, S J Hardy
The Journal of Biological Chemistry|November 20, 1997
Kinetic partitioning. Poising SecB to favor association with a rapidly folding ligandD L Diamond, L L Randall
Journal of Bacteriology|July 1, 1994
In vivo studies of the role of SecA during protein export in Escherichia coliS Y Chun, L L Randall
Antonie Van Leeuwenhoek|February 1, 1992
Protein folding in protein exportS J Hardy, L L Randall
Journal of Bacteriology|November 1, 1985
Export of alpha-amylase by Bacillus amyloliquefaciens requires proton motive forceE M Murén, L L Randall
Science (New York, N.Y.)|March 3, 1989
Unity in function in the absence of consensus in sequence: role of leader peptides in exportL L Randall, S J Hardy
Molecular & General Genetics : MGG|January 1, 1972
Identification of three 30S proteins contributing to the ribosomal A siteL L Randall-Hazelbauer, C G Kuland
Cellular and Molecular Life Sciences : CMLS|December 12, 2002
SecB, one small chaperone in the complex milieu of the cellL L Randall, S J S Hardy
Journal of Protein Chemistry|October 1, 1995
Chaperone SecB: conformational changes demonstrated by circular dichroismG D Fasman, K Park, 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
Pageof 8

Showing results (31-40 of 71) with videos related to

Sort By:
Pageof 8
Nature Structural Biology|December 2, 2000
The promiscuous and specific sides of SecBL L Randall, S J Hardy
The Journal of Biological Chemistry|November 20, 1997
Kinetic partitioning. Poising SecB to favor association with a rapidly folding ligandD L Diamond, L L Randall
Journal of Bacteriology|July 1, 1994
In vivo studies of the role of SecA during protein export in Escherichia coliS Y Chun, L L Randall
Antonie Van Leeuwenhoek|February 1, 1992
Protein folding in protein exportS J Hardy, L L Randall
Journal of Bacteriology|November 1, 1985
Export of alpha-amylase by Bacillus amyloliquefaciens requires proton motive forceE M Murén, L L Randall
Science (New York, N.Y.)|March 3, 1989
Unity in function in the absence of consensus in sequence: role of leader peptides in exportL L Randall, S J Hardy
Molecular & General Genetics : MGG|January 1, 1972
Identification of three 30S proteins contributing to the ribosomal A siteL L Randall-Hazelbauer, C G Kuland
Cellular and Molecular Life Sciences : CMLS|December 12, 2002
SecB, one small chaperone in the complex milieu of the cellL L Randall, S J S Hardy
Journal of Protein Chemistry|October 1, 1995
Chaperone SecB: conformational changes demonstrated by circular dichroismG D Fasman, K Park, 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
Pageof 8