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Altering the interaction between s70 and RNA polymerase generates complexes with distinct transcription-elongation properties
Online Contents | 2005|Contributors: Lu, Chi Zen -
PROTEIN CHEMISTRY AND STRUCTURE - Structural features required for the interaction of the Hsp70 molecular chaperone DnaK with its cochaperone DnaJ
Online Contents | 1999|Contributors: Lu, Chi Zen -
Lack of a Robust Unfoldase Activity Confers a Unique Level of Substrate Specificity to the Universal AAA Protease FtsH
Online Contents | 2003|Contributors: Lu, Chi Zen -
Analysis of three DnaK mutant proteins suggests that progression through the ATPase cycle requires conformational changes
Online Contents | 1995|Contributors: Lu, Chi Zen -
Biological Sciences - BIOCHEMISTRY - Interaction of the Hsp70 molecular chaperone, DnaK, with its cochaperone DnaJ
Online Contents | 1998|Contributors: Lu, Chi Zen -
A Coiled-Coil from the RNA Polymerase b' Subunit Allosterically Induces Selective Nontemplate Strand Binding by s70
Online Contents | 2001|Contributors: Lu, Chi Zen -
Binding of the Initiation Factor s70 to Core RNA Polymerase Is a Multistep Process
Online Contents | 2001|Contributors: Lu, Chi Zen
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