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Gierasch, Lila
One or more keywords matched the following items that are connected to Gierasch, Lila
Item TypeName
Academic Article Caught in the act: how ATP binding triggers cooperative conformational changes in a molecular machine.
Academic Article Nucleotide exchange from the high-affinity ATP-binding site in SecA is the rate-limiting step in the ATPase cycle of the soluble enzyme and occurs through a specialized conformational state.
Academic Article Direct comparison of a stable isolated Hsp70 substrate-binding domain in the empty and substrate-bound states.
Academic Article Structural insights into substrate binding by the molecular chaperone DnaK.
Academic Article Functional signal peptides bind a soluble N-terminal fragment of SecA and inhibit its ATPase activity.
Academic Article The chaperonin GroEL binds a polypeptide in an alpha-helical conformation.
Academic Article Allosteric signal transmission in the nucleotide-binding domain of 70-kDa heat shock protein (Hsp70) molecular chaperones.
Academic Article A new twist for an Hsp70 chaperone.
Academic Article Hsp70 chaperone ligands control domain association via an allosteric mechanism mediated by the interdomain linker.
Academic Article Electrophysiological studies in Xenopus oocytes for the opening of Escherichia coli SecA-dependent protein-conducting channels.
Academic Article Using a low denaturant model to explore the conformational features of translocation-active SecA.
Academic Article An interdomain energetic tug-of-war creates the allosterically active state in Hsp70 molecular chaperones.
Academic Article Molecular chaperones. Panning for chaperone-binding peptides.
Concept Adenosine Triphosphate
Academic Article Challenges and dreams: physics of weak interactions essential to life.
Academic Article Substrate-binding domain conformational dynamics mediate Hsp70 allostery.
Academic Article New insights into the structure and function of the complex?between the Escherichia coli Hsp70, DnaK, and its nucleotide-exchange factor, GrpE.
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  • Adenosine Triphosphate