Pages that link to "Q54561671"
Jump to navigation
Jump to search
The following pages link to Chaperone SecB from Escherichia coli Mediates Kinetic Partitioning via a Dynamic Equilibrium with Its Ligands (Q54561671):
Displaying 22 items.
- Maltose/maltodextrin system of Escherichia coli: transport, metabolism, and regulation (Q28266679) (← links)
- SecA, the motor of the secretion machine, binds diverse partners on one interactive surface (Q30485740) (← links)
- Sites of interaction of a precursor polypeptide on the export chaperone SecB mapped by site-directed spin labeling (Q30496200) (← links)
- The Sec system (Q33538582) (← links)
- Protein targeting to the bacterial cytoplasmic membrane. (Q33538949) (← links)
- The SecB chaperone is involved in the secretion of the Serratia marcescens HasA protein through an ABC transporter. (Q33888292) (← links)
- Protein traffic in bacteria: multiple routes from the ribosome to and across the membrane (Q34070563) (← links)
- Structural characterization of the complex of SecB and metallothionein-labeled proOmpA by cryo-electron microscopy. (Q34442682) (← links)
- The structural view of bacterial translocation-specific chaperone SecB: implications for function (Q34455348) (← links)
- Effect of hsp70 chaperone on the folding and misfolding of polypeptides modeling an elongating protein chain (Q35039971) (← links)
- The interaction between the chaperone SecB and its ligands: evidence for multiple subsites for binding (Q36280717) (← links)
- Calorimetric analyses of the interaction between SecB and its ligands (Q36280993) (← links)
- The observation of chaperone-ligand noncovalent complexes with electrospray ionization mass spectrometry (Q36281007) (← links)
- Folded HasA inhibits its own secretion through its ABC exporter (Q39645637) (← links)
- Export chaperone SecB uses one surface of interaction for diverse unfolded polypeptide ligands (Q41866614) (← links)
- Maximal efficiency of coupling between ATP hydrolysis and translocation of polypeptides mediated by SecB requires two protomers of SecA (Q42078600) (← links)
- Antifolding activity of the SecB chaperone is essential for secretion of HasA, a quickly folding ABC pathway substrate (Q44493487) (← links)
- Direct detection of glucose by surface plasmon resonance with bacterial glucose/galactose-binding protein. (Q44717015) (← links)
- The Sec System: Protein Export in Escherichia coli (Q47374398) (← links)
- The superoxide dismutase SodA is targeted to the periplasm in a SecA-dependent manner by a novel mechanism. (Q53410084) (← links)
- SecA supports a constant rate of preprotein translocation. (Q54467339) (← links)
- Mutational alterations in the homotetrameric chaperone SecB that implicate the structure as dimer of dimers (Q77927053) (← links)