Pages that link to "Q39953808"

The following pages link to Regulation of the Escherichia coli secA gene by protein secretion defects: analysis of secA, secB, secD, and secY mutants (Q39953808):

Displaying 31 items.

• The sec and prl genes of Escherichia coli (Q28251404) ‎ (← links)
• Nucleotide sequence of the secA gene and secA(Ts) mutations preventing protein export in Escherichia coli. (Q30401105) ‎ (← links)
• Revised translation start site for secM defines an atypical signal peptide that regulates Escherichia coli secA expression (Q33787527) ‎ (← links)
• SecA: the ubiquitous component of preprotein translocase in prokaryotes. (Q33807313) ‎ (← links)
• SecM facilitates translocase function of SecA by localizing its biosynthesis (Q33848928) ‎ (← links)
• Azide-resistant mutants of Escherichia coli alter the SecA protein, an azide-sensitive component of the protein export machinery (Q33858303) ‎ (← links)
• Carbon source-dependent synthesis of SecB, a cytosolic chaperone involved in protein translocation across Escherichia coli membranes (Q35619782) ‎ (← links)
• One of three transmembrane stretches is sufficient for the functioning of the SecE protein, a membrane component of the E. coli secretion machinery. (Q35926815) ‎ (← links)
• A mutation of Escherichia coli SecA protein that partially compensates for the absence of SecB. (Q36098219) ‎ (← links)
• Genetic and molecular characterization of the Escherichia coli secD operon and its products (Q36105112) ‎ (← links)
• In vivo studies of the role of SecA during protein export in Escherichia coli (Q36108969) ‎ (← links)
• Isolation and analysis of dominant secA mutations in Escherichia coli (Q36125831) ‎ (← links)
• Regulation of Escherichia coli secA mRNA translation by a secretion-responsive element. (Q36163727) ‎ (← links)
• The first gene in the Escherichia coli secA operon, gene X, encodes a nonessential secretory protein (Q36165846) ‎ (← links)
• Novel secA alleles improve export of maltose-binding protein synthesized with a defective signal peptide (Q36173206) ‎ (← links)
• SecA protein autogenously represses its own translation during normal protein secretion in Escherichia coli (Q36173585) ‎ (← links)
• Insertion of proteins into bacterial membranes: mechanism, characteristics, and comparisons with the eucaryotic process (Q37055727) ‎ (← links)
• Cryo-electron microscopic structure of SecA protein bound to the 70S ribosome (Q37622672) ‎ (← links)
• Reconstitution of protein translocation from detergent-solubilized Escherichia coli inverted vesicles: PrlA protein-deficient vesicles efficiently translocate precursor proteins (Q37714073) ‎ (← links)
• SecA protein: autoregulated initiator of secretory precursor protein translocation across the E. coli plasma membrane (Q37890386) ‎ (← links)
• Protein translocation in vitro: biochemical characterization of genetically defined translocation components (Q37890390) ‎ (← links)
• Suppression of signal sequence defects and azide resistance in Escherichia coli commonly result from the same mutations in secA (Q39837250) ‎ (← links)
• Influence of impaired chaperone or secretion function on SecB production in Escherichia coli (Q39843192) ‎ (← links)
• Escherichia coli preprotein translocase (Q41239605) ‎ (← links)
• Escherichia coli SecA helicase activity is not required in vivo for efficient protein translocation or autogenous regulation (Q43690465) ‎ (← links)
• The Sec System: Protein Export in Escherichia coli (Q47374398) ‎ (← links)
• SecA promotes preprotein translocation by undergoing ATP-driven cycles of membrane insertion and deinsertion. (Q52513940) ‎ (← links)
• Both transmembrane domains of SecG contribute to signal sequence recognition by the Escherichia coli protein export machinery. (Q52541487) ‎ (← links)
• SecE-depleted membranes of Escherichia coli are active. SecE is not obligatorily required for the in vitro translocation of certain protein precursors. (Q54565652) ‎ (← links)
• A significant fraction of functional SecA is permanently embedded in the membrane. SecA cycling on and off the membrane is not essential during protein translocation. (Q54576716) ‎ (← links)
• Elevated cytosolic concentrations of SecA compensate for a protein translocation defect in Escherichia coli cells with reduced levels of negatively charged phospholipids (Q67540651) ‎ (← links)