Pages that link to "Q63359903"

The following pages link to Preprotein transfer to the Escherichia coli translocase requires the co‐operative binding of SecB and the signal sequence to SecA (Q63359903):

Displaying 45 items.

• Signal peptide-dependent protein transport in Bacillus subtilis: a genome-based survey of the secretome (Q24548495) (← links)
• SecA, a remarkable nanomachine (Q24631210) (← links)
• Dynamic Organization of SecA and SecY Secretion Complexes in the B. subtilis Membrane (Q27337281) (← links)
• Structural determinants of SecB recognition by SecA in bacterial protein translocation (Q27642253) (← links)
• The Sec translocase (Q27691857) (← links)
• Biophysical characterization of the influence of salt on tetrameric SecB. (Q28367695) (← links)
• Phospholipids induce conformational changes of SecA to form membrane-specific domains: AFM structures and implication on protein-conducting channels (Q28535409) (← links)
• Insights into the structure and assembly of Escherichia coli outer membrane protein A (Q30155388) (← links)
• Substrate specificity of the SecB chaperone (Q30815173) (← links)
• Protein targeting to the bacterial cytoplasmic membrane. (Q33538949) (← links)
• Following the leader: bacterial protein export through the Sec pathway. (Q33702236) (← links)
• Bacterial protein translocase: a unique molecular machine with an army of substrates. (Q33957082) (← links)
• Overproduction of SecA suppresses the export defect caused by a mutation in the gene encoding the Escherichia coli export chaperone secB. (Q33991984) (← links)
• Sec-dependent protein export and the involvement of the molecular chaperone SecB. (Q34068950) (← links)
• Protein traffic in bacteria: multiple routes from the ribosome to and across the membrane (Q34070563) (← links)
• SecB is a bona fide generalized chaperone in Escherichia coli (Q34336036) (← links)
• Structural characterization of the complex of SecB and metallothionein-labeled proOmpA by cryo-electron microscopy. (Q34442682) (← links)
• Multitasking SecB chaperones in bacteria (Q34637739) (← links)
• SecB-like chaperone controls a toxin-antitoxin stress-responsive system in Mycobacterium tuberculosis (Q35003009) (← links)
• In Vitro Interaction of the Housekeeping SecA1 with the Accessory SecA2 Protein of Mycobacterium tuberculosis. (Q35654435) (← links)
• Functional implementation of the posttranslational SecB-SecA protein-targeting pathway in Bacillus subtilis (Q35688908) (← links)
• Emerging themes in SecA2-mediated protein export (Q36206572) (← links)
• Bacterial Sec protein transport is rate-limited by precursor length: a single turnover study (Q37369897) (← links)
• Biogenesis of bacterial inner-membrane proteins (Q37702858) (← links)
• Protein conducting channels-mechanisms, structures and applications (Q37976983) (← links)
• SecA Cotranslationally Interacts with Nascent Substrate Proteins In Vivo (Q38290386) (← links)
• The N terminus of the HasA protein and the SecB chaperone cooperate in the efficient targeting and secretion of HasA via the ATP-binding cassette transporter (Q38294961) (← links)
• The SecB chaperone is bifunctional in Serratia marcescens: SecB is involved in the Sec pathway and required for HasA secretion by the ABC transporter (Q39702705) (← links)
• Conformational dynamics of the plug domain of the SecYEG protein-conducting channel. (Q39935945) (← links)
• Signal Peptide Hydrophobicity Modulates Interaction with the Twin-Arginine Translocase (Q41205318) (← links)
• Defining the Escherichia coli SecA dimer interface residues through in vivo site-specific photo-cross-linking (Q41445854) (← links)
• Direct identification of the site of binding on the chaperone SecB for the amino terminus of the translocon motor SecA. (Q42739776) (← links)
• Functional and structural characterization of the minimal Sec translocase of the hyperthermophile Thermotoga maritima. (Q43017577) (← links)
• Sites of interaction between SecA and the chaperone SecB, two proteins involved in export (Q43095210) (← links)
• Kinetic analysis of the translocation of fluorescent precursor proteins into Escherichia coli membrane vesicles. (Q44133891) (← links)
• Two-stage binding of SecA to the bacterial translocon regulates ribosome-translocon interaction (Q44542398) (← links)
• SecA mediates cotranslational targeting and translocation of an inner membrane protein (Q46316930) (← links)
• The Sec System: Protein Export in Escherichia coli (Q47374398) (← links)
• Directed evolution of SecB chaperones toward toxin-antitoxin systems (Q47428505) (← links)
• The way is the goal: how SecA transports proteins across the cytoplasmic membrane in bacteria. (Q54201374) (← links)
• Allosteric communication between signal peptides and the SecA protein DEAD motor ATPase domain. (Q54551221) (← links)
• A molecular switch in SecA protein couples ATP hydrolysis to protein translocation (Q57976571) (← links)
• Sec Protein-Conducting Channel and SecA (Q63359819) (← links)
• Nucleotide binding activity of SecA homodimer is conformationally regulated by temperature and altered by prlD and azi mutations (Q73626344) (← links)
• Novel Sequence Feature of SecA Translocase Protein Unique to the Thermophilic Bacteria: Bioinformatics Analyses to Investigate Their Potential Roles (Q92442345) (← links)