Pages that link to "Q68208733"
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The following pages link to Peptide Binding by Chaperone SecB: Implications for Recognition of Nonnative Structure (Q68208733):
Displaying 50 items.
- Recognition of secretory proteins in Escherichia coli requires signals in addition to the signal sequence and slow folding (Q24799937) (← links)
- Sec-secretion and sortase-mediated anchoring of proteins in Gram-positive bacteria (Q26852214) (← links)
- Structural determinants of SecB recognition by SecA in bacterial protein translocation (Q27642253) (← links)
- Biophysical characterization of the influence of salt on tetrameric SecB. (Q28367695) (← links)
- Substrate specificity of the SecB chaperone (Q30815173) (← links)
- Site-directed mutations in the C-terminal extension of human alphaB-crystallin affect chaperone function and block amyloid fibril formation (Q33302904) (← links)
- Proteolysis and chaperones: the destruction/reconstruction dilemma (Q33538586) (← links)
- Surface proteins of gram-positive bacteria and mechanisms of their targeting to the cell wall envelope (Q33538951) (← links)
- Identification of a Sequence Motif That Confers SecB Dependence on a SecB-Independent Secretory Protein In Vivo (Q33726768) (← links)
- Yersinia enterocolitica type III secretion. On the role of SycE in targeting YopE into HeLa cells (Q33869068) (← links)
- The SecB chaperone is involved in the secretion of the Serratia marcescens HasA protein through an ABC transporter. (Q33888292) (← 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)
- Recognition between flexible protein molecules: induced and assisted folding (Q34141716) (← links)
- Yop fusions to tightly folded protein domains and their effects on Yersinia enterocolitica type III secretion. (Q34314497) (← links)
- SecB is a bona fide generalized chaperone in Escherichia coli (Q34336036) (← links)
- Asp2 and Asp3 Interact Directly with GspB, the Export Substrate of the Streptococcus gordonii Accessory Sec System (Q35096377) (← links)
- SurA assists the folding of Escherichia coli outer membrane proteins (Q35604222) (← links)
- Carbon source-dependent synthesis of SecB, a cytosolic chaperone involved in protein translocation across Escherichia coli membranes (Q35619782) (← links)
- Protein secretion and surface display in Gram-positive bacteria (Q35814726) (← links)
- Position-dependent effects of polylysine on Sec protein transport (Q35921553) (← links)
- Binding of SecB to ribosome-bound polypeptides has the same characteristics as binding to full-length, denatured proteins (Q35962797) (← links)
- PrlA and PrlG suppressors reduce the requirement for signal sequence recognition (Q35975083) (← links)
- Regions of maltose-binding protein that influence SecB-dependent and SecA-dependent export in Escherichia coli (Q36123480) (← links)
- Secretion genes as determinants of Bacillus anthracis chain length (Q36156338) (← links)
- Determination of the binding frame within a physiological ligand for the chaperone SecB. (Q36278522) (← links)
- Electrospray mass spectrometric investigation of the chaperone SecB. (Q36279705) (← links)
- Determination of the binding frame of the chaperone SecB within the physiological ligand oligopeptide‐binding protein (Q36280530) (← links)
- The interaction between the chaperone SecB and its ligands: evidence for multiple subsites for binding (Q36280717) (← links)
- The observation of chaperone-ligand noncovalent complexes with electrospray ionization mass spectrometry (Q36281007) (← links)
- Roles of SecG in ATP- and SecA-dependent protein translocation. (Q36793326) (← links)
- Assembly of the chlorophyll-protein complexes (Q38168769) (← links)
- SecB dependence of an exported protein is a continuum influenced by the characteristics of the signal peptide or early mature region (Q39500325) (← links)
- Secretion Chaperones PrsA2 and HtrA Are Required for Listeria monocytogenes Replication following Intracellular Induction of Virulence Factor Secretion (Q39535829) (← links)
- The YSIRK-G/S motif of staphylococcal protein A and its role in efficiency of signal peptide processing (Q39750212) (← links)
- How proteins cross the bacterial cytoplasmic membrane. (Q40609301) (← links)
- The molecular chaperone SecB is released from the carboxy-terminus of SecA during initiation of precursor protein translocation. (Q41006640) (← links)
- Principles of membrane protein assembly and structure (Q41491565) (← links)
- Structural and mechanistic consequences of polypeptide binding by GroEL. (Q41679938) (← links)
- Export chaperone SecB uses one surface of interaction for diverse unfolded polypeptide ligands (Q41866614) (← links)
- Antifolding activity of the SecB chaperone is essential for secretion of HasA, a quickly folding ABC pathway substrate (Q44493487) (← links)
- The Sec System: Protein Export in Escherichia coli (Q47374398) (← links)
- The biosynthesis of bacterial and plastidic c-type cytochromes (Q47704872) (← links)
- Reversal by GroES of the GroEL preference from hydrophobic amino acids toward hydrophilic amino acids (Q49164900) (← links)
- Specificity of DnaK for arginine/lysine and effect of DnaJ on the amino acid specificity of DnaK. (Q54586686) (← links)
- Mapping of the Binding Frame for the Chaperone SecB within a Natural Ligand, Galactose-binding Protein (Q54601274) (← links)
- Chaperone SecB: conformational changes demonstrated by circular dichroism. (Q54602395) (← links)
- The C terminus of SecA is involved in both lipid binding and SecB binding. (Q54614038) (← links)
- Proteomic analysis of Lactobacillus casei GCRL163 cell-free extracts reveals a SecB homolog and other biomarkers of prolonged heat stress (Q57788660) (← links)
- Interaction of SecB with soluble SecA 1 (Q63359914) (← links)