Pages that link to "Q27628763"
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The following pages link to Crystal structure of the bacterial protein export chaperone secB (Q27628763):
Displaying 50 items.
- Crystal structures of human DJ-1 and Escherichia coli Hsp31, which share an evolutionarily conserved domain (Q27641905) (← links)
- Structural determinants of SecB recognition by SecA in bacterial protein translocation (Q27642253) (← links)
- A new native EcHsp31 structure suggests a key role of structural flexibility for chaperone function (Q27642847) (← links)
- Structural Characterization of the ATPase Reaction Cycle of Endosomal AAA Protein Vps4 (Q27648853) (← links)
- Crystal Structure of YaeT: Conformational Flexibility and Substrate Recognition (Q27653156) (← links)
- Tic22 Is an Essential Chaperone Required for Protein Import into the Apicoplast (Q27673842) (← links)
- Structural basis for the antifolding activity of a molecular chaperone (Q27726706) (← links)
- Domain architecture and activity of human Pex19p, a chaperone-like protein for intracellular trafficking of peroxisomal membrane proteins (Q28271907) (← links)
- Assembly of Outer Membrane β-Barrel Proteins: the Bam Complex (Q30155422) (← links)
- Determination of protein function, evolution and interactions by structural genomics. (Q30328302) (← links)
- Using nanoelectrospray ion mobility spectrometry (GEMMA) to determine the size and relative molecular mass of proteins and protein assemblies: a comparison with MALLS and QELS. (Q30398578) (← links)
- Sites of interaction of a precursor polypeptide on the export chaperone SecB mapped by site-directed spin labeling (Q30496200) (← links)
- Interaction of the Bacillus subtilis chaperone CsaA with the secretory protein YvaY. (Q30982774) (← links)
- Getting a grip on non-native proteins (Q34236741) (← links)
- Protein translocation across membranes (Q34293903) (← links)
- The structural view of bacterial translocation-specific chaperone SecB: implications for function (Q34455348) (← links)
- Multitasking SecB chaperones in bacteria (Q34637739) (← links)
- Large-scale evolutionary analyses on SecB subunits of bacterial sec system. (Q35182130) (← links)
- The basis of asymmetry in the SecA:SecB complex (Q35207949) (← links)
- Functional implementation of the posttranslational SecB-SecA protein-targeting pathway in Bacillus subtilis (Q35688908) (← links)
- A little help from my friends: quality control of presecretory proteins in bacteria (Q35933897) (← links)
- Recombinant protein folding and misfolding in Escherichia coli (Q35940945) (← links)
- New Escherichia coli outer membrane proteins identified through prediction and experimental verification (Q36458292) (← links)
- The structure of the Sec complex and the problem of protein translocation (Q36640900) (← links)
- Bacterial protein secretion through the translocase nanomachine (Q36972407) (← links)
- Delivering proteins for export from the cytosol (Q37420386) (← links)
- SecB--a chaperone dedicated to protein translocation. (Q37710987) (← links)
- Breaking on through to the other side: protein export through the bacterial Sec system. (Q38065265) (← links)
- The Sec translocon mediated protein transport in prokaryotes and eukaryotes. (Q38206834) (← links)
- Protein export through the bacterial Sec pathway. (Q39021695) (← 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)
- Export chaperone SecB uses one surface of interaction for diverse unfolded polypeptide ligands (Q41866614) (← links)
- Characterization of three areas of interactions stabilizing complexes between SecA and SecB, two proteins involved in protein export (Q41904736) (← links)
- Maximal efficiency of coupling between ATP hydrolysis and translocation of polypeptides mediated by SecB requires two protomers of SecA (Q42078600) (← links)
- Sites of interaction between SecA and the chaperone SecB, two proteins involved in export (Q43095210) (← links)
- Electron spin resonance and fluorescence studies of the bound-state conformation of a model protein substrate to the chaperone SecB. (Q43660562) (← links)
- Antifolding activity of the SecB chaperone is essential for secretion of HasA, a quickly folding ABC pathway substrate (Q44493487) (← links)
- Navigating the structure-function-evolutionary relationship of CsaA chaperone in archaea (Q46305440) (← links)
- Direct observation of chaperone-induced changes in a protein folding pathway (Q46874460) (← links)
- The Sec System: Protein Export in Escherichia coli (Q47374398) (← links)
- The SecB-like chaperone Rv1957 from Mycobacterium tuberculosis: crystallization and X-ray crystallographic analysis (Q51702121) (← links)
- Defining the role of the Escherichia coli chaperone SecB using comparative proteomics. (Q54473734) (← links)
- DnaK promotes the selective export of outer membrane protein precursors in SecA-deficient Escherichia coli. (Q54535978) (← links)
- Trigger factor retards protein export in Escherichia coli. (Q54538999) (← links)
- Sec, drugs and rock’n’roll: antibiotic targeting of bacterial protein translocation (Q57976568) (← links)
- SatS is a chaperone for the SecA2 protein export pathway (Q60921483) (← links)
- Structural insights into chaperone addiction of toxin-antitoxin systems (Q61795910) (← links)
- Sec Protein-Conducting Channel and SecA (Q63359819) (← links)
- Co- and post-translational translocation through the protein-conducting channel: analogous mechanisms at work? (Q63359824) (← links)
- Thermodynamics of the protein translocation (Q84188995) (← links)