| scholarly article | Q13442814 |
| P2093 | author name string | Weibin Zhou | |
| François Baneyx | |||
| M S R Sastry | |||
| P2860 | cites work | Recombinant protein folding and misfolding in Escherichia coli | Q35940945 |
| Beyond transcription--new mechanisms for the regulation of molecular chaperones | Q36069364 | ||
| Making the most of affinity tags | Q36142429 | ||
| Some like it hot: the structure and function of small heat-shock proteins. | Q36277178 | ||
| Hsp31, the Escherichia coli yedU gene product, is a molecular chaperone whose activity is inhibited by ATP at high temperatures. | Q38362898 | ||
| Regulation of Escherichia coli hchA, a stress-inducible gene encoding molecular chaperone Hsp31. | Q39349479 | ||
| Chaperone Hsp31 contributes to acid resistance in stationary-phase Escherichia coli | Q42951949 | ||
| Characterization of the Escherichia coli YedU protein as a molecular chaperone | Q44301531 | ||
| Peptidase activity of the Escherichia coli Hsp31 chaperone | Q45154612 | ||
| Differential effects of short affinity tags on the crystallization of Pyrococcus furiosus maltodextrin-binding protein | Q45714169 | ||
| Escherichia coli Hsp31 functions as a holding chaperone that cooperates with the DnaK-DnaJ-GrpE system in the management of protein misfolding under severe stress conditions | Q47255584 | ||
| Evaluation of secondary structure of proteins from UV circular dichroism spectra using an unsupervised learning neural network. | Q52224746 | ||
| Overview of tag protein fusions: from molecular and biochemical fundamentals to commercial systems | Q22252788 | ||
| Crystal structure of an intracellular protease from Pyrococcus horikoshii at 2-A resolution | Q27628891 | ||
| The 1.6-A crystal structure of the class of chaperones represented by Escherichia coli Hsp31 reveals a putative catalytic triad | Q27640637 | ||
| Crystal structures of human DJ-1 and Escherichia coli Hsp31, which share an evolutionarily conserved domain | Q27641905 | ||
| The crystal structure of Escherichia coli heat shock protein YedU reveals three potential catalytic active sites | Q27642199 | ||
| A new native EcHsp31 structure suggests a key role of structural flexibility for chaperone function | Q27642847 | ||
| SWISS-MODEL and the Swiss-PdbViewer: an environment for comparative protein modeling | Q27860614 | ||
| Molecular chaperones in the cytosol: from nascent chain to folded protein | Q28205903 | ||
| Membrane protein expression and production: effects of polyhistidine tag length and position | Q30432750 | ||
| Identification of functional subclasses in the DJ-1 superfamily proteins | Q33270508 | ||
| A critical review of the methods for cleavage of fusion proteins with thrombin and factor Xa. | Q34228979 | ||
| The biochemistry of Parkinson's disease | Q34426026 | ||
| The linker-loop region of Escherichia coli chaperone Hsp31 functions as a gate that modulates high-affinity substrate binding at elevated temperatures | Q34513554 | ||
| Protein folding and degradation in bacteria: to degrade or not to degrade? That is the question. | Q35021869 | ||
| Sequence, expression in Escherichia coli, and analysis of the gene encoding a novel intracellular protease (PfpI) from the hyperthermophilic archaeon Pyrococcus furiosus | Q35606572 | ||
| P433 | issue | 7 | |
| P921 | main subject | molecular chaperones | Q422496 |
| Escherichia coli | Q25419 | ||
| P304 | page(s) | 1439-1447 | |
| P577 | publication date | 2009-07-01 | |
| P1433 | published in | Protein Science | Q7251445 |
| P1476 | title | Integrity of N- and C-termini is important for E. coli Hsp31 chaperone activity | |
| P478 | volume | 18 |
| Q27680748 | A Glutathione-independent Glyoxalase of the DJ-1 Superfamily Plays an Important Role in Managing Metabolically Generated Methylglyoxal in Candida albicans |
| Q33856954 | Biofabrication of ZnS:Mn luminescent nanocrystals using histidine, hexahistidine, and His-tagged proteins: a comparison study |
| Q39013649 | Cloning, expression, purification, crystallization and preliminary X-ray analysis of the 31 kDa Vibrio cholerae heat-shock protein VcHsp31. |
| Q33728879 | Deep interactome profiling of membrane proteins by co-interacting protein identification technology |
| Q36139835 | Hsp31 Is a Stress Response Chaperone That Intervenes in the Protein Misfolding Process |
| Q34194675 | Hsp31 of Escherichia coli K-12 is glyoxalase III. |
| Q42275188 | Overview of electron crystallography of membrane proteins: crystallization and screening strategies using negative stain electron microscopy |
| Q36290335 | Structural and biochemical studies on Vibrio cholerae Hsp31 reveals a novel dimeric form and Glutathione-independent Glyoxalase activity |
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