| P2093 | author name string | Yi Peng | |
| | Zhen Zhao | |
| | Shu-Feng Hao | |
| | Chih-Chen Wang | |
| | Zong-Hao Zeng | |
| P2860 | cites work | Identification of essential residues in the type II Hsp40 Sis1 that function in polypeptide binding | Q43937089 |
| | Dissociation and aggregation of D-glyceraldehyde-3-phosphate dehydrogenase during denaturation by guanidine hydrochloride | Q45013837 |
| | The folding catalyst protein disulfide isomerase is constructed of active and inactive thioredoxin modules | Q57077650 |
| | Purification and properties of bovine thioredoxin system | Q59276144 |
| | Contributions of protein disulfide isomerase domains to its chaperone activity | Q72999583 |
| | DsbG, a protein disulfide isomerase with chaperone activity | Q73731229 |
| | The N-terminal sequence (residues 1-65) is essential for dimerization, activities, and peptide binding of Escherichia coli DsbC | Q74127474 |
| | In vivo and in vitro function of the Escherichia coli periplasmic cysteine oxidoreductase DsbG | Q74602402 |
| | Chaperone activity of DsbC | Q77955138 |
| | The Protein Data Bank | Q24515306 |
| | Gapped BLAST and PSI-BLAST: a new generation of protein database search programs | Q24545170 |
| | Mutations in domain a′ of protein disulfide isomerase affect the folding pathway of bovine pancreatic ribonuclease A | Q24644793 |
| | Improved tools for biological sequence comparison | Q24652199 |
| | A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding | Q25938984 |
| | PROCHECK: a program to check the stereochemical quality of protein structures | Q26778411 |
| | The structure in solution of the b domain of protein disulfide isomerase | Q27618778 |
| | Crystal structure of the protein disulfide bond isomerase, DsbC, from Escherichia coli | Q27621623 |
| | The crystal structure of the peptide-binding fragment from the yeast Hsp40 protein Sis1 | Q27627141 |
| | Structure of the molecular chaperone prefoldin: unique interaction of multiple coiled coil tentacles with unfolded proteins | Q27628828 |
| | Thioredoxin fold as homodimerization module in the putative chaperone ERp29: NMR structures of the domains and experimental model of the 51 kDa dimer | Q27632929 |
| | Structure of CcmG/DsbE at 1.14 A resolution: high-fidelity reducing activity in an indiscriminately oxidizing environment | Q27639369 |
| | Crystal structure of thioredoxin from Escherichia coli at 1.68 A resolution | Q27671419 |
| | The crystal structure of the bacterial chaperonin GroEL at 2.8 A | Q27730725 |
| | Crystal structure of the DsbA protein required for disulphide bond formation in vivo | Q27732066 |
| | Structure determination of the N-terminal thioredoxin-like domain of protein disulfide isomerase using multidimensional heteronuclear 13C/15N NMR spectroscopy | Q27732861 |
| | Comparative protein modelling by satisfaction of spatial restraints | Q27860866 |
| | Thioredoxin--a fold for all reasons | Q29618984 |
| | Both the isomerase and chaperone activities of protein disulfide isomerase are required for the reactivation of reduced and denatured acidic phospholipase A2. | Q33886092 |
| | Disulfide bond isomerization in prokaryotes | Q35058901 |
| | Protein folding in the bacterial periplasm | Q35621918 |
| | A novel method for increasing production of mature proteins in the periplasm of Escherichia coli | Q36281243 |
| | Thermodynamics of lipid protein associations thermodynamics of helix formation in the association of high density apolipoprotein A-I (ApoA-I) to dimyristoyl phosphatidylcholine | Q39158514 |
| | Evolutionary domain fusion expanded the substrate specificity of the transmembrane electron transporter DsbD. | Q39647812 |
| | Turning a disulfide isomerase into an oxidase: DsbC mutants that imitate DsbA. | Q39714839 |
| | Characterization of Escherichia coli thioredoxin variants mimicking the active-sites of other thiol/disulfide oxidoreductases | Q42027032 |
| | Comparison of the activities of protein disulphide-isomerase and thioredoxin in catalysing disulphide isomerization in a protein substrate | Q42112518 |
| | Structural properties of homogeneous protein disulphide-isomerase from bovine liver purified by a rapid high-yielding procedure | Q42286207 |
| P433 | issue | 44 | |
| P407 | language of work or name | English | Q1860 |
| P921 | main subject | molecular chaperones | Q422496 |
| P304 | page(s) | 43292-43298 | |
| P577 | publication date | 2003-08-21 | |
| P1433 | published in | Journal of Biological Chemistry | Q867727 |
| P1476 | title | Dimerization by domain hybridization bestows chaperone and isomerase activities | |
| P478 | volume | 278 | |