scholarly article | Q13442814 |
P50 | author | Kurt Wüthrich | Q110957 |
P2093 | author name string | Erich Michel | |
P2860 | cites work | Tissue sulfhydryl groups | Q26778486 |
Two different neurodegenerative diseases caused by proteins with similar structures | Q27630179 | ||
Crystal structure of recombinant human interleukin-22 | Q27639495 | ||
NMR structure of the human doppel protein | Q27640537 | ||
Reassessment of Ellman's reagent | Q28274979 | ||
Oxidized redox state of glutathione in the endoplasmic reticulum | Q29619789 | ||
NMR structure of the integral membrane protein OmpX. | Q30164213 | ||
Optimal isotope labelling for NMR protein structure determinations. | Q30353197 | ||
Strategies for successful recombinant expression of disulfide bond-dependent proteins in Escherichia coli. | Q30377057 | ||
Providing an oxidizing environment for the cell-free expression of disulfide-containing proteins by exhausting the reducing activity of Escherichia coli S30 extract | Q33252893 | ||
Expression of proteins containing disulfide bonds in an insect cell-free system and confirmation of their arrangements by MALDI-TOF MS. | Q33309691 | ||
IL-22 is produced by innate lymphoid cells and limits inflammation in allergic airway disease | Q33971114 | ||
Preparative protein refolding | Q34831638 | ||
Selecting an appropriate method for expressing a recombinant protein | Q35011411 | ||
Refolding solubilized inclusion body proteins | Q35011420 | ||
Interleukin-22 forms dimers that are recognized by two interleukin-22R1 receptor chains | Q36459059 | ||
Disulfide-linked protein folding pathways | Q37202821 | ||
Production of disulfide-bonded proteins in Escherichia coli. | Q37956460 | ||
Cell-free protein synthesis system prepared from insect cells by freeze-thawing | Q40202531 | ||
DsbA and DsbC-catalyzed oxidative folding of proteins with complex disulfide bridge patterns in vitro and in vivo | Q44260052 | ||
Efficient synthesis of a disulfide‐containing protein through a batch cell‐free system from wheat germ | Q44658329 | ||
Efficient production of a bioactive, multiple disulfide-bonded protein using modified extracts of Escherichia coli | Q44713095 | ||
Development of cell-free protein synthesis platforms for disulfide bonded proteins | Q46749242 | ||
A solubility-enhancement tag (SET) for NMR studies of poorly behaving proteins. | Q52059754 | ||
Cell-free synthesis and amino acid-selective stable isotope labeling of proteins for NMR analysis. | Q54160536 | ||
Efficient production of isotopically labeled proteins by cell-free synthesis: a practical protocol. | Q54490146 | ||
The role of the thioredoxin and glutaredoxin pathways in reducing protein disulfide bonds in the Escherichia coli cytoplasm. | Q54563918 | ||
Functional antibody production using cell-free translation: effects of protein disulfide isomerase and chaperones. | Q54574290 | ||
[41] Preparation of a cell-free protein-synthesizing system from wheat germ | Q62058917 | ||
The genetics of disulfide bond metabolism | Q77936221 | ||
High-yield Escherichia coli-based cell-free expression of human proteins | Q83652889 | ||
P433 | issue | 17 | |
P407 | language of work or name | English | Q1860 |
P921 | main subject | structural biology | Q908902 |
P304 | page(s) | 3176-3184 | |
P577 | publication date | 2012-08-03 | |
P1433 | published in | FEBS Journal | Q1388041 |
P1476 | title | Cell-free expression of disulfide-containing eukaryotic proteins for structural biology. | |
P478 | volume | 279 |
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