The CXC motif: a functional mimic of protein disulfide isomerase

scientific article published on May 2003

The CXC motif: a functional mimic of protein disulfide isomerase is …
instance of (P31):
scholarly articleQ13442814

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P356DOI10.1021/BI026993Q
P932PMC publication ID2819094
P698PubMed publication ID12731880
P5875ResearchGate publication ID10773353

P50authorRonald T. RainesQ11205655
P2093author name stringKenneth J Woycechowsky
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Structural refinement and analysis of Mengo virusQ27667789
Crystal structure of the DsbA protein required for disulphide bond formation in vivoQ27732066
Structure determination of the N-terminal thioredoxin-like domain of protein disulfide isomerase using multidimensional heteronuclear 13C/15N NMR spectroscopyQ27732861
Characterization of Escherichia coli thioredoxins with altered active site residuesQ68510706
Mimicking the active site of protein disulfide-isomerase by substitution of proline 34 in Escherichia coli thioredoxinQ70155193
Rat liver thioredoxin and thioredoxin reductase: purification and characterizationQ70560152
Dissecting the mechanism of protein disulfide isomerase: catalysis of disulfide bond formation in a model peptideQ71629188
Functional properties of the individual thioredoxin-like domains of protein disulfide isomeraseQ71715190
Protein disulphide isomerase: building bridges in protein foldingQ72754787
Redox potentials of active-site bis(cysteinyl) fragments of thiol-protein oxidoreductasesQ72850823
Scanning and escape during protein-disulfide isomerase-assisted protein foldingQ73182455
A single dipeptide sequence modulates the redox properties of a whole enzyme familyQ74486160
The genetics of disulfide bond metabolismQ77936221
The extinction coefficients of the reduced band of pyridine nucleotidesQ82393206
Stabilization of gamma-turn conformations in peptides by disulfide bridgingQ93644707
Contribution of disulfide bonds to the conformational stability and catalytic activity of ribonuclease AQ28142467
Principles that govern the folding of protein chainsQ28236872
The Ribonucleolytic Activity of Angiogenin†Q29011743
Physiological functions of thioredoxin and thioredoxin reductaseQ29615600
ThioredoxinQ29619691
Catalysis of Protein Folding by Protein Disulfide Isomerase and Small-Molecule MimicsQ29999427
On the biosynthesis of bovine pancreatic trypsin inhibitor (BPTI). Structure, processing, folding and disulphide bond formation of the precursor in vitro and in microsomesQ30417977
A small-molecule catalyst of protein folding in vitro and in vivoQ30832472
The protein disulphide-isomerase family: unravelling a string of foldsQ33543247
Protein disulfide isomerases exploit synergy between catalytic and specific binding domainsQ33757536
Chaperone activity with a redox switchQ33852523
Catalysis of the oxidative folding of ribonuclease A by protein disulfide isomerase: dependence of the rate on the composition of the redox bufferQ34019971
Native disulfide bond formation in proteinsQ34046362
Thioredoxin reductase two modes of catalysis have evolvedQ34049898
Photoresponsive cyclic bis(cysteinyl)peptides as catalysts of oxidative protein folding.Q35030208
Thioredoxin-catalyzed refolding of disulfide-containing proteinsQ37402702
The essential function of protein-disulfide isomerase is to unscramble non-native disulfide bonds.Q38289017
Pro-sequence-assisted protein foldingQ40369319
The CXXC motif: imperatives for the formation of native disulfide bonds in the cell.Q41065191
Oxidative folding of cystine-rich peptides vs regioselective cysteine pairing strategiesQ41094522
Urea dependence of thiol-disulfide equilibria in thioredoxin: confirmation of the linkage relationship and a sensitive assay for structureQ41230313
Protein disulfide isomerase and assisted protein foldingQ41641785
Characterization of Escherichia coli thioredoxin variants mimicking the active-sites of other thiol/disulfide oxidoreductasesQ42027032
Comparison of the activities of protein disulphide-isomerase and thioredoxin in catalysing disulphide isomerization in a protein substrateQ42112518
Active site mutations in yeast protein disulfide isomerase cause dithiothreitol sensitivity and a reduced rate of protein folding in the endoplasmic reticulumQ42151080
Dependence of formation of small disulfide loops in two-cysteine peptides on the number and types of intervening amino acids.Q42199744
Structural properties of homogeneous protein disulphide-isomerase from bovine liver purified by a rapid high-yielding procedureQ42286207
Conformational specificity of mini-alphaA-crystallin as a molecular chaperoneQ43605981
The pro region of BPTI facilitates foldingQ43615298
Redox-active cyclic bis(cysteinyl)peptides as catalysts for in vitro oxidative protein foldingQ44038518
Recombinant expression and in vitro folding of proinsulin are stimulated by the synthetic dithiol Vectrase-P.Q44094290
Thioredoxin. 6. The Amino Acid Sequence of the Protein from Escherichia coli BQ47802974
Why is DsbA such an oxidizing disulfide catalyst?Q48068494
Identification of a protein required for disulfide bond formation in vivoQ48201805
Microscopic pKa values of Escherichia coli thioredoxin.Q52252586
The CXXC motif: a rheostat in the active site.Q52267222
Determination of the reduction-oxidation potential of the thioredoxin-like domains of protein disulfide-isomerase from the equilibrium with glutathione and thioredoxin.Q52393403
Folding motifs induced and stabilized by distinct cystine frameworks.Q52565927
Formation of three-dimensional structure in proteins. I. Rapid nonenzymic reactivation of reduced lysozymeQ54607526
Thermodynamic effects of reduction of the active-site disulfide of Escherichia coli thioredoxin explored by differential scanning calorimetry.Q54637378
A Pro to His mutation in active site of thioredoxin increases its disulfide-isomerase activity 10-fold. New refolding systems for reduced or randomly oxidized ribonucleaseQ54679075
ENZYMATIC SYNTHESIS OF DEOXYRIBONUCLEOTIDES.V. PURIFICATION AND PROPERTIES OF THIOREDOXIN REDUCTASE FROM ESCHERICHIA COLI BQ55037601
General Acid/Base Catalysis in the Active Site ofEscherichia coliThioredoxin†Q57961176
Efficient catalysis of disulphide bond rearrangements by protein disulphide isomeraseQ60066033
Evidence for a novel thioredoxin-like catalytic property of gonadotropic hormonesQ67266606
P433issue18
P407language of work or nameEnglishQ1860
P304page(s)5387-5394
P577publication date2003-05-01
P1433published inBiochemistryQ764876
P1476titleThe CXC motif: a functional mimic of protein disulfide isomerase
P478volume42

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