Extreme stabilization of a thermolysin-like protease by an engineered disulfide bond - Wikidata - awgldk - TriplyDB

Extreme stabilization of a thermolysin-like protease by an engineered disulfide bond

Extreme stabilization of a thermolysin-like protease by an engineered disulfide bond

http://www.wikidata.org/entity/Q28235527

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Determining biophysical protein stability in lysates by a fast proteolysis assay, FASTpp Signal peptide-dependent protein transport in Bacillus subtilis: a genome-based survey of the secretome Involvement of the TPR2 subdomain movement in the activities of phi29 DNA polymerase Structural and mutagenesis studies of leishmania triosephosphate isomerase: a point mutation can convert a mesophilic enzyme into a superstable enzyme without losing catalytic power Experimental verification of the 'stability profile of mutant protein' (SPMP) data using mutant human lysozymes Stabilization of a (betaalpha)8-barrel protein by an engineered disulfide bridge Structural basis of thermostability. Analysis of stabilizing mutations in subtilisin BPN'Insulin analog with additional disulfide bond has increased stability and preserved activity The role of disulfide bond in hyperthermophilic endocellulase Significant stabilization of ribonuclease A by additive effects Stability of isolated antibody-antigen complexes as a predictive tool for selecting toxin neutralizing antibodies Hyperthermophilic enzymes: sources, uses, and molecular mechanisms for thermostability Recent advances in our understanding of protein conformational stability from a pharmaceutical perspective.Quantification of free cysteines in membrane and soluble proteins using a fluorescent dye and thermal unfolding.Rational Design of Disulfide Bonds Increases Thermostability of a Mesophilic 1,3-1,4-β-Glucanase from Bacillus terquilensis The effect of engineered disulfide bonds on the stability of Drosophila melanogaster acetylcholinesterase.Single-point amino acid substitutions at the 119th residue of thermolysin and their pressure-induced activation.Enhancing the thermal robustness of an enzyme by directed evolution: least favorable starting points and inferior mutants can map superior evolutionary pathways.Disulfide linkage engineering for improving biophysical properties of human VH domains.Stabilizing the integrin alpha M inserted domain in alternative conformations with a range of engineered disulfide bonds.Engineering a disulfide bond in the lid hinge region of Rhizopus chinensis lipase: increased thermostability and altered acyl chain length specificity.Contribution of Disulfide Bridges to the Thermostability of a Type A Feruloyl Esterase from Aspergillus usamii Engineering an enzyme to resist boiling.Reversibly locking a protein fold in an active conformation with a disulfide bond: integrin alphaL I domains with high affinity and antagonist activity in vivo.From protein engineering to immobilization: promising strategies for the upgrade of industrial enzymes In silico rational design and systems engineering of disulfide bridges in the catalytic domain of an alkaline α-amylase from Alkalimonas amylolytica to improve thermostability.Implication of disulfide bridge induced thermal reversibility, structural and functional stability for luciferase.The role of calcium ions in the stability and instability of a thermolysin-like protease.Protein disulfide engineering.The road to the first, fully active and more stable human insulin variant with an additional disulfide bond.Influence of protein fold stability on immunogenicity and its implications for vaccine design.Bottleneck in secretion of α-amylase in Bacillus subtilis.Dihydrodipicolinate synthase from Thermotoga maritima.Effects of site-directed mutagenesis in the N-terminal domain of thermolysin on its stabilization.Evaluation of irreversible protein thermal inactivation caused by breakage of disulphide bonds using methanethiosulphonate.Novel disulfide engineering in human carbonic anhydrase II using the PAIRWISE side-chain geometry database.The roles of surface loop insertions and disulfide bond in the stabilization of thermophilic WF146 protease.Expression of Talaromyces emersonii cellobiohydrolase Cel7A in Saccharomyces cerevisiae and rational mutagenesis to improve its thermostability and activity.Improvement of Bacillus circulans beta-amylase activity attained using the ancestral mutation method.Protein rigidity and thermophilic adaptation.

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P2860

Extreme stabilization of a thermolysin-like protease by an engineered disulfide bond

http://www.wikidata.org/entity/Q28235527

description

1997 nî lūn-bûn

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1997 թուականի Ապրիլին հրատարակուած գիտական յօդուած

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1997 թվականի ապրիլին հրատարակված գիտական հոդված

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1997年の論文

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1997年論文

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1997年論文

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1997年論文

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1997年論文

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1997年論文

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1997年论文

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name

Extreme stabilization of a thermolysin-like protease by an engineered disulfide bond

@ast

Extreme stabilization of a thermolysin-like protease by an engineered disulfide bond

@en

Extreme stabilization of a thermolysin-like protease by an engineered disulfide bond

@nl

type

label

Extreme stabilization of a thermolysin-like protease by an engineered disulfide bond

@ast

Extreme stabilization of a thermolysin-like protease by an engineered disulfide bond

@en

Extreme stabilization of a thermolysin-like protease by an engineered disulfide bond

@nl

prefLabel

Extreme stabilization of a thermolysin-like protease by an engineered disulfide bond

@ast

Extreme stabilization of a thermolysin-like protease by an engineered disulfide bond

@en

Extreme stabilization of a thermolysin-like protease by an engineered disulfide bond

@nl

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Journal of Biological Chemistry

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Extreme stabilization of a thermolysin-like protease by an engineered disulfide bond

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P2093

B Van den Burg

http://www.w3.org/2001/XMLSchema#string

B W Dijkstra

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G Venema

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J Mansfeld

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O R Veltman

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R Ulbrich-Hofmann

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V G Eijsink

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P2860

Cleavage of structural proteins during the assembly of the head of bacteriophage T4

Tissue sulfhydryl groups

Thermostabilization of the Bacillus circulans xylanase by the introduction of disulfide bonds

WHAT IF: a molecular modeling and drug design program

Electrochemical photolysis of water at a semiconductor electrode

Role of Calcium in the thermal stability of thermolysin

Mapping the transition state and pathway of protein folding by protein engineering

Structure of thermolysin refined at 1.6 A resolution

Structural determinants of the stability of thermolysin-like proteinases

Crystal structure of neutral protease from Bacillus cereus refined at 3.0 A resolution and comparison with the homologous but more thermostable enzyme thermolysin.

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