About: The engineering of binding affinity at metal ion binding sites for the stabilization of proteins: subtilisin as a test case

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scientific article published on 01 November 1988

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rdf:type	Item
description	wetenschappelijk artikel (nl) наукова стаття, опублікована в листопаді 1988 (uk) scientific article published on 01 November 1988 (en) artículu científicu espublizáu en payares de 1988 (ast) im November 1988 veröffentlicher wissenschaftlicher Artikel (de)
publication date	wds:Q70259268-06EA07BB-C3FB-4201-97DF-8216F6560428
publication date	1988-11-01 00:00:00Z (xsd:dateTime)
language of work or name	wds:Q70259268-C4D363BC-AA9A-4770-BE62-61D31541588C
language of work or name	English
author name string	wds:Q70259268-05395A99-5925-4730-841E-F123433727A0 wds:Q70259268-1205EFF7-6557-4D57-8D20-BE12BB14843B wds:Q70259268-50907BF9-B374-466F-AA09-210B666246EF wds:Q70259268-80AA14F8-32B7-4010-A0B5-DFDB986573C2 wds:Q70259268-8E20DD01-BE33-4F28-97BE-2FC00620EEC3 wds:Q70259268-9567D554-92E8-4F37-A512-24C725965A5F wds:Q70259268-F388500D-C7EB-4C79-9663-9C2280EE5544
author name string	G L Gilliland T L Poulos J F Wood M W Pantoliano M Whitlow P N Bryan M L Rollence
rdfs:label	The engineering of binding affinity at metal ion binding sites for the stabilization of proteins: subtilisin as a test case (en) The engineering of binding affinity at metal ion binding sites for the stabilization of proteins: subtilisin as a test case (nl)
skos:prefLabel	The engineering of binding affinity at metal ion binding sites for the stabilization of proteins: subtilisin as a test case (en) The engineering of binding affinity at metal ion binding sites for the stabilization of proteins: subtilisin as a test case (nl)
name	The engineering of binding affinity at metal ion binding sites for the stabilization of proteins: subtilisin as a test case (en) The engineering of binding affinity at metal ion binding sites for the stabilization of proteins: subtilisin as a test case (nl)
author	wds:Q70259268-682EE661-54B2-404E-937B-3132783FC615
author	Barry C Finzel
title	wds:Q70259268-EB86FCB8-8558-49D5-B602-7851A243FECE
title	The engineering of binding affinity at metal ion binding sites for the stabilization of proteins: subtilisin as a test case (en)
page(s)	wds:Q70259268-3924F3C5-ABA4-410F-90EB-A521C12A47D6
page(s)	8311-8317
instance of	wds:Q70259268-B8FCD017-FAEC-4665-8E91-3127AF01CC44
instance of	scholarly article
PubMed ID	wds:Q70259268-8CE6886E-B665-4F71-BFE4-49850450D081
PubMed ID	http://rdf.ncbi.nlm.nih.gov/pubchem/reference/3072018
PubMed ID	3072018
published in	wds:Q70259268-7B424B4D-28C5-42C0-B201-F2EB66D12B15
published in	Biochemistry
issue	wds:Q70259268-1E58B743-C7CA-49B8-B4A0-352394C3F33C
volume	wds:Q70259268-D5B3D3D0-49A5-4493-A4A1-54DF4CFD7A83
issue	22
volume	27
DOI	wds:Q70259268-52BCA115-2E75-47CE-B05E-FE1F9B8ACF1C
DOI	http://dx.doi.org/10.1021/BI00422A004
DOI	10.1021/BI00422A004
is about of	https://www.wikidata.org/wiki/Special:EntityData/Q70259268
is cites work of	Serial increase in the thermal stability of 3-isopropylmalate dehydrogenase from Bacillus subtilis by experimental evolution Microbial alkaline proteases: from a bioindustrial viewpoint The 0.93Å Crystal Structure of Sphericase: A Calcium-loaded Serine Protease from Bacillus sphaericus Ca2+-dependent maturation of subtilisin from a hyperthermophilic archaeon, Thermococcus kodakaraensis: the propeptide is a potent inhibitor of the mature domain but is not required for its folding Patterns of adaptation in a laboratory evolved thermophilic enzyme Structural Biology of Zinc Structural basis of thermostability. Analysis of stabilizing mutations in subtilisin BPN' Protein engineering of subtilisin Thermostable variants of subtilisin selected by temperature-gradient gel electrophoresis Simultaneous enhancement of thermostability and catalytic activity of phospholipase A(1) by evolutionary molecular engineering Calcium-binding sites in proteins: a structural perspective Where metal ions bind in proteins Crystal structure of the alkaline proteinase Savinase™ from Bacillus lentus at 1.4 Å resolution The solution structure of serine protease PB92 from Bacillus alcalophilus presents a rigid fold with a flexible substrate-binding site Directed evolution of a subtilisin with calcium-independent stability. 1H, 13C and 15N NMR backbone assignments and secondary structure of the 269-residue protease subtilisin 309 from Bacillus lentus Chromatographic method involving inductively coupled plasma atomic emission spectrometric detection for the study of metal-protein complexes Zinc binding in proteins and solution: a simple but accurate nonbonded representation Stability of protein pharmaceuticals Close association of the N terminus of Kv1.3 with the pore region Design and creation of a Ca2+ binding site in human lysozyme to enhance structural stability Effect of polar side chains at position 172 on thermal stability of 3-isopropylmalate dehydrogenase from Thermus thermophilus. Do voltage-dependent K+ channels require Ca2+? A critical test employing a heterologous expression system Protein transport across the cell wall of monoderm Gram-positive bacteria Thermodynamics of melittin tetramerization determined by circular dichroism and implications for protein folding Divalent cations stabilize the conformation of plasma cell membrane glycoprotein PC-1 (alkaline phosphodiesterase I). Role of calcium in activity and stability of the Lactococcus lactis cell envelope proteinase Prediction and analysis of structure, stability and unfolding of thermolysin-like proteases Further stabilization of 3-isopropylmalate dehydrogenase of an extreme thermophile, Thermus thermophilus, by a suppressor mutation method Bivalent cations stabilize yeast alcohol dehydrogenase I. Progressive rearrangement of subtilisin Carlsberg into orderly and inflexible conformation with Ca(2+) binding Enzyme stabilization: state of the art. Breaking the low barrier hydrogen bond in a serine protease The complete amino acid substitutions at position 131 that are positively involved in cold adaptation of subtilisin BPN'. Thermal analysis of the plasma membrane Ca2+-ATPase. Improvement of a useful enzyme (subtilisin BPN') by an experimental evolution system. Streptomyces misionensis PESB-25 produces a thermoacidophilic endoglucanase using sugarcane bagasse and corn steep liquor as the sole organic substrates. Functionally-stabilized proteins — A review Induction of thermal and chemical stability of O6-methylguanine-DNA methyltransferase by Ca2+ "Fluctuograms" reveal the intermittent intra-protein communication in subtilisin Carlsberg and correlate mechanical coupling with co-evolution Cation-binding sites of subtilisin Carlsberg probed with Eu(III) luminescence Mechanism of Ca2+-dependent activity of human neutrophil gelatinase B An electrostatic model for the interaction between growth hormone and its receptor involving chelation of Ca2+ to the human growth hormone molecule. Calcium triggers the refolding of Bacillus subtilis chitosanase Evidence for Hidden Involvement of N3-Protonated Guanine in RNA Structure and Function Structure and selectivity of a monovalent cation binding site in cubic insulin crystals. Mutational analysis of the pro-peptide of a marine intracellular subtilisin protease supports its role in inhibition
is cites work of	wds:Q27642190-6888AFA7-AD7F-4ABE-BD95-C973F91BD924 wds:Q27638987-0283E104-EFDF-4BF1-B82F-1FABEFD3A74B

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