Triose-phosphate isomerase (TIM) of the psychrophilic bacterium Vibrio marinus. Kinetic and structural properties - Wikidata - wikimedia - TriplyDB

Triose-phosphate isomerase (TIM) of the psychrophilic bacterium Vibrio marinus. Kinetic and structural properties

Triose-phosphate isomerase (TIM) of the psychrophilic bacterium Vibrio marinus. Kinetic and structural properties

http://www.wikidata.org/entity/Q27748819

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Potential use of sugar binding proteins in reactors for regeneration of CO2 fixation acceptor D-Ribulose-1,5-bisphosphate Optimization to low temperature activity in psychrophilic enzymes Structural and mutagenesis studies of leishmania triosephosphate isomerase: a point mutation can convert a mesophilic enzyme into a superstable enzyme without losing catalytic power Lys13 plays a crucial role in the functional adaptation of the thermophilic triose-phosphate isomerase from Bacillus stearothermophilus to high temperatures Modeling, mutagenesis, and structural studies on the fully conserved phosphate-binding loop (loop 8) of triosephosphate isomerase: toward a new substrate specificity The structure of a cold-adapted family 8 xylanase at 1.3 A resolution. Structural adaptations to cold and investgation of the active site Reversibility and two state behaviour in the thermal unfolding of oligomeric TIM barrel proteins Discovery, Molecular Mechanisms, and Industrial Applications of Cold-Active Enzymes Molecular basis of cold adaptation.qPIPSA: relating enzymatic kinetic parameters and interaction fields.Comparative proteome analysis of psychrophilic versus mesophilic bacterial species: Insights into the molecular basis of cold adaptation of proteins Cloning, sequences, and characterization of two chitinase genes from the Antarctic Arthrobacter sp. strain TAD20: isolation and partial characterization of the enzymes.Function and biotechnology of extremophilic enzymes in low water activity.Molecular analysis of the gene encoding a novel cold-adapted chitinase (ChiB) from a marine bacterium, Alteromonas sp. strain O-7.Alkaline phosphatase from the Antarctic strain TAB5. Properties and psychrophilic adaptations.ConSole: using modularity of contact maps to locate solenoid domains in protein structures Structure and Stability of the Dimeric Triosephosphate Isomerase from the Thermophilic Archaeon Thermoplasma acidophilum.Crystallization and preliminary X-ray crystallographic studies of a psychrophilic subtilisin-like protease Apa1 from Antarctic Pseudoalteromonas sp. strain AS-11 Psychrophilic enzymes: from folding to function and biotechnology.Psychrophily and catalysis.Biotechnology of cold-active proteases.Engineering the properties of a cold active enzyme through rational redesign of the active site.Multifactorial level of extremostability of proteins: can they be exploited for protein engineering?A guide to the effects of a large portion of the residues of triosephosphate isomerase on catalysis, stability, druggability, and human disease.Structural insights from a novel invertebrate triosephosphate isomerase from Litopenaeus vannamei.Cold-adapted alanine dehydrogenases from two antarctic bacterial strains: gene cloning, protein characterization, and comparison with mesophilic and thermophilic counterparts.Metabolic enzymes from psychrophilic bacteria: challenge of adaptation to low temperatures in ornithine carbamoyltransferase from Moritella abyssi.Thermodynamic characterization of yeast triosephosphate isomerase refolding: insights into the interplay between function and stability as reasons for the oligomeric nature of the enzyme.NADP+-dependent glutamate dehydrogenase in the Antarctic psychrotolerant bacterium Psychrobacter sp. TAD1. Characterization, protein and DNA sequence, and relationship to other glutamate dehydrogenases.Genomic analysis of cold-active Colwelliaphage 9A and psychrophilic phage-host interactions.Structural and functional analysis of a novel psychrophilic β-mannanase from Glaciozyma antarctica PI12.Structural adaptation to low temperatures--analysis of the subunit interface of oligomeric psychrophilic enzymes.Archaeal cold-adapted proteins: structural and evolutionary analysis of the elongation factor 2 proteins from psychrophilic, mesophilic and thermophilic methanogens.Properties of a subtilisin-like proteinase from a psychrotrophic Vibrio species comparison with proteinase K and aqualysin I.A DNA ligase from the psychrophile Pseudoalteromonas haloplanktis gives insights into the adaptation of proteins to low temperatures.Structural adaptation of enzymes to low temperatures.A better enzyme to cope with cold. Comparative flexibility studies on psychrotrophic, mesophilic, and thermophilic IPMDHs.Cold-active citrate synthase: mutagenesis of active-site residues.Comparative structural analysis of psychrophilic and meso- and thermophilic enzymes.Characterization of a cloned subtilisin-like serine proteinase from a psychrotrophic Vibrio species.

P2860

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P2860

Triose-phosphate isomerase (TIM) of the psychrophilic bacterium Vibrio marinus. Kinetic and structural properties

http://www.wikidata.org/entity/Q27748819

description

1998 nî lūn-bûn

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1998 թուականի Յունուարին հրատարակուած գիտական յօդուած

@hyw

1998 թվականի հունվարին հրատարակված գիտական հոդված

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1998年の論文

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1998年学术文章

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1998年学术文章

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1998年学术文章

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1998年学术文章

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1998年学术文章

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1998年學術文章

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name

Triose-phosphate isomerase (TI ...... etic and structural properties

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Triose-phosphate isomerase (TI ...... etic and structural properties

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Triose-phosphate isomerase (TI ...... etic and structural properties

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Triose-phosphate isomerase (TI ...... etic and structural properties

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Triose-phosphate isomerase (TI ...... etic and structural properties

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Triose-phosphate isomerase (TI ...... etic and structural properties

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Triose-phosphate isomerase (TI ...... etic and structural properties

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Triose-phosphate isomerase (TI ...... etic and structural properties

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Triose-phosphate isomerase (TI ...... etic and structural properties

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P1433

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P2860

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P1433

Journal of Biological Chemistry

P1476

Triose-phosphate isomerase (TI ...... etic and structural properties

@en

P2093

D Maes

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F Rentier-Delrue

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J A Martial

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J P Zeelen

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L Wyns

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M Alvarez

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R K Wierenga

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P2860

Crystal structure of recombinant human triosephosphate isomerase at 2.8 A resolution. Triosephosphate isomerase-related human genetic disorders and comparison with the trypanosomal enzyme

A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding

Improved methods for building protein models in electron density maps and the location of errors in these models

PROCHECK: a program to check the stereochemical quality of protein structures

MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures

A comprehensive set of sequence analysis programs for the VAX

The crystal structure of the "open" and the "closed" conformation of the flexible loop of trypanosomal triosephosphate isomerase

Structure of yeast triosephosphate isomerase at 1.9-A resolution

Structures of the "open" and "closed" state of trypanosomal triosephosphate isomerase, as observed in a new crystal form: implications for the reaction mechanism

Protein engineering with monomeric triosephosphate isomerase (monoTIM): the modelling and structure verification of a seven-residue loop

P304

2199-206

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scholarly article

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3587536

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10.1074/JBC.273.4.2199

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4

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273

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1998-01-23T00:00:00Z

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13788614

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9442062

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