Toward a molecular understanding of cold activity of enzymes from psychrophiles.
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Perspectives on biotechnological applications of archaeaOptimization to low temperature activity in psychrophilic enzymesThe structure of a cold-adapted family 8 xylanase at 1.3 A resolution. Structural adaptations to cold and investgation of the active siteCrystal structure of a cold-adapted class C beta-lactamaseStructure of uracil-DNAN-glycosylase (UNG) fromVibrio cholerae: mapping temperature adaptation through structural and mutational analysisStructure-based investigation into the functional roles of the extended loop and substrate-recognition sites in an endo-β-1,4-D-mannanase from the Antarctic springtail, Cryptopygus antarcticusDiscovery, Molecular Mechanisms, and Industrial Applications of Cold-Active EnzymesRapid evolution of culture-impaired bacteria during adaptation to biofilm growthMicrobial Diversity and Its Relationship to Physicochemical Characteristics of the Water in Two Extreme Acidic Pit Lakes from the Iberian Pyrite Belt (SW Spain)Molecular basis of cold adaptation.A comparative study of cold- and warm-adapted Endonucleases A using sequence analyses and molecular dynamics simulationsBiochemical characterization of a beta-galactosidase with a low temperature optimum obtained from an Antarctic arthrobacter isolate.Use of a packed-column bioreactor for isolation of diverse protease-producing bacteria from antarctic soil.Moritella cold-active dihydrofolate reductase: are there natural limits to optimization of catalytic efficiency at low temperature?Environmental constraints on life histories in Antarctic ecosystems: tempos, timings and predictability.Comparative genomics of DNA fragments from six Antarctic marine planktonic bacteria.Psychrophilic microorganisms: challenges for life.Comparative proteome analysis of psychrophilic versus mesophilic bacterial species: Insights into the molecular basis of cold adaptation of proteinsMechanisms of thermal adaptation revealed from the genomes of the Antarctic Archaea Methanogenium frigidum and Methanococcoides burtonii.The genome sequence of Psychrobacter arcticus 273-4, a psychroactive Siberian permafrost bacterium, reveals mechanisms for adaptation to low-temperature growthStatus of genome projects for nonpathogenic bacteria and archaea.Cell biology in the Antarctic: studying life in the freezer.Function and biotechnology of extremophilic enzymes in low water activity.Psychrobacter arcticus 273-4 uses resource efficiency and molecular motion adaptations for subzero temperature growth.Ecophysiological properties of cultivable heterotrophic bacteria and yeasts dominating in phytocenoses of Galindez Island, maritime Antarctica.Characterization of single-stranded DNA-binding proteins from the psychrophilic bacteria Desulfotalea psychrophila, Flavobacterium psychrophilum, Psychrobacter arcticus, Psychrobacter cryohalolentis, Psychromonas ingrahamii, Psychroflexus torquis, aSome like it cold: biocatalysis at low temperatures.Molecular insights into cold active polygalacturonase enzyme for its potential application in food processing.Genomic mechanisms for cold tolerance and production of exopolysaccharides in the Arctic cyanobacterium Phormidesmis priestleyi BC1401.Coping with our cold planetKinetic and thermodynamic studies of peptidyltransferase in ribosomes from the extreme thermophile Thermus thermophilus.Expression at 279 K, purification, crystallization and preliminary X-ray crystallographic analysis of a novel cold-active β-1,4-D-mannanase from the Antarctic springtail Cryptopygus antarcticus.Antarctic marine bacterium Pseudoalteromonas sp. KNOUC808 as a source of cold-adapted lactose hydrolyzing enzyme.Psychrophilic enzymes: from folding to function and biotechnology.Proteome Evolution of Deep-Sea Hydrothermal Vent Alvinellid Polychaetes Supports the Ancestry of Thermophily and Subsequent Adaptation to Cold in Some Lineages.Recent developments in production and biotechnological applications of cold-active microbial proteases.Conformational heterogeneity within the LID domain mediates substrate binding to Escherichia coli adenylate kinase: function follows fluctuations.Extremophilic SHMTs: from structure to biotechnology.Engineering the properties of a cold active enzyme through rational redesign of the active site.The linker region plays a key role in the adaptation to cold of the cellulase from an Antarctic bacterium
P2860
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P2860
Toward a molecular understanding of cold activity of enzymes from psychrophiles.
description
2000 nî lūn-bûn
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2000 թուականի Ապրիլին հրատարակուած գիտական յօդուած
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2000 թվականի ապրիլին հրատարակված գիտական հոդված
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2000年の論文
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2000年論文
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2000年論文
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2000年論文
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2000年論文
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2000年論文
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2000年论文
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name
Toward a molecular understanding of cold activity of enzymes from psychrophiles.
@ast
Toward a molecular understanding of cold activity of enzymes from psychrophiles.
@en
type
label
Toward a molecular understanding of cold activity of enzymes from psychrophiles.
@ast
Toward a molecular understanding of cold activity of enzymes from psychrophiles.
@en
prefLabel
Toward a molecular understanding of cold activity of enzymes from psychrophiles.
@ast
Toward a molecular understanding of cold activity of enzymes from psychrophiles.
@en
P356
P1433
P1476
Toward a molecular understanding of cold activity of enzymes from psychrophiles.
@en
P2093
Russell NJ
P2888
P356
10.1007/S007920050141
P577
2000-04-01T00:00:00Z