Hot spots in cold adaptation: localized increases in conformational flexibility in lactate dehydrogenase A4 orthologs of Antarctic notothenioid fishes - Wikidata - wikimedia - TriplyDB

Hot spots in cold adaptation: localized increases in conformational flexibility in lactate dehydrogenase A4 orthologs of Antarctic notothenioid fishes

Hot spots in cold adaptation: localized increases in conformational flexibility in lactate dehydrogenase A4 orthologs of Antarctic notothenioid fishes

http://www.wikidata.org/entity/Q28776515

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Rational modulation of conformational fluctuations in adenylate kinase reveals a local unfolding mechanism for allostery and functional adaptation in proteins Optimization to low temperature activity in psychrophilic enzymes Functional motions of Candida antarctica lipase B: a survey through open-close conformations The first structure of a cold-adapted superoxide dismutase (SOD): biochemical and structural characterization of iron SOD fromAliivibrio salmonicida A Rigidifying Salt-Bridge Favors the Activity of Thermophilic Enzyme at High Temperatures at the Expense of Low-Temperature Activity Structure and activity of the cold-active and anion-activated carboxyl esterase OLEI01171 from the oil-degrading marine bacterium Oleispira antarctica Discovery, Molecular Mechanisms, and Industrial Applications of Cold-Active Enzymes Fin whale MDH-1 and MPI allozyme variation is not reflected in the corresponding DNA sequences Genome evolution in the cold: Antarctic icefish muscle transcriptome reveals selective duplications increasing mitochondrial function Evolution and biodiversity of Antarctic organisms: a molecular perspective Transition from ectothermy to endothermy: the development of metabolic capacity in a bird (Gallus gallus)Enzyme surface rigidity tunes the temperature dependence of catalytic rates Mutational Constraints on Local Unfolding Inhibit the Rheological Adaptation of von Willebrand Factor.Defying the activity-stability trade-off in enzymes: taking advantage of entropy to enhance activity and thermostability.A comparative study of cold- and warm-adapted Endonucleases A using sequence analyses and molecular dynamics simulations Functional determinants of temperature adaptation in enzymes of cold- versus warm-adapted mussels (Genus Mytilus).Coping with thermal challenges: physiological adaptations to environmental temperatures.Transcriptomic and genomic evolution under constant cold in Antarctic notothenioid fish.Moritella cold-active dihydrofolate reductase: are there natural limits to optimization of catalytic efficiency at low temperature?Urea-Dependent Adenylate Kinase Activation following Redistribution of Structural States.Microevolutionary dynamics of a macroevolutionary key innovation in a Lepidopteran herbivore Update 1 of: Tunneling and dynamics in enzymatic hydride transfer.Temperature differentially affects adenosine triphosphatase activity in Hsc70 orthologs from Antarctic and New Zealand notothenioid fishes From DNA to fitness differences: sequences and structures of adaptive variants of Colias phosphoglucose isomerase (PGI).Cell biology in the Antarctic: studying life in the freezer.Mitochondrial function in Antarctic nototheniids with ND6 translocation Function and biotechnology of extremophilic enzymes in low water activity.Joint effect of phosphorus limitation and temperature on alkaline phosphatase activity and somatic growth in Daphnia magna.Purification, characterization, and sequencing of an extracellular cold-active aminopeptidase produced by marine psychrophile Colwellia psychrerythraea strain 34H Model of gene expression in extreme cold - reference transcriptome for the high-Antarctic cryopelagic notothenioid fish Pagothenia borchgrevinki.Positive selection in glycolysis among Australasian stick insects Physiological adaptation of an Antarctic Na+/K+-ATPase to the cold.Millisecond time scale conformational flexibility in a hyperthermophile protein at ambient temperature.FK506-Binding protein 22 from a psychrophilic bacterium, a cold shock-inducible peptidyl prolyl isomerase with the ability to assist in protein folding.Protein surface softness is the origin of enzyme cold-adaptation of trypsin.Stepwise adaptations to low temperature as revealed by multiple mutants of psychrophilic α-amylase from Antarctic Bacterium.Some like it cold: biocatalysis at low temperatures.The emerging role of RNA editing in plasticity.Mechanism of Thermal Adaptation in the Lactate Dehydrogenases.Improving the Thermostability and Activity of a Thermophilic Subtilase by Incorporating Structural Elements of Its Psychrophilic Counterpart.

P2860

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P2860

Hot spots in cold adaptation: localized increases in conformational flexibility in lactate dehydrogenase A4 orthologs of Antarctic notothenioid fishes

http://www.wikidata.org/entity/Q28776515

description

1998 nî lūn-bûn

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1998 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած

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1998 թվականի սեպտեմբերին հրատարակված գիտական հոդված

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1998年の論文

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1998年論文

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1998年論文

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1998年論文

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1998年論文

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1998年論文

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1998年论文

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Hot spots in cold adaptation: ...... Antarctic notothenioid fishes

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Hot spots in cold adaptation: ...... Antarctic notothenioid fishes

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Hot spots in cold adaptation: ...... Antarctic notothenioid fishes

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Proceedings of the National Academy of Sciences of the United States of America

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Hot spots in cold adaptation: ...... Antarctic notothenioid fishes

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G N Somero

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P2860

Variable expression of myoglobin among the hemoglobinless Antarctic icefishes

Evolution of antifreeze glycoprotein gene from a trypsinogen gene in Antarctic notothenioid fish

Refined crystal structure of dogfish M4 apo-lactate dehydrogenase

Enhanced protein thermostability from site-directed mutations that decrease the entropy of unfolding

Analysis of protein loop closure. Two types of hinges produce one motion in lactate dehydrogenase

Vertebrates without erythrocytes and blood pigment.

Genomic remnants of alpha-globin genes in the hemoglobinless antarctic icefishes.

Temperature adaptation of enzymes: roles of the free energy, the enthalpy, and the entropy of activation.

The interaction of body temperature and acid-base balance in ectothermic vertebrates.

Adjustment of conformational flexibility is a key event in the thermal adaptation of proteins.

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11476-81

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