Stepwise adaptations of citrate synthase to survival at life's extremes. From psychrophile to hyperthermophile
about
Optimization to low temperature activity in psychrophilic enzymesDiscovery of a Thermophilic Protein Complex Stabilized by Topologically Interlinked ChainsCrystal structure of the cold-active aminopeptidase from Colwellia psychrerythraea, a close structural homologue of the human bifunctional leukotriene A4 hydrolaseCrystal structures ofPhanerochaete chrysosporiumpyranose 2-oxidase suggest that the N-terminus acts as a propeptide that assists in homotetramer assemblyDiscovery, Molecular Mechanisms, and Industrial Applications of Cold-Active EnzymesStructure and Function in Homodimeric Enzymes: Simulations of Cooperative and Independent Functional Motions.Structural features determining thermal adaptation of esterases.Thermostability in endoglucanases is fold-specificStructural comparison of tRNA m(1)A58 methyltransferases revealed different molecular strategies to maintain their oligomeric architecture under extreme conditionsFunction and biotechnology of extremophilic enzymes in low water activity.Stepwise adaptations to low temperature as revealed by multiple mutants of psychrophilic α-amylase from Antarctic Bacterium.Psychrophilic enzymes: from folding to function and biotechnology.Rigidity versus flexibility: the dilemma of understanding protein thermal stability.Preliminary X-ray crystallographic analysis of 2-methylcitrate synthase from Salmonella typhimurium.Adaptation to extreme environments: macromolecular dynamics in bacteria compared in vivo by neutron scattering.Crystal Structures of Two Isozymes of Citrate Synthase from Sulfolobus tokodaii Strain 7.Temperature dependent mistranslation in a hyperthermophile adapts proteins to lower temperatures.Structural comparison between the open and closed forms of citrate synthase from Thermus thermophilus HB8.Kinetic and structural optimization to catalysis at low temperatures in a psychrophilic cellulase from the Antarctic bacterium Pseudoalteromonas haloplanktisCitrate synthase proteins in extremophilic organisms: studies within a structure-based model.Contribution of inter-subunit interactions to the thermostability of Pyrococcus furiosus citrate synthase.Chaperone-client interactions between Hsp21 and client proteins monitored in solution by small angle X-ray scattering and captured by crosslinking mass spectrometry.Structures of mesophilic and extremophilic citrate synthases reveal rigidity and flexibility for function
P2860
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P2860
Stepwise adaptations of citrate synthase to survival at life's extremes. From psychrophile to hyperthermophile
description
2002 nî lūn-bûn
@nan
2002 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած
@hyw
2002 թվականի դեկտեմբերին հրատարակված գիտական հոդված
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2002年の論文
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2002年論文
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2002年論文
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2002年論文
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2002年論文
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2002年論文
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2002年论文
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name
Stepwise adaptations of citrat ...... ychrophile to hyperthermophile
@ast
Stepwise adaptations of citrat ...... ychrophile to hyperthermophile
@en
Stepwise adaptations of citrat ...... ychrophile to hyperthermophile
@nl
type
label
Stepwise adaptations of citrat ...... ychrophile to hyperthermophile
@ast
Stepwise adaptations of citrat ...... ychrophile to hyperthermophile
@en
Stepwise adaptations of citrat ...... ychrophile to hyperthermophile
@nl
prefLabel
Stepwise adaptations of citrat ...... ychrophile to hyperthermophile
@ast
Stepwise adaptations of citrat ...... ychrophile to hyperthermophile
@en
Stepwise adaptations of citrat ...... ychrophile to hyperthermophile
@nl
P2093
P2860
P3181
P1433
P1476
Stepwise adaptations of citrat ...... ychrophile to hyperthermophile
@en
P2093
David W Hough
Garry L Taylor
Graeme S Bell
Helen Connaris
Michael J Danson
Rupert J M Russell
P2860
P304
P3181
P356
10.1046/J.1432-1033.2002.03344.X
P407
P577
2002-12-01T00:00:00Z