The Oligomeric states of Haloarcula marismortui malate dehydrogenase are modulated by solvent components as shown by crystallographic and biochemical studies

scientific article (publication date: 21 February 2003)

The Oligomeric states of Haloarcula marismortui malate dehydrogenase are modulated by solvent components as shown by crystallographic and biochemical studies is …
instance of (P31):
scholarly articleQ13442814

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P356DOI10.1016/S0022-2836(02)01450-X
P3181OpenCitations bibliographic resource ID4320750
P698PubMed publication ID12581646
P5875ResearchGate publication ID8231860

P50authorChristine EbelQ61122869
P2093author name stringStéphane B Richard
Adriana Irimia
Dominique Madern
Frédéric M D Vellieux
Giuseppe Zaccaï
Lawrence W Cosenza
P2860cites workA rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye bindingQ25938984
Crystallography & NMR System: A New Software Suite for Macromolecular Structure DeterminationQ26778405
PROCHECK: a program to check the stereochemical quality of protein structuresQ26778411
MOLSCRIPT: a program to produce both detailed and schematic plots of protein structuresQ26778412
Halophilic adaptation: novel solvent protein interactions observed in the 2.9 and 2.6 A resolution structures of the wild type and a mutant of malate dehydrogenase from Haloarcula marismortuiQ27621140
The 2.0 A crystal structure of catalase-peroxidase from Haloarcula marismortuiQ27639486
Structural features that stabilize halophilic malate dehydrogenase from an archaebacteriumQ27647913
T and R states in the crystals of bacterial L–lactate dehydrogenase reveal the mechanism for allosteric controlQ27729846
Formylmethanofuran: tetrahydromethanopterin formyltransferase from Methanopyrus kandleri - new insights into salt-dependence and thermostabilityQ27739629
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An extensively modified version of MolScript that includes greatly enhanced coloring capabilitiesQ27860594
Refinement of macromolecular structures by the maximum-likelihood methodQ27861011
Efficient anisotropic refinement of macromolecular structures using FFTQ27861028
Halophilic adaptation of enzymesQ28144061
Torsion angle dynamics: reduced variable conformational sampling enhances crystallographic structure refinementQ28242162
Cross-validated maximum likelihood enhances crystallographic simulated annealing refinementQ29620831
AMoRe: an automated package for molecular replacementQ29642803
Stability and stabilization of globular proteins in solutionQ33950352
Protein stability in extremophilic archaeaQ34019689
Cloning, sequencing, and expression in Escherichia coli of the gene coding for malate dehydrogenase of the extremely halophilic archaebacterium Haloarcula marismortuiQ34061882
Stereochemical criteria for polypeptide and protein chain conformations. II. Allowed conformations for a pair of peptide unitsQ34356408
Analysis and modulation of protein stabilityQ35290771
A multicopy modeling of the water distribution in macromolecular crystalsQ36871044
Protein stability and molecular adaptation to extreme conditionsQ36890834
The effects of salt on the TATA binding protein-DNA interaction from a hyperthermophilic archaeonQ38336296
The control of protein stability and association by weak interactions with water: how do solvents affect these processes?Q40833005
Ion metabolism in a Halobacterium. I. Influence of age of culture on intracellular concentrationsQ42957843
Solution studies of elongation factor Tu from the extreme halophile Halobacterium marismortuiQ43017034
Denaturation of a halophilic enzyme monitored by small-angle neutron scatteringQ43019377
Solution structure of glyceraldehyde-3-phosphate dehydrogenase from Haloarcula vallismortis.Q43021247
Mutation at a Single Acidic Amino Acid Enhances the Halophilic Behaviour of Malate Dehydrogenase from Haloarcula Marismortui in Physiological SaltsQ43022200
Stabilisation of halophilic malate dehydrogenase from Haloarcula marismortui by divalent cations -- effects of temperature, water isotope, cofactor and pH.Q43024995
Relative role of anions and cations in the stabilization of halophilic malate dehydrogenase.Q43026646
Insights into the molecular relationships between malate and lactate dehydrogenases: structural and biochemical properties of monomeric and dimeric intermediates of a mutant of tetrameric L-[LDH-like] malate dehydrogenase from the halophilic archaeoQ43027178
Factors enhancing protein thermostabilityQ43027455
Solvent interactions of halophilic malate dehydrogenaseQ43031602
Link between protein-solvent and weak protein-protein interactions gives insight into halophilic adaptationQ43031610
Solute concentrations within cells of halophilic and non-halophilic bacteriaQ43034574
Extension of the theory of linked functions to incorporate the effects of protein hydrationQ44108208
Letter: Molecular symmetry axes and subunit interfaces in certain dehydrogenasesQ47907575
Analysis of effects of salts and uncharged solutes on protein and nucleic acid equilibria and processes: a practical guide to recognizing and interpreting polyelectrolyte effects, Hofmeister effects, and osmotic effects of salts.Q48007210
Boundary analysis in sedimentation velocity experiments.Q52386125
Accurate bond and angle parameters for X-ray protein structure refinementQ56485700
Improved Fourier coefficients for maps using phases from partial structures with errorsQ56877556
Between objectivity and subjectivityQ59051365
A mutation affecting the association equilibrium of formyltransferase from the hyperthermophilic Methanopyrus kandleri and its influence on the enzyme's activity and thermostabilityQ73129985
Lyotropic-salt-induced changes in monomer/dimer/tetramer association equilibrium of formyltransferase from the hyperthermophilic Methanopyrus kandleri in relation to the activity and thermostability of the enzymeQ77676522
Evaluation of single-crystal X-ray diffraction data from a position-sensitive detectorQ107329121
P433issue3
P407language of work or nameEnglishQ1860
P921main subjectbiochemistryQ7094
Haloarcula marismortuiQ25860043
P304page(s)859-873
P577publication date2003-02-01
P1433published inJournal of Molecular BiologyQ925779
P1476titleThe Oligomeric states of Haloarcula marismortui malate dehydrogenase are modulated by solvent components as shown by crystallographic and biochemical studies
P478volume326

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cites work (P2860)
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