Distribution of fructose diphosphate aldolase variants in biological systems
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Structure of human brain fructose 1,6-(bis)phosphate aldolase: linking isozyme structure with functionComplete amino acid sequence for human aldolase B derived from cDNA and genomic clonesThermodynamic analysis shows conformational coupling and dynamics confer substrate specificity in fructose-1,6-bisphosphate aldolaseEvolutionary implications of the human aldolase-A, -B, -C, and -pseudogene chromosome locationsCrystal structure of an archaeal class I aldolase and the evolution of (betaalpha)8 barrel proteinsActive-site remodelling in the bifunctional fructose-1,6-bisphosphate aldolase/phosphataseArchaeal fructose-1,6-bisphosphate aldolases constitute a new family of archaeal type class I aldolaseSpatial clustering of isozyme-specific residues reveals unlikely determinants of isozyme specificity in fructose-1,6-bisphosphate aldolaseThe crystal structure of human muscle aldolase at 3.0 A resolution.Amino acid positions subject to multiple coevolutionary constraints can be robustly identified by their eigenvector network centrality scoresTyrosine nitration impairs mammalian aldolase A activity.Comparative proteomic analysis of cell lines and scrapings of the human intestinal epithelium.Quantitative gene expression profiles in real time from expressed sequence tag databases.Molecular Characterization, Gene Evolution, and Expression Analysis of the Fructose-1, 6-bisphosphate Aldolase (FBA) Gene Family in Wheat (Triticum aestivum L.).Lactate dehydrogenase isoenzyme changes during facial development.Expression, purification, crystallization and preliminary X-ray crystallographic analysis of fructose-1,6-bisphosphate aldolase from Escherichia coliGlycolysis, tumor metabolism, cancer growth and dissemination. A new pH-based etiopathogenic perspective and therapeutic approach to an old cancer questionStabilization of the predominant disease-causing aldolase variant (A149P) with zwitterionic osmolytesCharacterization of fructose-1,6-bisphosphate aldolase during anoxia in the tolerant turtle, Trachemys scripta elegans: an assessment of enzyme activity, expression and structureAlteration of de novo glucose production contributes to fasting hypoglycaemia in Fyn deficient mice.A novel adaptation of aldolase regulates virulence in Streptococcus pyogenesRegulation of the multiple promoters of the human aldolase A gene: response of its two ubiquitous promoters to agents promoting cell proliferation.Subunit interface mutants of rabbit muscle aldolase form active dimersDetailed expression pattern of aldolase C (Aldoc) in the cerebellum, retina and other areas of the CNS studied in Aldoc-Venus knock-in mice.Gene duplication in tetraploid fish: model for gene silencing at unlinked duplicated loci.Isoenzymes and ontogeny.Biochemistry of Coxiella burnetii: Embden-Meyerhof pathway.Purification and properties of the native form of rabbit liver aldolase. Evidence for proteolytic modification after tissue extraction.Evolutionary and functional analysis of fructose bisphosphate aldolase of plant parasitic nematodes.A comparative study of aldolase from human muscle and liver.Human monoclonal antibody recognizing liver-type aldolase B.Substrate modulation of aldolase B binding in hepatocytes.Biochemical characterization of the mouse muscle-specific enolase: developmental changes in electrophoretic variants and selective binding to other proteins.Mechanistic characterization of a bacterial malonate semialdehyde decarboxylase: identification of a new activity on the tautomerase superfamily.Thermodynamic analysis of the dissociation of the aldolase tetramer substituted at one or both of the subunit interfaces.Two Class I Aldolases in the Green Alga Chara foetida (Charophyceae).Monoclonal antibody to aldolase C: a selective marker for Purkinje cells in the human cerebellum.Subunit-specific radioimmunoassay for aldolase A, B, and C subunits: clinical significance.ALDOB tetramer cleaves Fru-1-P to GA and DHAPStructure determinations of FDP aldolase and the fine resolution of some glycolytic enzymes by isoelectric focusing.
P2860
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P2860
Distribution of fructose diphosphate aldolase variants in biological systems
description
1969 թուականի Յունուարին հրատարակուած գիտական յօդուած
@hyw
1969 թվականի հունվարին հրատարակված գիտական հոդված
@hy
artículu científicu espublizáu en 1969
@ast
im Januar 1969 veröffentlicher wissenschaftlicher Artikel
@de
scientific journal article
@en
vedecký článok (publikovaný 1969/01/01)
@sk
vědecký článek publikovaný v roce 1969
@cs
wetenschappelijk artikel (gepubliceerd op 1969/01/01)
@nl
наукова стаття, опублікована в січні 1969
@uk
مقالة علمية (نشرت عام 1969)
@ar
name
Distribution of fructose diphosphate aldolase variants in biological systems
@ast
Distribution of fructose diphosphate aldolase variants in biological systems
@en
Distribution of fructose diphosphate aldolase variants in biological systems
@nl
type
label
Distribution of fructose diphosphate aldolase variants in biological systems
@ast
Distribution of fructose diphosphate aldolase variants in biological systems
@en
Distribution of fructose diphosphate aldolase variants in biological systems
@nl
prefLabel
Distribution of fructose diphosphate aldolase variants in biological systems
@ast
Distribution of fructose diphosphate aldolase variants in biological systems
@en
Distribution of fructose diphosphate aldolase variants in biological systems
@nl
P356
P1433
P1476
Distribution of fructose diphosphate aldolase variants in biological systems
@en
P2093
H. G. Lebherz
W. J. Rutter
P304
P356
10.1021/BI00829A016
P407
P577
1969-01-01T00:00:00Z