scholarly article | Q13442814 |
P356 | DOI | 10.1042/BJ1510037 |
P953 | full work available at URL | https://europepmc.org/articles/PMC1172322 |
https://europepmc.org/articles/PMC1172322?pdf=render | ||
https://portlandpress.com/biochemj/article-pdf/151/1/37/564985/bj1510037.pdf | ||
https://www.ncbi.nlm.nih.gov/pmc/articles/pmid/174555/?tool=EBI | ||
https://www.ncbi.nlm.nih.gov/pmc/articles/pmid/174555/pdf/?tool=EBI | ||
P932 | PMC publication ID | 1172322 |
P698 | PubMed publication ID | 174555 |
P5875 | ResearchGate publication ID | 22960354 |
P2093 | author name string | H. H. Osborne | |
M. R. Hollaway | |||
P2860 | cites work | Co-operative binding of nicotinamide-adenine dinucleotide to yeast glyceraldehyde-3-phosphate dehydrogenase. I. Equilibrium and temperature-jump studies at pH 8-5 and 40 degrees C | Q28239759 |
Activation of a covalent enzyme-substrate bond by noncovalent interaction with an effector | Q35108446 | ||
Rate-determining processes and the number of simultaneously active sties of D-glyceraldehyde 3-phosphate dehydrogenase | Q41761059 | ||
The hybridization of glyceraldehyde 3-phosphate dehydrogenases from rabbit muscle and yeast. Kinetics and thermodynamics of the reaction and isolation of the hybrid | Q41873191 | ||
Aspects of the chemistry of D-glyceraldehyde 3-phosphate dehydrogenase | Q42152246 | ||
Functional non-identity of subunits and isolation of active dimers of D-glyceraldehyde-3-phosphate dehydrogenase | Q44119202 | ||
Effect of D2O and nicotinamide adenine dinucleotide on the sedimentation properties and structure of glyceraldehyde phosphate dehydrogenase | Q44831169 | ||
Hybridization of glyceraldehyde-3-phosphate dehydrogenase | Q47841162 | ||
Binding of NAD + and NADH to rabbit-muscle glyceraldehydephosphate dehydrogenase. | Q53771251 | ||
Positive and negative cooperativity in yeast glyceraldehyde 3-phosphate dehydrogenase. | Q53913851 | ||
The binding of oxidized and reduced nicotinamide adenine-dinucleotide to yeast glyceraldehyde-3-phosphate dehydrogenase. | Q54123955 | ||
Half-of-the-sites and all-of-the-sites reactivity in rabbit muscle glyceraldehyde 3-phosphate dehydrogenase. | Q54335404 | ||
Glyceraldehyde 3-Phosphate Dehydrogenase from Pig Muscle | Q59056349 | ||
Amino-acid Sequence of Glyceraldehyde 3-Phosphate Dehydrogenase from Lobster Muscle | Q59076368 | ||
Coenzyme-induced changes in the optical rotatory dispersion properties of glyceraldehyde 3-phosphate dehydrogenase | Q68553044 | ||
Reversible inactivation of dehydrogenases | Q68560672 | ||
Negative cooperativity in enzyme action. The binding of diphosphopyridine nucleotide to glyceraldehyde 3-phosphate dehydrogenase | Q68586060 | ||
Co-operative binding of nicotinamide-adenine dinucleotide to yeast glyceraldehyde-3-phosphate dehydrogenase. II. Stopped-flow studies at pH 8-5 and 40 degrees C | Q68626180 | ||
The binding of NAD+ to rabbit muscle glyceraldehyde-3-phosphate dehydrogenase studied by protein fluorescence quenching | Q68626327 | ||
Structure-function studies on glyceraldehyde 3-phosphate dehydrogenase. IV. Subunit interactions of the rabbit muscle and yeast enzymes | Q68638480 | ||
Study of the position of NAD and its effect on the conformation of D-glyceraldehyde-3-phosphate dehydrogenase by small-angle x-ray scattering | Q68650322 | ||
Adenine nucleotide-mediated subunit exchange between isoenzymes of glyceraldehyde-3-phosphate dehydrogenase | Q68672490 | ||
Structure-function relationship in rabbit muscle glyceraldehyde-3-phosphate dehydrogenase. Trinitrophenylation of the lysine residues | Q68695919 | ||
Three-dimensional structure of D-glyceraldehyde-3-phosphate dehydrogenase | Q68708412 | ||
Half-of-the-sites reactivity and negative co-operativity: The case of yeast glyceraldehyde 3-phosphate dehydrogenase | Q69333311 | ||
Hybrid Molecules of Yeast and Rabbit GPD containing Native and Modified Subunits | Q71502868 | ||
Thermodynamics of nicotinamide-adenine dinucleotide addition to the glyceraldehyde 3-phosphate dehydrogenases of yeast and of rabbit skeletal muscle. An equilibrium and calorimetric analysis over a range of temperatures | Q71759956 | ||
On the mechanism of the dissociation of haemoglobin | Q72241605 | ||
The coenzyme content of rabbit muscle D-glyceraldehyde-3-phosphate dehydrogenase | Q74214919 | ||
AMINO ACID SEQUENCES AROUND THE REACTIVE CYSTEINE RESIDUES IN GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASES | Q76568884 | ||
Glyceraldehyde 3-phosphate dehydrogenase: Amino acid sequence of enzyme from baker's yeast | Q77919701 | ||
Inactivation of muscle triosephosphate dehydrogenase by reduced diphosphopyridine nucleotide at physiological concentrations | Q79431818 | ||
P433 | issue | 1 | |
P407 | language of work or name | English | Q1860 |
P921 | main subject | biochemistry | Q7094 |
cell biology | Q7141 | ||
P1104 | number of pages | 9 | |
P304 | page(s) | 37-45 | |
P577 | publication date | 1975-10-01 | |
P1433 | published in | Biochemical Journal | Q864221 |
P1476 | title | The investigation of substrate-induced changes in subunit interactions in glyceraldehyde 3-phosphate dehydrogenases by measurement of the kinetics and thermodynamics of subunit exchange | |
P478 | volume | 151 |
Q40013505 | An investigation of the nicotinamide-adenine dinucleotide-induced ‘tightening’ of the structure of glyceraldehyde 3-phosphate dehydrogenase |
Q41665016 | Effect of association-dissociation on the catalytic properties of glyceraldehyde 3-phosphate dehydrogenase |
Q47409048 | Interaction of enzymes involved in triosephosphate metabolism. Comparison of yeast and rabbit muscle cytoplasmic systems |
Q42268023 | Kinetic behaviour and oligomeric state of 3-phosphoglyceroyl-D-glyceraldehyde-3-phosphate dehydrogenase |
Q40123136 | Mechanism of Reactivation and Refolding of Glyceraldehyde-3-Phosphate Dehydrogenase from Yeast after Denaturation and Dissociation |
Q39657569 | Recombinant human sperm-specific glyceraldehyde-3-phosphate dehydrogenase (GAPDHS) is expressed at high yield as an active homotetramer in baculovirus-infected insect cells |
Q40857509 | Role of Lysine-183 in d-Glyceraldehyde-3-Phosphate Dehydrogenases. Properties of the N-Acetylated Yeast, Sturgeon Muscle and Rabbit Muscle Enzymes |
Q48633570 | Sevoflurane modulates the activity of glyceraldehyde 3-phosphate dehydrogenase |
Q27656083 | Structure of Insoluble Rat Sperm Glyceraldehyde-3-phosphate Dehydrogenase (GAPDH) via Heterotetramer Formation with Escherichia coli GAPDH Reveals Target for Contraceptive Design |
Q28330810 | Synthesis and use of bifunctional chloromethylalkanedione derivatives of variable chain length for cross-linking thiol groups in oligomeric proteins. Specific cross-linking in glyceraldehyde 3-phosphate dehydrogenase |
Q40264682 | The development of SS′-polymethylenebis(methanethiosulphonates) as reversible cross-linking reagents for thiol groups and their use to form stable catalytically active cross-linked dimers within glyceraldehyde 3-phosphate dehydrogenase |
Q39984485 | The effect of substrates on the association equilibrium of mammalian D-glyceraldehyde 3-phosphate dehydrogenase |
Q28326455 | The reaction of rabbit muscle creatine kinase with some derivatives of iodoacetamide |
Q70473244 | [Comparative study on the chemical modification of sulfhydryl groups of glyceraldehyde-3-phosphate dehydrogenases from yeast and rabbit muscle. The relationship between structure and chemical reactivity] |
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