| scholarly article | Q13442814 |
| P356 | DOI | 10.1016/0006-291X(75)90279-X |
| P953 | full work available at URL | https://api.elsevier.com/content/article/PII:0006291X7590279X?httpAccept=text/xml |
| https://api.elsevier.com/content/article/PII:0006291X7590279X?httpAccept=text/plain | ||
| P698 | PubMed publication ID | 1201027 |
| P2093 | author name string | J. Tang | |
| K. W. Jackson | |||
| K. D. Kulbe | |||
| P2860 | cites work | Chemical and biological evolution of nucleotide-binding protein | Q28240624 |
| Co-operative binding of nicotinamide-adenine dinucleotide to yeast glyceraldehyde-3-phosphate dehydrogenase | Q29395244 | ||
| Strategy and tactics in protein chemistry | Q39995528 | ||
| Liver 3-Phosphoglycerate Kinase. Physico-Chemical Characterization of the Bovine-Liver Enzyme | Q41782702 | ||
| The use of maleic anhydride for the reversible blocking of amino groups in polypeptide chains | Q42938457 | ||
| Glyceraldehydephosphate dehydrogenase from liver. I. Isolation and characterization of the bovine liver enzyme. | Q44372710 | ||
| Liver 3-phosphoglycerate kinase. Purification and some molecular properties of the bovine-liver enzyme. | Q53680729 | ||
| Micropolyamide thin-layer chromatography of phenylthiohydantoin amino acids (PTH) at subnanomolar level. A rapid microtechnique for simultaneous multisample identification after automated Edman degradations | Q54568142 | ||
| Glyceraldehyde 3-Phosphate Dehydrogenase from Pig Muscle | Q59056349 | ||
| Amino-acid Sequence of Glyceraldehyde 3-Phosphate Dehydrogenase from Lobster Muscle | Q59076368 | ||
| Identification of subnanomole amounts of phenylthiohydantoins of the cysteine and methionine derivatives most commonly obtained in protein sequencing | Q66918164 | ||
| Negative cooperativity in enzyme action. The binding of diphosphopyridine nucleotide to glyceraldehyde 3-phosphate dehydrogenase | Q68586060 | ||
| Structural and functional similarities within the coenzyme binding domains of dehydrogenases | Q68706024 | ||
| Three-dimensional structure of D-glyceraldehyde-3-phosphate dehydrogenase | Q68708412 | ||
| A convenient method for preparative peptide separation | Q70457479 | ||
| Glyceraldehyde 3-phosphate dehydrogenase: Amino acid sequence of enzyme from baker's yeast | Q77919701 | ||
| P433 | issue | 1 | |
| P407 | language of work or name | English | Q1860 |
| P921 | main subject | biochemistry | Q7094 |
| biophysics | Q7100 | ||
| cell biology | Q7141 | ||
| P304 | page(s) | 35-42 | |
| P577 | publication date | 1975-11-01 | |
| 1975-11-03 | |||
| P1433 | published in | Biochemical and Biophysical Research Communications | Q864228 |
| P1476 | title | Structural evidence for a liver-specific glyceraldehyde-3-phosphate dehydrogenase | |
| P478 | volume | 67 |
| Q67259792 | 81 Simultaneous purification of glyceraldehyde-3-phosphate dehydrogenase, 3-phosphoglycerate kinase, and phosphoglycerate mutase from pig liver and muscle |
| Q45041118 | Glyceraldehyde-3-phosphate dehydrogenase is a GABAA receptor kinase linking glycolysis to neuronal inhibition. |
| Q43820336 | Structural studies on glyceraldehyde-phosphate dehydrogenase from rat skeletal muscle |
| Q39739755 | The Role of Isozymes in Metabolism: A Model of Metabolic Pathways as the Basis for the Biological Role of Isozymes |
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