About: Glyceraldehyde 3-Phosphate Dehydrogenase from Pig Muscle

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scientific article published in Nature

Attributes	Values
rdf:type	Item
description	artículu científicu (ast) wetenschappelijk artikel (nl) article publié dans la revue scientifique Nature (fr) scientific article published in Nature (en) im September 1968 veröffentlichter wissenschaftlicher Artikel (de) наукова стаття, опублікована в Nature у вересні 1968 (uk)
publication date	wds:Q59056349-FA47E31E-296C-4CCD-8DA6-7186F289DFAD
publication date	1968-09-01 00:00:00Z (xsd:dateTime)
language of work or name	wds:Q59056349-A37A22FC-F170-48A1-8612-E8C8EEB63C08
language of work or name	English
exact match	wds:Q59056349-0F04AD1A-B385-4321-8C4C-D7FE61511D74
exact match	https://scigraph.springernature.com/pub.10.1038/2191025a0
cites work	wds:Q59056349-072DC87D-E6D9-4BE1-8FFF-CCBFD7455432 wds:Q59056349-604B638C-BD7F-4E72-85EC-B0976E7E279C wds:Q59056349-9DA98D22-15A3-44FC-BCFB-9C0E02C768C3 wds:Q59056349-AB11E98C-2126-454A-8733-DF25511FC77F wds:Q59056349-D6852A4F-CFA7-45EB-A2D5-D0302FAA0600 wds:Q59056349-E8574D51-CBAB-4B11-834A-BE258A05D9D6 wds:Q59056349-EB5C6FBF-0DA5-4828-B0E1-7523CF7724EC
cites work	Electrophoretic Mobilities of Peptides on Paper and their Use in the Determination of Amide Groups AMINO ACID SEQUENCES AROUND THE REACTIVE CYSTEINE RESIDUES IN GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASES Amino-acid Sequence of Glyceraldehyde 3-Phosphate Dehydrogenase from Lobster Muscle Chemical Nature of the Catalytic Sites in Glyceraldehyde-3-Phosphate Dehydrogenase Amino acid sequence around a reactive lysine in glyceraldehyde 3-phosphate dehydrogenase Structure of Glyceraldehyde-3-Phosphate Dehydrogenase: Structural Symmetry Within the Molecule THE CRYSTAL STRUCTURE OF LACTIC DEHYDROGENASE.
author name string	wds:Q59056349-35950637-7E8B-4396-BC92-23002806535C wds:Q59056349-FE45576B-4453-4D3E-A8C8-E2AD083A2F90
author name string	R N Perham J I Harris
rdfs:label	Glyceraldehyde 3-Phosphate Dehydrogenase from Pig Muscle (en) Glyceraldehyde 3-Phosphate Dehydrogenase from Pig Muscle (nl)
skos:prefLabel	Glyceraldehyde 3-Phosphate Dehydrogenase from Pig Muscle (en) Glyceraldehyde 3-Phosphate Dehydrogenase from Pig Muscle (nl)
name	Glyceraldehyde 3-Phosphate Dehydrogenase from Pig Muscle (en) Glyceraldehyde 3-Phosphate Dehydrogenase from Pig Muscle (nl)
title	wds:Q59056349-DD15AD6A-A3A1-4189-B197-ADC63A133624
title	Glyceraldehyde 3-phosphate dehydrogenase from pig muscle (en)
page(s)	wds:Q59056349-A8DE649A-A336-4626-934B-EB48013E5616
page(s)	1025-1028
instance of	wds:Q59056349-B7693B09-51B0-476A-BEF5-9C84AC1007CC
instance of	scholarly article
main subject	wds:Q59056349-AA725465-F0D0-4928-BECC-0BC8CAE0994E
main subject	pig
PubMed ID	wds:Q59056349-6890B068-2DF2-4FE4-A155-7D388D6EA401
PubMed ID	http://rdf.ncbi.nlm.nih.gov/pubchem/reference/4299800
PubMed ID	4299800
published in	wds:Q59056349-730AA623-18C3-41D7-A2DC-4666B7B4F2B6
published in	Nature
issue	wds:Q59056349-3DFE9581-1C24-46B7-9EB8-CE74FED540E1
volume	wds:Q59056349-8CC4CA8E-6BD9-4396-AB75-A15BA880343C
issue	5158
volume	219
DOI	wds:Q59056349-28644243-29BD-441F-AA60-295DB2A732CE
DOI	http://dx.doi.org/10.1038/2191025A0
DOI	10.1038/2191025A0
Dimensions Publication ID	wds:Q59056349-A73C93CE-7D09-49D2-B727-7B83E6AE374E
Dimensions Publication ID	1025244829
is about of	https://www.wikidata.org/wiki/Special:EntityData/Q59056349
is cites work of	The glyceraldehyde 3 phosphate dehydrogenase gene family: structure of a human cDNA and of an X chromosome linked pseudogene; amazing complexity of the gene family in mouse The coenzyme-binding domains of glutamate dehydrogenases Chemical and biological evolution of nucleotide-binding protein Differences between Alcohol Dehydeogenases. Structural Properties and Evolutionary Aspects Horse Liver Alcohol Dehydrogenase. The Primary Structure of the Protein Chain of the Ethanol-Active Isoenzyme Hela cytosolic protein isolated by poly (A)-sepharose chromatography is glyceraldehyde-3-P-dehydrogenase Half-site reactivity Structure of Lactate Dehydrogenase at 2.8 Å Resolution Triose phosphate isomerase from the coelacanth. An approach to the rapid determination of an amino acid sequence with small amounts of material Pressure stabilization of proteins from extreme thermophiles The isolation and functional identification of a protein from the human erythrocyte 'ghost'. The use of maleic anhydride for the reversible blocking of amino groups in polypeptide chains 9-azidoacridine, a new photoaffinity label for nucleotide- and aromatic-binding sites in proteins A simplified electrophoretic system for determining molecular weights of proteins The complete amino acid sequence of human muscle glyceraldehyde 3-phosphate dehydrogenase Mannitol-specific phosphoenolpyruvate-dependent phosphotransferase system of Enterococcus faecalis: molecular cloning and nucleotide sequences of the enzyme IIIMtl gene and the mannitol-1-phosphate dehydrogenase gene, expression in Escherichia coli, Temperature adaptation of enzymes: roles of the free energy, the enthalpy, and the entropy of activation The stoichiometry of polypeptide chains in the pyruvate dehydrogenase multienzyme complex of E. coli determined by a simple novel method A glyceraldehyde-3-phosphate dehydrogenase pseudogene on the short arm of the human X chromosomes defines a multigene family Studies on the subunit structure of thermostable glyceraldehyde-3-phosphate dehydrogenase from Bacillus stearothermophilus Molecular analysis of glyceraldehyde-3-phosphate dehydrogenase in Trypanoplasma borelli: an evolutionary scenario of subcellular compartmentation in kinetoplastida The complete sequence of a full length cDNA for human liver glyceraldehyde-3-phosphate dehydrogenase: evidence for multiple mRNA species. The investigation of substrate-induced changes in subunit interactions in glyceraldehyde 3-phosphate dehydrogenases by measurement of the kinetics and thermodynamics of subunit exchange 4-Hydroxy-2(E)-nonenal enantiomers: (S)-selective inactivation of glyceraldehyde-3-phosphate dehydrogenase and detoxification by rat glutathione S-transferase A4-4. Hybridization of glyceraldehyde-3-phosphate dehydrogenase. Purification and characterization of a novel form of 20 alpha-hydroxysteroid dehydrogenase from Clostridium scindens Human Glyceraldehyde-3-Phosphate Dehydrogenase in Man-Rodent Somatic Cell Hybrids A glyceraldehyde-3-phosphate dehydrogenase with eubacterial features in the amitochondriate eukaryote, Trichomonas vaginalis. Structure of the tubulin dimer Ion-Pair Formation as a Source of Enhanced Reactivity of the Essential Thiol Group of d-Glyceraldehyde-3-Phosphate Dehydrogenase Similarity in the sequence of Escherichia coli dihydrofolate reductase with other pyridine nucleotide-requiring enzymes Intron-dependent evolution of chicken glyceraldehyde phosphate dehydrogenase gene A comparison of the glyceraldehyde 3-phosphate dehydrogenase from ox muscle and liver Bovine Liver Glutamate Dehydrogenase: Tentative Amino Acid Sequence; Identification of a Reactive Lysine; Nitration of a Specific Tyrosine and Loss of Allosteric Inhibition by Guanosine Triphosphate The Primary Structure of Yeast Alcohol Dehydrogenase Glyceraldehyde-3-phosphate dehydrogenase from liver—II. Comparative studies from different species The primary structure of a glyceraldehyde-3-phosphate dehydrogenase gene from Saccharomyces cerevisiae Immunoglobulin production stimulating factor-II alpha (IPSF-II alpha) is glyceraldehyde-3-phosphate dehydrogenase like protein D-glyceraldehyde-3-phosphate dehydrogenase: three-dimensional structure and evolutionary significance A lysine in the ATP-binding site of P130gag-fps is essential for protein-tyrosine kinase activity.

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