About: Amino-acid Sequence of Glyceraldehyde 3-Phosphate Dehydrogenase from Lobster Muscle

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scientific article published in Nature

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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 Dezember 1967 veröffentlichter wissenschaftlicher Artikel (de) наукова стаття, опублікована в Nature в грудні 1967 (uk)
publication date	wds:Q59076368-A1773FA7-B2D3-4406-98E7-0639488D47FC
publication date	1967-12-01 00:00:00Z (xsd:dateTime)
language of work or name	wds:Q59076368-3C550BC5-8169-4FE3-B755-3C244243D0E9
language of work or name	English
exact match	wds:Q59076368-5C8B58DA-E6A6-453D-98E4-5968028D6776
exact match	https://scigraph.springernature.com/pub.10.1038/2161181a0
cites work	wds:Q59076368-109D5A09-0FF0-48A4-BC7D-8E69DE926C0D wds:Q59076368-26E6FAEF-4465-48D6-98C7-0D74BA6478CC wds:Q59076368-27ABADF6-BEDD-4CF0-BA39-EB8564D44EA5 wds:Q59076368-4BDD5549-4EF4-4FFC-AAA9-8D07220F91D0 wds:Q59076368-9431265C-B532-4646-B28C-3C2924AEF2EC wds:Q59076368-9639D93E-FD70-416A-BBC5-0CD695F16079 wds:Q59076368-96BC9DB3-48E8-4DA2-8155-62ACB8ABE011 wds:Q59076368-98871A96-8BA0-4862-A62E-4BE8EEE7B477 wds:Q59076368-9C86D87F-1616-4BFC-9A92-67ACEF691ADA wds:Q59076368-AC65EEE9-3F7A-4BBD-8753-5327944138ED wds:Q59076368-CD8565AE-3253-42BE-9E58-89E710F3541F wds:Q59076368-DA8205DA-2420-45D3-9358-9E23E1AA66CF wds:Q59076368-F6FD5845-DA9A-44FD-A3C5-31A08F4301EA
cites work	Electrophoretic Mobilities of Peptides on Paper and their Use in the Determination of Amide Groups Three-dimensional Structure of Tosyl-α-chymotrypsin THE STRUCTURE OF A CHYMOTRYPTIC PEPTIDE FROM PSEUDOMONAS CYTOCHROME C-551 The binding of nicotinamide-adenine dinucleotide to yeast d-glyceraldehyde-3-phosphate dehydrogenase: temperature-jump relaxation studies on the mechanism of an allosteric enzyme THE HEN EGG-WHITE LYSOZYME MOLECULE. AMINO ACID SEQUENCES AROUND THE REACTIVE CYSTEINE RESIDUES IN GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASES The isolation and specific activity of rabbit-muscle glyceraldehyde phosphate dehydrogenase Chemical Nature of the Catalytic Sites in Glyceraldehyde-3-Phosphate Dehydrogenase The determination of the order of lysine-containing tryptic peptides of proteins by diagonal paper electrophoresis. A carboxyl-terminal sequence for pepsin. Amino acid sequence around a reactive lysine in glyceraldehyde 3-phosphate dehydrogenase An extended amino acid sequence around the reactive cysteine residues of 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:Q59076368-3DD58019-C8D9-4C39-9EE3-6371C311675B wds:Q59076368-565DA7F9-2F22-4AA4-B25C-683F21C5DDD7 wds:Q59076368-A1A4300B-8E19-464B-B8DF-7BCD9F3C2563 wds:Q59076368-E2CE4535-1241-41FE-941E-93C347B61EB3
author name string	H F Noller B E Davidson J I Harris M Sajgò
rdfs:label	Amino-acid Sequence of Glyceraldehyde 3-Phosphate Dehydrogenase from Lobster Muscle (en) Amino-acid Sequence of Glyceraldehyde 3-Phosphate Dehydrogenase from Lobster Muscle (nl)
skos:prefLabel	Amino-acid Sequence of Glyceraldehyde 3-Phosphate Dehydrogenase from Lobster Muscle (en) Amino-acid Sequence of Glyceraldehyde 3-Phosphate Dehydrogenase from Lobster Muscle (nl)
name	Amino-acid Sequence of Glyceraldehyde 3-Phosphate Dehydrogenase from Lobster Muscle (en) Amino-acid Sequence of Glyceraldehyde 3-Phosphate Dehydrogenase from Lobster Muscle (nl)
title	wds:Q59076368-3E5E1D09-F842-4292-A369-5879178B3B1E
title	Amino-acid sequence of glyceraldehyde 3-phosphate dehydrogenase from lobster muscle (en)
page(s)	wds:Q59076368-25573E9A-7766-400E-A069-2A32B44A7165
page(s)	1181-1185
instance of	wds:Q59076368-94029B94-1521-499F-834F-444E386BCA7C
instance of	scholarly article
PubMed ID	wds:Q59076368-B18280C7-3DB5-4EE0-B273-40B893581C19
PubMed ID	http://rdf.ncbi.nlm.nih.gov/pubchem/reference/4294736
PubMed ID	4294736
published in	wds:Q59076368-483A825E-5462-49F8-9590-EF89A9A34433
published in	Nature
issue	wds:Q59076368-A0980366-B63C-4999-B598-443105514E09
volume	wds:Q59076368-04E5A915-54C8-42FD-9EB6-9FD68D2BFA2B
issue	5121
volume	216
DOI	wds:Q59076368-B974E377-BB3C-40A9-9933-31564C919FF9
DOI	http://dx.doi.org/10.1038/2161181A0
DOI	10.1038/2161181A0
Dimensions Publication ID	wds:Q59076368-BEF2F570-1FCE-4918-829A-43567FAA4FA8
Dimensions Publication ID	1006946284
is about of	https://www.wikidata.org/wiki/Special:EntityData/Q59076368
is cites work of	Analysis of the allosteric basis for positive and negative co-operativity and half-of-the-sites reactivity in yeast and rabbit muscle glyceraldehyde 3-phosphate dehydrogenase Molecular characterization of the gene cluster coxMSL encoding the molybdenum-containing carbon monoxide dehydrogenase of Oligotropha carboxidovorans The coenzyme-binding domains of glutamate dehydrogenases Chemical and biological evolution of nucleotide-binding protein Partial Similarities Between Yeast and Liver Alcohol Dehydrogenases 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 Predicted nucleotide-binding properties of p21 protein and its cancer-associated variant Hela cytosolic protein isolated by poly (A)-sepharose chromatography is glyceraldehyde-3-P-dehydrogenase Half-site reactivity Use of Dimethyl Suberimidate, a Cross-Linking Reagent, in Studying the Subunit Structure of Oligomeric Proteins Evidence that approximately eighty per cent of the soluble proteins from Ehrlich ascites cells are Nalpha-acetylated 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 use of maleic anhydride for the reversible blocking of amino groups in polypeptide chains The complete amino acid sequence of human muscle glyceraldehyde 3-phosphate dehydrogenase Complete sequence of the chicken glyceraldehyde-3-phosphate dehydrogenase gene. Purification and Properties of d-Glyceraldehyde-3-Phosphate Dehydrogenase from an Extreme Thermophile, Thermus thermophilus Strain HB 8 The comparative structure of mammalian glyceraldehyde 3-phosphate dehydrogenases Studies on the subunit structure of thermostable glyceraldehyde-3-phosphate dehydrogenase from Bacillus stearothermophilus 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 Sequence and structure of D-glyceraldehyde 3-phosphate dehydrogenase from Bacillus stearothermophilus Purification and characterization of a novel form of 20 alpha-hydroxysteroid dehydrogenase from Clostridium scindens Flavin reductase: sequence of cDNA from bovine liver and tissue distribution Intron-dependent evolution of chicken glyceraldehyde phosphate dehydrogenase gene

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