About: Chemical Nature of the Catalytic Sites in Glyceraldehyde-3-Phosphate Dehydrogenase

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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 April 1963 veröffentlichter wissenschaftlicher Artikel (de) наукова стаття, опублікована в Nature у квітні 1963 (uk)
publication date	wds:Q59086791-F0535405-51C3-4528-B8E5-7EC596E05262
publication date	1963-04-01 00:00:00Z (xsd:dateTime)
language of work or name	wds:Q59086791-DF5F6463-C8C2-402B-9D61-38244B6B4C59
language of work or name	English
exact match	wds:Q59086791-B73DA921-2C54-4576-BBC8-98CE2582BA6F
exact match	https://scigraph.springernature.com/pub.10.1038/198154a0
cites work	wds:Q59086791-5F3CC9BD-93C0-487E-BA44-F24671FB75A6 wds:Q59086791-6F14C3B7-8960-4C60-B0D2-AC7F17E6C298 wds:Q59086791-71A0807E-506B-4B8C-8058-2E4D2EA5358E wds:Q59086791-84EA282E-04FD-4553-BCB6-5F2E92190607 wds:Q59086791-8F80148D-CCD6-43EC-B11D-3DA37803E088 wds:Q59086791-B1827703-9B70-48AF-AE8F-73AE372B2D03 wds:Q59086791-B3B62C5F-0A66-43F3-9AA8-3305F78A04CB wds:Q59086791-DB72A575-BCC9-4D5E-A916-FE6474819235
cites work	Aldehyde mutase The active site of esterases The molecular weights of some crystalline enzymes from muscle and yeast. I. Aldolase and D-glyceraldehyde-3-phosphate dehydrogenase Sulphydryl groups and enzymic oxido-reduction Dismutations and oxidoreductions Acyl derivatives of glyceraldehyde-3-phosphate dehydrogenase Mechanism of Action and Properties of Pyridine Nucleotide-Linked Enzymes Amino-acid Sequence about the Reactive Serine of a Proteolytic Enzyme from Bacillus subtilis
author name string	wds:Q59086791-14348D52-5BFC-4A96-8DE1-3160BD9F732F wds:Q59086791-5D80AA0F-49F8-4753-BE06-84041CA4E75F wds:Q59086791-7BCE779A-DEAF-4203-B44C-18128290BD3B
author name string	B P MERIWETHER I HARRIS J H PARK
rdfs:label	Chemical Nature of the Catalytic Sites in Glyceraldehyde-3-Phosphate Dehydrogenase (en) Chemical Nature of the Catalytic Sites in Glyceraldehyde-3-Phosphate Dehydrogenase (nl)
skos:prefLabel	Chemical Nature of the Catalytic Sites in Glyceraldehyde-3-Phosphate Dehydrogenase (en) Chemical Nature of the Catalytic Sites in Glyceraldehyde-3-Phosphate Dehydrogenase (nl)
name	Chemical Nature of the Catalytic Sites in Glyceraldehyde-3-Phosphate Dehydrogenase (en) Chemical Nature of the Catalytic Sites in Glyceraldehyde-3-Phosphate Dehydrogenase (nl)
title	wds:Q59086791-C17697BD-41E4-4D85-9E7B-EBADE661DDFE
title	Chemical nature of the catalytic sites in glyceraldehyde-3-phosphate dehydrogenase (en)
page(s)	wds:Q59086791-AF4D75B3-82B5-4308-94CC-E48DEEADFCDF
page(s)	154-157
instance of	wds:Q59086791-4BDE9FC3-3A90-49B2-8ECB-5C682492B58B
instance of	scholarly article
PubMed ID	wds:Q59086791-4B92BFD7-D28F-46A6-B727-5253F867D135
PubMed ID	http://rdf.ncbi.nlm.nih.gov/pubchem/reference/13952929
PubMed ID	13952929
published in	wds:Q59086791-C807CBF3-0C27-4D74-BE53-698A0B88F43F
published in	Nature
issue	wds:Q59086791-F9ADCB2F-A5AA-489E-87DD-C7450141045E
volume	wds:Q59086791-13D5E34B-869F-417A-95C0-E57BE08BD248
issue	4876
volume	198
DOI	wds:Q59086791-C7A63E7C-095C-4762-9115-87FFF25C5C28
DOI	http://dx.doi.org/10.1038/198154A0
DOI	10.1038/198154A0
Dimensions Publication ID	wds:Q59086791-D24751E8-928F-4C21-B9B0-F3BEF45A5541
Dimensions Publication ID	1045789494
is about of	https://www.wikidata.org/wiki/Special:EntityData/Q59086791
is cites work of	Partial Similarities Between Yeast and Liver Alcohol Dehydrogenases Structure and Catalytic Activity of Alcohol Dehydrogenases Hydrolysis of Proteins Convergence of nitric oxide and lipid signaling: anti-inflammatory nitro-fatty acids. The role of biotin-dependent carboxylations in biosynthetic reactions The gel-filtration behaviour of proteins related to their molecular weights over a wide range Characterization of a Malonyl-Enzyme Intermediate and Identification of the Malonyl Binding Site in Malonyl Coenzyme A-Acyl Carrier Protein Transacylase of Escherichia coli Reversible post-translational modification of proteins by nitrated fatty acids in vivo The comparative structure of mammalian glyceraldehyde 3-phosphate dehydrogenases Mechanism of action of uridine diphosphoglucose dehydrogenase. Evidence for a second reversible dehydrogenation step involving an essential thiol group Udpglucose dehydrogenase Kinetics and their mechanistic implications Reaction of Yeast Fatty Acid Synthetase with Iodoacetamide. 2. Identification of the Amino Acid Residues Reacting with Iodoacetamide and Primary Structure of a Peptide Containing the Peripheral Sulfhydryl Group Structural and motional changes in glyceraldehyde-3-phosphate dehydrogenase upon binding to the band-3 protein of the erythrocyte membrane examined with [15N,2H]maleimide spin label and electron paramagnetic resonance Sequence and structure of D-glyceraldehyde 3-phosphate dehydrogenase from Bacillus stearothermophilus Covalent Labeling of Active Sites Structure and evolution of triose phosphate and lactate dehydrogenases Mechanism of Peroxide-Inactivation of the Sulphydryl Enzyme Glyceraldehyde-3-Phosphate Dehydrogenase AMINO ACID SEQUENCES AROUND THE REACTIVE CYSTEINE RESIDUES IN GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASES Properties of acyl glucuronides: implications for studies of the pharmacokinetics and metabolism of acidic drugs Amino-acid Sequence of Glyceraldehyde 3-Phosphate Dehydrogenase from Lobster Muscle The isolation and specific activity of rabbit-muscle glyceraldehyde phosphate dehydrogenase Glyceraldehyde-3-phosphate dehydrogenase from liver—II. Comparative studies from different species Cy5 maleimide labelling for sensitive detection of free thiols in native protein extracts: identification of seed proteins targeted by barley thioredoxin h isoforms Specificity of induced conformational changes. Case of yeast glyceraldehyde-3-phosphate dehydrogenase Catalytic and regulatory properties of D-glyceraldehyde-3-phosphate dehydrogenase in the crystal. Spectral properties and chemical reactivity of a chromophoric acyl-enzyme intermediate Covalent Enzyme-Substrate Intermediates Glyceraldehyde 3-Phosphate Dehydrogenase from Pig Muscle Aspects of the chemistry of D-glyceraldehyde 3-phosphate dehydrogenase 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 Use of methanethiolation to investigate the catalytic role of sulphydryl groups in rabbit skeletal muscle pyruvate kinase 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 Subunit conformation and catalytic function in rabbit-muscle glyceraldehyde-3-phosphate dehydrogenase The Mechanism of Inactivation of Glyceraldehyde 3-Phosphate Dehydrogenase by Tetrathionate, o-Iodosobenzoate, and Iodine Monochloride Effect of sodium nitrite inhibition on intracellular thiol groups and on the activity of certain glycolytic enzymes in Clostridium perfringens The subunit size of alcohol dehydrogenates. Structural Studies of Pig Heart Malate Dehydrogenase Amino acid sequence homology in alcohol dehydrogenase Reversible dinitrophenylation of glyceraldehyde 3-phosphate dehydrogenase. Identification of the labeled site

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