Folding domains and intramolecular ionic interactions of lysine residues in glyceraldehyde 3-phosphate dehydrogenase

scientific article published on January 1, 1977

Folding domains and intramolecular ionic interactions of lysine residues in glyceraldehyde 3-phosphate dehydrogenase is …
instance of (P31):
scholarly articleQ13442814

External links are
P356DOI10.1042/BJ1610049
P953full work available at URLhttps://europepmc.org/articles/PMC1164473
https://europepmc.org/articles/PMC1164473?pdf=render
https://www.ncbi.nlm.nih.gov/pmc/articles/pmid/851424/?tool=EBI
https://www.ncbi.nlm.nih.gov/pmc/articles/pmid/851424/pdf/?tool=EBI
P932PMC publication ID1164473
P698PubMed publication ID851424
P5875ResearchGate publication ID22304365

P2093author name stringJ. M. Lambert
R. N. Perham
P2860cites workStudies of asymmetry in the three-dimensional structure of lobster D-glyceraldehyde-3-phosphate dehydrogenaseQ27641366
Intramolecular ionic interactions of lysine residues and a possible folding domain in fructose diphosphate aldolaseQ28331213
Identification of the lysine residue modified during the activation of acetimidylation of horse liver alcohol dehydrogenaseQ28339802
Molecular weight estimation of polypeptides by SDS-polyacrylamide gel electrophoresis: further data concerning resolving power and general considerationsQ36506307
Formation of non-amidine products in the reaction of primary amines with imido estersQ39066714
Formation of non-amidine products in the chemical modification of horse liver alcohol dehydrogenase with imido estersQ39066721
The action of trypsin on polylysineQ39222583
Studies of coenzyme binding to rabbit muscle glyceraldehyde-3-phosphate dehydrogenaseQ39941451
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Strategy and tactics in protein chemistryQ39995528
An amino acid sequence in the active site of lipoamide dehydrogenase from pig heartQ41767885
The reactivity of functional groups as a probe for investigating the topography of tobacco mosaic virus. The use of mutants with additional lysine residues in the coat proteinQ41789131
Competitive labelling, a method for determining the reactivity of individual groups in proteins. The amino groups of porcine elastaseQ42922762
The reaction of aldolase with 2-methylmaleic anhydrideQ42935293
The relation between pyridoxin and tryptophan metabolism, studied in the rat.Q42951791
Reactivity of Tobacco Mosaic Virus and Its Protein toward Acetic Anhydride*Q45808027
Reactivity and structural role of protein amino groups in tobacco mosaic virusQ45810508
The reaction between NAD+ and rabbit-muscle glyceraldehydephosphate dehydrogenase.Q54387300
The glyceraldehyde 3-phosphate dehydrogenases of liver and muscle. Cooperative interactions and conditions for functional reversibility.Q54728509
Glyceraldehyde 3-Phosphate Dehydrogenase from Pig MuscleQ59056349
Electrophoretic Mobilities of Peptides on Paper and their Use in the Determination of Amide GroupsQ59061104
Amino-acid Sequence of Glyceraldehyde 3-Phosphate Dehydrogenase from Lobster MuscleQ59076368
Stereochemical basis of heat stability in bacterial ferredoxins and in haemoglobin A2Q59089724
Sequence variability and structure of D-glyceraldehyde-3-phosphate dehydrogenaseQ66902906
Cross-linking of troponin with dimethylimido estersQ67513855
Enhancement of the activity of horse liver alcohol dehydrogenase by modification of amino groups at the active sitesQ68608000
The binding of NAD+ to rabbit muscle glyceraldehyde-3-phosphate dehydrogenase studied by protein fluorescence quenchingQ68626327
Glyceraldehyde 3-phosphate dehydrogenase of Bacillus stearothermophilus. Kinetics and physicochemical studiesQ68675330
Three-dimensional structure of D-glyceraldehyde-3-phosphate dehydrogenaseQ68708412
A comparison of the glyceraldehyde 3-phosphate dehydrogenase from ox muscle and liverQ69810201
Determination of free amino groups in proteins by trinitrobenzenesulfonic acidQ70066383
The reactivity of thiol groups in aldolaseQ71640203
Acetimidation of bovine pancreatic ribonuclease AQ72121434
Amino acid sequence around a reactive lysine in glyceraldehyde 3-phosphate dehydrogenaseQ72696587
S-N Transfer and Dual Acetylation in the S-Acetylation and N-Acetylation of 3-Phosphoglyceraldehyde Dehydrogenase by SubstratesQ72772036
THE COMPARATIVE ENZYMOLOGY OF TRIOSEPHOSPHATE DEHYDROGENASEQ76959925
Glyceraldehyde-3-phosphate dehydrogenase from Bacillus stearothermophilusQ77916086
P433issue1
P407language of work or nameEnglishQ1860
P921main subjectglyceraldehyde-3-phosphate dehydrogenasesQ75009903
P1104number of pages14
P304page(s)49-62
P577publication date1977-01-01
P1433published inBiochemical JournalQ864221
P1476titleFolding domains and intramolecular ionic interactions of lysine residues in glyceraldehyde 3-phosphate dehydrogenase
P478volume161

Reverse relations

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Q28366199Identification of tissue transglutaminase-reactive lysine residues in glyceraldehyde-3-phosphate dehydrogenase
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Q42910203Recombinant human sperm-specific glyceraldehyde-3-phosphate dehydrogenase: Structural basis for enhanced stability
Q39255729Reversible inactivation of (Na+ + K+)-ATPase by use of a cleavable bifunctional reagent
Q42093524The use of naturally occurring hybrid variants of chloramphenicol acetyltransferase to investigate subunit contacts