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Amino acid sequence in the region of the reactive serine residue of eel acetylcholinesterase
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What this work says
Outgoing claims: the papers this work cites, builds on, or argues with.
inferredcites →https://doi.org/10.1016/0003-2697(66)90073-xopenalex-snapshot
Decompositior of serine during acid hydrolysis of phosphorylserine
inferredcites →https://doi.org/10.1016/0003-2697(66)90251-xopenalex-snapshot
O-ring joint tubes for protein hydrolyzates
inferredcites →https://doi.org/10.1016/0003-9861(67)90006-9openalex-snapshot
Ageing and dealkylation of soman (pinacolylmethylphosphonofluoridate)-inactivated eel cholinesterase
inferredcites →https://doi.org/10.1016/0005-2744(68)90108-3openalex-snapshot
The primary structure at the DFP-reacting site of a proteolytic enzyme from a strain of arthrobacter
inferredcites →https://doi.org/10.1016/0006-291x(64)90075-0openalex-snapshot
Hydrolysis of phenylthiohydantoins of amino acids
inferredcites →https://doi.org/10.1016/0006-291x(66)90418-9openalex-snapshot
Alkaline hydrolysis of phenylthiohydantoins of amino acids
inferredcites →https://doi.org/10.1016/0006-2944(69)90011-8openalex-snapshot
A specific radioisotopic assay for acetylcholinesterase and pseudocholinesterase in brain and plasma
inferredcites →https://doi.org/10.1016/0006-3002(58)90386-xopenalex-snapshot
The reaction of chymotrypsin and diisopropylphosphorofluoridate II. The structure of two DP-substituted peptides from chymotrypsin-DP
inferredcites →https://doi.org/10.1016/0006-3002(59)90254-9openalex-snapshot
The amino acid sequence around the reactive serine of elastase
inferredcites →https://doi.org/10.1016/0006-3002(59)90320-8openalex-snapshot
Chemical nature of the DFP-binding site of pseudocholinesterase
inferredcites →https://doi.org/10.1016/0006-3002(60)90364-4openalex-snapshot
Determination of amino acids as phenyl thiohydantoin derivatives III. Quantitative determination of 3-phenyl-2-thiohydantoins from paper chromatograms
inferredcites →https://doi.org/10.1016/s0021-9258(18)49344-1openalex-snapshot
Amino Acid Sequence in the Region of Diisopropylphosphoryl Binding in Diisopropylphosphoryl-Trypsin
inferredcites →https://doi.org/10.1016/s0021-9258(18)64922-1openalex-snapshot
PHOSPHOPEPTIDES FROM ACID-HYDROLYZED P32-LABELED DIISOPROPYLPHOSPHORYL CHYMOTRYPSIN
inferredcites →https://doi.org/10.1016/s0021-9258(18)69910-7openalex-snapshot
Structure of the Site Phosphorylated in the Phosphorylase b to a Reaction
inferredcites →https://doi.org/10.1016/s0021-9258(18)70553-xopenalex-snapshot
PHOSPHOPEPTIDES FROM ACID-HYDROLYZED P32-LABELED ISOPROPYL METHYLPHOSPHONOFLUORIDATE-INACTIVATED TRYPSIN
inferredcites →https://doi.org/10.1016/s0021-9258(18)71310-0openalex-snapshot
SERINE PHOSPHORIC ACID FROM DIISOPROPYLPHOSPHORYL DERIVATIVE OF EEL CHOLINESTERASE
inferredcites →https://doi.org/10.1016/s0021-9258(19)57107-1openalex-snapshot
SERINE PHOSPHORIC ACID FROM DIISOPROPYLPHOSPHORYL CHYMOTRYPSIN
inferredcites →https://doi.org/10.1021/bi00802a013openalex-snapshot
Quantitative procedures for use with the Edman-Begg sequenator. Partial sequences of two unusual immunoglobulin light chains, Rzf and Sac
inferredcites →https://doi.org/10.1021/bi00844a007openalex-snapshot
Critical evaluation of the selective tritiation method of determining C-terminal amino acids and its application to luteinizing hormone
inferredcites →https://doi.org/10.1021/bi00887a036openalex-snapshot
The Amino Acid Sequence at the Catalytic Site of Phosphoglucomutase from Rabbit Muscle*
inferredcites →https://doi.org/10.1021/bi00900a020openalex-snapshot
A Partial Characterization of Acetylcholinesterase*
inferredcites →https://doi.org/10.1038/187872a0openalex-snapshot
Amino-acid Sequence about the Reactive Serine of a Proteolytic Enzyme from Bacillus subtilis
inferredcites →https://doi.org/10.1042/bj0760381openalex-snapshot
The ultraviolet fluorescence of proteins in neutral solution
inferredcites →https://doi.org/10.1071/ch9630411openalex-snapshot
The Formation of 3-Phenyl-2-thiohydantoins from Phenylthiocarbamyl Amino Acids
inferredcites →https://doi.org/10.1515/bchm2.1931.202.1-3.67openalex-snapshot
Über die Reinigung von Sojaurease durch Fällung mit Aceton und Kohlensäure.
inferredcites →https://doi.org/10.1515/bchm2.1932.206.4-5.201openalex-snapshot
Über Ferro- und Glaukobilin.
inferredcites →https://doi.org/10.1515/bchm2.1934.225.4.197openalex-snapshot
Die Überführung von Koprostanon in Koprosterin.
inferredcites →https://doi.org/10.1515/bchm2.1934.230.1-6.185openalex-snapshot
Die Konstitution des Oxyketons C21H34O2aus Corpus luteum.
What points at this work
Incoming claims: where this work appears in other papers’ reference lists and arguments.
inferred← citeshttps://doi.org/10.2139/ssrn.4782909openalex-extracted
New 2-Hydrazinothiazole Derivatives as Potential Mao-A, Mao-B, Ache, and Bche Inhibitorsri
inferred← citeshttps://doi.org/10.1007/978-1-4615-7488-0_6openalex-snapshot
Molecular Biology Approach to the Expression and Properties of Mammalian Cholinesterases
inferred← citeshttps://doi.org/10.1007/978-1-4757-6429-1_2openalex-snapshot
Blood Cholinesterases as Human Biomarkers of Organophosphorus Pesticide Exposure
inferred← citeshttps://doi.org/10.1007/bf00598678openalex-snapshot
Effect of a hydrophobic interaction in the reaction of S-(β-alkylthioethyl) O-propyl methylphosphonothionates and their methyl methosulfates with cholinesterases of warm-blooded animals
inferred← citeshttps://doi.org/10.1007/bf01024984openalex-snapshot
The active site and partial sequence of cobra venom acetylcholinesterase
inferred← citeshttps://doi.org/10.1007/bf02395397openalex-snapshot
Amino acid sequence of the active site of human pseudocholinesterase
inferred← citeshttps://doi.org/10.1016/0003-9861(88)90032-xopenalex-snapshot
Physical and chemical characterization of a horse serum carboxylesterase
inferred← citeshttps://doi.org/10.1016/0005-2744(77)90197-8openalex-snapshot
Kinetic analysis of calcium activation of brain acetylcholinesterase forms
inferred← citeshttps://doi.org/10.1016/0014-5793(86)80655-xopenalex-snapshot
Sequence determination of a peptide fragment from electric eel acetylcholinesterase, involved in the binding of quaternary ammonium
inferred← citeshttps://doi.org/10.1016/0165-6147(91)90621-xopenalex-snapshot
Substrate-binding sites in acetylcholinesterase
inferred← citeshttps://doi.org/10.1016/0167-4838(91)90227-qopenalex-snapshot
General occurrence of binding to acetylcholinesterase-substrate complex in noncompetitive inhibition and in inhibition by substrate
inferred← citeshttps://doi.org/10.1016/0167-4838(94)90120-1openalex-snapshot
Active-site peptides of acetylcholinesterase of Electrophorus electricus: labelling of His-440 by 1-bromo-[2-14C]pinacolone and Ser-200 by tritiated diisopropyl fluorophosphate
inferred← citeshttps://doi.org/10.1016/0301-0082(88)90004-4openalex-snapshot
Evolution of neurotransmitter receptor systems
inferred← citeshttps://doi.org/10.1016/0305-0491(84)90246-3openalex-snapshot
Propionylcholinesterase from Helix pomatia and acetylcholinesterase from Asterias bispinosa: A kinetic comparative study
inferred← citeshttps://doi.org/10.1016/0742-8413(88)90037-0openalex-snapshot
Main kinetic characteristics of acetylcholinesterase from brain of Hypostomus punctatus, a Brazilian bentonic fish (cascudo)
inferred← citeshttps://doi.org/10.1016/j.ejmech.2013.09.050openalex-snapshot
Acetylcholinesterase inhibitors as Alzheimer therapy: From nerve toxins to neuroprotection
inferred← citeshttps://doi.org/10.1016/s0008-6215(00)87061-5openalex-snapshot
Purification and properties of an endo-(1→3)-β-d-glucanase from malted barley
inferred← citeshttps://doi.org/10.1016/s0021-9258(18)90614-9openalex-snapshot
Direct determination of acetyl-enzyme intermediate in the acetylcholinesterase-catalyzed hydrolysis of acetylcholine and acetylthiocholine.
inferred← citeshttps://doi.org/10.1016/s0021-9258(19)83644-xopenalex-snapshot
Fluorescent phosphonate labels for serine hydrolases. Kinetic and spectroscopic properties of (7-nitrobenz-2-oxa-1,3-diazole)aminoalkyl methylphosphonofluoridates and their conjugates with acetylcholinesterase molecular forms.
inferred← citeshttps://doi.org/10.1021/bi00447a029openalex-snapshot
Inhibition kinetics of acetylcholinesterase with fluoromethyl ketones
inferred← citeshttps://doi.org/10.1021/bi00551a036openalex-snapshot
Fluorescence energy transfer on acetylcholinesterase: spatial relationship between peripheral site and active center
inferred← citeshttps://doi.org/10.1021/bi00712a012openalex-snapshot
Structure of 11S acetylcholinesterase. Subunit composition
inferred← citeshttps://doi.org/10.1073/pnas.72.10.3834openalex-snapshot
Catalysis by acetylcholinesterase: evidence that the rate-limiting step for acylation with certain substrates precedes general acid-base catalysis.
inferred← citeshttps://doi.org/10.1080/10426507.2024.2427148openalex-snapshot
New 2-hydrazinothiazole derivatives as potential MAO-A, MAO-B, AChE, and BChE inhibitors
inferred← citeshttps://doi.org/10.1111/j.1432-1033.1985.tb09134.xopenalex-snapshot
Reactivation Kineties of diethylphosphoryl acetylcholine esterase
inferred← citeshttps://doi.org/10.1111/j.1432-1033.1992.tb16572.xopenalex-snapshot
Photoaffinity labelling of cholinesterases
inferred← citeshttps://doi.org/10.1111/j.1471-4159.1975.tb04417.xopenalex-snapshot
ACETYLCHOLINESTERASE TURNOVER IN BRAIN, CEREBROSPINAL FLUID AND PLASMA
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