On the public citation graph

A simple linearization method unveils hidden enzymatic assay interferences

https://doi.org/10.1016/j.bpc.2019.106193

0 signed · 66 inferred · view as graph

Inferred edges come from two machine sources: sweeps of open repository metadata (mostly SSRN and Zenodo), and a bulk OpenAlex citation snapshot. Every row below is labelled with the one it came from. Neither is a complete citation index — absence here is not evidence of absence.

Is this your work? Sign in with ORCID and put your name on the claims that are yours.

Claim with ORCID

Reference health. See whether every reference in this work resolves to a known work and none has been retracted — and get a dated CiteStamped badge you can embed.

See reference health

What this work says

Outgoing claims: the papers this work cites, builds on, or argues with.

inferredcites →https://doi.org/10.1002/bit.26454openalex-snapshot

One pot synthesis of GDP‐mannose by a multi‐enzyme cascade for enzymatic assembly of lipid‐linked oligosaccharides

inferredcites →https://doi.org/10.1002/btpr.2390openalex-snapshot

Influence of the experimental setup on the determination of enzyme kinetic parameters

inferredcites →https://doi.org/10.1002/cbic.201600462openalex-snapshot

BioCatNet: A Database System for the Integration of Enzyme Sequences and Biocatalytic Experiments

inferredcites →https://doi.org/10.1002/jctb.2564openalex-snapshot

Fundamentals and applications of immobilized microfluidic enzymatic reactors

inferredcites →https://doi.org/10.1006/jtbi.1997.0425openalex-snapshot

Closed Form Solution for Time-dependent Enzyme Kinetics

inferredcites →https://doi.org/10.1006/meth.2001.1177openalex-snapshot

Quantitative Analysis of the Time Courses of Enzyme-Catalyzed Reactions

inferredcites →https://doi.org/10.1007/978-1-4939-0357-3_1openalex-snapshot

General In Vitro Caspase Assay Procedures

inferredcites →https://doi.org/10.1007/978-3-7091-1402-5openalex-snapshot

Kinetics of Enzyme-Modifier Interactions

inferredcites →https://doi.org/10.1016/0005-2744(69)90420-3openalex-snapshot

Kinetics of the reversible inhibition of enzyme-catalysed reactions by tight-binding inhibitors

inferredcites →https://doi.org/10.1016/0076-6879(79)63010-0openalex-snapshot

[8] Kinetic analysis of progress curves

inferredcites →https://doi.org/10.1016/0076-6879(95)49034-5openalex-snapshot

[6] Kinetics of slow and tight-binding inhibitors

inferredcites →https://doi.org/10.1016/c2013-0-04130-8openalex-snapshot

Fundamentals of Enzyme Kinetics

inferredcites →https://doi.org/10.1016/j.bpc.2006.08.010openalex-snapshot

A test for measuring the effects of enzyme inactivation

inferredcites →https://doi.org/10.1016/j.bpc.2016.09.004openalex-snapshot

On the estimation errors of KM and V from time-course experiments using the Michaelis–Menten equation

inferredcites →https://doi.org/10.1016/j.cbpa.2010.03.020openalex-snapshot

Apparent activity in high-throughput screening: origins of compound-dependent assay interference

inferredcites →https://doi.org/10.1016/j.ceb.2003.10.009openalex-snapshot

Mechanisms of caspase activation

inferredcites →https://doi.org/10.1016/j.celrep.2016.01.076openalex-snapshot

Specific Inhibition of β-Secretase Processing of the Alzheimer Disease Amyloid Precursor Protein

inferredcites →https://doi.org/10.1016/j.drudis.2006.05.014openalex-snapshot

Screening in a spirit haunted world

inferredcites →https://doi.org/10.1016/j.ejmech.2011.02.067openalex-snapshot

Aspartic vinyl sulfones: Inhibitors of a caspase-3-dependent pathway

inferredcites →https://doi.org/10.1016/j.ejps.2013.12.017openalex-snapshot

Potential small-molecule activators of caspase-7 identified using yeast-based caspase-3 and -7 screening assays

inferredcites →https://doi.org/10.1016/j.enzmictec.2011.06.007openalex-snapshot

A high-throughput colorimetric assay to measure the activity of glutamate decarboxylase

inferredcites →https://doi.org/10.1016/j.ibmb.2009.07.003openalex-snapshot

Tick-derived Kunitz-type inhibitors as antihemostatic factors

inferredcites →https://doi.org/10.1016/j.pisc.2014.02.005openalex-snapshot

Enzyme assays

inferredcites →https://doi.org/10.1016/j.pisc.2014.12.002openalex-snapshot

One hundred years of Michaelis–Menten kinetics

inferredcites →https://doi.org/10.1016/j.pisc.2016.03.024openalex-snapshot

In search of lost time constants and of non-Michaelis–Menten parameters

inferredcites →https://doi.org/10.1016/s0926-6593(65)80190-4openalex-snapshot

A simple test for inactivation of an enzyme during assay

inferredcites →https://doi.org/10.1021/ac400480zopenalex-snapshot

A Fully Unsupervised Compartment-on-Demand Platform for Precise Nanoliter Assays of Time-Dependent Steady-State Enzyme Kinetics and Inhibition

inferredcites →https://doi.org/10.1021/acscentsci.7b00069openalex-snapshot

The Ecstasy and Agony of Assay Interference Compounds

inferredcites →https://doi.org/10.1021/bi034998xopenalex-snapshot

An Uncleavable Procaspase-3 Mutant Has a Lower Catalytic Efficiency but an Active Site Similar to That of Mature Caspase-3

inferredcites →https://doi.org/10.1021/ja01114a027openalex-snapshot

Curve Fitting of Enzymatic Reactions Based on the Michaelis—Menten Equation1

inferredcites →https://doi.org/10.1021/jm901743xopenalex-snapshot

Leech-Derived Thrombin Inhibitors: From Structures to Mechanisms to Clinical Applications

inferredcites →https://doi.org/10.1021/jp1055528openalex-snapshot

Precise, Facile Initial Rate Measurements

inferredcites →https://doi.org/10.1021/jp8026226openalex-snapshot

Reactant Stationary Approximation in Enzyme Kinetics

inferredcites →https://doi.org/10.1038/nchem.2744openalex-snapshot

Tyrosine sulfation modulates activity of tick-derived thrombin inhibitors

inferredcites →https://doi.org/10.1038/nprot.2006.77openalex-snapshot

A detergent-based assay for the detection of promiscuous inhibitors

inferredcites →https://doi.org/10.1038/nrd.2017.219openalex-snapshot

Mechanistic enzymology in drug discovery: a fresh perspective

inferredcites →https://doi.org/10.1038/nrd.2017.257openalex-snapshot

Erratum: Mechanistic enzymology in drug discovery: a fresh perspective

inferredcites →https://doi.org/10.1038/srep02658openalex-snapshot

Quantitative full time course analysis of nonlinear enzyme cycling kinetics

inferredcites →https://doi.org/10.1039/tf9534900696openalex-snapshot

Analytical description of the effects of modifiers and of enzyme multivalency upon the steady state catalyzed reaction rate

inferredcites →https://doi.org/10.1042/bj0190338openalex-snapshot

A Note on the Kinetics of Enzyme Action

inferredcites →https://doi.org/10.1042/bj1350101openalex-snapshot

Steady-state enzyme kinetics with high-affinity substrates or inhibitors. A statistical treatment of dose–response curves

inferredcites →https://doi.org/10.1042/bj1490305openalex-snapshot

The use of the direct linear plot for determining initial velocities

inferredcites →https://doi.org/10.1073/pnas.1905177116openalex-snapshot

Rapid assembly and profiling of an anticoagulant sulfoprotein library

inferredcites →https://doi.org/10.1074/jbc.m115.658930openalex-snapshot

Temperature Effects on Kinetic Parameters and Substrate Affinity of Cel7A Cellobiohydrolases

inferredcites →https://doi.org/10.1093/biohorizons/hzw015openalex-snapshot

Evolution of salivary secretions in haematophagous animals

inferredcites →https://doi.org/10.1093/nar/gkx1134openalex-snapshot

The MEROPS database of proteolytic enzymes, their substrates and inhibitors in 2017 and a comparison with peptidases in the PANTHER database

inferredcites →https://doi.org/10.1111/febs.12564openalex-snapshot

Validity of the Michaelis–Menten equation – steady‐state or reactant stationary assumption: that is the question

inferredcites →https://doi.org/10.1111/febs.13275openalex-snapshot

Enzyme kinetics: the whole picture reveals hidden meanings

inferredcites →https://doi.org/10.1111/febs.14427openalex-snapshot

STRENDA DB: enabling the validation and sharing of enzyme kinetics data

inferredcites →https://doi.org/10.1111/j.1538-7836.2007.02500.xopenalex-snapshot

The central role of thrombin in hemostasis

inferredcites →https://doi.org/10.1111/mve.12276openalex-snapshot

Peptidase inhibitors in tick physiology

inferredcites →https://doi.org/10.1146/annurev-pharmtox-011613-135943openalex-snapshot

The Druggable Genome: Evaluation of Drug Targets in Clinical Trials Suggests Major Shifts in Molecular Class and Indication

inferredcites →https://doi.org/10.2741/3363openalex-snapshot

The role of saliva in tick feeding

inferredcites →https://doi.org/10.3390/metabo2040818openalex-snapshot

Determining Enzyme Kinetics for Systems Biology with Nuclear Magnetic Resonance Spectroscopy

What points at this work

Incoming claims: where this work appears in other papers’ reference lists and arguments.

inferred← uses_datahttps://doi.org/10.5281/zenodo.3956679zenodo-depositor-declared

inferred← uses_datahttps://doi.org/10.5281/zenodo.3957320zenodo-depositor-declared

inferred← uses_datahttps://doi.org/10.5281/zenodo.3957375zenodo-depositor-declared

inferred← citeshttps://doi.org/10.1007/s11144-026-03171-4openalex-snapshot

Conditions that can lead to biased kinetic parameters in reactions with enzymes simultaneously inhibited by reaction product and another inhibitor

inferred← citeshttps://doi.org/10.1016/j.chembiol.2020.10.002openalex-snapshot

Sulfotyrosine-Mediated Recognition of Human Thrombin by a Tsetse Fly Anticoagulant Mimics Physiological Substrates

inferred← citeshttps://doi.org/10.1016/j.jmb.2020.07.025openalex-snapshot

interferENZY: A Web-Based Tool for Enzymatic Assay Validation and Standardized Kinetic Analysis

inferred← citeshttps://doi.org/10.1016/j.jmb.2026.169654openalex-snapshot

ACCU-RATES: A Web Tool for Accurate Enzyme Kinetics and Initial Reaction Rate Measurements

inferred← citeshttps://doi.org/10.1016/j.slasd.2024.100170openalex-snapshot

High-throughput kinetics in drug discovery

inferred← citeshttps://doi.org/10.1021/acs.accounts.3c00388openalex-snapshot

Exploiting Chemical Protein Synthesis to Study the Role of Tyrosine Sulfation on Anticoagulants from Hematophagous Organisms

inferred← citeshttps://doi.org/10.1080/10242422.2020.1746771openalex-snapshot

Estimation of initial rate from discontinuous progress data

inferred← citeshttps://doi.org/10.1177/2472555220958386openalex-snapshot

Major Improvements in Robustness and Efficiency during the Screening of Novel Enzyme Effectors by the 3-Point Kinetics Assay

inferred← citeshttps://doi.org/10.3390/app12010102openalex-snapshot

Kinetic Analysis Misinterpretations Due to the Occurrence of Enzyme Inhibition by Reaction Product: Comparison between Initial Velocities and Reaction Time Course Methodologies

Editorial review for independent work. ICSAC — the Institute for Complexity Science and Advanced Computing — runs a structured editorial panel for researchers publishing outside journals, and publishes on CiteStamp rails. Submission is free and goes through ORCID: icsacinstitute.org/submit.