On the public citation graph
Enzyme Isoselective Inhibitors: Application to Drug Design
0 signed · 44 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.
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known work and none has been retracted — and get a dated CiteStamped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.
What this work says
Outgoing claims: the papers this work cites, builds on, or argues with.
inferredcites →https://doi.org/10.1002/(sici)1097-0134(20000701)40:1<154::aid-prot170>3.0.co;2-vopenalex-snapshot
Factors determining the relative stability of anionic tetrahedral complexes in serine protease catalysis and inhibition
inferredcites →https://doi.org/10.1002/0471721204.ch22openalex-snapshot
Principles and Methods of Docking and Ligand Design
inferredcites →https://doi.org/10.1002/ange.200200539openalex-snapshot
Anwendung und Grenzen kristallographischer Daten im strukturbezogenen Liganden‐ und Wirkstoff‐Design
inferredcites →https://doi.org/10.1002/anie.200200539openalex-snapshot
Application and Limitations of X‐ray Crystallographic Data in Structure‐Based Ligand and Drug Design
inferredcites →https://doi.org/10.1002/path.1706openalex-snapshot
Molecular mechanisms of drug resistance
inferredcites →https://doi.org/10.1002/prot.10610openalex-snapshot
Is there a weak H‐bond → LBHB transition on tetrahedral complex formation in serine proteases?
inferredcites →https://doi.org/10.1002/prot.20058openalex-snapshot
Identification of protons position in acid–base enzyme catalyzed reactions: The hepatitis C viral NS3 protease
inferredcites →https://doi.org/10.1007/s0089460020390openalex-snapshot
Anionic Tetrahedral Complexes as Serine Protease Inhibitors
inferredcites →https://doi.org/10.1016/j.chembiol.2003.09.002openalex-snapshot
The Process of Structure-Based Drug Design
inferredcites →https://doi.org/10.1016/s0168-6445(99)00039-xopenalex-snapshot
Molecular basis of antibiotic resistance and β-lactamase inhibition by mechanism-based inactivators: perspectives and future directions
inferredcites →https://doi.org/10.1016/s0301-4622(03)00066-8openalex-snapshot
Thermodynamic and extrathermodynamic requirements of enzyme catalysis
inferredcites →https://doi.org/10.1016/s0960-894x(01)00842-3openalex-snapshot
A designed P1 cysteine mimetic for covalent and non-covalent inhibitors of HCV NS3 protease
inferredcites →https://doi.org/10.1016/s1386-6532(03)00115-xopenalex-snapshot
Drug resistance in non-subtype B HIV-1
inferredcites →https://doi.org/10.1021/bi050247eopenalex-snapshot
Mechanistic Basis of Enzyme-Targeted Drugs
inferredcites →https://doi.org/10.1021/cc000073eopenalex-snapshot
Diverse Viewpoints on Computational Aspects of Molecular Diversity
inferredcites →https://doi.org/10.1021/ja00105a030openalex-snapshot
Accurate First Principles Calculation of Molecular Charge Distributions and Solvation Energies from Ab Initio Quantum Mechanics and Continuum Dielectric Theory
inferredcites →https://doi.org/10.1021/ja00158a004openalex-snapshot
A simulation of the sulfur attack in catalytic pathway of papain using molecular mechanics and semiempirical quantum mechanics
inferredcites →https://doi.org/10.1021/ja00160a020openalex-snapshot
Conformations of cycloheptadecane. A comparison of methods for conformational searching
inferredcites →https://doi.org/10.1021/ja00194a035openalex-snapshot
An internal-coordinate Monte Carlo method for searching conformational space
inferredcites →https://doi.org/10.1021/ja00229a040openalex-snapshot
OH- versus SH- nucleophilic attack on amides: dramatically different gas-phase and solvation energetics
inferredcites →https://doi.org/10.1021/ja954261yopenalex-snapshot
Peptidyl Epoxides: Novel Selective Inactivators of Cysteine Proteases1
inferredcites →https://doi.org/10.1021/jm00001a013openalex-snapshot
Peptidyl .alpha.-ketoheterocyclic inhibitors of human neutrophil elastase. 2. Effect of varying the heterocyclic ring on in vitro potency
inferredcites →https://doi.org/10.1021/jm0303857openalex-snapshot
In-Depth Study of Tripeptide-Based α-Ketoheterocycles as Inhibitors of Thrombin. Effective Utilization of the S1‘ Subsite and Its Implications to Structure-Based Drug Design
inferredcites →https://doi.org/10.1021/jm960603eopenalex-snapshot
Design, Synthesis, and Evaluation of Nonpeptidic Inhibitors of Human Rhinovirus 3C Protease
inferredcites →https://doi.org/10.1021/jp953087xopenalex-snapshot
New Model for Calculation of Solvation Free Energies: Correction of Self-Consistent Reaction Field Continuum Dielectric Theory for Short-Range Hydrogen-Bonding Effects
inferredcites →https://doi.org/10.1038/223704a0openalex-snapshot
Transition State Analogues for Enzyme Catalysis
inferredcites →https://doi.org/10.1039/b402399dopenalex-snapshot
Theoretical analysis of peptidyl α-ketoheterocyclic inhibitors of human neutrophil elastase: Insight into the mechanism of inhibition and the application of QM/MM calculations in structure-based drug design
inferredcites →https://doi.org/10.1073/pnas.251265598openalex-snapshot
Computational study of protein specificity: The molecular basis of HIV-1 protease drug resistance
inferredcites →https://doi.org/10.1073/pnas.97.10.5044openalex-snapshot
Exceptionally potent inhibitors of fatty acid amide hydrolase: The enzyme responsible for degradation of endogenous oleamide and anandamide
inferredcites →https://doi.org/10.1126/science.180.4082.149openalex-snapshot
Enzymatic Catalysis and Transition-State Theory
inferredcites →https://doi.org/10.1146/annurev.biophys.32.110601.141807openalex-snapshot
Computer Simulations of Enzyme Catalysis: Methods, Progress, and Insights
What points at this work
Incoming claims: where this work appears in other papers’ reference lists and arguments.
inferred← citeshttps://doi.org/10.1002/cbic.200700241openalex-snapshot
The Cooperative Effect Between Active Site Ionized Groups and Water Desolvation Controls the Alteration of Acid/Base Catalysis in Serine Proteases
inferred← citeshttps://doi.org/10.1002/cbic.201000459openalex-snapshot
Differentiating Serine and Cysteine Protease Mechanisms by New Covalent QSAR Descriptors
inferred← citeshttps://doi.org/10.1002/cmdc.200600029openalex-snapshot
Enzyme Isoselective Inhibitors: A Tool for Binding‐Trend Analysis
inferred← citeshttps://doi.org/10.1002/ijch.201300144openalex-snapshot
From Catalytic Mechanism to Rational Design of Reversible Covalent Inhibitors of Serine and Cysteine Hydrolases
inferred← citeshttps://doi.org/10.1002/minf.201300099openalex-snapshot
Application of EMBM to Structure‐Based Design of Warheads for Protease Inhibitors
inferred← citeshttps://doi.org/10.1002/prot.22516openalex-snapshot
Challenging a paradigm: Theoretical calculations of the protonation state of the Cys25‐His159 catalytic diad in free papain
inferred← citeshttps://doi.org/10.1007/978-981-99-8401-5_15openalex-snapshot
Unveiling the Dynamic Role of Bioinformatics in Automation for Efficient and Accurate Data Processing and Interpretation
inferred← citeshttps://doi.org/10.1016/j.ejmech.2014.02.059openalex-snapshot
A new method for filtering of reactive “warheads” of transition-state analog protease inhibitors
inferred← citeshttps://doi.org/10.1021/ci100330yopenalex-snapshot
EMBM − A New Enzyme Mechanism-Based Method for Rational Design of Chemical Sites of Covalent Inhibitors
inferred← citeshttps://doi.org/10.11606/d.76.2008.tde-01042008-172626openalex-snapshot
Planejamento racional de inibidores da purina nucleosídeo fosforilase de Schistosoma mansoni
inferred← citeshttps://doi.org/10.1586/14787210.6.1.51openalex-snapshot
Role of bioinformatics in the development of new antibacterial therapy
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.