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Profiling the Structural Determinants for the Selectivity of Representative Factor-Xa and Thrombin Inhibitors Using Combined Ligand-Based and Structure-Based Approaches

https://doi.org/10.1021/ci200185q

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What this work says

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

inferredcites →https://doi.org/10.1002/anie.200804695openalex-snapshot

Cation–π Interactions at the Active Site of Factor Xa: Dramatic Enhancement upon Stepwise N‐Alkylation of Ammonium Ions

inferredcites →https://doi.org/10.1006/jmbi.1993.1441openalex-snapshot

Structure of Human Des(1-45) Factor Xa at 2·2 Å Resolution

inferredcites →https://doi.org/10.1006/jmbi.1998.2069openalex-snapshot

Unexpected binding mode of tick anticoagulant peptide complexed to bovine factor Xa

inferredcites →https://doi.org/10.1006/jmbi.2001.5062openalex-snapshot

Factorising ligand affinity: a combined thermodynamic and crystallographic study of trypsin and thrombin inhibition†

inferredcites →https://doi.org/10.1016/0014-5793(95)01190-popenalex-snapshot

Crystal structures of factor Xa specific inhibitors in complex with trypsin: structural grounds for inhibition of factor Xa and selectivity against thrombin

inferredcites →https://doi.org/10.1016/0223-5234(96)88248-1openalex-snapshot

Molecular model of an interaction between factor Xa and DX-9065a, a novel factor Xa inhibitor: Contribution of the acetimidoylpyrrolidine moiety of the inhibitor to potency and selectivity for serine proteases

inferredcites →https://doi.org/10.1016/j.bmc.2005.02.027openalex-snapshot

3D-QSAR CoMFA studies on trypsin-like serine protease inhibitors: a comparative selectivity analysis

inferredcites →https://doi.org/10.1016/j.bmc.2006.12.019openalex-snapshot

Substituted thiophene-anthranilamides as potent inhibitors of human factor Xa

inferredcites →https://doi.org/10.1016/j.bmcl.2007.03.105openalex-snapshot

From selective substrate analogue factor Xa inhibitors to dual inhibitors of thrombin and factor Xa. Part 3

inferredcites →https://doi.org/10.1016/j.jmgm.2008.04.006openalex-snapshot

An investigation of structurally diverse carbamates for acetylcholinesterase (AChE) inhibition using 3D-QSAR analysis

inferredcites →https://doi.org/10.1016/s0960-894x(02)00213-5openalex-snapshot

Optimization of the β-Aminoester class of factor Xa inhibitors. part 2: Identification of FXV673 as a potent and selective inhibitor with excellent In vivo anticoagulant activity

inferredcites →https://doi.org/10.1016/s0960-894x(02)00938-1openalex-snapshot

Structure–Activity relationships of substituted benzothiophene-anthranilamide factor Xa inhibitors

inferredcites →https://doi.org/10.1016/s0969-2126(00)00551-7openalex-snapshot

Structural Basis for Inhibition Promiscuity of Dual Specific Thrombin and Factor Xa Blood Coagulation Inhibitors

inferredcites →https://doi.org/10.1021/bi001477qopenalex-snapshot

Preparation, Characterization, and the Crystal Structure of the Inhibitor ZK-807834 (CI-1031) Complexed with Factor Xa,

inferredcites →https://doi.org/10.1021/bi9926781openalex-snapshot

Identification of a Binding Site for Quaternary Amines in Factor Xa

inferredcites →https://doi.org/10.1021/ci2000874openalex-snapshot

Structural Basis for the β-Adrenergic Receptor Subtype Selectivity of the Representative Agonists and Antagonists

inferredcites →https://doi.org/10.1021/ci600224nopenalex-snapshot

3D QSAR Studies on Protein Tyrosine Phosphatase 1B Inhibitors: Comparison of the Quality and Predictivity among 3D QSAR Models Obtained from Different Conformer-Based Alignments

inferredcites →https://doi.org/10.1021/ci800015sopenalex-snapshot

An Integrated Approach to Ligand- and Structure-Based Drug Design: Development and Application to a Series of Serine Protease Inhibitors

inferredcites →https://doi.org/10.1021/ci900049eopenalex-snapshot

Consensus Superiority of the Pharmacophore-Based Alignment, Over Maximum Common Substructure (MCS): 3D-QSAR Studies on Carbamates as Acetylcholinesterase Inhibitors

inferredcites →https://doi.org/10.1021/jm00050a010openalex-snapshot

Molecular Similarity Indices in a Comparative Analysis (CoMSIA) of Drug Molecules to Correlate and Predict Their Biological Activity

inferredcites →https://doi.org/10.1021/jm000934yopenalex-snapshot

GRID/CPCA: A New Computational Tool To Design Selective Ligands

inferredcites →https://doi.org/10.1021/jm000940uopenalex-snapshot

Crystal Structures of Human Factor Xa Complexed with Potent Inhibitors

inferredcites →https://doi.org/10.1021/jm0111346openalex-snapshot

Design and Quantitative Structure−Activity Relationship of 3-Amidinobenzyl-1 H -indole-2-carboxamides as Potent, Nonchiral, and Selective Inhibitors of Blood Coagulation Factor Xa

inferredcites →https://doi.org/10.1021/jm030303eopenalex-snapshot

Discovery and Evaluation of Potent P1 Aryl Heterocycle-Based Thrombin Inhibitors

inferredcites →https://doi.org/10.1021/jm049187lopenalex-snapshot

Structural Requirements for Factor Xa Inhibition by 3-Oxybenzamides with Neutral P1 Substituents: Combining X-ray Crystallography, 3D-QSAR, and Tailored Scoring Functions

inferredcites →https://doi.org/10.1021/jm060350hopenalex-snapshot

Comparative Binding Energy Analysis Considering Multiple Receptors: A Step toward 3D-QSAR Models for Multiple Targets

inferredcites →https://doi.org/10.1021/jm070125fopenalex-snapshot

Thiophene-Anthranilamides as Highly Potent and Orally Available Factor Xa Inhibitors

inferredcites →https://doi.org/10.1021/jm100146hopenalex-snapshot

Factor Xa Inhibitors: Next-Generation Antithrombotic Agents

inferredcites →https://doi.org/10.1021/jm970493ropenalex-snapshot

Discovery of a Novel, Selective, and Orally Bioavailable Class of Thrombin Inhibitors Incorporating Aminopyridyl Moieties at the P1 Position

inferredcites →https://doi.org/10.1021/jm981062ropenalex-snapshot

Three-Dimensional Quantitative Structure−Activity Relationship Analyses Using Comparative Molecular Field Analysis and Comparative Molecular Similarity Indices Analysis To Elucidate Selectivity Differences of Inhibitors Binding to Trypsin, Thrombin, and Factor Xa

inferredcites →https://doi.org/10.1023/a:1008047919606openalex-snapshot

Comparative Molecular Similarity Index Analysis (CoMSIA) to study hydrogen-bonding properties and to score combinatorial libraries

inferredcites →https://doi.org/10.1024/0301-1526.38.1.13openalex-snapshot

New anticoagulants – towards the development of an "ideal" anticoagulant

inferredcites →https://doi.org/10.1038/clpt.2009.98openalex-snapshot

New Antithrombotic Drugs

inferredcites →https://doi.org/10.1073/pnas.95.12.6630openalex-snapshot

Structural basis for chemical inhibition of human blood coagulation factor Xa

inferredcites →https://doi.org/10.1074/jbc.271.47.29988openalex-snapshot

X-ray Structure of Active Site-inhibited Clotting Factor Xa

inferredcites →https://doi.org/10.1111/j.1538-7836.2007.02473.xopenalex-snapshot

Factor Xa or thrombin: is factor Xa a better target?

inferredcites →https://doi.org/10.1111/j.1538-7836.2009.03503.xopenalex-snapshot

Favorable therapeutic index of the direct factor Xa inhibitors, apixaban and rivaroxaban, compared with the thrombin inhibitor dabigatran in rabbits

What points at this work

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

inferred← citeshttps://doi.org/10.1007/7355_2016_24openalex-snapshot

Integration on Ligand and Structure Based Approaches in GPCRs

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Neglected Tropical Bacterial Diseases

inferred← citeshttps://doi.org/10.1007/7355_2021_130openalex-snapshot

Ligand- and Structure-Based Virtual Screening in Drug Discovery

inferred← citeshttps://doi.org/10.1007/s10822-025-00758-2openalex-snapshot

Interpretable machine learning-driven QSAR modeling for coagulation factor X inhibitors: from molecular descriptors to predictive potency

inferred← citeshttps://doi.org/10.1007/s10822-026-00846-xopenalex-snapshot

Residue‑resolved dynamically averaged interaction analysis of direct factor Xa inhibitors by MD‑FMO combination calculations

inferred← citeshttps://doi.org/10.1016/b978-0-323-99988-5.00005-xopenalex-snapshot

Advanced therapeutics for targeting atherosclerosis

inferred← citeshttps://doi.org/10.1016/j.bmc.2026.118764openalex-snapshot

Novel furo[2,3-d]pyrimidinones as direct thrombin inhibitors: Design, synthesis and biological evaluation

inferred← citeshttps://doi.org/10.1016/j.compbiomed.2022.105640openalex-snapshot

Simple method for assessment of activities of thrombin inhibitors through their molecular structure parameters

inferred← citeshttps://doi.org/10.1016/j.ejmech.2016.05.039openalex-snapshot

Contemporary developments in the discovery of selective factor Xa inhibitors: A review

inferred← citeshttps://doi.org/10.1016/j.jmgm.2019.03.017openalex-snapshot

New factor Xa inhibitors based on 1,2,3,4-tetrahydroquinoline developed by molecular modelling

inferred← citeshttps://doi.org/10.1016/j.molstruc.2022.133974openalex-snapshot

Design, synthesis and biological evaluation of Piperazinylanthranilamides as potential factor Xa inhibitors

inferred← citeshttps://doi.org/10.1016/s1875-5364(15)30085-6openalex-snapshot

Pharmacodynamics and potential synergistic effects of Mai-Luo-Ning injection on cardiovascular protection, based on molecular docking

inferred← citeshttps://doi.org/10.1021/acs.jcim.5b00477openalex-snapshot

Integration of Ligand and Structure Based Approaches for CSAR-2014

inferred← citeshttps://doi.org/10.1021/bi500770popenalex-snapshot

Molecular Dynamics Characterization of Five Pathogenic Factor X Mutants Associated with Decreased Catalytic Activity

inferred← citeshttps://doi.org/10.1021/ci300153dopenalex-snapshot

GRID-Based Three-Dimensional Pharmacophores I: FLAPpharm, a Novel Approach for Pharmacophore Elucidation

inferred← citeshttps://doi.org/10.1055/s-0038-1649507openalex-snapshot

Mechanistic Basis for the Differential Effects of Rivaroxaban and Apixaban on Global Tests of Coagulation

inferred← citeshttps://doi.org/10.1080/07391102.2021.1940282openalex-snapshot

Structural basis for the binding of a selective inverse agonist AF64394 with the human G-protein coupled receptor 3 (GPR3)

inferred← citeshttps://doi.org/10.1080/1062936x.2012.664561openalex-snapshot

Docking studies of novel pyrazinopyridoindoles class of antihistamines with the homology modelled H1-receptor

inferred← citeshttps://doi.org/10.1080/1062936x.2015.1088572openalex-snapshot

Molecular modelling studies on 2-substituted octahydropyrazinopyridoindoles for histamine H2receptor antagonism

inferred← citeshttps://doi.org/10.1080/1062936x.2017.1396247openalex-snapshot

Molecular modelling studies in explaining the higher GPVI antagonistic activity of the racemic 2-(4-methoxyphenylsulfonyl)-2,3,4,9-tetrahydro-1H-pyrido[3,4-b]indole-3-carboxamide than its enantiomers

inferred← citeshttps://doi.org/10.1134/s1990747814040059openalex-snapshot

Molecular mechanisms of thrombosis. Fundamental and applied aspects of the contact activation

inferred← citeshttps://doi.org/10.1155/2015/120802openalex-snapshot

Application of Molecular Modeling to Development of New Factor Xa Inhibitors

inferred← citeshttps://doi.org/10.1155/joch/4469525openalex-snapshot

New s ‐Triazine–Hydrazone Hybrids Targeting EGFR: Design and Anticancer Activity Against A549 Lung Adenocarcinoma

inferred← citeshttps://doi.org/10.1177/0003319719840861openalex-snapshot

Nonhemostatic Activities of Factor Xa: Are There Pleiotropic Effects of Anti-FXa Direct Oral Anticoagulants?

inferred← citeshttps://doi.org/10.1371/journal.pone.0084491openalex-snapshot

Phage Display of the Serpin Alpha-1 Proteinase Inhibitor Randomized at Consecutive Residues in the Reactive Centre Loop and Biopanned with or without Thrombin

inferred← citeshttps://doi.org/10.1371/journal.pone.0142774openalex-snapshot

Study of the Differential Activity of Thrombin Inhibitors Using Docking, QSAR, Molecular Dynamics, and MM-GBSA

inferred← citeshttps://doi.org/10.2174/0929867329666220906105200openalex-snapshot

An Overview of Thrombin Inhibitors in the Perspective of Structureactivity Relationships

inferred← citeshttps://doi.org/10.2174/1568026620666200908165250openalex-snapshot

Efficiency of Homology Modeling Assisted Molecular Docking in G-protein Coupled Receptors

inferred← citeshttps://doi.org/10.3390/molecules25030491openalex-snapshot

Innovative Three-Step Microwave-Promoted Synthesis of N-Propargyltetrahydroquinoline and 1,2,3-Triazole Derivatives as a Potential Factor Xa (FXa) Inhibitors: Drug Design, Synthesis, and Biological Evaluation

inferred← citeshttps://doi.org/10.3390/ph19071017openalex-snapshot

Small-Molecule Factor Xa Inhibitors: Translational SAR, Assay-Aware Data Quality, and QSAR-Readiness for CADD-Oriented Discovery

inferred← citeshttps://doi.org/10.3390/pharmaceutics14010033openalex-snapshot

Green by Design: Convergent Synthesis, Computational Analyses, and Activity Evaluation of New FXa Inhibitors Bearing Peptide Triazole Linking Units

inferred← citeshttps://doi.org/10.4155/fmc-2015-0020openalex-snapshot

Structure–Activity Relationship Studies for Multitarget Antithrombotic Drugs

inferred← citeshttps://doi.org/10.71548/15282openalex-snapshot

Applying Phage Display to Screen a Library of α1-Proteinase Inhibitor Mutants for Improved Thrombin Binding Activity

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