On the public citation graph

A Fragment-Based Approach for the Discovery of Isoform-Specific p38α Inhibitors

0 signed · 76 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 See whether every reference in this work resolves to a known work and none has been retracted — and get a dated CiteStamped badge you can embed.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/anie.200500503openalex-snapshot
The INPHARMA Method: Protein‐Mediated Interligand NOEs for Pharmacophore Mapping
inferredcites →https://doi.org/10.1002/chem.200500636openalex-snapshot
SAR by ILOEs: An NMR‐Based Approach to Reverse Chemical Genetics
inferredcites →https://doi.org/10.1016/j.chembiol.2004.05.022openalex-snapshot
Targeting Apoptosis via Chemical Design
inferredcites →https://doi.org/10.1016/j.chembiol.2005.08.013openalex-snapshot
Solution Nuclear Magnetic Resonance Spectroscopy Techniques for Probing Intermolecular Interactions
inferredcites →https://doi.org/10.1016/s0162-3109(00)00206-xopenalex-snapshot
Inhibition of p38 MAP kinase as a therapeutic strategy
inferredcites →https://doi.org/10.1016/s1074-5521(00)80022-8openalex-snapshot
The SHAPES strategy: an NMR-based approach for lead generation in drug discovery
inferredcites →https://doi.org/10.1016/s1359-6446(03)02831-9openalex-snapshot
A ‘Rule of Three’ for fragment-based lead discovery?
inferredcites →https://doi.org/10.1021/ci000403iopenalex-snapshot
Molecular Complexity and Its Impact on the Probability of Finding Leads for Drug Discovery
inferredcites →https://doi.org/10.1021/ci049714+openalex-snapshot
ZINC − A Free Database of Commercially Available Compounds for Virtual Screening
inferredcites →https://doi.org/10.1021/ja017830copenalex-snapshot
Structure-Based Screening As Applied to Human FABP4: A Highly Efficient Alternative to HTS for Hit Generation
inferredcites →https://doi.org/10.1021/jm010533yopenalex-snapshot
A Common Mechanism Underlying Promiscuous Inhibitors from Virtual and High-Throughput Screening
inferredcites →https://doi.org/10.1021/jm020057ropenalex-snapshot
Pyrazole Urea-Based Inhibitors of p38 MAP Kinase: From Lead Compound to Clinical Candidate
inferredcites →https://doi.org/10.1021/jm0255466openalex-snapshot
SAR by MS: A Ligand Based Technique for Drug Lead Discovery Against Structured RNA Targets
inferredcites →https://doi.org/10.1021/jm040031vopenalex-snapshot
Fragment-Based Drug Discovery
inferredcites →https://doi.org/10.1021/jm0495778openalex-snapshot
Fragment-Based Lead Discovery Using X-ray Crystallography
inferredcites →https://doi.org/10.1021/jm049798dopenalex-snapshot
Comparison of Automated Docking Programs as Virtual Screening Tools
inferredcites →https://doi.org/10.1038/372739a0openalex-snapshot
A protein kinase involved in the regulation of inflammatory cytokine biosynthesis
inferredcites →https://doi.org/10.1038/80319openalex-snapshot
Discovering novel ligands for macromolecules using X-ray crystallographic screening
inferredcites →https://doi.org/10.1038/nchembio718openalex-snapshot
High-throughput assays for promiscuous inhibitors
inferredcites →https://doi.org/10.1038/nchembio799openalex-snapshot
Rational design of inhibitors that bind to inactive kinase conformations
inferredcites →https://doi.org/10.1038/nrd1063openalex-snapshot
Designing screens: how to make your hits a hit
inferredcites →https://doi.org/10.1038/nrd1177openalex-snapshot
p38 MAP kinases: key signalling molecules as therapeutic targets for inflammatory diseases
inferredcites →https://doi.org/10.1038/nrd1467openalex-snapshot
Fragment-based lead discovery
inferredcites →https://doi.org/10.1038/nsb770openalex-snapshot
Inhibition of p38 MAP kinase by utilizing a novel allosteric binding site
inferredcites →https://doi.org/10.1073/pnas.0603460103openalex-snapshot
Structure–activity relationships by interligand NOE-based design and synthesis of antiapoptotic compounds targeting Bid
inferredcites →https://doi.org/10.1126/science.274.5292.1531openalex-snapshot
Discovering High-Affinity Ligands for Proteins: SAR by NMR
inferredcites →https://doi.org/10.2174/1570163053175484openalex-snapshot
Combinatorial Chemistry and Fragment Screening - Two Unlike Siblings?
inferredcites →https://doi.org/10.2174/157016306778108884openalex-snapshot
The Nuclear Overhauser Effect in the Lead Identification Process Pharmacophore Models

What points at this work

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

inferred← citeshttps://doi.org/10.1002/0471140864.ps1718s81openalex-snapshot
Overview of Probing Protein‐Ligand Interactions Using NMR
inferred← citeshttps://doi.org/10.1002/9780470027318.a9915openalex-snapshot
Nuclear Magnetic Resonance of Large Molecules in Natural Products
inferred← citeshttps://doi.org/10.1002/9780470524961.ch18openalex-snapshot
Fragment‐Based Drug Discovery of Kinase Inhibitors
inferred← citeshttps://doi.org/10.1002/9780470559277.ch130118openalex-snapshot
Saturation Transfer Difference NMR for Fragment Screening
inferred← citeshttps://doi.org/10.1002/9781119099512.ch10openalex-snapshot
Applications of Ligand and Protein‐Observed NMR in Ligand Discovery
inferred← citeshttps://doi.org/10.1002/9783527644506.refsopenalex-snapshot
References
inferred← citeshttps://doi.org/10.1002/9783527677016.ch6openalex-snapshot
Hit and Lead Identification from Fragments
inferred← citeshttps://doi.org/10.1002/cbic.200800704openalex-snapshot
On‐Chip Fragment‐Based Approach for Discovery of High‐Affinity Bivalent Inhibitors
inferred← citeshttps://doi.org/10.1002/cbic.201600637openalex-snapshot
Hit‐Validation Methodologies for Ligands Isolated from DNA‐Encoded Chemical Libraries
inferred← citeshttps://doi.org/10.1002/cmdc.201600039openalex-snapshot
The Cell Surface Receptor CD44: NMR‐Based Characterization of Putative Ligands
inferred← citeshttps://doi.org/10.1002/jmr.909openalex-snapshot
A survey of the year 2007 literature on applications of isothermal titration calorimetry
inferred← citeshttps://doi.org/10.1007/7355_2009_5openalex-snapshot
NMR Spectroscopy in Fragment Based Drug Design
inferred← citeshttps://doi.org/10.1007/978-1-4939-2020-4_7openalex-snapshot
A Fragment-Based Selection Approach for the Discovery of Peptide Macrocycles Targeting Protein Kinases
inferred← citeshttps://doi.org/10.1007/s00216-013-6931-0openalex-snapshot
NMR-based analysis of protein–ligand interactions
inferred← citeshttps://doi.org/10.1007/s00216-014-7834-4openalex-snapshot
Size does matter! Label-free detection of small molecule–protein interaction
inferred← citeshttps://doi.org/10.1007/s10969-011-9102-6openalex-snapshot
Leveraging structure determination with fragment screening for infectious disease drug targets: MECP synthase from Burkholderia pseudomallei
inferred← citeshttps://doi.org/10.1016/b978-0-12-381274-2.00004-2openalex-snapshot
Predicting the Success of Fragment Screening by X-Ray Crystallography
inferred← citeshttps://doi.org/10.1016/b978-0-12-401676-7.00007-3openalex-snapshot
AEG-1/MTDH/LYRIC in Liver Cancer
inferred← citeshttps://doi.org/10.1016/bs.armc.2017.07.002openalex-snapshot
Fragment-Based Lead Discovery
inferred← citeshttps://doi.org/10.1016/j.chembiol.2017.01.006openalex-snapshot
Potent and Selective EphA4 Agonists for the Treatment of ALS
inferred← citeshttps://doi.org/10.1016/j.copbio.2007.09.003openalex-snapshot
Fragment-based approaches to enzyme inhibition
inferred← citeshttps://doi.org/10.1016/j.drudis.2009.03.009openalex-snapshot
Transforming fragments into candidates: small becomes big in medicinal chemistry
inferred← citeshttps://doi.org/10.1016/j.pnmrs.2016.09.001openalex-snapshot
NMR in drug discovery: A practical guide to identification and validation of ligands interacting with biological macromolecules
inferred← citeshttps://doi.org/10.1016/j.sbi.2010.04.003openalex-snapshot
Structural biology in fragment-based drug design
inferred← citeshttps://doi.org/10.1021/acs.jafc.5b01133openalex-snapshot
Uptake, Translocation, and Metabolism of Phenols by Submerged Rooted Macrophyte, Water Milfoil (Myriophyllum elatinoides)
inferred← citeshttps://doi.org/10.1021/acs.jmedchem.3c00467openalex-snapshot
Characterization of a Potent and Orally Bioavailable Lys-Covalent Inhibitor of Apoptosis Protein (IAP) Antagonist
inferred← citeshttps://doi.org/10.1021/acs.jmedchem.3c01073openalex-snapshot
Mixture-Based Screening of Focused Combinatorial Libraries by NMR: Application to the Antiapoptotic Protein hMcl-1
inferred← citeshttps://doi.org/10.1021/acs.jmedchem.7b01075openalex-snapshot
In Silico Identification of a Novel Hinge-Binding Scaffold for Kinase Inhibitor Discovery
inferred← citeshttps://doi.org/10.1021/bi3005126openalex-snapshot
Fragment-Based Approaches in Drug Discovery and Chemical Biology
inferred← citeshttps://doi.org/10.1021/ci100340wopenalex-snapshot
Sequence, Structure, and Active Site Analyses of p38 MAP Kinase: Exploiting DFG-out Conformation as a Strategy to Design New Type II Leads
inferred← citeshttps://doi.org/10.1021/ci200003copenalex-snapshot
Novel Strategy for Three-Dimensional Fragment-Based Lead Discovery
inferred← citeshttps://doi.org/10.1021/ci200159gopenalex-snapshot
Molecular Dynamics Simulation and Free Energy Calculation Studies of the Binding Mechanism of Allosteric Inhibitors with p38α MAP Kinase
inferred← citeshttps://doi.org/10.1021/cr500043bopenalex-snapshot
NMR-Based Approaches for the Identification and Optimization of Inhibitors of Protein–Protein Interactions
inferred← citeshttps://doi.org/10.1021/ja100595uopenalex-snapshot
Optimization of the Interligand Overhauser Effect for Fragment Linking: Application to Inhibitor Discovery against Mycobacterium tuberculosis Pantothenate Synthetase
inferred← citeshttps://doi.org/10.1021/jm8000373openalex-snapshot
Recent Developments in Fragment-Based Drug Discovery
inferred← citeshttps://doi.org/10.1021/jm800068wopenalex-snapshot
Development of Paramagnetic Probes for Molecular Recognition Studies in Protein Kinases
inferred← citeshttps://doi.org/10.1021/jm800747wopenalex-snapshot
Multiple and Single Binding Modes of Fragment-Like Kinase Inhibitors Revealed by Molecular Modeling, Residue Type-Selective Protonation, and Nuclear Overhauser Effects
inferred← citeshttps://doi.org/10.1038/nrd2606openalex-snapshot
Perspectives on NMR in drug discovery: a technique comes of age
inferred← citeshttps://doi.org/10.1038/s41419-019-2083-2openalex-snapshot
MKK3 sustains cell proliferation and survival through p38DELTA MAPK activation in colorectal cancer
inferred← citeshttps://doi.org/10.1039/9781782620938-00049openalex-snapshot
Applications of NMR in Fragment-Based Drug Design
inferred← citeshttps://doi.org/10.1074/jbc.m112.414516openalex-snapshot
Thiolactomycin-based β-Ketoacyl-AcpM Synthase A (KasA) Inhibitors
inferred← citeshttps://doi.org/10.1111/j.1747-0285.2010.01010.xopenalex-snapshot
Fragment‐based discovery of novel thymidylate synthase leads by NMR screening and group epitope mapping
inferred← citeshttps://doi.org/10.13070/mm.en.4.599openalex-snapshot
NMR Spectroscopy in Drug Discovery and Development
inferred← citeshttps://doi.org/10.1371/journal.pcbi.1000528openalex-snapshot
High-Performance Drug Discovery: Computational Screening by Combining Docking and Molecular Dynamics Simulations
inferred← citeshttps://doi.org/10.1517/14728222.2014.959495openalex-snapshot
Targeting tumor invasion: the roles of MDA-9/Syntenin
inferred← citeshttps://doi.org/10.3390/cancers10050131openalex-snapshot
Insights of Crosstalk between p53 Protein and the MKK3/MKK6/p38 MAPK Signaling Pathway in Cancer
inferred← citeshttps://doi.org/10.3390/molecules21070854openalex-snapshot
Process of Fragment-Based Lead Discovery—A Perspective from NMR
inferred← citeshttps://doi.org/10.5167/uzh-3725openalex-snapshot
A survey of the year 2006 literature on applications of isothermal titration calorimetry
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.