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Identification and characterization of fragment binding sites for allosteric ligand design using the site identification by ligand competitive saturation hotspots approach (SILCS-Hotspots)

Biochimica et Biophysica Acta (BBA) - General Subjects(2020)10.1016/j.bbagen.2020.129519Source: DataRank Database

Identification and characterization of fragment binding sites for allosteric ligand design using the site identification by ligand competitive saturation hotspots approach (SILCS-Hotspots) is a research paper published in Biochimica et Biophysica Acta (BBA) - General Subjects (2020). On theSindex it has a DataRank of 0. It has been cited 69 times.

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Open Access69 citations

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Enrichment:Funding (6 grants)Impact (FWCI 2.70)OA: greenTopics (47)IDs (PubMed, PMC, OpenAlex)Annotations (1)

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Context only (not used in score)

Findable (1/2)

Has DOI

Accessible (1/2)

Open Access

Interoperable (0/2)

Reusable (0/3)

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Authors (5)

Sunhwan Jo ORCID,Sirish Kaushik Lakkaraju ORCID,Christoffer Lind ORCID,Wenbo Yu ORCID,Alexander D. MacKerell ORCID

Live enrichment

PubMed:31911242 PMC:PMC7029399 OpenAlex:https://openalex.org/W2996822411

NIGMS NIH HHS

Grant: R44 GM109635

NIGMS NIH HHS

Grant: R43 GM109635

NIGMS NIH HHS

Grant: R35 GM131710

National Institutes of Health

Grant: 5R35GM131710-02

Macromolecular Conformational Heterogeneity

National Institutes of Health

Grant: 5R44GM109635-05

Pre-computed free energy maps for rapid structure-based ligand design

National Institutes of Health

FWCI

2.70

Citation Percentile

0.9%

Citation Trend

2020

2021

2022

2023

2024

2025

2026

greenLicense: Elsevier TDM

repositoryhttps://www.ncbi.nlm.nih.gov/pmc/articles/7029399

publisherhttps://api.elsevier.com/content/article/PII:S030441652030009X?httpAccept=text/xml

publisherhttps://api.elsevier.com/content/article/PII:S030441652030009X?httpAccept=text/plain

journalhttps://doi.org/10.1016/j.bbagen.2020.129519

Fields of Study

Receptor Mechanisms and SignalingComputational Drug Discovery MethodsEstrogen and related hormone effects0301 basic medicine0303 health sciences03 medical and health sciences

MeSH Terms

Allosteric SiteBinding SitesHumansLigandsReceptors, AndrogenProtein Tyrosine PhosphatasesReceptors, Adrenergic, beta-2Receptors, G-Protein-CoupledReceptor, Muscarinic M2Mitogen-Activated Protein Kinase 7Cyclin-Dependent Kinase 5Molecular Docking Simulation

Keywords

Allosteric regulationBinding siteComputational biologyLigand (biochemistry)Drug discoveryLigand efficiencyChemistryG protein-coupled receptorBiologyReceptorBiochemistrycomputer-aided drug designCompetitive InhibitorOrthostericAllosteric PocketFragment-based Drug DesignCryptic PocketReceptor, Muscarinic M2Binding SitesCyclin-Dependent Kinase 5LigandsReceptors, G-Protein-CoupledMolecular Docking SimulationReceptors, AndrogenHumansReceptors, Adrenergic, beta-2Protein Tyrosine PhosphatasesAllosteric SiteMitogen-Activated Protein Kinase 7

Identification and characterization of fragment binding sites for allosteric ligand design using the site identification by ligand competitive saturation hotspots approach (SILCS-Hotspots)

FAIR Checklist

Authors (5)

Funding (6 grants)

Impact

Open Access

Topics

Annotations (Europe PMC)