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Repertoire Analysis of Antibody CDR-H3 Loops Suggests Affinity Maturation Does Not Typically Result in Rigidification

Frontiers in Immunology(2018)10.3389/fimmu.2018.00413Source: DataRank Database

Repertoire Analysis of Antibody CDR-H3 Loops Suggests Affinity Maturation Does Not Typically Result in Rigidification is a research paper published in Frontiers in Immunology (2018). On theSindex it has a DataRank of 2.1. It has been cited 66 times, with 56 citing works in its 1-hop citation network.

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2.1DataRank · unranked

Scored on demand from live citation data

66 citations · 56 citing works in its network

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›Methodology & internals

datarank_citation_only_1hop_v6· scope data_onlyMethodology

Pipeline:MetadataData-paper checkEnrichmentCitation networkScoring

Enrichment:Funding (10 grants)OA: goldTopics (64)IDs (PubMed)SDGs (2)

FAIR Checklist

Context only (not used in score)

Findable (1/2)

Has DOI

Accessible (0/2)

Interoperable (0/2)

Reusable (0/3)

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DataRank Breakdown

Base Score 30%Citation Network 70%

Base Score Contribution

0.631

From this paper's citation signal

Citation Network Contribution

1.5

From 45 citing papers with measurable signal

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Top 5 citers driving the network score

Ranked by each citer's contribution to N(p) — log1p(C_q) divided by its reference count — out of 56 citers.

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Characterizing the Diversity of the CDR-H3 Loop Conformational Ensembles in Relationship to Antibody Binding Properties
Frontiers in Immunology201999 citations79 referencesContributes 0.058

Authors (7)

Adnan Sljoka,Daisuke Kuroda ORCID,Nobuyuki Tsuchimura,Naoki Katoh,Kouhei Tsumoto ORCID

Live enrichment

PubMed:29545810

National Institute of General Medical Sciences

Grant: F31-GM123616, R01-GM078221, T32-GM008403

Core Research for Evolutional Science and Technology

Grant: JPMJCR1402

Japan Society for the Promotion of Science

Grant: 17K18113

National Institutes of Health

Grant: 5T32GM008403-22

PROGRAM IN MOLECULAR BIOPHYSICS

National Institutes of Health

Grant: 2R01GM078221-06

Prediction of the Structure of Therapeutic Antibodies with their Antigens

National Institutes of Health

Grant: 5F31GM123616-02

Computational Design of Crystal Lattice Interactions to Determine Recalcitrant Protein Structures

Natural Sciences and Engineering Research Council of Canada

Grant: unidentified

unidentified

NIGMS NIH HHS

Grant: F31 GM123616

NIGMS NIH HHS

Grant: R01 GM078221

NIGMS NIH HHS

Grant: T32 GM008403

goldLicense: cc-by

publisherhttps://doi.org/10.3389/fimmu.2018.00413

publisherhttp://journal.frontiersin.org/article/10.3389/fimmu.2018.00413/full

repositoryhttps://doaj.org/article/71ffaa1387714ac493a4968650387caa

repositoryhttps://www.ncbi.nlm.nih.gov/pmc/articles/5840193

https://www.frontiersin.org/articles/10.3389/fimmu.2018.00413/pdf

Fields of Study

0301 basic medicine03 medical and health sciences0303 health sciencesAnimalsAntibody AffinityAntibody SpecificityAntigensBinding Sites, AntibodyComplementarity Determining RegionsCrystallography, X-RayDatabases, ProteinHumansImmunity, HumoralImmunoglobulin Heavy ChainsImmunologic MemoryMiceModels, ChemicalMolecular Dynamics SimulationProtein ConformationStructure-Activity Relationship

MeSH Terms

AnimalsAntibody AffinityAntibody SpecificityAntigensBinding Sites, AntibodyComplementarity Determining RegionsCrystallography, X-RayDatabases, ProteinHumansImmunity, HumoralImmunoglobulin Heavy ChainsImmunologic MemoryMiceModels, ChemicalMolecular Dynamics SimulationProtein ConformationStructure-Activity Relationship

Keywords

antibody repertoiresconformational flexibilityProtein ConformationImmunologyAntibody AffinityMolecular Dynamics SimulationCrystallography, X-RayMiceStructure-Activity RelationshipAntibody SpecificityAnimalsHumansAntigensDatabases, Proteinaffinity maturationrigidity theorycomplementarity determining regionsRC581-607Immunity, HumoralModels, Chemicalpebble game algorithmBinding Sites, AntibodyImmunologic diseases. AllergyImmunoglobulin Heavy ChainsImmunologic MemoryRosettaAntibodymolecular dynamics simulations

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