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Structure of LNX1:Ubc13 ~ Ubiquitin Complex Reveals the Role of Additional Motifs for the E3 Ligase Activity of LNX1

Journal of Molecular Biology(2018)10.1016/j.jmb.2018.02.016Source: DataRank Database

Structure of LNX1:Ubc13 ~ Ubiquitin Complex Reveals the Role of Additional Motifs for the E3 Ligase Activity of LNX1 is a research paper published in Journal of Molecular Biology (2018). On theSindex it has a DataRank of 0.810. It has been cited 14 times, with 11 citing works in its 1-hop citation network.

N/A

0.810DataRank · unranked

Scored on demand from live citation data

14 citations · 11 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 (5 grants)Impact (FWCI 0.91)OA: hybridTopics (52)IDs (PubMed, OpenAlex)

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 50%Citation Network 50%

Base Score Contribution

0.406

From this paper's citation signal

Citation Network Contribution

0.404

From 11 citing papers with measurable signal

Learn more about DataRank methodology →

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 11 citers.

MicroRNA-325-3p Facilitates Immune Escape of Mycobacterium tuberculosis through Targeting LNX1 via NEK6 Accumulation to Promote Anti-Apoptotic STAT3 Signaling
mBio202062 citations47 referencesContributes 0.088
A tri-ionic anchor mechanism drives Ube2N-specific recruitment and K63-chain ubiquitination in TRIM ligases
Nature Communications201948 citations45 referencesContributes 0.086
Modes of allosteric regulation of the ubiquitination machinery
Current Opinion in Structural Biology202037 citations64 referencesContributes 0.057
Structural basis of generic versus specific E2–RING E3 interactions in protein ubiquitination
Protein Science201970 citations94 referencesContributes 0.045
Zinc finger 1 of the RING E3 ligase, RNF125, interacts with the E2 to enhance ubiquitylation
Structure202311 citations55 referencesContributes 0.045

Authors (2)

J. Sivaraman ORCID,Digant Nayak ORCID

Live enrichment

PubMed:29496391 OpenAlex:https://openalex.org/W2793770360

Ministry of Education - Singapore

Grant: MoE Tier-2

Ministry of Education - Singapore

Grant: R-154-000-625-112

Ministry of Education - Singapore

Grant: R154-000-A72-114

Argonne National Laboratory

National University of Singapore

FWCI

0.91

Citation Percentile

0.7%

Influential Citations

Citation Trend

2018

2019

2020

2021

2023

2025

hybridLicense: cc-by-nc-nd

journalhttps://doi.org/10.1016/j.jmb.2018.02.016

HYBRIDhttps://doi.org/10.1016/j.jmb.2018.02.016

publisherhttps://doi.org/10.1016/j.jmb.2018.02.016

publisherhttps://api.elsevier.com/content/article/PII:S0022283618300895?httpAccept=text/xml

publisherhttps://api.elsevier.com/content/article/PII:S0022283618300895?httpAccept=text/plain

Fields of Study

Ubiquitin and proteasome pathwaysCancer-related Molecular PathwaysMicrotubule and mitosis dynamicsChemistryMedicineBiologyAmino Acid MotifsBinding SitesCatalysisHumansModels, MolecularProtein BindingProtein ConformationProtein MultimerizationRING Finger DomainsUbiquitin-Conjugating EnzymesUbiquitin-Protein LigasesUbiquitinationZinc Fingers

MeSH Terms

Binding SitesCatalysisHumansModels, MolecularProtein BindingProtein ConformationZinc FingersAmino Acid MotifsUbiquitin-Conjugating EnzymesUbiquitin-Protein LigasesRING Finger DomainsUbiquitinationProtein Multimerization

Keywords

Ubiquitin ligaseUbiquitinDNA ligaseRing fingerUbiquitin-conjugating enzymeUbiquitin-Protein LigasesRING finger domainZinc fingerChemistryBiochemistryRing (chemistry)Cell biologyBiologyEnzymeTranscription factorGeneUbiquitinationE3 LigaseRing DomainZn-finger

Related Papers (1)

RING-type E3 ligases: Master manipulators of E2 ubiquitin-conjugating enzymes and ubiquitination

N/A

9.6DataRank · unranked

Biochimica et Biophysica Acta (BBA) - Molecular Cell Research(2014)

co-cited

10.1016/j.bbamcr.2013.05.026

Structure of LNX1:Ubc13 ~ Ubiquitin Complex Reveals the Role of Additional Motifs for the E3 Ligase Activity of LNX1

FAIR Checklist

DataRank Breakdown

Top 5 citers driving the network score

Authors (2)

Funding (5 grants)

Impact

Open Access

Topics

Related Papers (1)