Demo corpus. Scores are computed on a select set of biomedical paper/datasets and may be inaccurate for papers outside this corpus — DataRank relies on network effects that improve with scale. We aim to expand this into a fully open resource pending additional funding.

Lens β-crystallins: The role of deamidation and related modifications in aging and cataract

Progress in Biophysics and Molecular Biology(2014)10.1016/j.pbiomolbio.2014.02.004Source: DataRank Database

Lens β-crystallins: The role of deamidation and related modifications in aging and cataract is a research paper published in Progress in Biophysics and Molecular Biology (2014). On theSindex it has a DataRank of 4.4. It has been cited 141 times, with 134 citing works in its 1-hop citation network.

N/A

4.4DataRank · unranked

4.4

141 citations · base score 5.0

Cite:

datarank_citation_only_1hop_v6· scope data_onlyMethodology

›Data sources & pipeline

Pipeline:MetadataData-paper checkEnrichmentCitation networkScoring

Enrichment:Pending

FAIR Checklist

Context only (not used in score)

Findable (1/2)

Has DOI

Accessible (0/2)

Interoperable (0/2)

Reusable (0/3)

FAIR checklist signals are shown for context only and do not affect DataRank scoring.

Run a calibrated FAIR evaluation for this paper →

DataRank Breakdown

Base Score 17%Citation Network 83%

Base Score Contribution

0.743

From this paper's citation signal

Citation Network Contribution

3.7

From 110 citing papers with measurable signal

Learn more about DataRank methodology →

Top 5 citers driving the network score

Ranked by citation count — the same ordering the engine uses when summing log1p(C_q) over citers.

Alpha-crystallin can function as a molecular chaperone.
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High-resolution X-ray Crystal Structures of Human γD Crystallin (1.25Å) and the R58H Mutant (1.15Å) Associated with Aculeiform Cataract
Journal of Molecular Biology2003218 citationsDataRank 8.8
Small heat-shock proteins: important players in regulating cellular proteostasis
Cellular and Molecular Life Sciences2015196 citationsDataRank 5.6
Partially Folded Aggregation Intermediates of Human γD-, γC-, and γS-Crystallin Are Recognized and Bound by Human αB-Crystallin Chaperone
Journal of Molecular Biology201076 citationsDataRank 3.3
Deamidation in Human γS-Crystallin from Cataractous Lenses Is Influenced by Surface Exposure
Biochemistry200273 citationsDataRank 4.0

Why this DataRank?

DataRank blends this paper's own citation count with the influence of the papers that cite it. Here, roughly 17% comes from its base citations and 83% from the citation network (110 citing papers contributed measurable signal).

Base score B(p): log1p(citation_count) — grows sub-linearly, so a paper with 1,000 citations is not 10× a paper with 100.
Network N(p): Σ over citers of log1p(C_q) ÷ max(outdegree_q, 1). Being cited by a highly-cited paper with few references counts most.
Damping factor d = 0.85: DataRank = (1−d)·B(p) + d·N(p) — the two cards above are each already multiplied by their share.
Self-citations excluded: Citers sharing any OpenAlex author ID with this paper are filtered out before the network sum.

Citers are pulled from OpenAlex sorted by cited_by_count:descand capped per paper, so when the cap binds we keep the highest-signal references and the score is reproducible across reruns.

Read the full methodology →

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Node colors:CenterData PaperData + Open AccessNon-dataSelected & links| Node size = percentile rank