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.

Design, Synthesis, and Biological Evaluation of Retinoic Acid-Related Orphan Receptor γt (RORγt) Agonist Structure-Based Functionality Switching Approach from In House RORγt Inverse Agonist to RORγt Agonist

Journal of Medicinal Chemistry(2019)10.1021/acs.jmedchem.8b01181Source: DataRank Database

Design, Synthesis, and Biological Evaluation of Retinoic Acid-Related Orphan Receptor γt (RORγt) Agonist Structure-Based Functionality Switching Approach from In House RORγt Inverse Agonist to RORγt Agonist is a research paper published in Journal of Medicinal Chemistry (2019). On theSindex it has a DataRank of 1.6. It has been cited 24 times, with 25 citing works in its 1-hop citation network.

N/A

1.6DataRank · unranked

1.6

24 citations · base score 3.2

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 (2/2)

Has DOI
Indexed in repositories

Accessible (0/2)

Interoperable (2/2)

DataCite relations
Linked datasets

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 29%Citation Network 71%

Base Score Contribution

0.483

From this paper's citation signal

Citation Network Contribution

1.2

From 25 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.

A short history of<i>SHELX</i>
Acta Crystallographica Section A Foundations of Crystallography200786,960 citationsDataRank 1.7
[20] Processing of X-ray diffraction data collected in oscillation mode
Methods in Enzymology199733,562 citationsDataRank 1.6
<i>Phaser</i>crystallographic software
Journal of Applied Crystallography200720,761 citationsDataRank 1.5
Refinement of Macromolecular Structures by the Maximum-Likelihood Method
Acta Crystallographica Section D Biological Crystallography199714,826 citationsDataRank 1.4
On enantiomorph-polarity estimation
Acta Crystallographica Section A Foundations of Crystallography198310,373 citationsDataRank 1.4

Why this DataRank?

DataRank blends this paper's own citation count with the influence of the papers that cite it. Here, roughly 29% comes from its base citations and 71% from the citation network (25 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 →

Click a node to highlight its connections. Use scroll to zoom. Drag to pan.

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