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Investigation Report: 'Neuronal Sensitization Drives Bone Regeneration via Energy Metabolism and BMP2-ErbB1 Signaling' (Adv. Funct. Mater., DOI: 10.1002/adfm.76607)

Academic fraud report · Geng Detector

Summary

This report assesses multiple data-integrity concerns in Dai et al. (Advanced Functional Materials, DOI: 10.1002/adfm.76607). The most serious finding is an implausible ZDOCK docking score of 13553.6 for ErbB1 in Table 1, far exceeding the typical 1000–3000 range of the rigid-body FFT-based algorithm and inconsistent with all other receptors in the table (1528–1967), suggesting fabrication or technical illiteracy. A second concern is identical binding energies of exactly −17.7 kcal/mol for ErbB1 and ErbB2, statistically improbable and indicative of copy-paste. Third, the Methods claim ICP-OES quantification but cite a PerkinElmer PinAAcle 900T, which is an atomic absorption spectrometer (AAS), not an ICP-OES instrument, indicating methodological error or copy-paste from an unrelated protocol. Fourth, the STRING network p-value of 0.0173 for a 37-node network is implausibly high for the platform's enrichment algorithm. Image-based analyses were not performed due to unavailable pixel data. Verdict: strong suspicion of data fabrication and methodological misrepresentation; formal investigation recommended.

Verdict

🔴 Strong suspicion of data fabrication and methodological misrepresentation. Multiple independent anomalies in tabular and methodological content are mutually reinforcing. Formal institutional and editorial investigation is warranted.

Key findings

  • Implausible ZDOCK score for ErbB1 (13553.6) exceeding the algorithmic range of rigid-body FFT docking, while all other receptors fall within 1528–1967.
  • Identical binding energy of −17.7 kcal/mol reported for both ErbB1 and ErbB2 in Table 1, indicative of copy-paste duplication.
  • Methods section (5.8) cites a PerkinElmer PinAAcle 900T for ICP-OES measurements; PinAAcle 900T is an atomic absorption spectrometer (AAS), not an ICP-OES instrument.
  • STRING protein-interaction network p-value of 0.0173 for a 37-node (Src + 36 partners) network is implausibly high relative to typical STRING enrichment outputs.
  • Image reuse / splicing analysis (Findings 1 and 3 of detection suite) could not be performed due to absence of pixel-level image data.
  • Evidence highlights

  • Table 1 / Page 9 — ZDOCK scores: ErbB1 = 13553.6; BMPR1A = 1528.46; BMPR1B = 1967.40; BMPR2 = 1601.76; ErbB2 = 1937.10; ErbB3 = 1778.69; ErbB4 = 1879.33. The single outlier is ~7–9× the magnitude of peers.
  • Table 1 / Page 9 — Binding energies: ErbB1 = −17.7 kcal/mol; ErbB2 = −17.7 kcal/mol (exact match to one decimal place).
  • Methods 5.8 / Page 15 — Stated technique: ICP-OES. Stated instrument: "PerkinElmer PinAAcle 900T" (an AAS platform).
  • Page 6 (text) — STRING v11 network: Src as central hub interacting with 36 partners; reported p = 0.0173.
  • DOI: 10.1002/adfm.76607
  • Notes

  • The ZDOCK outlier alone is sufficient to cast serious doubt on the molecular-docking component; authors should be asked to provide raw ZDOCK output logs.
  • The ICP-OES / AAS mismatch is either a critical methodological error or evidence that the described measurement was not actually performed with the cited instrument; raw instrument printouts should be requested.
  • The p = 0.0173 anomaly is suggestive but depends on STRING algorithm version specifics; should be re-verified by re-running STRING v11 with the same gene list.
  • Image-level verification (Western blots, immunofluorescence, histology) is strongly recommended once raw TIFF files are obtained, given the pattern of tabular irregularities.
  • All findings derive from textual and tabular content of the published PDF; pixel-level image forensics were not conducted.

Tags

#academic-fraud#data-fabrication#molecular-docking#image-not-analyzed#methodology-mismatch#statistics-anomaly#advanced-functional-materials#pubpeer-candidate

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