Christina Schoenherr

Institute for Research and Innovation in Social Services

MedicineChemistry

Pilot corpus only

This score is computed over theSindex pilot corpus and does not cover the full scientific literature. Scores are relative to papers we have ingested — papers, authors, and institutions outside the pilot are not represented. Methodology.

Top 100%percentile

0Author DataRank

Indexed papers

0in pilot corpus

datarank_citation_only_1hop_v6· scope data_onlyMethodology

Papers

Driven by 4 papers. Top paper: “TGM6, a helminth secretory product, mimics TGF-β binding to TβRII to antagonize TGF-β signaling in fibroblasts”.

TGM6, a helminth secretory product, mimics TGF-β binding to TβRII to antagonize TGF-β signaling in fibroblasts

bioRxiv (Cold Spring Harbor Laboratory)(2023)10.1101/2023.12.22.573140

N/A

0DataRank · unranked

5 citations

Tristin A. Schwartze, Ananya Mukundan, Christina Schoenherr, Shashi Prakash Singh, Maarten van Dinther +10 more

The helminth TGF-β mimic TGM4 is a modular ligand that binds CD44, CD49d and TGF-β receptors to preferentially target myeloid cells

bioRxiv (Cold Spring Harbor Laboratory)(2023)10.1101/2023.11.13.566701

N/A

0DataRank · unranked

1 citations

Danielle J. Smyth, Kyle T. Cunningham, Ananya Mukundan, Chang‐Hyeock Byeon, Cynthia S. Hinck +14 more

The TGF-β mimic TGM4 achieves cell specificity through combinatorial surface co-receptor binding

EMBO Reports(2024)10.1038/s44319-024-00323-2

N/A

0DataRank · unranked

10 citations

Danielle J. Smyth, Kyle T. Cunningham, Ananya Mukundan, Chang‐Hyeock Byeon, Cynthia S. Hinck +15 more

TGM6 is a helminth secretory product that mimics TGF-β binding to TGFBR2 to antagonize signaling in fibroblasts

Nature Communications(2025)10.1038/s41467-025-56954-z

N/A

0DataRank · unranked

11 citations

Tristin A. Schwartze, Ananya Mukundan, Christina Schoenherr, Shashi Prakash Singh, Maarten van Dinther +10 more