W. Michael Babinchak

MedicineBiochemistry, Genetics and Molecular Biology

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 5 papers. Top paper: “Small molecules as potent biphasic modulators of protein liquid-liquid phase separation”.

Small molecules as potent biphasic modulators of protein liquid-liquid phase separation

Nature Communications(2020)10.1038/s41467-020-19211-z

N/A

0DataRank · unranked

213 citations

Benjamin K. Dumm, Sarah Venus, Solomiia Boyko, Andrea Putnam, Eckhard Jankowsky +2 more

Liquid–Liquid Phase Separation and Its Mechanistic Role in Pathological Protein Aggregation

Journal of Molecular Biology(2020)10.1016/j.jmb.2020.03.004

N/A

0DataRank · unranked

305 citations

Witold K. Surewicz, W. Michael Babinchak

Studying Protein Aggregation in the Context of Liquid-liquid Phase Separation Using Fluorescence and Atomic Force Microscopy, Fluorescence and Turbidity Assays, and FRAP

BIO-PROTOCOL(2020)10.21769/bioprotoc.3489

N/A

0DataRank · unranked

24 citations

W. Michael Babinchak, Witold K. Surewicz

Cryo-EM structure of amyloid fibrils formed by the entire low complexity domain of TDP-43

bioRxiv (Cold Spring Harbor Laboratory)(2020)10.1101/2020.12.14.422689

N/A

0DataRank · unranked

27 citations

W. Michael Babinchak, Witold K. Surewicz, Qiuye Li

Cryo-EM structure of amyloid fibrils formed by the entire low complexity domain of TDP-43

Nature Communications(2021)10.1038/s41467-021-21912-y

N/A

0DataRank · unranked

144 citations

W. Michael Babinchak, Witold K. Surewicz, Qiuye Li